193 results on '"Craig B. Faulds"'
Search Results
2. Genome sequencing of Porostereum spadiceum to study the degradation of levofloxacin
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Amal Ben Ayed, Imen Akrout, Karima Staita, Quentin Albert, Stéphane Greff, Charlotte Simmler, Steven Ahrendt, Kurt LaButti, Anna Lipzen, Guifen He, Emily Savage, Jean Armengaud, Mélodie Kielbasa, David Navarro, Elodie Drula, Annick Turbé-Doan, Emmanuel Bertrand, Anne Lomascolo, Delphine Chaduli, Craig B. Faulds, Mohamed Chamkha, Amina Maalej, Kerrie Barry, Igor V. Grigoriev, Francis Martin, Héla Zouari-Mechichi, Giuliano Sciara, Tahar Mechichi, and Eric Record
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Biotransformation ,Fluoroquinolone ,Fungi ,Peroxidases ,Hazardous substance ,Environmental pollution ,TD172-193.5 ,Environmental sciences ,GE1-350 - Abstract
Despite various plans to rationalize antibiotic use, antibiotic resistance in environmental bacteria is increasing due to the accumulation of antibiotic residues in the environment. This study aimed to test the ability of basidiomycete fungal strains to biotransform the antibiotic levofloxacin, a widely-used third-generation broad-spectrum fluoroquinolone, and to propose enzyme targets potentially involved in this biotransformation. The biotransformation process was performed using fungal strains. Levofloxacin biotransformation reached 100% after 9 days of culture with Porostereum spadiceum BS34. Using genomics and proteomics analyses coupled with activity tests, we showed that P. spadiceum produces several heme-peroxidases together with H2O2-producing enzymes that could be involved in the antibiotic biotransformation process. Using UV and high-resolution mass spectrometry, we were able to detect five levofloxacin degradation products. Their putative identity based on their MS2 fragmentation patterns led to the conclusion that the piperazine moiety was the main target of oxidative modification of levofloxacin by P. spadiceum, leading to a decrease in antibiotic activity.
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- 2024
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3. Modification of a Marine Pine Kraft Lignin Sample by Enzymatic Treatment with a Pycnoporus cinnabarinus Laccase
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Sona Malric-Garajova, Florian Fortuna, Florian Pion, Elise Martin, Adithya Raveendran Thottathil, Audrey Guillemain, Annick Doan, Anne Lomascolo, Craig B. Faulds, Stéphanie Baumberger, Laurence Foulon, Brigitte Chabbert, Hélène de Baynast, Pascal Dubessay, Fabrice Audonnet, Emmanuel Bertrand, Giuliano Sciara, Sandra Tapin-Lingua, Paul-Henri Ducrot, Philippe Michaud, Véronique Aguié-Béghin, and Eric Record
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Pycnoporus cinnabarinus laccase ,kraft lignin ,industrial lignins ,depolymerization ,polymerization ,Organic chemistry ,QD241-441 - Abstract
Here, we report work on developing an enzymatic process to improve the functionalities of industrial lignin. A kraft lignin sample prepared from marine pine was treated with the high-redox-potential laccase from the basidiomycete fungus Pycnoporus cinnabarinus at three different concentrations and pH conditions, and with and without the chemical mediator 1-hydroxybenzotriazole (HBT). Laccase activity was tested in the presence and absence of kraft lignin. The optimum pH of PciLac was initially 4.0 in the presence and absence of lignin, but at incubation times over 6 h, higher activities were found at pH 4.5 in the presence of lignin. Structural changes in lignin were investigated by Fourier-transform infrared spectroscopy (FTIR) with differential scanning calorimetry (DSC), and solvent-extractable fractions were analyzed using high-performance size-exclusion chromatography (HPSEC) and gas chromatography–mass spectrometry (GC–MS). The FTIR spectral data were analyzed with two successive multivariate series using principal component analysis (PCA) and ANOVA statistical analysis to identify the best conditions for the largest range of chemical modifications. DSC combined with modulated DSC (MDSC) revealed that the greatest effect on glass transition temperature (Tg) was obtained at 130 U g cm−1 and pH 4.5, with the laccase alone or combined with HBT. HPSEC data suggested that the laccase treatments led to concomitant phenomena of oligomerization and depolymerization, and GC–MS revealed that the reactivity of the extractable phenolic monomers depended on the conditions tested. This study demonstrates that P. cinnabarinus laccase can be used to modify marine pine kraft lignin, and that the set of analytical methods implemented here provides a valuable tool for screening enzymatic treatment conditions.
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- 2023
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4. Screening of five marine-derived fungal strains for their potential to produce oxidases with laccase activities suitable for biotechnological applications
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Wissal Ben Ali, Delphine Chaduli, David Navarro, Christian Lechat, Annick Turbé-Doan, Emmanuel Bertrand, Craig B. Faulds, Giuliano Sciara, Laurence Lesage-Meessen, Eric Record, and Tahar Mechichi
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Marine-derived fungi ,Trichoderma asperellum ,Laccase-like activity ,Laccase ,Dyes ,Biotechnology ,TP248.13-248.65 - Abstract
Abstract Background Environmental pollution is one of the major problems that the world is facing today. Several approaches have been taken, from physical and chemical methods to biotechnological strategies (e.g. the use of oxidoreductases). Oxidative enzymes from microorganisms offer eco-friendly, cost–effective processes amenable to biotechnological applications, such as in industrial dye decolorization. The aim of this study was to screen marine-derived fungal strains isolated from three coastal areas in Tunisia to identify laccase-like activities, and to produce and characterize active cell-free supernatants of interest for dye decolorization. Results Following the screening of 20 fungal strains isolated from the harbors of Sfax and Monastir (Tunisia), five strains were identified that displayed laccase-like activities. Molecular-based taxonomic approaches identified these strains as belonging to the species Trichoderma asperellum, Stemphylium lucomagnoense and Aspergillus nidulans. Among these five isolates, one T. asperellum strain (T. asperellum 1) gave the highest level of secreted oxidative activities, and so was chosen for further studies. Optimization of the growth medium for liquid cultures was first undertaken to improve the level of laccase-like activity in culture supernatants. Finally, the culture supernatant of T. asperellum 1 decolorized different synthetic dyes belonging to diverse dye families, in the presence or absence of 1-hydroxybenzotriazole (HBT) as a mediator. Conclusions The optimal growth conditions to produce laccase-like active cell-free supernatants from T. asperellum 1 were 1.8 mM CuSO4 as an inducer, 1% NaCl to mimic a seawater environment and 3% sucrose as a carbon source. The culture supernatant of T. asperellum 1 effectively decolorized different synthetic dyes belonging to diverse chemical classes, and the presence of HBT as a mediator improved the decolorization process.
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- 2020
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5. Pycnoporus cinnabarinus glyoxal oxidases display differential catalytic efficiencies on 5-hydroxymethylfurfural and its oxidized derivatives
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Marianne Daou, Bassem Yassine, Saowanee Wikee, Eric Record, Françoise Duprat, Emmanuel Bertrand, and Craig B. Faulds
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5-Hydroxymethylfurfural ,Bio-catalysis ,Glyoxal oxidase ,2,5-Furancarboxylic acid ,Furan derivatives ,Biotechnology ,TP248.13-248.65 - Abstract
Abstract Background 5-Hydroxymethylfurfural (HMF), a major residual component of a lignocellulosic bio-refinery process, can be transformed into fundamental building blocks for green chemistry via oxidation. While chemical methods are well established, interest is also being directed into the enzymatic oxidation of HMF into the bio-plastic precursor 2,5-furandicarboxylic acid (FDCA). Results We demonstrate that three glyoxal oxidases (PciGLOX) isoenzymes from the Basidiomycete fungus Pycnoporus cinnabarinus were able to oxidize HMF, with PciGLOX2 and PciGLOX3 being the most efficient. The major reaction product obtained with the three isoenzymes was 5-hydroxymethyl-2-furancarboxylic (HMFCA), a precursor in polyesters and pharmaceuticals production, and very little subsequent conversion of this compound was observed. However, small concentrations of FDCA, a substitute for terephthalic acid in the production of polyesters, were also obtained. The oxidation of HMF was significantly boosted in the presence of catalase for PciGLOX2, leading to 70% HMFCA yield. The highest conversion percentages were observed on 2,5-furandicarboxaldehyde (DFF), a minor product from the reaction of PciGLOX on HMF. To bypass HMFCA accumulation and exploit the efficiency of PciGLOX in oxidizing DFF and 5-formyl-2-furan carboxylic acid (FFCA) towards FDCA production, HMF was oxidized in a cascade reaction with an aryl alcohol oxidase (UmaAAO). After 2 h of reaction, UmaAAO completely oxidized HMF to DFF and further to FFCA, with FDCA only being detected when PciGLOX3 was added to the reaction. The maximum yield of 16% FDCA was obtained 24 h after the addition of PciGLOX3 in the presence of catalase. Conclusions At least two conversion pathways for HMF oxidation can be considered for PciGLOX; however, the highest selectivity was seen towards the production of the valuable polyester precursor HMFCA. The three isoenzymes showed differences in their catalytic efficiencies and substrate specificities when reacted with HMF derivatives.
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- 2019
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6. Biotransformation of the Fluoroquinolone, Levofloxacin, by the White-Rot Fungus Coriolopsis gallica
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Amal Ben Ayed, Imen Akrout, Quentin Albert, Stéphane Greff, Charlotte Simmler, Jean Armengaud, Mélodie Kielbasa, Annick Turbé-Doan, Delphine Chaduli, David Navarro, Emmanuel Bertrand, Craig B. Faulds, Mohamed Chamkha, Amina Maalej, Héla Zouari-Mechichi, Giuliano Sciara, Tahar Mechichi, and Eric Record
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fluoroquinolones ,levofloxacin ,Coriolopsis gallica ,biotransformation ,laccases ,dye-decolorizing peroxidase ,Biology (General) ,QH301-705.5 - Abstract
The wastewater from hospitals, pharmaceutical industries and more generally human and animal dejections leads to environmental releases of antibiotics that cause severe problems for all living organisms. The aim of this study was to investigate the capacity of three fungal strains to biotransform the fluoroquinolone levofloxacin. The degradation processes were analyzed in solid and liquid media. Among the three fungal strains tested, Coriolopsis gallica strain CLBE55 (BRFM 3473) showed the highest removal efficiency, with a 15% decrease in antibiogram zone of inhibition for Escherichia coli cultured in solid medium and 25% degradation of the antibiotic in liquid medium based on high-performance liquid chromatography (HPLC). Proteomic analysis suggested that laccases and dye-decolorizing peroxidases such as extracellular enzymes could be involved in levofloxacin degradation, with a putative major role for laccases. Degradation products were proposed based on mass spectrometry analysis, and annotation suggested that the main product of biotransformation of levofloxacin by Coriolopsis gallica is an N-oxidized derivative.
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- 2022
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7. Optimization of the Decolorization of the Reactive Black 5 by a Laccase-like Active Cell-Free Supernatant from Coriolopsis gallica
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Amal Ben Ayed, Bilel Hadrich, Giuliano Sciara, Anne Lomascolo, Emmanuel Bertrand, Craig B. Faulds, Héla Zouari-Mechichi, Eric Record, and Tahar Mechichi
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RB5 decolorization ,Coriolopsis gallica ,laccase-like activity ,optimization ,response surface methodology ,Biology (General) ,QH301-705.5 - Abstract
The textile industry generates huge volumes of colored wastewater that require multiple treatments to remove persistent toxic and carcinogenic dyes. Here we studied the decolorization of a recalcitrant azo dye, Reactive Black 5, using laccase-like active cell-free supernatant from Coriolopsis gallica. Decolorization was optimized in a 1 mL reaction mixture using the response surface methodology (RSM) to test the influence of five variables, i.e., laccase-like activity, dye concentration, redox mediator (HBT) concentration, pH, and temperature, on dye decolorization. Statistical tests were used to determine regression coefficients and the quality of the models used, as well as significant factors and/or factor interactions. Maximum decolorization was achieved at 120 min (82 ± 0.6%) with the optimized protocol, i.e., laccase-like activity at 0.5 U mL−1, dye at 25 mg L−1, HBT at 4.5 mM, pH at 4.2 and temperature at 55 °C. The model proved significant (ANOVA test with p < 0.001): coefficient of determination (R²) was 89.78%, adjusted coefficient of determination (R²A) was 87.85%, and root mean square error (RMSE) was 10.48%. The reaction conditions yielding maximum decolorization were tested in a larger volume of 500 mL reaction mixture. Under these conditions, the decolorization rate reached 77.6 ± 0.4%, which was in good agreement with the value found on the 1 mL scale. RB5 decolorization was further evaluated using the UV-visible spectra of the treated and untreated dyes.
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- 2022
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8. Lavender- and lavandin-distilled straws: an untapped feedstock with great potential for the production of high-added value compounds and fungal enzymes
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Laurence Lesage-Meessen, Marine Bou, Christian Ginies, Didier Chevret, David Navarro, Elodie Drula, Estelle Bonnin, José C. del Río, Elise Odinot, Alexandra Bisotto, Jean-Guy Berrin, Jean-Claude Sigoillot, Craig B. Faulds, and Anne Lomascolo
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Lavender and lavandin straws ,Sugar and lignin ,Terpenes and phenolics ,Antioxidant ,Pycnoporus cinnabarinus ,Laccase ,Fuel ,TP315-360 ,Biotechnology ,TP248.13-248.65 - Abstract
Abstract Background Lavender (Lavandula angustifolia) and lavandin (a sterile hybrid of L. angustifolia × L. latifolia) essential oils are among those most commonly used in the world for various industrial purposes, including perfumes, pharmaceuticals and cosmetics. The solid residues from aromatic plant distillation such as lavender- and lavandin-distilled straws are generally considered as wastes, and consequently either left in the fields or burnt. However, lavender- and lavandin-distilled straws are a potentially renewable plant biomass as they are cheap, non-food materials that can be used as raw feedstocks for green chemistry industry. The objective of this work was to assess different pathways of valorization of these straws as bio-based platform chemicals and fungal enzymes of interest in biorefinery. Results Sugar and lignin composition analyses and saccharification potential of the straw fractions revealed that these industrial by-products could be suitable for second-generation bioethanol prospective. The solvent extraction processes, developed specifically for these straws, released terpene derivatives (e.g. τ-cadinol, β-caryophyllene), lactones (e.g. coumarin, herniarin) and phenolic compounds of industrial interest, including rosmarinic acid which contributed to the high antioxidant activity of the straw extracts. Lavender and lavandin straws were also suitable inducers for the secretion of a wide panel of lignocellulose-acting enzymes (cellulases, hemicellulases and oxido-reductases) from the white-rot model fungus Pycnoporus cinnabarinus. Interestingly, high amounts of laccase and several lytic polysaccharide monooxygenases were identified in the lavender and lavandin straw secretomes using proteomics. Conclusions The present study demonstrated that the distilled straws of lavender and lavandin are lignocellulosic-rich materials that can be used as raw feedstocks for producing high-added value compounds (antioxidants, aroma) and fungal oxidative enzymes, which represent opportunities to improve the decomposition of recalcitrant lignocellulose into biofuel. Hence, the structure and the physico-chemical properties of these straws clearly open new perspectives for use in biotechnological processes involving especially filamentous fungi. These approaches represent sustainable strategies to foster the development of a local circular bioeconomy.
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- 2018
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9. A Putative Lignin Copper Oxidase from Trichoderma reesei
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Mariane Daou, Alexandra Bisotto, Mireille Haon, Lydie Oliveira Correia, Betty Cottyn, Elodie Drula, Soňa Garajová, Emmanuel Bertrand, Eric Record, David Navarro, Sana Raouche, Stéphanie Baumberger, and Craig B. Faulds
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Trichoderma reesei ,technical lignin ,copper radical oxidase ,Biology (General) ,QH301-705.5 - Abstract
The ability of Trichoderma reesei, a fungus widely used for the commercial production of hemicellulases and cellulases, to grow and modify technical soda lignin was investigated. By quantifying fungal genomic DNA, T. reesei showed growth and sporulation in solid and liquid cultures containing lignin alone. The analysis of released soluble lignin and residual insoluble lignin was indicative of enzymatic oxidative conversion of phenolic lignin side chains and the modification of lignin structure by cleaving the β-O-4 linkages. The results also showed that polymerization reactions were taking place. A proteomic analysis conducted to investigate secreted proteins at days 3, 7, and 14 of growth revealed the presence of five auxiliary activity (AA) enzymes in the secretome: AA6, AA9, two AA3 enzymes), and the only copper radical oxidase encoded in the genome of T. reesei. This enzyme was heterologously produced and characterized, and its activity on lignin-derived molecules was investigated. Phylogenetic characterization demonstrated that this enzyme belonged to the AA5_1 family, which includes characterized glyoxal oxidases. However, the enzyme displayed overlapping physicochemical and catalytic properties across the AA5 family. The enzyme was remarkably stable at high pH and oxidized both, alcohols and aldehydes with preference to the alcohol group. It was also active on lignin-derived phenolic molecules as well as simple carbohydrates. HPSEC and LC-MS analyses on the reactions of the produced protein on lignin dimers (SS ββ, SS βO4 and GG β5) uncovered the polymerizing activity of this enzyme, which was accordingly named lignin copper oxidase (TrLOx). Polymers of up 10 units were formed by hydroxy group oxidation and radical formation. The activations of lignin molecules by TrLOx along with the co-secretion of this enzyme with reductases and FAD flavoproteins oxidoreductases during growth on lignin suggest a synergistic mechanism for lignin breakdown.
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- 2021
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10. Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity
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Corinne Ivaldi, Mariane Daou, Laurent Vallon, Alexandra Bisotto, Mireille Haon, Sona Garajova, Emmanuel Bertrand, Craig B. Faulds, Giuliano Sciara, Adrien Jacotot, Cyril Marchand, Mylène Hugoni, Harivony Rakotoarivonina, Marie-Noëlle Rosso, Caroline Rémond, Patricia Luis, and Eric Record
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lignocellulose degrading enzymes ,xylanases ,heterologous expression ,biomass degradation ,marine fungus ,mangrove ,Biology (General) ,QH301-705.5 - Abstract
Mangrove sediments from New Caledonia were screened for xylanase sequences. One enzyme was selected and characterized both biochemically and for its industrial potential. Using a specific cDNA amplification method coupled with a MiSeq sequencing approach, the diversity of expressed genes encoding GH11 xylanases was investigated beneath Avicenia marina and Rhizophora stylosa trees during the wet and dry seasons and at two different sediment depths. GH11 xylanase diversity varied more according to tree species and season, than with respect to depth. One complete cDNA was selected (OFU29) and expressed in Pichia pastoris. The corresponding enzyme (called Xyn11-29) was biochemically characterized, revealing an optimal activity at 40–50 °C and at a pH of 5.5. Xyn11-29 was stable for 48 h at 35 °C, with a half-life of 1 h at 40 °C and in the pH range of 5.5–6. Xyn11-29 exhibited a high hydrolysis capacity on destarched wheat bran, with 40% and 16% of xylose and arabinose released after 24 h hydrolysis. Its activity on wheat straw was lower, with a release of 2.8% and 6.9% of xylose and arabinose, respectively. As the protein was isolated from mangrove sediments, the effect of sea salt on its activity was studied and discussed.
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- 2021
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11. Exploring the Diversity of Fungal DyPs in Mangrove Soils to Produce and Characterize Novel Biocatalysts
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Amal Ben Ayed, Geoffroy Saint-Genis, Laurent Vallon, Dolores Linde, Annick Turbé-Doan, Mireille Haon, Marianne Daou, Emmanuel Bertrand, Craig B. Faulds, Giuliano Sciara, Martino Adamo, Roland Marmeisse, Sophie Comtet-Marre, Pierre Peyret, Danis Abrouk, Francisco J. Ruiz-Dueñas, Cyril Marchand, Mylène Hugoni, Patricia Luis, Tahar Mechichi, and Eric Record
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lignocellulose degrading enzymes ,dye-decolorizing peroxidases ,heterologous expression ,dye decolorization ,marine fungus ,mangrove ,Biology (General) ,QH301-705.5 - Abstract
The functional diversity of the New Caledonian mangrove sediments was examined, observing the distribution of fungal dye-decolorizing peroxidases (DyPs), together with the complete biochemical characterization of the main DyP. Using a functional metabarcoding approach, the diversity of expressed genes encoding fungal DyPs was investigated in surface and deeper sediments, collected beneath either Avicennia marina or Rhizophora stylosa trees, during either the wet or the dry seasons. The highest DyP diversity was observed in surface sediments beneath the R. stylosa area during the wet season, and one particular operational functional unit (OFU1) was detected as the most abundant DyP isoform. This OFU was found in all sediment samples, representing 51–100% of the total DyP-encoding sequences in 70% of the samples. The complete cDNA sequence corresponding to this abundant DyP (OFU 1) was retrieved by gene capture, cloned, and heterologously expressed in Pichia pastoris. The recombinant enzyme, called DyP1, was purified and characterized, leading to the description of its physical–chemical properties, its ability to oxidize diverse phenolic substrates, and its potential to decolorize textile dyes; DyP1 was more active at low pH, though moderately stable over a wide pH range. The enzyme was very stable at temperatures up to 50 °C, retaining 60% activity after 180 min incubation. Its ability to decolorize industrial dyes was also tested on Reactive Blue 19, Acid Black, Disperse Blue 79, and Reactive Black 5. The effect of hydrogen peroxide and sea salt on DyP1 activity was studied and compared to what is reported for previously characterized enzymes from terrestrial and marine-derived fungi.
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- 2021
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12. Fungal Treatment for the Valorization of Technical Soda Lignin
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Mariane Daou, Clementina Farfan Soto, Amel Majira, Laurent Cézard, Betty Cottyn, Florian Pion, David Navarro, Lydie Oliveira Correia, Elodie Drula, Eric Record, Sana Raouche, Stéphanie Baumberger, and Craig B. Faulds
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filamentous fungi ,technical lignin ,oxidoreductases ,secretomic analysis ,Polyporus brumalis ,Pycnoporus sanguineus ,Biology (General) ,QH301-705.5 - Abstract
Technical lignins produced as a by-product in biorefinery processes represent a potential source of renewable carbon. In consideration of the possibilities of the industrial transformation of this substrate into various valuable bio-based molecules, the biological deconstruction of a technical soda lignin by filamentous fungi was investigated. The ability of three basidiomycetes (Polyporus brumalis, Pycnoporus sanguineus and Leiotrametes menziesii) to modify this material, the resultant structural and chemical changes, and the secreted proteins during growth on this substrate were investigated. The three fungi could grow on the technical lignin alone, and the growth rate increased when the media were supplemented with glucose or maltose. The proteomic analysis of the culture supernatants after three days of growth revealed the secretion of numerous Carbohydrate-Active Enzymes (CAZymes). The secretomic profiles varied widely between the strains and the presence of technical lignin alone triggered the early secretion of many lignin-acting oxidoreductases. The secretomes were notably rich in glycoside hydrolases and H2O2-producing auxiliary activity enzymes with copper radical oxidases being induced on lignin for all strains. The lignin treatment by fungi modified both the soluble and insoluble lignin fractions. A significant decrease in the amount of soluble higher molar mass compounds was observed in the case of P. sanguineus. This strain was also responsible for the modification of the lower molar mass compounds of the lignin insoluble fraction and a 40% decrease in the thioacidolysis yield. The similarity in the activities of P. sanguineus and P. brumalis in modifying the functional groups of the technical lignin were observed, the results suggest that the lignin has undergone structural changes, or at least changes in its composition, and pave the route for the utilization of filamentous fungi to functionalize technical lignins and produce the enzymes of interest for biorefinery applications.
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- 2021
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13. Characterization of the CAZy Repertoire from the Marine-Derived Fungus Stemphylium lucomagnoense in Relation to Saline Conditions
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Wissal Ben Ali, David Navarro, Abhishek Kumar, Elodie Drula, Annick Turbé-Doan, Lydie Oliveira Correia, Stéphanie Baumberger, Emmanuel Bertrand, Craig B. Faulds, Bernard Henrissat, Giuliano Sciara, Tahar Mechichi, and Eric Record
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marine-derived fungus ,Stemphylium lucomagnoense ,saline adaptation ,lignocellulose-degrading enzymes ,secretome ,Biology (General) ,QH301-705.5 - Abstract
Even if the ocean represents a large part of Earth’s surface, only a few studies describe marine-derived fungi compared to their terrestrial homologues. In this ecosystem, marine-derived fungi have had to adapt to the salinity and to the plant biomass composition. This articles studies the growth of five marine isolates and the tuning of lignocellulolytic activities under different conditions, including the salinity. A de novo transcriptome sequencing and assembly were used in combination with a proteomic approach to characterize the Carbohydrate Active Enzymes (CAZy) repertoire of one of these strains. Following these approaches, Stemphylium lucomagnoense was selected for its adapted growth on xylan in saline conditions, its high xylanase activity, and its improved laccase activities in seagrass-containing cultures with salt. De novo transcriptome sequencing and assembly indicated the presence of 51 putative lignocellulolytic enzymes. Its secretome composition was studied in detail when the fungus was grown on either a terrestrial or a marine substrate, under saline and non-saline conditions. Proteomic analysis of the four S. lucomagnoense secretomes revealed a minimal suite of extracellular enzymes for plant biomass degradation and highlighted potential enzyme targets to be further studied for their adaptation to salts and for potential biotechnological applications.
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- 2020
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14. A Two-Step Bioconversion Process for Canolol Production from Rapeseed Meal Combining an Aspergillus niger Feruloyl Esterase and the Fungus Neolentinus lepideus
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Elise Odinot, Frédéric Fine, Jean-Claude Sigoillot, David Navarro, Oscar Laguna, Alexandra Bisotto, Corinne Peyronnet, Christian Ginies, Jérôme Lecomte, Craig B. Faulds, and Anne Lomascolo
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Aspergillus niger ,canolol ,feruloyl esterase ,Neolentinus lepideus ,rapeseed meal ,sinapic acid ,Biology (General) ,QH301-705.5 - Abstract
Rapeseed meal is a cheap and abundant raw material, particularly rich in phenolic compounds of biotechnological interest. In this study, we developed a two-step bioconversion process of naturally occurring sinapic acid (4-hydroxy-3,5-dimethoxycinnamic acid) from rapeseed meal into canolol by combining the complementary potentialities of two filamentous fungi, the micromycete Aspergillus niger and the basidiomycete Neolentinus lepideus. Canolol could display numerous industrial applications because of its high antioxidant, antimutagenic and anticarcinogenic properties. In the first step of the process, the use of the enzyme feruloyl esterase type-A (named AnFaeA) produced with the recombinant strain A. niger BRFM451 made it possible to release free sinapic acid from the raw meal by hydrolysing the conjugated forms of sinapic acid in the meal (mainly sinapine and glucopyranosyl sinapate). An amount of 39 nkat AnFaeA per gram of raw meal, at 55 °C and pH 5, led to the recovery of 6.6 to 7.4 mg of free sinapic acid per gram raw meal, which corresponded to a global hydrolysis yield of 68 to 76% and a 100% hydrolysis of sinapine. Then, the XAD2 adsorbent (a styrene and divinylbenzene copolymer resin), used at pH 4, enabled the efficient recovery of the released sinapic acid, and its concentration after elution with ethanol. In the second step, 3-day-old submerged cultures of the strain N. lepideus BRFM15 were supplied with the recovered sinapic acid as the substrate of bioconversion into canolol by a non-oxidative decarboxylation pathway. Canolol production reached 1.3 g/L with a molar yield of bioconversion of 80% and a productivity of 100 mg/L day. The same XAD2 resin, when used at pH 7, allowed the recovery and purification of canolol from the culture broth of N. lepideus. The two-step process used mild conditions compatible with green chemistry.
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- 2017
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15. Modification of a Marine Pine Kraft Lignin Sample by Enzymatic Treatment with a Pycnoporus cinnabarinus Laccase
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Record, Sona Malric-Garajova, Florian Fortuna, Florian Pion, Elise Martin, Adithya Raveendran Thottathil, Audrey Guillemain, Annick Doan, Anne Lomascolo, Craig B. Faulds, Stéphanie Baumberger, Laurence Foulon, Brigitte Chabbert, Hélène de Baynast, Pascal Dubessay, Fabrice Audonnet, Emmanuel Bertrand, Giuliano Sciara, Sandra Tapin-Lingua, Paul-Henri Ducrot, Philippe Michaud, Véronique Aguié-Béghin, and Eric
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Pycnoporus cinnabarinus laccase ,kraft lignin ,industrial lignins ,depolymerization ,polymerization - Abstract
Here, we report work on developing an enzymatic process to improve the functionalities of industrial lignin. A kraft lignin sample prepared from marine pine was treated with the high-redox-potential laccase from the basidiomycete fungus Pycnoporus cinnabarinus at three different concentrations and pH conditions, and with and without the chemical mediator 1-hydroxybenzotriazole (HBT). Laccase activity was tested in the presence and absence of kraft lignin. The optimum pH of PciLac was initially 4.0 in the presence and absence of lignin, but at incubation times over 6 h, higher activities were found at pH 4.5 in the presence of lignin. Structural changes in lignin were investigated by Fourier-transform infrared spectroscopy (FTIR) with differential scanning calorimetry (DSC), and solvent-extractable fractions were analyzed using high-performance size-exclusion chromatography (HPSEC) and gas chromatography–mass spectrometry (GC–MS). The FTIR spectral data were analyzed with two successive multivariate series using principal component analysis (PCA) and ANOVA statistical analysis to identify the best conditions for the largest range of chemical modifications. DSC combined with modulated DSC (MDSC) revealed that the greatest effect on glass transition temperature (Tg) was obtained at 130 U g cm−1 and pH 4.5, with the laccase alone or combined with HBT. HPSEC data suggested that the laccase treatments led to concomitant phenomena of oligomerization and depolymerization, and GC–MS revealed that the reactivity of the extractable phenolic monomers depended on the conditions tested. This study demonstrates that P. cinnabarinus laccase can be used to modify marine pine kraft lignin, and that the set of analytical methods implemented here provides a valuable tool for screening enzymatic treatment conditions.
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- 2023
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16. Biotransformation of the fluoroquinolone, levofloxacin, by the white-rot fungus $Coriolopsis\ gallica$
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Amal Ben Ayed, Imen Akrout, Quentin Albert, Stéphane Greff, Charlotte Simmler, Jean Armengaud, Mélodie Kielbasa, Annick Turbé-Doan, Delphine Chaduli, David Navarro, Emmanuel Bertrand, Craig B. Faulds, Mohamed Chamkha, Amina Maalej, Héla Zouari-Mechichi, Giuliano Sciara, Tahar Mechichi, Eric Record, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), École Nationale d'Ingénieurs de Sfax | National School of Engineers of Sfax (ENIS), Institut méditerranéen de biodiversité et d'écologie marine et continentale (IMBE), Avignon Université (AU)-Aix Marseille Université (AMU)-Institut de recherche pour le développement [IRD] : UMR237-Centre National de la Recherche Scientifique (CNRS), Service de Pharmacologie et Immunoanalyse (SPI), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Centre de Biotechnologie de Sfax (CBS), and The authors thank PHC-Utique project FUNZYBIO (Campus France Code: 47572QD, CMCU Code: 22G0814) for financial support.
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Microbiology (medical) ,levofloxacin ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,laccases ,fluoroquinolones ,Coriolopsis gallica ,biotransformation ,dye-decolorizing peroxidase ,Plant Science ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Ecology, Evolution, Behavior and Systematics - Abstract
International audience; The wastewater from hospitals, pharmaceutical industries and more generally human and animal dejections leads to environmental releases of antibiotics that cause severe problems for all living organisms. The aim of this study was to investigate the capacity of three fungal strains to biotransform the fluoroquinolone levofloxacin. The degradation processes were analyzed in solid and liquid media. Among the three fungal strains tested, $Coriolopsis\ gallica$ strain CLBE55 (BRFM 3473) showed the highest removal efficiency, with a 15% decrease in antibiogram zone of inhibition for Escherichia coli cultured in solid medium and 25% degradation of the antibiotic in liquid medium based on high-performance liquid chromatography (HPLC). Proteomic analysis suggested that laccases and dye-decolorizing peroxidases such as extracellular enzymes could be involved in levofloxacin degradation, with a putative major role for laccases. Degradation products were proposed based on mass spectrometry analysis, and annotation suggested that the main product of biotransformation of levofloxacin by $Coriolopsis\ gallica$ is an N-oxidized derivative.
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- 2022
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17. A Putative Lignin Copper Oxidase from Trichoderma reesei
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Craig B. Faulds, Sana Raouche, Emmanuel Bertrand, Alexandra Bisotto, Eric Record, Soňa Garajová, Mireille Haon, Mariane Daou, Elodie Drula, Betty Cottyn, Stéphanie Baumberger, Lydie Oliveira Correia, David Navarro, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Institut Jean-Pierre Bourgin (IJPB)
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Microbiology (medical) ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,QH301-705.5 ,Trichoderma reesei ,Flavoprotein ,Plant Science ,Cellulase ,macromolecular substances ,complex mixtures ,03 medical and health sciences ,chemistry.chemical_compound ,Lignin ,[CHIM]Chemical Sciences ,Biology (General) ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Ecology, Evolution, Behavior and Systematics ,[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Oxidase test ,copper radical oxidase ,biology ,030306 microbiology ,Chemistry ,fungi ,technology, industry, and agriculture ,food and beverages ,biology.organism_classification ,[SDE.ES]Environmental Sciences/Environmental and Society ,Enzyme ,Biochemistry ,Polymerization ,technical lignin ,biology.protein ,Glyoxal - Abstract
International audience; This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY)The ability of Trichoderma reesei, a fungus widely used for the commercial production of hemicellulases and cellulases, to grow and modify technical soda lignin was investigated. By quantifying fungal genomic DNA, T. reesei showed growth and sporulation in solid and liquid cultures containing lignin alone. The analysis of released soluble lignin and residual insoluble lignin was indicative of enzymatic oxidative conversion of phenolic lignin side chains and the modification of lignin structure by cleaving the β-O-4 linkages. The results also showed that polymerization reactions were taking place. A proteomic analysis conducted to investigate secreted proteins at days 3, 7, and 14 of growth revealed the presence of five auxiliary activity (AA) enzymes in the secretome: AA6, AA9, two AA3 enzymes), and the only copper radical oxidase encoded in the genome of T. reesei. This enzyme was heterologously produced and characterized, and its activity on lignin-derived molecules was investigated. Phylogenetic characterization demonstrated that this enzyme belonged to the AA5_1 family, which includes characterized glyoxal oxidases. However, the enzyme displayed overlapping physicochemical and catalytic properties across the AA5 family. The enzyme was remarkably stable at high pH and oxidized both, alcohols and aldehydes with preference to the alcohol group. It was also active on lignin-derived phenolic molecules as well as simple carbohydrates. HPSEC and LC-MS analyses on the reactions of the produced protein on lignin dimers (SS ββ, SS βO4 and GG β5) uncovered the polymerizing activity of this enzyme, which was accordingly named lignin copper oxidase (TrLOx). Polymers of up 10 units were formed by hydroxy group oxidation and radical formation. The activations of lignin molecules by TrLOx along with the co-secretion of this enzyme with reductases and FAD flavoproteins oxidoreductases during growth on lignin suggest a synergistic mechanism for lignin breakdown.
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- 2021
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18. Pycnoporus cinnabarinus glyoxal oxidases display differential catalytic efficiencies on 5-hydroxymethylfurfural and its oxidized derivatives
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Saowanee Wikee, Craig B. Faulds, Marianne Daou, Eric Record, Françoise Duprat, Bassem Yassine, Emmanuel Bertrand, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), École Centrale de Marseille (ECM), INDOX, Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Daou, Mariane, Duprat, Françoise, and Bertrand, Emmanuel
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Green chemistry ,2,5-Furancarboxylic acid ,Furan derivative ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Carboxylic acid ,lcsh:Biotechnology ,oxydation enzymatique ,Biotechnologies ,Mycology ,5-Hydroxymethylfurfural ,Bio-catalysis ,glyoxal oxidase ,010402 general chemistry ,01 natural sciences ,Applied Microbiology and Biotechnology ,Catalysis ,03 medical and health sciences ,chemistry.chemical_compound ,lcsh:TP248.13-248.65 ,Organic chemistry ,Aryl-alcohol oxidase ,pycnoporus cinnabarinus ,Molecular Biology ,Ecology, Evolution, Behavior and Systematics ,[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology ,030304 developmental biology ,pycnoporus ,Terephthalic acid ,chemistry.chemical_classification ,0303 health sciences ,hydroxymethyl furfural ,Glyoxal oxidase ,biology ,Research ,Cell Biology ,Pycnoporus cinnabarinus ,biology.organism_classification ,activité catalytique ,0104 chemical sciences ,Mycologie ,chemistry ,Yield (chemistry) ,Glyoxal ,Furan derivatives ,Biotechnology - Abstract
Background 5-Hydroxymethylfurfural (HMF), a major residual component of a lignocellulosic bio-refinery process, can be transformed into fundamental building blocks for green chemistry via oxidation. While chemical methods are well established, interest is also being directed into the enzymatic oxidation of HMF into the bio-plastic precursor 2,5-furandicarboxylic acid (FDCA). Results We demonstrate that three glyoxal oxidases (PciGLOX) isoenzymes from the Basidiomycete fungus Pycnoporus cinnabarinus were able to oxidize HMF, with PciGLOX2 and PciGLOX3 being the most efficient. The major reaction product obtained with the three isoenzymes was 5-hydroxymethyl-2-furancarboxylic (HMFCA), a precursor in polyesters and pharmaceuticals production, and very little subsequent conversion of this compound was observed. However, small concentrations of FDCA, a substitute for terephthalic acid in the production of polyesters, were also obtained. The oxidation of HMF was significantly boosted in the presence of catalase for PciGLOX2, leading to 70% HMFCA yield. The highest conversion percentages were observed on 2,5-furandicarboxaldehyde (DFF), a minor product from the reaction of PciGLOX on HMF. To bypass HMFCA accumulation and exploit the efficiency of PciGLOX in oxidizing DFF and 5-formyl-2-furan carboxylic acid (FFCA) towards FDCA production, HMF was oxidized in a cascade reaction with an aryl alcohol oxidase (UmaAAO). After 2 h of reaction, UmaAAO completely oxidized HMF to DFF and further to FFCA, with FDCA only being detected when PciGLOX3 was added to the reaction. The maximum yield of 16% FDCA was obtained 24 h after the addition of PciGLOX3 in the presence of catalase. Conclusions At least two conversion pathways for HMF oxidation can be considered for PciGLOX; however, the highest selectivity was seen towards the production of the valuable polyester precursor HMFCA. The three isoenzymes showed differences in their catalytic efficiencies and substrate specificities when reacted with HMF derivatives. Electronic supplementary material The online version of this article (10.1186/s40694-019-0067-8) contains supplementary material, which is available to authorized users.
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- 2019
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19. Treatment of wood fibres with laccases: improved hardboard properties through phenolic oligomerization
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Frédéric Legée, Craig B. Faulds, Laurent Cézard, Anne Lomascolo, Ilabahen Patel, Emmanuel Bertrand, Sandra Tapin-Lingua, Betty Cottyn, Giuliano Sciara, Eric Record, Soňa Garajová, Stéphanie Baumberger, Michael Lecourt, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), InTechFibres Division, European Commission under the INDOX projectKBBE-2013-7-613549French National Research Agency (ANR)ANR-19-CE43-0007-01, Institut Technologique Forêt Cellulose Bois-construction Ameublement (FCBA), and ANR-19-CE43-0007,FuncLIPRO,Preuve de concept pour la fonctionnalisation des lignines par l'application de traitements enzymatiques laccase-déshydrogénase pour l'obtention de matériaux biosourcés(2019)
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0106 biological sciences ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,engineering.material ,01 natural sciences ,Redox ,03 medical and health sciences ,chemistry.chemical_compound ,010608 biotechnology ,Lignin ,Organic chemistry ,General Materials Science ,Hardboard ,ComputingMilieux_MISCELLANEOUS ,030304 developmental biology ,Laccase ,0303 health sciences ,biology ,Pulp (paper) ,fungi ,Forestry ,Picea abies ,Pycnoporus cinnabarinus ,biology.organism_classification ,chemistry ,engineering ,Myceliophthora thermophila - Abstract
International audience; Laccase-treated wood fibres were tested for small-scale wet-process manufacture of hardboards. Two laccases of distinct redox potentials, one from Pycnoporus cinnabarinus and one from Myceliophthora thermophila, were compared in terms of their effect on the physical-chemical properties of the treated fibres and hardboards. Wood fibres were produced from Norway spruce (Picea abies) by thermomechanical pulping. The thermomechanical pulp was treated with each laccase in parallel, in the presence or absence of the synthetic laccase mediator 1-hydroxybenzotriazole (HBT). High-performance size-exclusion chromatography revealed that the ethanolic extractable phenolic compounds in the fibres underwent oligomerization upon enzymatic treatment, and that the extent of oligomerization was dependent on the enzyme source and concentration and on the presence or absence of mediator. Lower lignin oligomerization levels led to higher (up to twofold) fibre internal bonding, whereas higher lignin oligomerization levels led to higher fibre hydrophobisation. X-ray photoelectron spectroscopy revealed a significant change in surface lignin content. These results demonstrate pre-treatment of spruce fibres with laccase-mediator systems prior to hot processing can improve the mechanical resistance of hardboards while using lower amounts of enzyme.
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- 2021
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20. Effects of successive microwave and enzymatic treatments on the release of p-hydroxycinnamic acids from two types of grass biomass
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Aurélie Bichot, Sana Raouche, Craig B. Faulds, Valérie Méchin, Nicolas Bernet, Jean-Philippe Delgenès, Diana García-Bernet, Laboratoire de Biotechnologie de l'Environnement [Narbonne] (LBE), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro Montpellier, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Ph.D. Grant allocated by GAIA Ph.D. School, and Carnot 3BCAR France research network (Valéoris project)
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grass biomass ,Environmental Engineering ,Enzymatic hydrolysis ,[SDE.IE]Environmental Sciences/Environmental Engineering ,Biomedical Engineering ,Bioengineering ,p-hydroxycinnamic acids ,microwave pretreatment ,Biotechnology - Abstract
International audience; Biomass recalcitrance is one of the main bottlenecks in lignocellulosic biorefinery deployment. Physico-chemical pretreatments and enzymatic hydrolysis are two procedures that can be combined to overcome this recalcitrance. In this study microwave pretreatment has been selected for its relevant conditions that allow for biomass recalcitrance to be reduced, along with the maintenance of a low consumption of energy and reactants. A xylanolytic enzymatic cocktail, Rovabio® Advance, was investigated for its ability to hydrolyze maize stalks and Miscanthus leaves after pressurized, chemical-free microwave pretreatment. This combination was implemented to increase the breakage of ester bonds and thus facilitate the release of p-hydroxycinnamic acids. This study demonstrates how, in comparison with Miscanthus, both pretreatments are more effective in releasing p-hydroxycinnamic acids from maize stalks, due to their lower parietal content. The successive free-chemical process seems to be particularly promising on maize stalks, since it led to a ferulic acid release yield of 18.2%, compared to 5.5% for microwave pretreatment only or 7.6% when performing enzymatic hydrolysis without a microwave pretreatment step.
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- 2022
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21. Screening of five marine-derived fungal strains for their potential to produce oxidases with laccase activities suitable for biotechnological applications
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Emmanuel Bertrand, Christian Lechat, Craig B. Faulds, Eric Record, Laurence Lesage-Meessen, Delphine Chaduli, Wissal Ben Ali, Tahar Mechichi, Annick Turbé-Doan, Giuliano Sciara, David Navarro, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), École Nationale d'Ingénieurs de Sfax | National School of Engineers of Sfax (ENIS), ASCOfrance, Institut des Matériaux Jean Rouxel (IMN), Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-Université de Nantes (UN), Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Nantes (UN)-Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), and Université de Nantes (UN)-Université de Nantes (UN)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
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food.ingredient ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,lcsh:Biotechnology ,Microorganism ,[SDV]Life Sciences [q-bio] ,Environmental pollution ,010501 environmental sciences ,01 natural sciences ,Aspergillus nidulans ,Marine-derived fungi ,Laccase-like activity ,03 medical and health sciences ,chemistry.chemical_compound ,food ,Ascomycota ,lcsh:TP248.13-248.65 ,Oxidative enzyme ,Mass Screening ,Seawater ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Food science ,Coloring Agents ,Phylogeny ,Dyes ,030304 developmental biology ,0105 earth and related environmental sciences ,Laccase ,0303 health sciences ,Growth medium ,biology ,Stemphylium ,Fungi ,biology.organism_classification ,Seaweed ,Trichoderma asperellum ,chemistry ,13. Climate action ,Hypocreales ,[SDE]Environmental Sciences ,LaccaseDyes ,Research Article ,Biotechnology - Abstract
Background Environmental pollution is one of the major problems that the world is facing today. Several approaches have been taken, from physical and chemical methods to biotechnological strategies (e.g. the use of oxidoreductases). Oxidative enzymes from microorganisms offer eco-friendly, cost–effective processes amenable to biotechnological applications, such as in industrial dye decolorization. The aim of this study was to screen marine-derived fungal strains isolated from three coastal areas in Tunisia to identify laccase-like activities, and to produce and characterize active cell-free supernatants of interest for dye decolorization. Results Following the screening of 20 fungal strains isolated from the harbors of Sfax and Monastir (Tunisia), five strains were identified that displayed laccase-like activities. Molecular-based taxonomic approaches identified these strains as belonging to the species Trichoderma asperellum, Stemphylium lucomagnoense and Aspergillus nidulans. Among these five isolates, one T. asperellum strain (T. asperellum 1) gave the highest level of secreted oxidative activities, and so was chosen for further studies. Optimization of the growth medium for liquid cultures was first undertaken to improve the level of laccase-like activity in culture supernatants. Finally, the culture supernatant of T. asperellum 1 decolorized different synthetic dyes belonging to diverse dye families, in the presence or absence of 1-hydroxybenzotriazole (HBT) as a mediator. Conclusions The optimal growth conditions to produce laccase-like active cell-free supernatants from T. asperellum 1 were 1.8 mM CuSO4 as an inducer, 1% NaCl to mimic a seawater environment and 3% sucrose as a carbon source. The culture supernatant of T. asperellum 1 effectively decolorized different synthetic dyes belonging to diverse chemical classes, and the presence of HBT as a mediator improved the decolorization process.
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- 2020
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22. Enzyme Properties of a Laccase Obtained from the Transcriptome of the Marine-Derived Fungus
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Wissal Ben, Ali, Amal Ben, Ayed, Annick, Turbé-Doan, Emmanuel, Bertrand, Yann, Mathieu, Craig B, Faulds, Anne, Lomascolo, Giuliano, Sciara, Eric, Record, and Tahar, Mechichi
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enzyme properties ,Aquatic Organisms ,Salinity ,salt tolerance ,Laccase ,heterologous expression ,Hydrogen-Ion Concentration ,Article ,Ascomycota ,Stemphylium ,Aspergillus niger ,alkaline ,Cloning, Molecular ,Transcriptome ,Oxidation-Reduction - Abstract
Only a few studies have examined how marine-derived fungi and their enzymes adapt to salinity and plant biomass degradation. This work concerns the production and characterisation of an oxidative enzyme identified from the transcriptome of marine-derived fungus Stemphylium lucomagnoense. The laccase-encoding gene SlLac2 from S. lucomagnoense was cloned for heterologous expression in Aspergillus niger D15#26 for protein production in the extracellular medium of around 30 mg L−1. The extracellular recombinant enzyme SlLac2 was successfully produced and purified in three steps protocol: ultrafiltration, anion-exchange chromatography, and size exclusion chromatography, with a final recovery yield of 24%. SlLac2 was characterised by physicochemical properties, kinetic parameters, and ability to oxidise diverse phenolic substrates. We also studied its activity in the presence and absence of sea salt. The molecular mass of SlLac2 was about 75 kDa, consistent with that of most ascomycete fungal laccases. With syringaldazine as substrate, SlLac2 showed an optimal activity at pH 6 and retained nearly 100% of its activity when incubated at 50°C for 180 min. SlLac2 exhibited more than 50% of its activity with 5% wt/vol of sea salt.
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- 2020
23. Characterization of the CAZy Repertoire from the Marine-Derived Fungus Stemphylium lucomagnoense in Relation to Saline Conditions
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Annick Turbé-Doan, Tahar Mechichi, Stéphanie Baumberger, Wissal Ben Ali, Bernard Henrissat, Craig B. Faulds, Giuliano Sciara, Lydie Oliveira Correia, Emmanuel Bertrand, David Navarro, Eric Record, Elodie Drula, Abhishek Kumar, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Manipal academy of Higher Education, Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Aix Marseille Université (AMU), Centre National de la Recherche Scientifique (CNRS), Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and École Nationale d'Ingénieurs de Sfax | National School of Engineers of Sfax (ENIS)
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Proteomics ,Salinity ,food.ingredient ,CAZy ,Proteome ,[SDV]Life Sciences [q-bio] ,Pharmaceutical Science ,Fungus ,Stemphylium lucomagnoense ,Lignin ,Article ,Substrate Specificity ,Fungal Proteins ,03 medical and health sciences ,food ,Ascomycota ,Drug Discovery ,Databases, Genetic ,saline adaptation ,Seawater ,Pharmacology, Toxicology and Pharmaceutics (miscellaneous) ,lcsh:QH301-705.5 ,030304 developmental biology ,Laccase ,chemistry.chemical_classification ,0303 health sciences ,Stemphylium ,biology ,030306 microbiology ,Gene Expression Profiling ,lignocellulose-degrading enzymes ,Salt Tolerance ,15. Life on land ,biology.organism_classification ,Xylan ,Enzymes ,secretome ,Enzyme ,chemistry ,Biochemistry ,lcsh:Biology (General) ,Xylanase ,marine-derived fungus ,Transcriptome ,Water Microbiology - Abstract
Even if the ocean represents a large part of Earth&rsquo, s surface, only a few studies describe marine-derived fungi compared to their terrestrial homologues. In this ecosystem, marine-derived fungi have had to adapt to the salinity and to the plant biomass composition. This articles studies the growth of five marine isolates and the tuning of lignocellulolytic activities under different conditions, including the salinity. A de novo transcriptome sequencing and assembly were used in combination with a proteomic approach to characterize the Carbohydrate Active Enzymes (CAZy) repertoire of one of these strains. Following these approaches, Stemphylium lucomagnoense was selected for its adapted growth on xylan in saline conditions, its high xylanase activity, and its improved laccase activities in seagrass-containing cultures with salt. De novo transcriptome sequencing and assembly indicated the presence of 51 putative lignocellulolytic enzymes. Its secretome composition was studied in detail when the fungus was grown on either a terrestrial or a marine substrate, under saline and non-saline conditions. Proteomic analysis of the four S. lucomagnoense secretomes revealed a minimal suite of extracellular enzymes for plant biomass degradation and highlighted potential enzyme targets to be further studied for their adaptation to salts and for potential biotechnological applications.
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- 2020
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24. Rheology and microstructure of gels based on wheat arabinoxylans enzymatically modified in arabinose to xylose ratio
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Agustín Rascón-Chu, Madhuvanti S. Kale, Craig B. Faulds, Jorge A. Márquez-Escalante, Yolanda L. López-Franco, Elisa M. Valenzuela-Soto, Alfonso A. Gardea, Madhav P. Yadav, Jaime Lizardi-Mendoza, and Elizabeth Carvajal-Millan
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Arabinose ,chemistry.chemical_classification ,Nutrition and Dietetics ,genetic structures ,010405 organic chemistry ,Scanning electron microscope ,02 engineering and technology ,Xylose ,021001 nanoscience & nanotechnology ,Microstructure ,Polysaccharide ,01 natural sciences ,0104 chemical sciences ,Ferulic acid ,chemistry.chemical_compound ,Crystallography ,chemistry ,Rheology ,Covalent bond ,0210 nano-technology ,Agronomy and Crop Science ,Food Science ,Biotechnology - Abstract
Background Arabinoxylans (AX) are polysaccharides constituted by a backbone of xyloses with arabinose substituents ester-linked to ferulic acid (FA). The arabinose to xylose ratio (A/X) in AX may vary from 0.3 to 1.1. AX form covalent gels by cross-linking of FA but physical interactions between AX chains also contribute to the network formation. The objective of this study was to investigate the rheological and microstructural characteristics of gels based on AX enzymatically modified in A/X. Results Tailored AX presented A/X ranging from 0.68 to 0.51 and formed covalent gels. Dimers of FA content and elasticity (G’) increased from 0.31 to 0.39 g kg−1 AX and from 106 to 164 Pa when the A/X in the polysaccharide decreased from 0.68 to 0.51. Atomic Force Microscopy (AFM) images of AX gels showed a sponge-like microstructure at A/X = 0.68 while at lower values, gels presented a more compact microstructure. Scanning electron microscopy (SEM) analysis of AX gels show an arrangement of different morphology, passing from an imperfect honeycomb (A/X = 0.68) to a flakes-like microstructure (A/X = 0.51). Conclusion Lower A/X values favor the aggregation of AX chains resulting in an increase in di-FA content which improve the rheological and microstructural characteristics of the gel formed.
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- 2017
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25. Characterization and Dye Decolorization Potential of Two Laccases from the Marine-Derived Fungus Pestalotiopsis sp
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Craig B. Faulds, Giuliano Sciara, Anne Lomascolo, Eric Record, Abhishek Kumar, Saowanee Wikee, Saisamorn Lumyong, Annick Turbé-Doan, Yann Mathieu, Juliette Hatton, Marianne Daou, Chiang Mai University, Sup'Biotech, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Christian-Albrechts University of Kiel, Chiang Mai University (CMU), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), and European Project: 613549,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,INDOX(2013)
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0106 biological sciences ,0301 basic medicine ,Salinity ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Pestalotiopsis ,01 natural sciences ,propriété catalytique ,Substrate Specificity ,laccase ,lcsh:Chemistry ,Enzyme Stability ,Cloning, Molecular ,Coloring Agents ,lcsh:QH301-705.5 ,Spectroscopy ,dye decolorization ,chemistry.chemical_classification ,application biotechnologique ,biology ,Chemistry ,[SDE.IE]Environmental Sciences/Environmental Engineering ,Temperature ,heterologous expression ,General Medicine ,Hydrogen-Ion Concentration ,Recombinant Proteins ,3. Good health ,Computer Science Applications ,Solvent ,mécanisme physicochimique ,Aspergillus niger ,medicine.drug ,food.ingredient ,Biotechnologies ,Article ,Catalysis ,Inorganic Chemistry ,hydroxybenzotriazole ,Industrial Microbiology ,03 medical and health sciences ,food ,expression hétérologue ,medicine ,Amino Acid Sequence ,Physical and Theoretical Chemistry ,salt tolerance ,Molecular Biology ,Laccase ,Sea salt ,Organic Chemistry ,Fungi ,Cresol ,biology.organism_classification ,030104 developmental biology ,Enzyme ,lcsh:Biology (General) ,lcsh:QD1-999 ,pestalotiopsis funerea ,Heterologous expression ,010606 plant biology & botany ,Nuclear chemistry - Abstract
Two laccase-encoding genes from the marine-derived fungus Pestalotiopsis sp. have been cloned in Aspergillus niger for heterologous production, and the recombinant enzymes have been characterized to study their physicochemical properties, their ability to decolorize textile dyes for potential biotechnological applications, and their activity in the presence of sea salt. The optimal pH and temperature of PsLac1 and PsLac2 differed in relation to the substrates tested, and both enzymes were shown to be extremely stable at temperatures up to 50 °, C, retaining 100% activity after 3 h at 50 °, C. Both enzymes were stable between pH 4&ndash, 6. Different substrate specificities were exhibited, and the lowest Km and highest catalytic efficiency values were obtained against syringaldazine and 2,6-dimethoxyphenol (DMP) for PsLac1 and PsLac2, respectively. The industrially important dyes&mdash, Acid Yellow, Bromo Cresol Purple, Nitrosulfonazo III, and Reactive Black 5&mdash, were more efficiently decolorized by PsLac1 in the presence of the redox mediator 1-hydroxybenzotriazole (HBT). Activities were compared in saline conditions, and PsLac2 seemed more adapted to the presence of sea salt than PsLac1. The overall surface charges of the predicted PsLac three-dimensional models showed large negatively charged surfaces for PsLac2, as found in proteins for marine organisms, and more balanced solvent exposed charges for PsLac1, as seen in proteins from terrestrial organisms.
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- 2019
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26. Arthrospira maxima OF15 biomass cultivation at laboratory and pilot scale from sugarcane vinasse for potential biological new peptides production
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Grecia E. Barriga Montalvo, Carlos Ricardo Soccol, Emmanuel Bertrand, Craig B. Faulds, Júlio Cesar de Carvalho, Sandro J.R. Bonatto, Vanete Thomaz-Soccol, Luciana Porto de Souza Vandenberghe, Maria Rosa Machado Prado, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Institut Pascal (IP), SIGMA Clermont (SIGMA Clermont)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Institut Pascal - Clermont Auvergne (IP), and Sigma CLERMONT (Sigma CLERMONT)-Université Clermont Auvergne (UCA)-Centre National de la Recherche Scientifique (CNRS)
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0106 biological sciences ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Food industry ,Biomass ,Pilot Projects ,010501 environmental sciences ,01 natural sciences ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Microalgae ,Food science ,Waste Management and Disposal ,Wastewater quality indicators ,ComputingMilieux_MISCELLANEOUS ,2. Zero hunger ,Chemistry ,anti-inflammatoire ,General Medicine ,peptide ,Saccharum ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM] ,Biofuel ,Antioxidant ,Peptide Biosynthesis ,Environmental Engineering ,Vinasse ,Bioengineering ,Biotechnologies ,Sugarcane liquid residue ,Hydrolysis ,Peptides ,Antimicrobial ,Anti-inflammatory ,antioxydant ,Bioenergy ,010608 biotechnology ,Enzymatic hydrolysis ,Spirulina ,biomasse ,[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering ,produit de canne à sucre ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,0105 earth and related environmental sciences ,micro-algue ,Biological Products ,Renewable Energy, Sustainability and the Environment ,business.industry ,antimicrobien ,business ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition - Abstract
International audience; An environmental friendly process was developed to produce Arthrospira maxima's biomass from sugarcane vinasse, which was generated in a bioethanol production chain, at laboratory and pilot scale. Peptides fractions were than obtained from enzymatically hydrolyzed biomass. High microalgae biomass productivities were reached (0.150 g L-1day-1) coupled with a significant reduction of BOD and COD (89.2 and 81%, respectively). Three peptide fractions were obtained from microalgae biomass through single or sequential enzymatic hydrolysis. Antioxidant, antimicrobial, anti-inflammatory, and/or anti-collagenase activities of biopetides’ fractions were observed. The PHS showed multi-biological activities. The three peptides fractions could be potential candidates for different applications in pharmaceutical, cosmetic and food industry.
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- 2019
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27. The amazing potential of fungi: 50 ways we can exploit fungi industrially
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Nimali I. de Silva, Rajesh Jeewon, Jake Winiski, Pattana Kakumyan, Marc Stadler, Jaturong Kumla, Jiye Yan, Ruvishika S. Jayawardena, Chayanard Phukhamsakda, Kanaporn Sujarit, Siraprapa Brooks, Achala R. Rathnayaka, Meghan O’Brien, Naritsada Thongklang, Eleni Gentekaki, Pranami D. Abeywickrama, Peter E. Mortimer, Dulanjalee Harishchandra, Peter Mueller, Nakarin Suwannarach, Thatsanee Luangharn, Kevin D. Hyde, Sylvie Rapior, Benjarong Thongbai, Thitipone Suwunwong, Karaba N. Nataraja, Jianchu Xu, Rashika S. Brahamanage, Craig B. Faulds, Hridya Hemachandran, Sehroon Khan, Samantha C. Karunarathna, Trichur S. Suryanarayanan, Sinang Hongsanan, Boontiya Chuankid, Birthe Sandargo, Ning-Guo Liu, Sadia Nadir, Janith V. S. Aluthmuhandiram, Mingkwan Doilom, Diana S. Marasinghe, Watsana Penkhrue, K. W. Thilini Chethana, Anuruddha Karunarathna, Venkat Gopalan, Allen Grace Niego, Resurreccion B. Sadaba, Clara Chepkirui, Putarak Chomnunti, Erandi Yasanthika, Uma Shaanker Ramanan, Danushka S. Tennakoon, Saisamorn Lumyong, Binu C. Samarakoon, Amornrat Chaiyasen, Sureeporn Nontachaiyapoom, Wasan Sriprom, Jian-Kui Liu, S. Nuwanthika Wijesinghe, Ramamoorthy Siva, Allan Patrick G. Macabeo, Dan Meeks, De-Ping Wei, Mae Fah Luang University [Thaïlande] (MFU), Kunming Institute of Botany [CAS] (KIB), Chinese Academy of Sciences [Beijing] (CAS), Centre d’Ecologie Fonctionnelle et Evolutive (CEFE), Université Paul-Valéry - Montpellier 3 (UPVM)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Faculty of Computer Science, Dalhousie University [Halifax], Institute of Excellence in Fungal Research and School of Science, German Centre for Infection Research (DZIF), XDB31000000, DBG6180015, 621C1535, DBG6180033, 2018PC0006, 256108A3070006, 41761144055 41771063 Y4ZK111B01, PHD57I0015, DBT-NER/Agri/24/2013, NAHEP/CAAST/2018-19, HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany., Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Université Paul-Valéry - Montpellier 3 (UPVM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut de Recherche pour le Développement (IRD [France-Sud]), Kunming Institute of Botany, Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Paul-Valéry - Montpellier 3 (UM3), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), and Université Paul-Valéry - Montpellier 3 (UM3)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)
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Fungal biodiversity ,Resource (biology) ,Biocontrôle ,Exploit ,Mushrooms ,[SDV]Life Sciences [q-bio] ,champignon ,Biotechnologies ,Biology ,biodiversité ,03 medical and health sciences ,application industrielle ,Mycology ,[CHIM]Chemical Sciences ,Ecology, Evolution, Behavior and Systematics ,Economic potential ,030304 developmental biology ,2. Zero hunger ,Biocontrol ,Biodiversity ,Biotechnology ,Food ,Fungi ,0303 health sciences ,Ecology ,030306 microbiology ,Agroforestry ,fungi ,biotechnologie alimentaire ,Flow chart ,[SDE]Environmental Sciences - Abstract
Fungi are an understudied, biotechnologically valuable group of organisms. Due to the immense range of habitats that fungi inhabit, and the consequent need to compete against a diverse array of other fungi, bacteria, and animals, fungi have developed numerous survival mechanisms. The unique attributes of fungi thus herald great promise for their application in biotechnology and industry. Moreover, fungi can be grown with relative ease, making production at scale viable. The search for fungal biodiversity, and the construction of a living fungi collection, both have incredible economic potential in locating organisms with novel industrial uses that will lead to novel products. This manuscript reviews fifty ways in which fungi can potentially be utilized as biotechnology. We provide notes and examples for each potential exploitation and give examples from our own work and the work of other notable researchers. We also provide a flow chart that can be used to convince funding bodies of the importance of fungi for biotechnological research and as potential products. Fungi have provided the world with penicillin, lovastatin, and other globally significant medicines, and they remain an untapped resource with enormous industrial potential. © 2019, The Author(s).
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- 2019
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28. Release of phenolic acids from sunflower and rapeseed meals using different carboxylic esters hydrolases from Aspergillus niger
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Jean-Claude Sigoillot, Oscar Laguna, Craig B. Faulds, Pierre Villeneuve, Elise Odinot, Laurence Lesage-Meessen, Frédéric Fine, Jérôme Lecomte, Bruno Baréa, Anne Lomascolo, Eric Record, Alexandra Bisotto, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Terres Inovia, Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), French Government under the reference ANR-001-01 supported this work, as part of the Investments for the Future, Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)
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0106 biological sciences ,Sous-produit d'huilerie ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Hydrolyse enzymatique ,chlorogenate esterase ,01 natural sciences ,rapeseed and sunflower meals ,chemistry.chemical_compound ,Hydrolysis ,Tourteau de tournesol ,Feruloyl esterase ,Acide phénolique ,Enzymatic hydrolysis ,Sinapine ,Caffeic acid ,Q51 - Technologie des aliments pour animaux ,feruloyl esterase ,sinapic acid ,Food science ,2. Zero hunger ,biology ,010405 organic chemistry ,Chemistry ,Aspergillus niger ,Q70 - Traitement des déchets agricoles ,Transesterification ,Quinic acid ,Hydrolase ester carboxylique ,biology.organism_classification ,0104 chemical sciences ,caffeic acid ,Agronomy and Crop Science ,Tourteau de colza ,010606 plant biology & botany - Abstract
Sunflower and rapeseed meals are agro-industrial coproducts that contain high amount of phenolics (1–4 % dry matter), mostly as esters of caffeic acid (CA) and sinapic acid (SA), respectively. The enzymatic hydrolysis of the ester bonds enables to recover the corresponding free phenolic acids that are bioactive compounds and platform molecules for various applications in green chemistry. Here we aimed to find the best route for producing free CA and SA by applying various fungal carboxylic ester hydrolases from recombinant Aspergillus niger strains either directly on crude meal or on their phenolic extracts obtained by methanolic extraction. Two types of meals were studied: (i) industrial (commercial) meals (I-meals), produced by a process that includes cooking at 95–100 °C and steam desolventizing at 105–107 °C, and (ii) non-industrial meals (NI-meals) obtained at pilot-scale with much milder heat treatment, that offer a higher total phenolic content. CA release through hydrolysis of sunflower meal (SFM) was successfully achieved with A. niger type-B feruloyl esterase (AnFaeB) and chlorogenic acid esterase (ChlE). Maximal amount of free CA released was of 54.0 ± 1.1 to 59.8 ± 2.1 μmol/g defatted dry matter (DDM) from I-SFM (94–100% hydrolysis yield) against 42.0 ± 1.1 to 52.3 ± 0.2 μmol/g DDM (59–73% hydrolysis yield) from NI- SFM in which CA release was hampered by a phenolic oxidation side-reaction, seemingly due to meal endogenous polyphenol oxidase activities. AnFaeB and ChlE hydrolysis of phenolic extracts from NI-SFM increased the CA amount obtained to 55.0–68.1 μmol/g DDM (77–95% hydrolysis yield). In all cases, AnFaeB showed broader specificity towards SFM caffeoyl quinic acid isomers than ChlE. In particular, ChlE did not hydrolyze 3-O-caffeoylquinic acid. The maximal amount of free SA released by AnFaeA hydrolysis was 41.3 ± 0.3 μmol/g DDM from NI-SFM (50% hydrolysis yield) and 32.3 ± 0.4 μmol/g DDM from the phenolic extract (64% hydrolysis yield), with AnFaeA also having sinapine transesterification activity that led to the synthesis of 1,2-di-O-sinapoyl-β-D-glucose. Finally, of all the substrates tested for enzymatic hydrolysis in our conditions, I-RSM and NI-SFM extract showed the best compromise between initial total phenolic content, hydrolysis yields and amounts of CA/SA released.
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- 2019
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29. Feruloyl esterases: Biocatalysts to overcome biomass recalcitrance and for the production of bioactive compounds
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Craig B. Faulds, Bianca Oliva, Fernando Segato, Wanderley Dantas dos Santos, Dyoni Matias de Oliveira, Thatiane R. Mota, Rogério Marchiosi, Osvaldo Ferrarese-Filho, Universidade Estadual de Maringà (UEM), Universidade de São Paulo (USP), Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), FAPESP, contract numbers 2014/18714-2 and 2017/00525-0, and Universidade de São Paulo = University of São Paulo (USP)
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0106 biological sciences ,Agriculture and Food Sciences ,ENZYMATIC-SYNTHESIS ,Microorganism ,Biomass ,010501 environmental sciences ,SACARIFICAÇÃO ,01 natural sciences ,Substrate Specificity ,Ferulic acid ,chemistry.chemical_compound ,Basic knowledge ,ACID ESTERASE ,Genome mining ,Waste Management and Disposal ,2. Zero hunger ,Vegetal Biology ,Cell wall ,SUGARCANE BAGASSE ,General Medicine ,SUBSTRATE-SPECIFICITY ,PHENOLIC-ACIDS ,TRICHODERMA-REESEI ,Biochemistry ,Biofuel ,Carbohydrate esterases ,TALAROMYCES-STIPITATUS ,Lignocellulose ,Biotechnology ,Environmental Engineering ,Coumaric Acids ,HETEROLOGOUS EXPRESSION ,Bioengineering ,ASPERGILLUS-NIGER ,POTENTIAL APPLICATION ,Saccharification ,010608 biotechnology ,Animals ,Humans ,[SDV.BV]Life Sciences [q-bio]/Vegetal Biology ,Biorefinery ,0105 earth and related environmental sciences ,Renewable Energy, Sustainability and the Environment ,chemistry ,Substrate specificity ,Carboxylic Ester Hydrolases ,Function (biology) ,Biologie végétale - Abstract
International audience; Ferulic acid and its hydroxycinnamate derivatives represent one of the most abundant forms of low molecular weight phenolic compounds in plant biomass. Feruloyl esterases are part of a microorganism’s plant cell wall-degrading enzymatic arsenal responsible for cleaving insoluble wall-bound hydroxycinnamates and soluble cytosolic conjugates. Stimulated by industrial requirements, accelerating scientific discoveries and knowledge transfer, continuous improvement efforts have been made to identify, create and repurposed biocatalysts dedicated to plant biomass conversion and biosynthesis of high-added value molecules. Here we review the basic knowledge and recent advances in biotechnological characteristics and the gene content encoding for feruloyl esterases. Information about several enzymes is systematically organized according to their function, biochemical properties, substrate specificity, and biotechnological applications. This review contributes to further structural, functional, and biotechnological R&D both for obtaining hydroxycinnamates from agricultural by-products as well as for lignocellulose biomass treatments aiming for production of bioethanol and other derivatives of industrial interest.
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- 2019
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30. Biological contamination and its chemical control in microalgal mass cultures
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Denisse Molina, Craig B. Faulds, Antonio Irineudo Magalhães Júnior, Emmanuel Bertrand, Júlio Cesar de Carvalho, Carlos Ricardo Soccol, Department of Bioprocess Engineering and Biotechnology, Federal University of Paraná, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Aix Marseille Université (AMU), and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)
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algal parasites ,Environmental remediation ,Microorganism ,[SDV]Life Sciences [q-bio] ,Cell Culture Techniques ,Early detection ,Applied Microbiology and Biotechnology ,03 medical and health sciences ,Bioreactors ,contamination ,Bioproducts ,Biomass ,mass cultures ,030304 developmental biology ,0303 health sciences ,Axenic Culture ,030306 microbiology ,microalgae ,General Medicine ,Contamination ,Coculture Techniques ,Culture Media ,Microbial Interactions ,Environmental science ,Biochemical engineering ,Chemical control ,control ,Biotechnology - Abstract
Microalgae are versatile sources of bioproducts, a solution for many environmental problems. However, and despite its importance, one of the main problems in large-scale cultures—the presence of contaminants—is rarely systematically approached. Contamination, or the presence of undesirable organisms in a culture, is deleterious for the culture and frequently leads to culture crashes. To avoid contamination, closed systems can be used; however, for very large-scale open systems, contamination is unavoidable and remediation procedures are necessary—ranging from physicochemical treatment to addition of biocidal substances. In all cases, early detection and culture monitoring are paramount. This article describes the biological contaminants, contamination mechanisms, and control systems used in open and closed cultures, discussing the latest advances and techniques in the area. It also discusses the complex interactions of algae with other microorganisms that can be expected in cultivation systems.
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- 2019
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31. Heterologous Production and Characterization of Two Glyoxal Oxidases from Pycnoporus cinnabarinus: Glyoxal Oxidases from Pycnoporus cinnabarinus
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Eric Record, Daniel Cullen, François Piumi, Marianne Daou, Craig B. Faulds, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), USDA, Forest Products Laboratory, Madison, Wisconsin, USA, European Project: 613549,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,INDOX(2013), and École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
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0301 basic medicine ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,glyoxal oxydase ,030106 microbiology ,génome végétal ,[SDV.BID]Life Sciences [q-bio]/Biodiversity ,Applied Microbiology and Biotechnology ,dégradation de la lignocellulose ,Substrate Specificity ,Fungal Proteins ,03 medical and health sciences ,chemistry.chemical_compound ,oxydase ,Amino Acid Sequence ,Enzymology and Protein Engineering ,pycnoporus cinnabarinus ,Phylogeny ,Oxidase test ,Fungal protein ,Organisms, Genetically Modified ,Ecology ,biology ,Aspergillus niger ,oxidase ,Pycnoporus cinnabarinus ,biology.organism_classification ,Pycnoporus ,Alcohol Oxidoreductases ,chemistry ,Biochemistry ,13. Climate action ,biology.protein ,Glyoxal ,Phanerochaete ,Oxidation-Reduction ,Sequence Alignment ,Food Science ,Biotechnology ,Peroxidase - Abstract
The genome of the white rot fungus Pycnoporus cinnabarinus includes a large number of genes encoding enzymes implicated in lignin degradation. Among these, three genes are predicted to encode glyoxal oxidase, an enzyme previously isolated from Phanerochaete chrysosporium . The glyoxal oxidase of P. chrysosporium is physiologically coupled to lignin-oxidizing peroxidases via generation of extracellular H 2 O 2 and utilizes an array of aldehydes and α-hydroxycarbonyls as the substrates. Two of the predicted glyoxal oxidases of P. cinnabarinus , GLOX1 ( Pci GLOX1) and GLOX2 ( Pci GLOX2), were heterologously produced in Aspergillus niger strain D15#26 ( pyrG negative) and purified using immobilized metal ion affinity chromatography, yielding 59 and 5 mg of protein for Pci GLOX1 and Pci GLOX2, respectively. Both proteins were approximately 60 kDa in size and N-glycosylated. The optimum temperature for the activity of these enzymes was 50°C, and the optimum pH was 6. The enzymes retained most of their activity after incubation at 50°C for 4 h. The highest relative activity and the highest catalytic efficiency of both enzymes occurred with glyoxylic acid as the substrate. The two P. cinnabarinus enzymes generally exhibited similar substrate preferences, but Pci GLOX2 showed a broader substrate specificity and was significantly more active on 3-phenylpropionaldehyde. IMPORTANCE This study addresses the poorly understood role of how fungal peroxidases obtain an in situ supply of hydrogen peroxide to enable them to oxidize a variety of organic and inorganic compounds. This cooperative activity is intrinsic in the living organism to control the amount of toxic H 2 O 2 in its environment, thus providing a feed-on-demand scenario, and can be used biotechnologically to supply a cheap source of peroxide for the peroxidase reaction. The secretion of multiple glyoxal oxidases by filamentous fungi as part of a lignocellulolytic mechanism suggests a controlled system, especially as these enzymes utilize fungal metabolites as the substrates. Two glyoxal oxidases have been isolated and characterized to date, and the differentiation of the substrate specificity of the two enzymes produced by Pycnoporus cinnabarinus illustrates the alternative mechanisms existing in a single fungus, together with the utilization of these enzymes to prepare platform chemicals for industry.
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- 2016
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32. Lignin as a potential source of high-added value compounds: A review
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Valcineide Oliveira de Andrade Tanobe, Luiza Chemim Guimarães Lorenci, Luis Alberto Zevallos Torres, Susan Grace Karp, Craig B. Faulds, Carlos Ricardo Soccol, and Adenise Lorenci Woiciechowski
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020209 energy ,Strategy and Management ,macromolecular substances ,02 engineering and technology ,complex mixtures ,Industrial and Manufacturing Engineering ,chemistry.chemical_compound ,Research community ,0202 electrical engineering, electronic engineering, information engineering ,Added value ,Lignin ,Ethanol fuel ,Potential source ,0505 law ,General Environmental Science ,chemistry.chemical_classification ,Renewable Energy, Sustainability and the Environment ,Depolymerization ,fungi ,05 social sciences ,technology, industry, and agriculture ,food and beverages ,Polymer ,Pulp and paper industry ,chemistry ,050501 criminology ,Polymer composites - Abstract
Biorenewable polymers from different natural sources have attracted the attention of the research community in different fields such as food, biomedicine, cosmetic, and polymer composite industries. Lignin, as the second most abundant natural polymer in the world and mainly produced as a residue from the pulp and paper industry and ethanol production, is an attractive material for the development of ecofriendly, low-cost, and biodegradable products. During the last decades, different applications of lignin have been investigated, using it as a macromolecule or depolymerizing it for the production of fuels and low molecular weight chemicals. This review article assesses these investigations into the different applications/uses of lignin. Different lignin transformation processes are described, together with the main resulting products. First, the isolation processes or types of produced lignin are outlined together with the current lignin-producing companies. Then, information is provided about the analytical methods used to characterize it. Finally, this review presents the current products/applications of lignin as a macromolecule and current efforts focused on lignin depolymerization, motivating new catalysts being tested today.
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- 2020
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33. Current advances in gibberellic acid (GA3) production, patented technologies and potential applications
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Marcela C. Camara, Craig B. Faulds, Carlos Ricardo Soccol, Juliana de Oliveira, Emmanuel Bertrand, Luciana Porto de Souza Vandenberghe, Cristine Rodrigues, Bioprocess Engineering and Biotechnology Department, Federal University of Parana, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), and École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
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0106 biological sciences ,0301 basic medicine ,scientific stride ,Plant growth regulators ,[SDV]Life Sciences [q-bio] ,Plant Science ,01 natural sciences ,innovation technologique ,Terpene ,03 medical and health sciences ,chemistry.chemical_compound ,rooting compounds ,Downstream ,Division (horticulture) ,Genetics ,Cultivar ,Gibberellic acid ,fusarium ,2. Zero hunger ,régulateur de croissance ,biology ,business.industry ,Alternative substrate ,fungi ,food and beverages ,acide gibbérellique ,biology.organism_classification ,Biotechnology ,Submerged fermentation ,030104 developmental biology ,progrès scientifique ,fermentation à l'état solide ,chemistry ,Formulation ,Germination ,économie de production ,Gibberella fujikuroi ,Fermentation ,Gibberellin ,substance de croissance végétale ,business ,Fusarium fujikuroi ,010606 plant biology & botany - Abstract
Gibberellic acid is a plant growth hormone that promotes cell expansion and division. Studies have aimed at optimizing and reducing production costs, which could make its application economically viable for different cultivars. Gibberellins consist of a large family of plant growth hormones discovered in the 1930s, which are synthesized via the terpenes route from the geranylgeranyl diphosphate and feature a basic structure formed by an ent-gibberellane tetracyclic skeleton. Among them, only four have biological activity, including gibberellic acid (GA3), which acts as a natural plant growth regulator, especially for stem elongation, seed germination, and increased fruit size. It can be obtained from plants, fungi, and bacteria. There are also some reports about microalgae GA3 producers. Fungi, especially Gibberella fujikuroi, are preferred for GA3 production via submerged fermentation or solid-state fermentation. Many factors may affect its production, some of which are related to the control and scale-up of fermentation parameters. Different GA3 products are available on the market. They can be found in liquid or solid formulations containing only GA3 or a mixture of other biological active gibberellins, which can be applied on a wide variety of cultivars, including crops and fruits. However, the product’s cost still limits its large and continuous application. New low-cost and efficient GA3 production alternatives are surely welcome. This review deals with the latest scientific and technological advances on production, recovery, formulation, and applications of this important plant growth hormone.
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- 2018
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34. The Maillard Reaction in Food: An Introduction
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Craig B. Faulds, Patricia El Boustany, Jean-Louis Berdagué, Emmanuel Bertrand, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Aix Marseille Université (AMU), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), and Peter Varelis
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0301 basic medicine ,Taste ,Food industry ,propriété sensorielle ,Flavour ,modelling ,03 medical and health sciences ,symbols.namesake ,polymère ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Browning ,Food science ,modélisation ,2. Zero hunger ,030109 nutrition & dietetics ,Amadori ,nonenzymic browning ,Chemistry ,business.industry ,Deoxyosone ,Advanced stage ,Multi-response modelling ,melanoidin ,brunissement non enzymatique ,Caramelization ,Brown colour ,Maillard reaction ,030104 developmental biology ,composé d'arôme ,Flavour formation ,Food ,industrie alimentaire ,réaction de maillard ,symbols ,business ,mélanoïdine - Abstract
In modern societies, most of the food being consumed has been processed. This introduction to the Maillard Reaction in Food provides information's about the main reactions that are occurring during the backing and cooking of food products. The processing of food is promoting non-enzymatic browning reaction involving proteins and reducing sugars. The products formed during this reaction are key players in the development of taste, flavour and colour and affects the consumer's preferences. Maillard reaction products (MRP) can have positive or adverse effects on health with respect to anti/pro-oxidant potential, immunogenicity, allergenicity and carcinogenicity. Therefore, one century after its discovery by Louis Camille Maillard, the reaction still harbours many challenges for the scientific community and for the food. The development of increasingly more sensitive analytical techniques, including multi-omics approaches, and big data analysis are promising for a more refined understanding of this reaction. The Maillard reaction was discovered in 1912 by the French chemist and doctor Louis-Camille Maillard. This reaction is part of the non-enzymatic browning reactions with caramelization due to the formation of polymers called melanoidins that produce a characteristic brown colour at the advanced stages of this reaction. This is a very important reaction for the food industry as it explains a large part of the sensory properties, aroma and taste of cooked products.
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- 2018
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35. Enzyme Activities of Two Recombinant Heme-Containing Peroxidases, TvDyP1 and TvVP2, Identified from the Secretome of Trametes versicolor
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Aurélie Deroy, Jean-Guy Berrin, Didier Chevret, David Navarro, Thomas Perrot, Amine Benkhelfallah, Eric Gelhaye, Eric Record, Mélanie Morel-Rouhier, Marianne Daou, Amani Chalak, Sawsan Amara, Craig B. Faulds, Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, ANR-11-LABX-0002-01, European Project: 613549,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,INDOX(2013), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)
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0301 basic medicine ,enzymic activity ,peroxydase fongique ,Trametes versicolor ,composé phénolique ,approche protéomique ,Applied Microbiology and Biotechnology ,class II heme peroxidase ,decoloration ,03 medical and health sciences ,chemistry.chemical_compound ,ferroprotoporphyrin ,secrétome ,pourriture blanche ,discoloration ,fungal secretome ,Lignin ,[SDV.BV]Life Sciences [q-bio]/Vegetal Biology ,dye-decolorizing peroxidase ,versatile peroxidase ,analyse moléculaire ,Versatile peroxidase ,heme ,Dye decolorizing peroxidase ,Thermostability ,peroxydase ,chemistry.chemical_classification ,phenolic compound ,030102 biochemistry & molecular biology ,Ecology ,biology ,activité enzymatique ,15. Life on land ,biology.organism_classification ,Enzyme assay ,030104 developmental biology ,Enzyme ,chemistry ,Biochemistry ,white-rot fungus ,biology.protein ,escherichia coli ,Food Science ,Biotechnology ,Peroxidase - Abstract
Trametes versicolor is a wood-inhabiting agaricomycete known for its ability to cause strong white-rot decay on hardwood and for its high tolerance of phenolic compounds. The goal of the present work was to gain insights into the molecular biology and biochemistry of the heme-including class II and dye-decolorizing peroxidases secreted by this fungus. Proteomic analysis of the secretome of T. versicolor BRFM 1218 grown on oak wood revealed a set of 200 secreted proteins, among which were the dye-decolorizing peroxidase Tv DyP1 and the versatile peroxidase Tv VP2. Both peroxidases were heterologously produced in Escherichia coli , biochemically characterized, and tested for the ability to oxidize complex substrates. Both peroxidases were found to be active against several substrates under acidic conditions, and Tv DyP1 was very stable over a relatively large pH range of 2.0 to 6.0, while Tv VP2 was more stable at pH 5.0 to 6.0 only. The thermostability of both enzymes was also tested, and Tv DyP1 was globally found to be more stable than Tv VP2. After 180 min of incubation at temperatures ranging from 30 to 50°C, the activity of Tv VP2 drastically decreased, with 10 to 30% of the initial activity retained. Under the same conditions, Tv DyP1 retained 20 to 80% of its enzyme activity. The two proteins were catalytically characterized, and Tv VP2 was shown to accept a wider range of reducing substrates than Tv DyP1. Furthermore, both enzymes were found to be active against two flavonoids, quercetin and catechin, found in oak wood, with Tv VP2 displaying more rapid oxidation of the two compounds. They were tested for the ability to decolorize five industrial dyes, and Tv VP2 presented a greater ability to oxidize and decolorize the dye substrates than Tv DyP1. IMPORTANCE Trametes versicolor is a wood-inhabiting agaricomycete known for its ability to cause strong white-rot decay on hardwood and for its high tolerance of phenolic compounds. Among white-rot fungi, the basidiomycete T. versicolor has been extensively studied for its ability to degrade wood, specifically lignin, thanks to an extracellular oxidative enzymatic system. The corresponding oxidative system was previously studied in several works for classical lignin and manganese peroxidases, and in this study, two new components of the oxidative system of T. versicolor , one dye-decolorizing peroxidase and one versatile peroxidase, were biochemically characterized in depth and compared to other fungal peroxidases.
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- 2018
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36. Enzyme Activities of Two Recombinant Heme-Containing Peroxidases
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Sawsan, Amara, Thomas, Perrot, David, Navarro, Aurélie, Deroy, Amine, Benkhelfallah, Amani, Chalak, Marianne, Daou, Didier, Chevret, Craig B, Faulds, Jean-Guy, Berrin, Mélanie, Morel-Rouhier, Eric, Gelhaye, and Eric, Record
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Fungal Proteins ,Proteomics ,Trametes ,Peroxidases ,Enzymology and Protein Engineering ,Coloring Agents ,Oxidation-Reduction ,Water Pollutants, Chemical - Abstract
Trametes versicolor is a wood-inhabiting agaricomycete known for its ability to cause strong white-rot decay on hardwood and for its high tolerance of phenolic compounds. The goal of the present work was to gain insights into the molecular biology and biochemistry of the heme-including class II and dye-decolorizing peroxidases secreted by this fungus. Proteomic analysis of the secretome of T. versicolor BRFM 1218 grown on oak wood revealed a set of 200 secreted proteins, among which were the dye-decolorizing peroxidase TvDyP1 and the versatile peroxidase TvVP2. Both peroxidases were heterologously produced in Escherichia coli, biochemically characterized, and tested for the ability to oxidize complex substrates. Both peroxidases were found to be active against several substrates under acidic conditions, and TvDyP1 was very stable over a relatively large pH range of 2.0 to 6.0, while TvVP2 was more stable at pH 5.0 to 6.0 only. The thermostability of both enzymes was also tested, and TvDyP1 was globally found to be more stable than TvVP2. After 180 min of incubation at temperatures ranging from 30 to 50°C, the activity of TvVP2 drastically decreased, with 10 to 30% of the initial activity retained. Under the same conditions, TvDyP1 retained 20 to 80% of its enzyme activity. The two proteins were catalytically characterized, and TvVP2 was shown to accept a wider range of reducing substrates than TvDyP1. Furthermore, both enzymes were found to be active against two flavonoids, quercetin and catechin, found in oak wood, with TvVP2 displaying more rapid oxidation of the two compounds. They were tested for the ability to decolorize five industrial dyes, and TvVP2 presented a greater ability to oxidize and decolorize the dye substrates than TvDyP1.
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- 2017
37. Glyoxal oxidases: their nature and properties
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Craig B. Faulds, Marianne Daou, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), KBBE-2013-7-613549, European Project: 613549,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,INDOX(2013), and École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
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0301 basic medicine ,Filamentous fungi ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Physiology ,030106 microbiology ,[SDV.BID]Life Sciences [q-bio]/Biodiversity ,Lignin ,Applied Microbiology and Biotechnology ,Microbiology ,Fungal Proteins ,03 medical and health sciences ,chemistry.chemical_compound ,Oxidoreductase ,Lignocellulose degradation ,Vitis ,Biomass ,ComputingMilieux_MISCELLANEOUS ,Plant Proteins ,chemistry.chemical_classification ,Aldehydes ,biology ,Fungi ,Active site ,Hydrogen Peroxide ,General Medicine ,Pycnoporus cinnabarinus ,biology.organism_classification ,Alcohol Oxidoreductases ,Biodegradation, Environmental ,030104 developmental biology ,Enzyme ,chemistry ,Biochemistry ,Galactose oxidase ,biology.protein ,Carbohydrate Metabolism ,Phanerochaete ,Detoxification ,Oxidation-Reduction ,Biotechnology ,Peroxidase - Abstract
International audience; H2O2 has been found to be required for the activity of the main microbial enzymes responsible for lignin oxidative cleavage, peroxidases. Along with other small radicals, it is implicated in the early attack of plant biomass by fungi. Among the few extracellular H2O2-generating enzymes known are the glyoxal oxidases (GLOX). GLOX is a copper-containing enzyme, sharing high similarity at the level of active site structure and chemistry with galactose oxidase. Genes encoding GLOX enzymes are widely distributed among wood-degrading fungi especially white-rot degraders, plant pathogenic and symbiotic fungi. GLOX has also been identified in plants. Although widely distributed, only few examples of characterized GLOX exist. The first characterized fungal GLOX was isolated from Phanerochaete chrysosporium. The GLOX from Utilago maydis has a role in filamentous growth and pathogenicity. More recently, two other glyoxal oxidases from the fungus Pycnoporus cinnabarinus were also characterized. In plants, GLOX from Vitis pseudor-eticulata was found to be implicated in grapevine defence mechanisms. Fungal GLOX were found to be activated by peroxidases in vitro suggesting a synergistic and regulatory relationship between these enzymes. The substrates oxidized by GLOX are mainly aldehydes generated during lignin and carbohydrates degradation. The reactions catalysed by this enzyme such as the oxidation of toxic molecules and the production of valuable compounds (organic acids) makes GLOX a promising target for biotechnological applications. This aspect on GLOX remains new and needs to be investigated.
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- 2017
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38. Lignocellulolytic capability of endophytic phyllosticta sp
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Ekachai Chukeatirote, A. Al Kanghae, Saowanee Wikee, Craig B. Faulds, P. Chumnunti, Saisamorn Lumyong, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Department of Biology, Faculty of Science, University of Isfahan, Institute of Excellence in Fungal Research, School of Science, Mae Fah Luang University [Thaïlande] (MFU), Chiang Mai University, École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), School of Science, Beijing University of Astronautics and Aeronautics, and Chiang Mai University (CMU)
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0106 biological sciences ,Phyllosticta ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Agro-industrial residues ,[SDV]Life Sciences [q-bio] ,Lignocellulosic biomass ,Cellulase ,Lignocellulytic enzyme ,Biological pretreatment ,enzyme lignolytique ,biomasse lignocellulosique ,7. Clean energy ,010603 evolutionary biology ,01 natural sciences ,030308 mycology & parasitology ,03 medical and health sciences ,Dothideomycetes ,phyllosticta ,Phyllosticta capitalensis ,Pectinase ,biological treatment ,déchet agricole ,[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology ,2. Zero hunger ,0303 health sciences ,biology ,ascomycète ,phase endophyte ,15. Life on land ,Straw ,biology.organism_classification ,résidu industriel ,traitement biologique ,Horticulture ,Xylanase ,biology.protein ,farm wastes - Abstract
International audience; The Dothideomycetes represent the largest fungal class of Ascomycota. It is an ubiquitous class of fungi whose members span a wide spectrum of lifestyles and host interactions. The endophytic fungus Phyllosticta is one members of the Dothideomycetes, causing disease in economic crops. Phyllosticta was screened for the degradation of lignocellulosic biomass of commercial relevance, such as rice straw, rice husk, sorghum, wheat straw, miscanthus, lavender flower, and lavender straw. The highest degrading strains were identified from an initial screen and further analyzed for the secretion of lignocellulosic enzymes during growth on the different biomasses. With Phyllosticta capitalensis (MFLUCC14-0233), maximum activity of arabinase (944.18 U/ml culture), cellulase (27.10 U/ml), xylanase (10.85 U/ml), pectinase (465.47 U/ml), and laccase (35.68 U/ml) activities could be detected in the secretome during growth on lavender flowers and lavender straw. Phyllosticta capitalensis is thus an interesting new strain for the production of lignocellulosic enzymes during growth on cheap agro-industrial biomass.
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- 2017
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39. A two-step bioconversion process for canolol production from rapeseed meal combining an Aspergillus niger feruloyl esterase and the fungus Neolentinus lepideus
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Alexandra Bisotto, David Navarro, Christian Ginies, Frédéric Fine, Craig B. Faulds, Jean-Claude Sigoillot, Oscar Laguna, Jérôme Lecomte, Anne Lomascolo, Corinne Peyronnet, Elise Odinot, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Terres Inovia, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Terres Univia, Sécurité et Qualité des Produits d'Origine Végétale (SQPOV), Avignon Université (AU)-Institut National de la Recherche Agronomique (INRA), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Avignon Université (AU)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Technical Centre for Oilseed Crops, Grain Legumes and Industrial Hemp (TERRES INOVIA, Pessac, France), Inter-Branch Organization for Vegetable Oils and Proteins (TERRES UNIVIA, Paris, France)., Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Lomascolo, Anne
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0106 biological sciences ,0301 basic medicine ,Microbiology (medical) ,canolol ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,bioconversion ,composé volatil ,Bioconversion ,composé phénolique ,chromatographie en phase gazeuse ,chimie verte ,Raw material ,01 natural sciences ,7. Clean energy ,Microbiology ,Aspergillus niger ,feruloyl esterase ,Neolentinus lepideus ,rapeseed meal ,sinapic acid ,Article ,chromatographie en phase liquide ,03 medical and health sciences ,Hydrolysis ,chemistry.chemical_compound ,Q02 - Traitement et conservation des produits alimentaires ,Feruloyl esterase ,010608 biotechnology ,Virology ,Sinapine ,tourteau de colza ,Food science ,lcsh:QH301-705.5 ,ComputingMilieux_MISCELLANEOUS ,Q60 - Traitement des produits agricoles non alimentaires ,biology ,Canolol ,activité enzymatique ,Q70 - Traitement des déchets agricoles ,biology.organism_classification ,030104 developmental biology ,lcsh:Biology (General) ,Biochemistry ,chemistry - Abstract
International audience; Rapeseed meal is a cheap and abundant raw material, particularly rich in phenolic compounds of biotechnological interest. In this study, we developed a two-step bioconversion process of naturally occurring sinapic acid (4-hydroxy-3,5-dimethoxycinnamic acid) from rapeseed meal into canolol by combining the complementary potentialities of two filamentous fungi, the micromycete Aspergillus niger and the basidiomycete Neolentinus lepideus. Canolol could display numerous industrial applications because of its high antioxidant, antimutagenic and anticarcinogenic properties. In the first step of the process, the use of the enzyme feruloyl esterase type-A (named AnFaeA) produced with the recombinant strain A. niger BRFM451 made it possible to release free sinapic acid from the raw meal by hydrolysing the conjugated forms of sinapic acid in the meal (mainly sinapine and glucopyranosyl sinapate). An amount of 39 nkat AnFaeA per gram of raw meal, at 55 °C and pH 5, led to the recovery of 6.6 to 7.4 mg of free sinapic acid per gram raw meal, which corresponded to a global hydrolysis yield of 68 to 76% and a 100% hydrolysis of sinapine. Then, the XAD2 adsorbent (a styrene and divinylbenzene copolymer resin), used at pH 4, enabled the efficient recovery of the released sinapic acid, and its concentration after elution with ethanol. In the second step, 3-day-old submerged cultures of the strain N.lepideus BRFM15 were supplied with the recovered sinapic acid as the substrate of bioconversion into canolol by a non-oxidative decarboxylation pathway. Canolol production reached 1.3 g/L with a molar yield of bioconversion of 80% and a productivity of 100 mg/L day. The same XAD2 resin, when used at pH 7, allowed the recovery and purification of canolol from the culture broth of N. lepideus. The two-step process used mild conditions compatible with green chemistry.
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- 2017
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40. Release of Small Phenolic Compounds from Brewer’s Spent Grain and Its Lignin Fractions by Human Intestinal Microbiota in Vitro
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Craig B. Faulds, Ismo Mattila, Johanna Buchert, Kaisa Poutanen, Tarja Tamminen, Annika Smeds, Anna-Marja Aura, Klaus Niemelä, and Piritta Niemi
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intestinal microbiota ,lignan ,Chromatography, Gas ,lignin ,Fraction (chemistry) ,macromolecular substances ,Lignin ,complex mixtures ,Lignans ,Hydrolysis ,chemistry.chemical_compound ,Phenols ,Humans ,Lignan ,chemistry.chemical_classification ,Chemistry ,business.industry ,Microbiota ,fungi ,technology, industry, and agriculture ,food and beverages ,Fatty acid ,General Chemistry ,Fatty Acids, Volatile ,Intestines ,brewer's spent grain ,Biochemistry ,Polyphenol ,Fermentation ,Metabolome ,Brewing ,Edible Grain ,Plant Structures ,General Agricultural and Biological Sciences ,business ,in vitro colon model - Abstract
Brewer's spent grain (BSG), the major side-stream from brewing, is rich in protein, lignin, and nonstarch polysaccharides. Lignin is a polyphenolic macromolecule considered resilient toward breakdown and utilization by colon microbiota, although some indications of release of small phenolic components from lignin in animals have been shown. The aim of this study was to investigate if the human intestinal microbiota can release lignans and small phenolic compounds from whole BSG, a lignin-enriched insoluble fraction from BSG and a deferuloylated fraction, in a metabolic in vitro colon model. The formation of short-chain fatty acid (SCFA) was also investigated. More lignin-related monomers and dilignols were detected from the lignin-enriched fraction than from BSG or deferuloylated BSG. SCFA formation was not suppressed by any of the fractions. It was shown that small lignin-like compounds were released from these samples in the in vitro colon model, originating most likely from lignin.
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- 2013
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41. Interactions of a Lignin-Rich Fraction from Brewer’s Spent Grain with Gut Microbiota in Vitro
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Kaisa Poutanen, Ismo Mattila, Annika Smeds, Tarja Tamminen, Johanna Buchert, Piritta Niemi, Klaus Niemelä, Johanna Maukonen, Craig B. Faulds, and Anna-Marja Aura
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lactobacilli ,lignan ,in vitro fermentation ,Colon ,Microbial metabolism ,lignin ,bifidobacteria ,Fraction (chemistry) ,macromolecular substances ,Gut flora ,Lignin ,Models, Biological ,complex mixtures ,Cell wall ,Feces ,chemistry.chemical_compound ,Humans ,Waste Products ,Lignan ,chemistry.chemical_classification ,Bacteria ,biology ,Microbiota ,fungi ,technology, industry, and agriculture ,food and beverages ,Fatty acid ,General Chemistry ,dietary fiber ,biology.organism_classification ,brewer's spent grain ,chemistry ,Biochemistry ,Fermentation ,colon microbiota ,Edible Grain ,General Agricultural and Biological Sciences - Abstract
Lignin is a constituent of plant cell walls and thus is classified as part of dietary fiber. However, little is known about the role of lignin in gastrointestinal fermentation. In this work, a lignin-rich fraction was prepared from brewer’s spent grain and subjected to an in vitro colon model to study its potential bioconversions and interactions with fecal microbiota. No suppression of microbial conversion by the fraction was observed in the colon model, as measured as short-chain fatty acid production. Furthermore, no inhibition on the growth was observed when the fraction was incubated with strains of lactobacilli and bifidobacteria. In fact, the lignin-rich fraction enabled bifidobacteria to survive longer than with glucose. Several transiently appearing phenolic compounds, very likely originating from lignin, were observed during the fermentation. This would indicate that the gut microbiota was able to partially degrade lignin and metabolize the released compounds.
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- 2013
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42. Hydrolysis of nonpolar n-Alkyl ferulates by feruloyl esterases
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Evangelos Topakas, Isabel Sprecher, Craig B. Faulds, Laura Nyström, Aline Schär, Institute of Food, Nutrition and Health, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens [Athens] (NTUA), Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Swiss National Science Foundation, SNSF 200021_141268, and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)
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0106 biological sciences ,0301 basic medicine ,synthèse enzymatique ,Coumaric Acids ,Stereochemistry ,alkyl ferulates ,A. niger feruloyl esterase ,01 natural sciences ,Cell wall ,Ferulic acid ,Fungal Proteins ,03 medical and health sciences ,chemistry.chemical_compound ,Hydrolysis ,hydrolyse ,Feruloyl esterase ,010608 biotechnology ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,lipase ,Organic chemistry ,feruloyl esterase ,Lipase ,biology ,phenolic acid ,activité hydrolytique ,Substrate (chemistry) ,C. thermocellum feruloyl esterase ,General Chemistry ,Phenolic acid ,enzymatic synthesis ,saccharification ,acide phénolique ,Kinetics ,030104 developmental biology ,chemistry ,R. miehei lipase ,Lipophilicity ,biology.protein ,acide férulique ,Aspergillus niger ,General Agricultural and Biological Sciences ,Carboxylic Ester Hydrolases ,alkyl ,ferulic acid - Abstract
Ferulic acid is one of the major phenolic acids in plants and can be found esterified to plant cell wall components, but also as long-chain n-alkyl and steryl esters. Microbial feruloyl esterases may play a role in the bioavailability of phenolic acids during human and animal digestion. It is therefore of interest if feruloyl esterases are capable of hydrolyzing nonpolar ferulic acid esters. A series of n-alkyl ferulates with increasing lipophilicity were enzymatically synthesized, and the kinetic constants of their hydrolysis by four feruloyl esterases and a lipase as control were determined. A decrease in k(m) and k(cat), could be observed with decreased substrate polarity for all of the feruloyl esterases. Only one feruloyl esterase and the control lipase showed hydrolytic activity toward octadecyl ferulate. These results led to the conclusion that lipophilic ferulates are poor substrates for known feruloyl esterases and more specific esterases/lipases need to be identified.
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- 2016
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43. Green Fuels Technology
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Carlos Ricardo Soccol, Craig B. Faulds, Luiz Pereira Ramos, and Satinder Kaur Brar
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Waste management ,Environmental science ,Renewable fuels - Published
- 2016
- Full Text
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44. Activities of secreted aryl alcohol quinone oxidoreductases from [i]Pycnoporus cinnabarinus[/i] provide insights into fungal degradation of plant biomass
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Juan Carro Aramburu, François Piumi, Richard Valli, Craig B. Faulds, Patricia Ferreira, Eric Record, Yann Mathieu, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Biotechnology for Lignocellulosic Biomass Lab, Centro de Investigaciones Biológicas (CIB), Instituto de Biocomputación y Física de Sistemas Complejos, University of Zaragoza - Universidad de Zaragoza [Zaragoza], Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), and Instituto de Biocomputación y Física de Sistemas Complejos = Institute for Biocomputation and Physics of Complex Systems (BIFI)
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0301 basic medicine ,Models, Molecular ,CAZy ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Protein Conformation ,030106 microbiology ,Coenzymes ,Applied Microbiology and Biotechnology ,Lignin ,Cofactor ,Substrate Specificity ,03 medical and health sciences ,chemistry.chemical_compound ,Glucose dehydrogenase ,Aryl-alcohol oxidase ,Biomass ,Enzymology and Protein Engineering ,Biotransformation ,Laccase ,Flavin adenine dinucleotide ,Oxidase test ,Ecology ,biology ,Flavoproteins ,Sequence Homology, Amino Acid ,Quinones ,Pycnoporus cinnabarinus ,biology.organism_classification ,Pycnoporus ,Alcohol Oxidoreductases ,chemistry ,Biochemistry ,biology.protein ,Flavin-Adenine Dinucleotide ,Food Science ,Biotechnology - Abstract
Auxiliary activities family 3 subfamily 2 (AA3_2) from the CAZy database comprises various functions related to ligninolytic enzymes, such as fungal aryl alcohol oxidases (AAO) and glucose oxidases, both of which are flavoenzymes. The recent study of the Pycnoporus cinnabarinus CIRM BRFM 137 genome combined with its secretome revealed that four AA3_2 enzymes are secreted during biomass degradation. One of these AA3_2 enzymes, scf184803.g17, has recently been produced heterologously in Aspergillus niger . Based on the enzyme's activity and specificity, it was assigned to the glucose dehydrogenases ( P . cinnabarinus GDH [ Pc GDH]). Here, we analyze the distribution of the other three AA3_2 enzymes (scf185002.g8, scf184611.g7, and scf184746.g13) to assess their putative functions. These proteins showed the highest homology with aryl alcohol oxidase from Pleurotus eryngii . Biochemical characterization demonstrated that they were also flavoenzymes harboring flavin adenine dinucleotide (FAD) as a cofactor and able to oxidize a wide variety of phenolic and nonphenolic aryl alcohols and one aliphatic polyunsaturated primary alcohol. Though presenting homology with fungal AAOs, these enzymes exhibited greater efficiency in reducing electron acceptors (quinones and one artificial acceptor) than molecular oxygen and so were defined as aryl-alcohol:quinone oxidoreductases (AAQOs) with two enzymes possessing residual oxidase activity ( Pc AAQO2 and Pc AAQO3). Structural comparison of Pc AAQO homology models with P. eryngii AAO demonstrated a wider substrate access channel connecting the active-site cavity to the solvent, explaining the absence of activity with molecular oxygen. Finally, the ability of Pc AAQOs to reduce radical intermediates generated by laccase from P. cinnabarinus was demonstrated, shedding light on the ligninolytic system of this fungus.
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- 2016
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45. Second Generation Bioethanol
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Craig B. Faulds and Jean-Claude Sigoillot
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0106 biological sciences ,0301 basic medicine ,food and beverages ,Lignocellulosic biomass ,Biomass ,Pulp and paper industry ,01 natural sciences ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,Corn stover ,chemistry ,Biofuel ,010608 biotechnology ,Lignin ,Hemicellulose ,Fermentation ,Cellulose - Abstract
Second generation bioethanol, i.e., ethanol from lignocellulosic biomass is envisaged as a renewable source of transport fuel in the next years to complement or replace the first generation and the fossil fuel. At present, the most economic solution seems to be the enzymatic way that produces fermentable sugars from cellulose and hemicellulose. To make this process commercially viable, several improvements are needed to enhance the process. Currently, stocks of biomass are constituted by available agro-industrial residues such as corn stover and straws, wood and wood processing residues and dedicated crops such as miscanthus and other grasses. The biological process for converting the lignocellulose to fuel ethanol requires: a pretreatment to liberate cellulose and hemicellulose from their complex with lignin, a depolymerization of the carbohydrate polymers to produce free sugars, and a fermentation of mixed hexose and pentose sugars to produce ethanol. Pretreatment must be cost effective and must be adapted to the type of biomass. They must not produce high amount of inhibitors such as 5-hydroxymethyl furfural, even if different technique are currently available to detoxify fermentation broths. Saccharification by enzymes and fermentation should be conducted separately (SHF) or simultaneously (SSF). Integration of the process the development of cofermentation of pentoses produced through the pretreatment of the biomass (SSCF). Progress in genetic engineering allows us to consider the development of Consolidated BioProcesses (CBP) in which a single microbial strain is able to ferment polysaccharides to produce ethanol in one step. The economic viability of ethanol recovery from the fermentation mash depends of the overall process, as distillation heat balance is dependant of ethanol concentration. The future of ethanol from biomass is widely dependent on the oil price and on the political will of the different countries.
- Published
- 2016
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46. New salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. Nci6
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Craig B. Faulds, Jean-Guy Berrin, Ilabahen Patel, Su Ma, Sona Garajova, Mireille Haon, Eric Record, Daniel Kracher, Roland Ludwig, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Department of Food Sciences and Technology, Food Biotechnology Laboratory, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, 1190 Austria, EU [KBBE-2013-7-613549], École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Patel, Ilabahen, and Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM)
- Subjects
0301 basic medicine ,Cellobiose dehydrogenase ,CAZy ,[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Lignocellulosic biomass ,Cellobiose ,[SDV.BID]Life Sciences [q-bio]/Biodiversity ,Management, Monitoring, Policy and Law ,Biology ,7. Clean energy ,Applied Microbiology and Biotechnology ,complex mixtures ,Pichia pastoris ,03 medical and health sciences ,Hydrolysis ,chemistry.chemical_compound ,AA9 ,Botany ,14. Life underwater ,LPMO ,Cellulose ,Renewable Energy, Sustainability and the Environment ,Research ,Biorefinery ,fungi ,biology.organism_classification ,Yeast ,030104 developmental biology ,General Energy ,chemistry ,Biochemistry ,13. Climate action ,Biotechnology - Abstract
Background Lytic polysaccharide monooxygenases (LPMOs) belong to the “auxiliary activities (AA)” enzyme class of the CAZy database. They are known to strongly improve the saccharification process and boost soluble sugar yields from lignocellulosic biomass, which is a key step in the efficient production of sustainable economic biofuels. To date, most LPMOs have been characterized from terrestrial fungi, but novel fungal LPMOs isolated from more extreme environments such as an estuary mangrove ecosystem could offer enzymes with unique properties in terms of salt tolerance and higher stability under harsh condition. Results Two LPMOs secreted by the mangrove-associated fungus Pestalotiopsis sp. NCi6 (PsLPMOA and PsLPMOB) were expressed in the yeast Pichia pastoris and produced in a bioreactor with >85 mg L−1 for PsLPMOA and >260 mg L−1 for PsLPMOB. Structure-guided homology modeling of the PsLPMOs showed a high abundance of negative surface charges, enabling enhanced protein stability and activity in the presence of sea salt. Both PsLPMOs were activated by a cellobiose dehydrogenase (CDH) from Neurospora crassa, with an apparent optimum of interaction at pH 5.5. Investigation into their regioselective mode of action revealed that PsLPMOA released C1- and C4-oxidized cello-oligosaccharide products, while PsLPMOB released only C4-oxidized products. PsLPMOA was found to cleave polymeric cellulose in the presence of up to 6 % sea salt, which emphasizes the use of sea water in the industrial saccharification process with improved ecological footprints. Conclusions Two new LPMOs from the mangrove fungus Pestalotiopsis sp. NCi6 were found to be fully reactive against cellulose. The combined hydrolytic activities of these salt-responsive LPMOs could therefore facilitate the saccharification process using sea water as a reaction medium for large-scale biorefineries. Electronic supplementary material The online version of this article (doi:10.1186/s13068-016-0520-3) contains supplementary material, which is available to authorized users.
- Published
- 2016
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47. First Generation Bioethanol
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Luciana Porto de Souza Vandenberghe, Emmanuel Bertrand, Carlos Ricardo Soccol, Craig B. Faulds, and Jean-Claude Sigoillot
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0301 basic medicine ,2. Zero hunger ,020209 energy ,Context (language use) ,02 engineering and technology ,Biorefinery ,7. Clean energy ,12. Responsible consumption ,03 medical and health sciences ,030104 developmental biology ,13. Climate action ,Biofuel ,Bioenergy ,Sustainability ,0202 electrical engineering, electronic engineering, information engineering ,Environmental science ,Production (economics) ,Ethanol fuel ,Biochemical engineering ,Bagasse - Abstract
At the beginning of 2016, first generation bioethanol still contributes to the majority of the 25 billion of gallons’ bioethanol produced worldwide, with the United States and Brazil producing approximately 85 % of the global production predominantly based on corn and sugarcane, respectively. However, concerns over the long-term sustainability of first generation bioethanol, such as the impacts on land use, water resource, the potential contamination of soils with the distillation residues, and the competition for food and feed production is frequently highlighted. Current fuel ethanol research and development strives to minimize these negative externalities. The fundamental role that process design plays during the development of cost-effective technologies is evaluated through the modification of the major pathways in first generation ethanol synthesis. In this context, the central role that better performing enzymes and microorganisms play in the intensity and integration of the process, such as the typical example of simultaneous saccharification and fermentation from starchy material in first generation facilities is acknowledged. Compensating ethanol production costs by the integrated valorization of energy and by-products for feed and green chemistry in a typical biorefinery concept are striking outputs of the first generation ethanol real scale experiment. Finally, rather than a mistake, first generation bioethanol should be considered as the first step that made it possible to gain the necessary experience for the successful implementation of the future greener generations biofuels from the field to the tank, starting with second generation lignocellulosic that is now coming on the market. In this context, integrated biorefineries are a promising way to diversify the usable feedstocks, leading to reduced facilities size and optimized supply-chains, to valorize more efficiently bagasse’s from sugarcane and corn stover or even to exploit the potential of microalgae to capture the carbon dioxide that is produced during the fermentation steps. Major stakeholders in bioenergy production are taking advantage of the large-scale successful development of first generation bioethanol, using the most promising processing schemes for next generation facilities, although the industry is still facing uncertainties with respect to its economic viability and longevity.
- Published
- 2016
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48. Effect of a milling pre-treatment on the enzymatic hydrolysis of carbohydrates in brewer’s spent grain
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Juhani Sibakov, Johanna Buchert, Craig B. Faulds, Kaisa Poutanen, Ulla Holopainen, and Piritta Niemi
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metabolism [Enzymes] ,Waste Products: analysis ,Time Factors ,Environmental Engineering ,Carbohydrates ,Cereals ,Industrial Waste ,Cereals: metabolism ,Bioengineering ,Cellulase ,Fractionation ,Hydrolysis ,Enzymatic hydrolysis ,chemistry [Carbohydrates] ,methods [Biotechnology] ,Food science ,Particle Size ,Solubility ,analysis [Waste Products] ,Waste Management and Disposal ,Waste Products ,metabolism [Cereals] ,Biotechnology: methods ,Chromatography ,biology ,Renewable Energy, Sustainability and the Environment ,Chemistry ,business.industry ,digestive, oral, and skin physiology ,technology, industry, and agriculture ,food and beverages ,analysis [Industrial Waste] ,Industrial Waste: analysis ,Enzymes: metabolism ,General Medicine ,Carbohydrate ,Enzymes ,biology.protein ,Carbohydrate Metabolism ,Carbohydrates: chemistry ,Brewing ,Particle size ,Edible Grain ,business ,Biotechnology - Abstract
Millions of tonnes of brewer's spent grain (BSG) are annually produced worldwide as a by-product of the brewing industry. BSG has the potential to be a valuable source of food, chemicals and energy if cost-efficient fractionation methods can be developed. A 2-fold improvement in carbohydrate solubilisation could be achieved through the introduction of a milling step prior to enzymatic hydrolysis. Course and fine milled fractions were characterized by particle size distribution and light microscopy. Fine milling decreased particle size down to the micron level and this in turn improved the carbohydrate solubility yield by a multi-enzyme mixture from 23% up to 45%. Carbohydrate solubilisation could be further increased through the supplementation of this enzyme preparation with additional cellulases. The physical degradation caused by the milling also liberated soluble carbohydrates without the requirement of any enzymatic treatment.
- Published
- 2012
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49. Enzymatic and Chemical Treatment Limits on the Controlled Solubilization of Brewers’ Spent Grain
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James A. Robertson, Craig B. Faulds, Keith W. Waldron, Luis Castro-Mariñas, and Samuel R. A. Collins
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Glycoside Hydrolases ,Fractionation ,Chemical Fractionation ,Polysaccharide ,Lignin ,Hydrolysis ,chemistry.chemical_compound ,Polysaccharides ,Enzymatic hydrolysis ,Cellulose ,chemistry.chemical_classification ,Chromatography ,biology ,food and beverages ,Hordeum ,General Chemistry ,Phenolic acid ,Hydrogen-Ion Concentration ,Enzyme assay ,Enzyme ,Solubility ,chemistry ,Seeds ,biology.protein ,General Agricultural and Biological Sciences ,Peptide Hydrolases - Abstract
The enzymatic hydrolysis of brewers' spent grain (BSG) has been investigated through treatment with commercial carbohydrases and proteases. Resultant residues were then chemically fractionated and delignified. Enzymatic treatments released 25-30% of the BSG mass and yielded precursors suitable for subsequent conversion to potentially value-added products. Controlled chemical fractionation selectively solubilized arabinoxylan but with no differences apparent due to prior enzyme treatment. The loss of non-polysaccharide components during alkali treatment suggests the presence of a high proportion of alkali-soluble lignin. Further delignification of the alkali-insoluble residues and further chemical fractionation released the remaining hemicellulose, to yield a residue which was90% cellulose. Further knowledge of the properties and interaction between BSG polymers will facilitate an improved enzyme-assisted total deconstruction of BSG and hence the exploitation of its biomass.
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- 2011
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50. Enzyme-Aided Fractionation of Brewer's Spent Grains in Pilot Scale
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Keith W. Waldron, Johanna Buchert, Sandra W.A. Hinz, Tarja Tamminen, Olavi Myllymäki, Henk A. Schols, Janneke Treimo, Vincent G. H. Eijsink, Samuel R. A. Collins, J. Zoldners, Kaarina Viljanen, Craig B. Faulds, and Pirkko Forssell
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medicine.medical_treatment ,antioxidant activity ,Carbohydrase ,Fractionation ,Applied Microbiology and Biotechnology ,Hydrolysate ,ferulic acid release ,esterases ,chemistry.chemical_compound ,Hydrolysis ,oligosaccharides ,Levensmiddelenchemie ,medicine ,Lignin ,Hemicellulose ,Cellulose ,Hydrolysis residue ,VLAG ,Protease ,Chromatography ,Food Chemistry ,biology ,cell-wall components ,humicola-insolens ,Fiber-degrading enzymes ,Proteases ,proteins ,Brewer's spent grain ,hydrolysis ,chemistry ,biology.protein ,identification ,solubilization ,Food Science ,Biotechnology - Abstract
Brewer’s spent grain (BSG) is an important coproduct of the brewing industry and is generally used in animal feed. Recently, there has been considerable research into the use of enzymes to convert BSG into more value-added products. In this study, the efficiency of enzymatic fractionation of freshly produced BSG was studied in pilot scale. Carbohydrateand protein-degrading enzymes were applied sequentially to produce three fractions: carbohydrate hydrolysate, protein hydrolysate, and a solid lignin- carbohydrate residue. To minimize microbial contamination, processing was performed at 60°C for 4 hr. In all, 14 and 36% of the original dry matter was liberated by carbohydrase and protease, respectively. The carbohydrate- degrading enzyme cocktail produced cellulose- and hemicellulose- derived mono- and oligosaccharides. The protease treatment released peptide-enriched hydrolysate. Approximately half of the original BSG solids were solubilized during the two-stage enzymatic process. Although the protease efficiently released the majority of BSG proteins, the carbohydrate matrix was much less accessible to enzyme attack. The impact of scale-up to pilot scale was compared with previous laboratory-scale studies, and the results were found to be in good agreement.
- Published
- 2011
- Full Text
- View/download PDF
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