195 results on '"Dumon, Claire"'
Search Results
2. PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses
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Monschein, Mareike, Jurak, Edita, Paasela, Tanja, Koitto, Taru, Lambauer, Vera, Pavicic, Mirko, Enjalbert, Thomas, Dumon, Claire, and Master, Emma R.
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- 2022
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3. Probing the determinants of the transglycosylation/hydrolysis partition in a retaining α-l-arabinofuranosidase
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Zhao, Jiao, Tandrup, Tobias, Bissaro, Bastien, Barbe, Sophie, Poulsen, Jens-Christian N., André, Isabelle, Dumon, Claire, Lo Leggio, Leila, O’Donohue, Michael J., and Fauré, Régis
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- 2021
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4. Functional exploration of in vivo and in vitro lignocellulose-fed rumen bacterial microbiomes reveals novel enzymes involved in polysaccharide breakdown
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Ufarte, Lisa, primary, Laville, Elisabeth, additional, Lazuka, Adele, additional, Lajus, Sophie, additional, Bouhajja, Emna, additional, Cecchini, Davide, additional, Rizzo, Angeline, additional, Amblard, Emilie, additional, Drula, Elodie, additional, Lombard, Vincent, additional, Terrapon, Nicolas, additional, Henrissat, Bernard, additional, Cleret, Megane, additional, Morgavi, Diego P., additional, Dumon, Claire, additional, Robe, Patrick, additional, Klopp, Christophe, additional, Bozonnet, Sophie, additional, Hernandez-Raquet, Guillermina, additional, and Potocki-Veronese, Gabrielle, additional
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- 2024
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5. Arabinoxylan in Water through SANS: Single-Chain Conformation, Chain Overlap, and Clustering
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Petermann, Maike, primary, Dianteill, Lucie, additional, Zeidi, Amal, additional, Vaha Ouloassekpa, Roméo, additional, Budisavljevic, Paul, additional, Le Men, Claude, additional, Montanier, Cédric, additional, Roblin, Pierre, additional, Cabane, Bernard, additional, Schweins, Ralf, additional, Dumon, Claire, additional, and Bouchoux, Antoine, additional
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- 2023
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6. GH62 arabinofuranosidases: Structure, function and applications
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Wilkens, Casper, Andersen, Susan, Dumon, Claire, Berrin, Jean-Guy, and Svensson, Birte
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- 2017
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7. Enzyme synergy for plant cell wall polysaccharide degradation
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Khamassi, Ahmed, primary and Dumon, Claire, additional
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- 2023
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8. Quantifying CBM–Carbohydrate Interactions Using Microscale Thermophoresis
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Wu, Haiyang, Montanier, Cédric, Dumon, Claire, Toulouse Biotechnology Institute (TBI), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
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Binding studies ,Fluorescence quenching ,Microscale thermophoresis (MST) ,Microscale thermophoresis (MST) Binding studies Fluorescence quenching Fluorescent label K d (dissociation constant) ,[SDV]Life Sciences [q-bio] ,Fluorescent label ,K d (dissociation constant) - Abstract
International audience; Microscale thermophoresis (MST) is an emerging technology for studying a broad range of biomolecular interactions with a high sensitivity. The affinity constant can be obtained for a wide range of molecules within minutes based on reactions in microliters. Here we describe the application of MST in quantifying protein-carbohydrate interactions. A CBM3a and a CBM4 are titrated with insoluble substrate (cellulose nanocrystal) and soluble oligosaccharide (xylohexaose), respectively.
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- 2023
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9. Impact of an N-terminal extension on the stability and activity of the GH11 xylanase from Thermobacillus xylanilyticus
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Song, Letian, Dumon, Claire, Siguier, Béatrice, André, Isabelle, Eneyskaya, Elena, Kulminskaya, Anna, Bozonnet, Sophie, and O’Donohue, Michael Joseph
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- 2014
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10. Quantifying CBM Carbohydrate Interactions Using Microscale Thermophoresis
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Wu, Haiyang, primary, Montanier, Cédric Y., additional, and Dumon, Claire, additional
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- 2017
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11. Enhanced enzymatic hydrolysis of corn stover using twin‐screw extrusion under mild conditions
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Elalami, Doha, primary, Aouine, Mouna, additional, Monlau, Florian, additional, Guillon, Fabienne, additional, Dumon, Claire, additional, Hernandez Raquet, Guillermina, additional, and Barakat, Abdellatif, additional
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- 2022
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12. Progress and future prospects for pentose-specific biocatalysts in biorefining
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Dumon, Claire, Song, Letian, Bozonnet, Sophie, Fauré, Régis, and O’Donohue, Michael J.
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- 2012
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13. Additional file 1 of PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses
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Monschein, Mareike, Jurak, Edita, Paasela, Tanja, Koitto, Taru, Lambauer, Vera, Pavicic, Mirko, Enjalbert, Thomas, Dumon, Claire, and Master, Emma R.
- Abstract
Additional file 1: Figure S1. Impact of loosenin-like proteins on NpXyn11A hydrolysis of azo-xylan in solution. Figure S2. Impact of loosenin-like proteins on cellulose/azo-xylan composites. Figure S3. In-solution hydrolysis of azo-xylan by Pm25 and its mutants. Figure S4. SDS-PAGE analysis of CmXyn10B (lane 2), NpXyn11A (lane 3) and TfXyn11A (lane 4). Figure S5. Replicate cellulose/azo-xylan composites after treatment for 1-h with (A) NpXyn11A or (B) TfXyn11A.
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- 2022
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14. Evidence That Family 35 Carbohydrate Binding Modules Display Conserved Specificity but Divergent Function
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Montanier, Cedric, van Bueren, Alicia Lammerts, Dumon, Claire, Flint, James E., Correia, Marcia A., Prates, Jose A., Firbank, Susan J., Lewis, Richard J., Grondin, Gilles G., Ghinet, Mariana G., Gloster, Tracey M., Herve, Cecile, Knox, J. Paul, Talbot, Brian G., Turkenburg, Johan P., Kerovuo, Janne, Brzezinski, Ryszard, Fontes, Carlos M. G. A., Davies, Gideon J., Boraston, Alisdair B., Gilbert, Harry J., and Doi, Roy H.
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- 2009
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15. MINTIA: a metagenomic INserT integrated assembly and annotation tool
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Bardou, Philippe, Laguerre, Sandrine, Maman Haddad, Sarah, Legoueix Rodriguez, Sabrina, Laville, Elisabeth, Dumon, Claire, Potocki-Veronese, Gabrielle, Klopp, Christophe, Génétique Physiologie et Systèmes d'Elevage (GenPhySE ), Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-École nationale supérieure agronomique de Toulouse [ENSAT]-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Toulouse Biotechnology Institute (TBI), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Toulouse White Biotechnology (TWB), Unité de Mathématiques et Informatique Appliquées de Toulouse (MIAT INRA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Université de Toulouse (UT)-École nationale supérieure agronomique de Toulouse (ENSAT), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Unité de Mathématiques et Informatique Appliquées de Toulouse (MIAT INRAE)
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Bioinformatics ,Activity-based metagenomics ,Functional annotation ,[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology ,Biodiversity ,Software package ,Biochemistry ,Microbiology ,[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN] ,Medicine ,Functional metagenomics ,Biotechnology ,Metagenomic fosmid ,Sequence assembly - Abstract
International audience; The earth harbors trillions of bacterial species adapted to very diverse ecosystems thanks to specific metabolic function acquisition. Most of the genes responsible for these functions belong to uncultured bacteria and are still to be discovered. Functional metagenomics based on activity screening is a classical way to retrieve these genes from microbiomes. This approach is based on the insertion of large metagenomic DNA fragments into a vector and transformation of a host to express heterologous genes. Metagenomic libraries are then screened for activities of interest, and the metagenomic DNA inserts of active clones are extracted to be sequenced and analysed to identify genes that are responsible for the detected activity. Hundreds of metagenomics sequences found using this strategy have already been published in public databases. Here we present the MINTIA software package enabling biologists to easily generate and analyze large metagenomic sequence sets, retrieved after activity-based screening. It filters reads, performs assembly, removes cloning vector, annotates open reading frames and generates user friendly reports as well as files ready for submission to international sequence repositories. The software package can be downloaded from https://github.com/Bios4Biol/MINTIA .
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- 2021
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16. Enantioselective Reductive Oligomerization of Carbon Dioxide into l-Erythrulose via a Chemoenzymatic Catalysis
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Desmons, Sarah, primary, Grayson-Steel, Katie, additional, Nuñez-Dallos, Nelson, additional, Vendier, Laure, additional, Hurtado, John, additional, Clapés, Pere, additional, Fauré, Régis, additional, Dumon, Claire, additional, and Bontemps, Sébastien, additional
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- 2021
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17. Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome
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Wu, Haiyang, Ioannou, Eleni, Henrissat, Bernard, Montanier, Cédric Y., Bozonnet, Sophie, O’Donohue, Michael J., and Dumon, Claire
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termite gut ,xylanase ,animal structures ,Endo-1,4-beta Xylanases ,Bacteroidetes ,digestive, oral, and skin physiology ,food and beverages ,macromolecular substances ,Isoptera ,protein domain insertion ,Gastrointestinal Microbiome ,carbohydrates (lipids) ,lignocellulose ,Bacterial Proteins ,Animals ,Metagenome ,glycoside hydrolase ,Xylans ,PUL ,GH10 ,Enzymology and Protein Engineering ,functional genomics ,CBM4 ,carbohydrate-binding module - Abstract
Xylan is the major hemicellulosic polysaccharide in cereals and contributes to the recalcitrance of the plant cell wall toward degradation. Bacteroidetes, one of the main phyla in rumen and human gut microbiota, have been shown to encode polysaccharide utilization loci dedicated to the degradation of xylan. Here, we present the biochemical characterization of a xylanase encoded by a bacteroidetes strain isolated from the termite gut metagenome., The functional screening of a Pseudacanthotermes militaris termite gut metagenomic library revealed an array of xylan-degrading enzymes, including P. militaris 25 (Pm25), a multimodular glycoside hydrolase family 10 (GH10). Sequence analysis showed details of the unusual domain organization of this enzyme. It consists of one catalytic domain, which is intercalated by two carbohydrate binding modules (CBMs) from family 4. The genes upstream of the genes encoding Pm25 are susC-susD-unk, suggesting Pm25 is a Xyn10C-like enzyme belonging to a polysaccharide utilization locus. The majority of Xyn10C-like enzymes shared the same interrupted domain architecture and were vastly distributed in different xylan utilization loci found in gut Bacteroidetes, indicating the importance of this enzyme in glycan acquisition for gut microbiota. To understand its unusual multimodularity and the possible role of the CBMs, a detailed characterization of the full-length Pm25 and truncated variants was performed. Results revealed that the GH10 catalytic module is specific toward the hydrolysis of xylan. Ligand binding results indicate that the GH10 module and the CBMs act independently, whereas the tandem CBM4s act synergistically with each other and improve enzymatic activity when assayed on insoluble polysaccharides. In addition, we show that the UNK protein upstream of Pm25 is able to bind arabinoxylan. Altogether, these findings contribute to a better understanding of the potential role of Xyn10C-like proteins in xylan utilization systems of gut bacteria. IMPORTANCE Xylan is the major hemicellulosic polysaccharide in cereals and contributes to the recalcitrance of the plant cell wall toward degradation. Members of the Bacteroidetes, one of the main phyla in rumen and human gut microbiota, have been shown to encode polysaccharide utilization loci dedicated to the degradation of xylan. Here, we present the biochemical characterization of a xylanase encoded by a Bacteroidetes strain isolated from the termite gut metagenome. This xylanase is a multimodular enzyme, the sequence of which is interrupted by the insertion of two CBMs from family 4. Our results show that this enzyme resembles homologues that were shown to be important for xylan degradation in rumen or human diet and show that the CBM insertion in the middle of the sequence seems to be a common feature in xylan utilization systems. This study shed light on our understanding of xylan degradation and plant cell wall deconstruction, which can be applied to several applications in food, feed, and bioeconomy.
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- 2021
18. Enantioselective Reductive Oligomerization of Carbon Dioxide into l-Erythrulose via a Chemoenzymatic Catalysis
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Ministerio de Ciencia e Innovación (España), Desmons, Sarah, Grayson-Steel, Katie, Nuñez-Dallos, Nelson, Vendier, Laure, Hurtado, John, Clapés Saborit, Pere, Fauré, Regis, Dumon, Claire, Bontemps, Sébastien, Ministerio de Ciencia e Innovación (España), Desmons, Sarah, Grayson-Steel, Katie, Nuñez-Dallos, Nelson, Vendier, Laure, Hurtado, John, Clapés Saborit, Pere, Fauré, Regis, Dumon, Claire, and Bontemps, Sébastien
- Abstract
A cell-free enantioselective transformation of the carbon atom of CO2 has never been reported. In the urgent context of transforming CO2 into products of high value, the enantiocontrolled synthesis of chiral compounds from CO2 would be highly desirable. Using an original hybrid chemoenzymatic catalytic process, we report herein the reductive oligomerization of CO2 into C3 (dihydroxyacetone, DHA) and C4 (l-erythrulose) carbohydrates, with perfect enantioselectivity of the latter chiral product. This was achieved with the key intermediacy of formaldehyde. CO2 is first reduced selectively by 4e– by an iron-catalyzed hydroboration reaction, leading to the isolation and complete characterization of a new bis(boryl)acetal compound derived from dimesitylborane. In an aqueous buffer solution at 30 °C, this compound readily releases formaldehyde, which is then involved in selective enzymatic transformations, giving rise either (i) to DHA using a formolase (FLS) catalysis or (ii) to l-erythrulose with a cascade reaction combining FLS and d-fructose-6-phosphate aldolase (FSA) A129S variant. Finally, the nature of the synthesized products is noteworthy, since carbohydrates are of high interest for the chemical and pharmaceutical industries. The present results prove that the cell-free de novo synthesis of carbohydrates from CO2 as a sustainable carbon source is a possible alternative pathway in addition to the intensely studied biomass extraction and de novo syntheses from fossil resources.
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- 2021
19. Redefining XynA from Penicillium funiculosum IMI 378536 as a GH7 cellobiohydrolase
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Texier, Hélène, Dumon, Claire, Neugnot-Roux, Virginie, Maestracci, Marc, and O’Donohue, Michael J.
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- 2012
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20. A Comparative Study to Decipher the Structural and Dynamics Determinants Underlying the Activity and Thermal Stability of GH-11 Xylanases
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Vucinic, Jelena, primary, Novikov, Gleb, additional, Montanier, Cédric, additional, Dumon, Claire, additional, Schiex, Thomas, additional, and Barbe, Sophie, additional
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- 2021
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21. In vivo fucosylation of lacto-N-neotetraose and lacto-N-neohexaose by heterologous expression of Helicobacter pylori α-1,3 fucosyltransferase in engineered Escherichia coli
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Dumon, Claire, Priem, Bernard, Martin, Steve L., Heyraud, Alain, Bosso, Claude, and Samain, Eric
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- 2001
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22. Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l-arabinofuranosidase from Thermobacillus xylanilyticus
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Arab-Jaziri, Faten, Bissaro, Bastien, Barbe, Sophie, Saurel, Olivier, Débat, Hélène, Dumon, Claire, Gervais, Virginie, Milon, Alain, André, Isabelle, Fauré, Régis, and OʼDonohue, Michael J.
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- 2012
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23. Characterization and Enzyme Engineering of a Hyperthermophilic Laccase Toward Improving Its Activity in Ionic Liquid
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Stevens, Joseph Craig, primary, Rodgers, David W., additional, Dumon, Claire, additional, and Shi, Jian, additional
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- 2020
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24. Characterisation of the Effect of the Spatial Organisation of Hemicellulases on the Hydrolysis of Plant Biomass Polymer
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Enjalbert, Thomas, primary, De La Mare, Marion, additional, Roblin, Pierre, additional, Badruna, Louise, additional, Vernet, Thierry, additional, Dumon, Claire, additional, and Montanier, Cédric Y., additional
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- 2020
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25. Characterizationof a muli-modular GH3-CBM48-CE1 isolated for termite gut microbiota
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Fermon, Laurence, Franck, Moncassin, Fauré, Régis, Montanier, Cédric, O'Donohue, Michael, Tranier, Samuel, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Université Toulouse III - Paul Sabatier (UT3), and Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2019
26. Development and characterization of multi-enzymatic system for lignocellulose degration
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Dumon, Claire, Monties, Nelly, Enjalbert, Thomas, Akkerman, Roos, Ioannou, Eleni, O'Donohue, Michael, Wu, Haiyang, Montanier, Cédric, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Institute of Biological, Environmental and Rural Sciences (IBERS), Biotechnology and Biological Sciences Research Council (BBSRC)-Aberystwyth University, Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), and Aberystwyth University
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2019
27. Tools for structural bioinformatics; design of a chimeric GH10 CBM-containing hydrolase
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Fernandez-Fuentes, Narcis, Ioannou, Eleni, Bryant, David, Dumon, Claire, O'Donohue, Michael, Aberystwyth University, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Institute of Biological, Environmental and Rural Sciences (IBERS), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Biotechnology and Biological Sciences Research Council (BBSRC)-Aberystwyth University
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2019
28. Enzymatic degration of semidilute hemicellulose solutions: a small-angle neutron scattering study
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Bouchoux, Antoine, Dianteill, Lucie, Dumon, Claire, Montanier, Cédric, LE MEN, Claude, Cabane, Bernard, Roblin, Pierre, Schweins, Ralf, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Physique et mécanique des milieux hétérogenes (UMR 7636) (PMMH), Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Institut Laue-Langevin (ILL), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), and ILL
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2019
29. Investigating the multimodularity of a Xyn10C-like protein found in a termite gut
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Wu, Haiyang, Ioannou, Eleni, Arnal, Grégory, Montanier, Cédric, Bozonnet, Sophie, Bryant, David, Fernandez-Fuentes, Narcis, O'Donohue, Michael, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institute of Biological, Environmental and Rural Sciences (IBERS), Aberystwyth University, Aberystwyth Univ, Inst Biol Environm & Rural Sci, Aberystwyth SY23 3EB, Dyfed, Wales, Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Biotechnology and Biological Sciences Research Council (BBSRC)-Aberystwyth University
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2019
30. Engineering better biomass-degrading ability into a GH11 xylanase using a directed evolution strategy
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Song Letian, Siguier Béatrice, Dumon Claire, Bozonnet Sophie, and O'Donohue Michael J
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Directed evolution ,high-throughput screening ,endo-β-1,4-xylanase ,lignocellulosic biomass ,synergistic interaction ,biorefining ,Fuel ,TP315-360 ,Biotechnology ,TP248.13-248.65 - Abstract
Abstract Background Improving the hydrolytic performance of hemicellulases on lignocellulosic biomass is of considerable importance for second-generation biorefining. To address this problem, and also to gain greater understanding of structure-function relationships, especially related to xylanase action on complex biomass, we have implemented a combinatorial strategy to engineer the GH11 xylanase from Thermobacillus xylanilyticus (Tx-Xyn). Results Following in vitro enzyme evolution and screening on wheat straw, nine best-performing clones were identified, which display mutations at positions 3, 6, 27 and 111. All of these mutants showed increased hydrolytic activity on wheat straw, and solubilized arabinoxylans that were not modified by the parental enzyme. The most active mutants, S27T and Y111T, increased the solubilization of arabinoxylans from depleted wheat straw 2.3-fold and 2.1-fold, respectively, in comparison to the wild-type enzyme. In addition, five mutants, S27T, Y111H, Y111S, Y111T and S27T-Y111H increased total hemicellulose conversion of intact wheat straw from 16.7%tot. xyl (wild-type Tx-Xyn) to 18.6% to 20.4%tot. xyl. Also, all five mutant enzymes exhibited a better ability to act in synergy with a cellulase cocktail (Accellerase 1500), thus procuring increases in overall wheat straw hydrolysis. Conclusions Analysis of the results allows us to hypothesize that the increased hydrolytic ability of the mutants is linked to (i) improved ligand binding in a putative secondary binding site, (ii) the diminution of surface hydrophobicity, and/or (iii) the modification of thumb flexibility, induced by mutations at position 111. Nevertheless, the relatively modest improvements that were observed also underline the fact that enzyme engineering alone cannot overcome the limits imposed by the complex organization of the plant cell wall and the lignin barrier.
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- 2012
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31. Signature active site architectures illuminate the molecular basis for ligand specificity in family 35 carbohydrate binding module
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Correia, Marcia A.S., Abbott, D. Wade, Gloster, Tracey M., Fernandes, Vania O., Prates, Jose A.M., Montanier, Cedric, Dumon, Claire, Williamson, Michael P., Tunnicliffe, Richard B., Ziyuan Liu, Flint, James E., Davies, Gideon J., Henrissat, Bernard, Coutinho, Pedro M., Fontes, Carlos M.G.A., and Gilbert, Harry J.
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Carbohydrates -- Chemical properties ,Galactose -- Structure ,Galactose -- Chemical properties ,Glucans -- Structure ,Glucans -- Chemical properties ,Mutagenesis -- Analysis ,Protein binding -- Analysis ,Biological sciences ,Chemistry - Abstract
A study is conducted to show that a family 35 carbohydrate binding module (CBM) member (CBM35), designated CtCBM35-Gal, binds to [alpha]-d-galactose (Gal) and, within the context of the plant cell wall, targets the [alpha]-1,6-Gal residues of galactomannan but not the [beta]-d-Gal residues in xyloglucan. The results from the site-directed mutagenesis revealed that although there is conservation of several functional residues within the binding sites of endo- and exo-CBM35s, the endo-CBM does not utilize Asn113 in mannan binding, despite the importance of the equivalent residue in ligand recognition across the CBM35 and CBM6 landscape.
- Published
- 2010
32. Etude des cinétiques enzymatiques au niveau des interfaces et en milieu confiné : le cas de la biomasse lignocellulosique
- Author
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Dianteill, Lucie, Dumon, Claire, Bouchoux, Antoine, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,[SDV]Life Sciences [q-bio] ,ComputingMilieux_MISCELLANEOUS - Abstract
Etude des cinétiques enzymatiques au niveau des interfaces et en milieu confiné : le cas de la biomasse lignocellulosique. Journées du GDR 2980 AMC2
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- 2016
33. Design of chromogenic probes for identification and evaluation of hetroxylan active enzymes
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Fauré, Régis, Borsenberger, Vinciane, LEFEVRE - GHERBOVET, Olga, F., Ferreira, Montanier, Cédric, Dumon, Claire, Bozonnet, Sophie, O’Donohue, Michael J., Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
34. Functional exploration of naturally and artificially enriched rumen microbiomes reveals novel enzymatic synergies involved in plant cell wall breakdown
- Author
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Ufarté, Lisa, Laville, Elisabeth, Cecchini, Davide, Rizzo, Davide, Amblard, Etienne, Drula, Elodie, Henrissat, Bernard, Cleret, M., Lazuka, Adèle, Hernandez Raquet, Guillermina, Morgavi, Diego, Dumon, Claire, P., Robe, Klopp, Christophe, Bozonnet, Sophie, Potocki Veronese, Gabrielle, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA), Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Unité de Mathématiques et Informatique Appliquées de Toulouse (MIAT INRA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Unité de Mathématiques et Informatique Appliquées de Toulouse (MIAT INRAE)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
35. Characterization of plant cell wallacting esterases: the effect of ionic liquids on ferulic acid release from corn stover
- Author
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Paola A., Palacio, Bulot, Suzy, Haon, Mireille, Alvira, Pablo, Record, Eric, Dumon, Claire, Raouche, Sana, Faulds, Craig B., 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), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
36. Elucidation of a hemicellulotytic cocktail for efficient partial conversion of lignocellulolytic biomass at high solid loading
- Author
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RAY, Sayani, ALVIRA, Pablo, Bakarat, Abdellatif, Hernandez Raquet, Guillermina, Bonnin, Estelle, Guillon, Fabienne, O’Donohue, Michael, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
37. Hemicellulytic potential of invertebrate microbiome for biorefinery
- Author
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Arnal, Grégory, Alvira, Pablo, Bozonnet, Sophie, Melgosa, Silvia Vidal, Willats, William G.T, Lefevre - Gherbovet, Olga, Fauré, Régis, Henrissat, Bernard, O'Donohue, M., Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Architecture et fonction des macromolécules biologiques (AFMB), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
38. Inciter l'activité de synthèse chez les enzymes hydrolytiques
- Author
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Bissaro, Bastien, DURAND, Julien, Biarnes, Xevi, Tandrup, Tobias, Dumon, Claire, Monsan, Pierre, Lo Leggio, Leila, Planas, Antoni, Bozonnet, Sophie, O'Donohue, Michael, Fauré, Régis, Biodiversité et Biotechnologie Fongiques (BBF), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Universitat Ramon Llull [Barcelona] (URL), University of Coppenhagen, Department of chemistry, Toulouse White Biotechnology (TWB), University of coppenhagen, department of chemistry, Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
39. Exploration of the lignocellulolytic potential of invertebrate microbiome
- Author
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Arnal, Grégory, ALVIRA, Pablo, Bozonnet, S., Melgosa, Silvia Vidal, Willats, W. G. T., Faure, R., Henrissat, Bernard, O'Donohue, Michael, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), University of Copenhagen, Department of Plant Biology and Biotechnology, 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), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
40. Structural and functional characterization of a hypothetical new glycoside hydrolase
- Author
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Guyez, Barbara, Franck, Moncassin, Raingeval, Claire, Bozonnet, Sophie, Henrissat, Bernard, Mourey, L, O'Donohue, Michael, Tranier, S., Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Institut de pharmacologie et de biologie structurale (IPBS), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2016
41. MOESM6 of The GH51 α-l-arabinofuranosidase from Paenibacillus sp. THS1 is multifunctional, hydrolyzing main-chain and side-chain glycosidic bonds in heteroxylans
- Author
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Hanen Bouraoui, Marie-Laure Desrousseaux, Ioannou, Eleni, Alvira, Pablo, Manaï, Mohamed, Rémond, Caroline, Dumon, Claire, Fernandez-Fuentes, Narcis, and O’Donohue, Michael
- Abstract
Additional file 6. Hydrolysis of DWB using different enzyme combinations. Figure S6A, B, C and D show the progress of hydrolysis of DWB by (A) TxAbf + TxXyn, (B) THSAbf + TxXyn, (C) THSAbf + TxAbf and (D) THSAbf + TxAbf + TxXyn. Several reactions products are monitored, including xylose, arabinose and xylooligosaccharides (X2-X6).
- Published
- 2016
- Full Text
- View/download PDF
42. Hemicellulose-degrading compositions and uses thereof
- Author
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O'Donohue, Michael, Alvira, Pablo, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), BPI France - perojet THANAPLAST, Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Application ,hémicellulases ,[SDV]Life Sciences [q-bio] ,glycoside hydrolase - Abstract
Hemicellulose-degrading compositions and uses thereof
- Published
- 2016
43. Biotechnologies et bioprocédés : clé de voute de la chimie verte.
- Author
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DUMON, Claire, FILLAUDEAU, Luc, and MONTANIER, Cédric Y.
- Subjects
SUSTAINABLE chemistry ,BOTANICAL chemistry ,ENZYMES ,FOSSILS ,BIOCATALYSIS - Abstract
Copyright of IAA Industries Agro-Alimentaires is the property of Ste Ad hoc and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
- Published
- 2021
44. Impact du pré-traitement par le procédé d'extrusion réactive sur la diversité fonctionnelle d'un consortia microbien responsable de la transformation de la lignocellulose à haute teneur en solides
- Author
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Flajollet, Emeline, Barakat, Abdellatif, Dumas, Claire, Dumon, Claire, Escudié, Renaud, Guillon, Fabienne, Hernandez Raquet, Guillermina, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), 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), Laboratoire de Biotechnologie de l'Environnement [Narbonne] (LBE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), 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 de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), 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 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 National de la Recherche Agronomique (INRA), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering - Abstract
Impact du pré-traitement par le procédé d'extrusion réactive sur la diversité fonctionnelle d'un consortia microbien responsable de la transformation de la lignocellulose à haute teneur en solides. 3. Colloque de Génomique Environnementale
- Published
- 2015
45. Discovery and characterization of novel bacterial Carbohydrate Esterases
- Author
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Alvira, Pablo, Gherbovet, Olga, Fauré, Régis, Bozonnet, Sophie, O'Donohue, Michael, Dumon, Claire, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), and Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2015
46. Exploration of the lignocellulotytic potential of invertebrate microbiome
- Author
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Arnal, Grégory, Bastien-Uluis, Geraldine, Alvira, Pablo, Bozonnet, Sophie, Laguerre, Sandrine, Fauré, Régis, Henrissat, Bernard, Dumon, Claire, O'Donohue, M., Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-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), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA)
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2015
47. How to quantify enzyme activity and kinetics in 'non-bulk' systems? An example through the enzymatic hydrolysis of hemicellulose thin films
- Author
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Zeidi, Amal, Dianteill, Lucie, LEFEVRE - GHERBOVET, Olga, Dumon, Claire, Montanier, Cédric, Fauré, Régis, Morchain, Jérôme, Lebaz, Noureddine, Séverac, Childérick, Bouchoux, Antoine, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut des Technologies Avancées en sciences du Vivant (ITAV), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), ITAV-USR 3505, Université Fédérale Toulouse Midi-Pyrénées, Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), University of Helsinki [Helsinki]. FIN. Aalto University., Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
[SPI.OTHER]Engineering Sciences [physics]/Other - Abstract
In the carbohydrate-based bioindustry, enzymes are often used in conditions where they have to work on solid surfaces and/or penetrate within structures that are locally highly concentrated. The effect of such physical constraints on the enzyme activity and kinetics is however poorly understood; mostly because following and quantifying the hydrolysis in such conditions is still a challenge. With this work, our intention is to provide a detailed characterization of an enzyme's activity when its substrate is both concentrated and immobilized at a solid interface. This is essentially done by monitoring the in-situ degradation of a thin film of a model hemicellulose using a Quartz Crystal Microbalance with Dissipation (QCM-D). The thin film is composed of a unique arabinoxylan, extracted from wheat bran, and that is chemically modified for covalently binding onto gold.1 The film is partly swollen by water, and its water content (hence its local dry concentration) can be tuned by partially removing the Larabinofuranosyl units that decorate the xylan chain.2 The film is then put into contact with a solution containing an endo-1,4-β-xylanase (NpXyn11A3 ), into the QCM-D cell, and the loss of mass in the film is followed with time as degradation occurs. Using mathematical models that are under development in our laboratory, we aim at converting the raw QCM-D data into kinetics curves that give the reaction rate as a function of the polymer concentration in the film. Such a procedure would allow us to accurately compare the behavior of the enzyme in a film with its "bulk" behavior; the latter having been characterized classically with a dilute solution of the same substrate. Our results should reveal precious indications about the effect of substrate immobilization and conformation/concentration on the action of an enzyme.
- Published
- 2015
48. Investigating the function of an arabinan utilization locus isolated from a termite gut community
- Author
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Arnal , Grégory, Bastien , Géraldine, Monties , Nelly, Abot , Anne, Anton Leberre , Véronique, Bozonnet , Sophie, O'Donohue , Michael, Dumon , Claire, Liu , S.-J., Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), OSEO Innovation, Institut National de la Recherche Agronomique, Midi-Pyrenes regional authorities R2390070/12053333, Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés ( LISBP ), Institut National de la Recherche Agronomique ( INRA ) -Institut National des Sciences Appliquées - Toulouse ( INSA Toulouse ), and Institut National des Sciences Appliquées ( INSA ) -Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS )
- Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology ,Glycoside Hydrolases ,Locus (genetics) ,Biotechnologies ,Isoptera ,Biology ,Applied Microbiology and Biotechnology ,chemistry.chemical_compound ,Polysaccharides ,Gene cluster ,Animals ,Bacteroides ,Glycoside hydrolase ,ORFS ,Enzymology and Protein Engineering ,ComputingMilieux_MISCELLANEOUS ,2. Zero hunger ,chemistry.chemical_classification ,Ecology ,[ SDV ] Life Sciences [q-bio] ,Computational Biology ,Gastrointestinal Tract ,Open reading frame ,Enzyme ,chemistry ,Biochemistry ,Metagenomics ,Multigene Family ,DNA ,Metabolic Networks and Pathways ,Food Science ,Biotechnology - Abstract
Biocatalysts are essential for the development of bioprocesses efficient for plant biomass degradation. Previously, a metagenomic clone containing DNA from termite gut microbiota was pinpointed in a functional screening that revealed the presence of arabinofuranosidase activity. Subsequent genetic and bioinformatic analysis revealed that the DNA fragment belonged to a member of the genus Bacteroides and encoded 19 open reading frames (ORFs), and annotation suggested the presence of hypothetical transporter and regulator proteins and others involved in the catabolism of pentose sugar. In this respect and considering the phenotype of the metagenomic clone, it was noted that among the ORFs, there are four putative arabinose-specific glycoside hydrolases, two from family GH43 and two from GH51. In this study, a thorough bioinformatics analysis of the metagenomic clone gene cluster has been performed and the four aforementioned glycoside hydrolases have been characterized. Together, the results provide evidence that the gene cluster is a polysaccharide utilization locus dedicated to the breakdown of the arabinan component in pectin and related substrates. Characterization of the two GH43 and the two GH51 glycoside hydrolases has revealed that each of these enzymes displays specific catalytic capabilities and that when these are combined the enzymes act synergistically, increasing the efficiency of arabinan degradation.
- Published
- 2015
- Full Text
- View/download PDF
49. CAZyChip: dynamic assessment of exploration of glycoside hydrolases in microbial ecosystems
- Author
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Abot, Anne, primary, Arnal, Gregory, additional, Auer, Lucas, additional, Lazuka, Adèle, additional, Labourdette, Delphine, additional, Lamarre, Sophie, additional, Trouilh, Lidwine, additional, Laville, Elisabeth, additional, Lombard, Vincent, additional, Potocki-Veronese, Gabrielle, additional, Henrissat, Bernard, additional, O’Donohue, Michael, additional, Hernandez-Raquet, Guillermina, additional, Dumon, Claire, additional, and Leberre, Véronique Anton, additional
- Published
- 2016
- Full Text
- View/download PDF
50. The GH51 α-l-arabinofuranosidase from Paenibacillus sp. THS1 is multifunctional, hydrolyzing main-chain and side-chain glycosidic bonds in heteroxylans
- Author
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Bouraoui, Hanen, primary, Desrousseaux, Marie-Laure, additional, Ioannou, Eleni, additional, Alvira, Pablo, additional, Manaï, Mohamed, additional, Rémond, Caroline, additional, Dumon, Claire, additional, Fernandez-Fuentes, Narcis, additional, and O’Donohue, Michael J., additional
- Published
- 2016
- Full Text
- View/download PDF
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