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134 results on '"Segato F"'

1. Use of Tunable Copolymers in Aqueous Biphasic Systems for Extractive Bioconversion Aimed at Continuous Fructooligosaccharide Production

Author

Mendonc, C.M.N., Verissimo, N.V., Pereira, W.A., Cunha, P.M., Vitolo, M., Converti, A., Kurnia, K.A., Segato, F., Azevedo, P.O.S.D., Freire, M.G., Venema, K., Santos, J.H.P.M., Oliveira, R.P.S., Mendonc, C.M.N., Verissimo, N.V., Pereira, W.A., Cunha, P.M., Vitolo, M., Converti, A., Kurnia, K.A., Segato, F., Azevedo, P.O.S.D., Freire, M.G., Venema, K., Santos, J.H.P.M., and Oliveira, R.P.S.

Abstract

Aqueous biphasic systems (ABSs) based on sodium polyacrylate (NaPA), ethylene oxide/propylene oxide (EO/PO) polymers, and (EO)x- (PO)y-(EO)x triblock copolymers were prepared and applied aiming at continuous fructooligosaccharide (FOS) production and separation. EO/PO hydrophilicity/hydrophobicity balance had a significant effect on ABS formation. To develop an integrated process including the continuous enzymatic (levansucrase) production of FOSs and their purification while improving the production yield by further glucose separation, the potential of these novel polymer-based ABSs as alternative platforms was investigated. They were used for the partitioning of different carbohydrates (FOS, sucrose, D- fructose, and D-glucose) and levansucrase. Results revealed a highly polymer-dependent partition of carbohydrates and a poorly dependent one of the enzymes. Changing EO/PO and copolymers, FOS was purified with high yields (72.94-100.0%). Using polypropylene glycol 400 + NaPA 8000-based ABS, the FOS was precipitated in the interphase and separated from the other components. Pluronic PE-6800 + NaPA 8000 was identified as the best ABS for FOS continuous production and in situ purification, while minimizing levansucrase inhibition by D-glucose. This system allowed selective partition of FOSs and D-glucose toward the top phase and that of levansucrase and its substrates toward the bottom one. COnductor-like Screening MOdel for Real Solvent (COSMO-RS) suggested that ABS formation may have been due to NaPA and polymer/copolymer competition to form hydrogen bonds with water molecules. Moreover, the partition of FOSs and sugar may have been the result of a subtle balance between hydrogen bonding of sugar and polymer/copolymer and electrostatic misfit of solute with NaPA. Finally, two integrated processes were proposed to be applied with real FOS extracts obtained by chemical or enzymatic hydrolysis of inulin or by transfructosylation of concentrated sucrose solutions using

Published
2023

12. Correlation between compositional and refractive index profiles in LiNbO[sub 3]:Zn diffused optical waveguides.

Author

Nevado, R., Cussó, F., Lifante, G., Caccavale, F., Sada, C., and Segato, F.

Subjects
WAVEGUIDES, SECONDARY ion mass spectrometry, DIFFUSION
Abstract

Waveguides fabrication in Z- and X-cut LiNbO[sub 3] crystals by vapor zinc diffusion has been studied by secondary ion mass spectrometry and optical measurements. Compositional analysis of diffused substrates shows the formation of a Zn rich superficial layer, followed by a deeper region with decreasing Zn concentration. A subsequent thermal annealing process has been performed to let zinc ions further diffuse into the substrates. The composition profiles have been correlated with the refractive index profiles, reconstructed by optical reflectivity measurements. The results and the nature of the detected layers are discussed and correlated with previous x-ray studies obtained in the same samples. © 2000 American Institute of Physics. [ABSTRACT FROM AUTHOR]

Published
2000
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14. Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields.

Author

Vieira, F.R., Pecchia, J.A., Segato, F., and Polikarpov, I.

Subjects
PLEUROTUS ostreatus, BACTERIAL communities, BIOMASS, MUSHROOMS, LIGNOCELLULOSE
Abstract

Aims: To investigate characterization of the bacterial community composition and functionality and their impact on substrate biodegradation as well as mushroom yield. Methods and Results: Bacterial diversity, composition and functionality were accessed by DNA‐derived analysis for a sugarcane straw‐based substrate composted for either 5, 10 or 15 days. In addition, carbon and nitrogen losses, carbohydrate conversion and mushroom yields were measured for the different treatments. Changes were observed in the bacterial community diversity and composition after the process started, but not during the composting process itself. Following phase I, Acinetobacter sequences were recovered in high numbers, and selected genes associated with nitrogen metabolism and lignocellulose deconstruction were mapped. Substrate physicochemical composition showed elevated carbon and nitrogen losses after 10 and 15 days of phase I with reductions in mushroom yield. Conclusions: Acinetobacter species appear to play an important role in substrate degradation processes, and a 5‐day phase I period showed a significant higher mushroom yield compared to composting for either 10 or 15 days. Significance and Impact of the Study: This study confers a better understanding of the bacterial community manipulation during the substrate preparation and their influence in substrate selectivity for the Pleurotus ostreatus cultivation. [ABSTRACT FROM AUTHOR]

Published
2019
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15. Thermodynamic Optimization of the HAT Cycle Plant Structure--Part II: Structure of the Heat Exchanger Network

Author

Lazzaretto, A. and Segato, F.

Subjects
Thermodynamics -- Research, Heat exchangers -- Evaluation, Air-turbines -- Design and construction, Engineering and manufacturing industries, Science and technology
Abstract

In Part I of the paper a thermodynamic optimization methodology was presented for the 'basic' configuration of a humid air turbine cycle plant in which the heat exchange section is viewed as a black-box separated from the rest of the plant (basic components), having a fixed structure. The results of the optimization apply to all the heat exchanger networks that fulfill the optimal boundary conditions between the black-box and the rest of the plant. The aim of this part is to define these heat exchanger networks using a combination of Pinch Technology and Second Law insights. The possibility of a further reduction in the number of heat exchangers is then investigated in order to achieve the best compromise between high performances and structural simplicity. [DOI: 10.1115/1.1339000]

Published
2001

16. Thermodynamic Optimization of the HAT Cycle Plant Structure--Part I: Optimization of the 'Basic Plant Configuration'

Author

Lazzaretto, A. and Segato, F.

Subjects
Hydraulic machinery -- Design and construction, Boundary value problems -- Analysis, Thermodynamics -- Research, Engineering and manufacturing industries, Science and technology
Abstract

A method for the thermodynamic optimization of the humid air turbine cycle plant structure is presented here. The method is based on the optimization of a 'basic configuration of the plant' including 'basic components' (compressor, turbine, combustion chamber, regenerator, and saturator), always present and connected in the same way in the plant structure and a heat exchange section which is viewed as a 'black-box' where the heat transfer between hot and cold thermal flows occurs regardless of how many heat exchangers there are and of how they are interconnected. The optimal boundary conditions between the basic components and black-box are determined by calculating the conditions of maximum heat transfer in the black-box independently of the structure of the heat exchanger network. This is done by defining optimal composite curves in a Fortran routine at each step in the main optimization procedure. Once the structure of the heat exchanger networks that fulfill the optimal boundary conditions have been found, the optimal structure of the whole plant is obtained (see Section 2). The method is useful in a general sense as it can be applied to highly integrated energy systems in which it is difficult to define the optimal structure of the heat exchanger network in advance. [DOI: 10.1115/1.1338999]

Published
2001

17. A transcript finishing initiative for closing gaps in the human transcriptome

Author

Sogayar, M. C., Camargo, A. A., Bettoni, F., Carraro, D. M., Pires, L. C., Parmigiani, M. B., Ferreira, E. N., Moreira, E. S., Latorre, MRDO, Simpson, AJG, Cruz, L. O., Degaki, T. L., Festa, F., Massirer, K. B., Camargo, F., Camargo, L. P., Cunha, MAV, De Souza, S. J., Faria, M., Giuliatti, S., Kopp, Oliviera, PSL, Paiva, P. B., Pereira, A. A., Pinheiro, D. G., Puga, R. D., Souza, JES, Albuquerque, D. M., Andrade, LEC, Baia, G. S., Briones, MRS, Cavaleiro-Luna, AMS, Cerutti, J. M., Costa, F. F., Constanzi-Strauss, E., Espreafico, E. M., Ferrasi, A. C., Ferro, E. S., Fortes, MAHZ, Furchi, JRF, Gianella-Neto, D., Goldman, G. H., Goldman, MHS, Gruber, A., Guimaraes, G. S., Hackel, C., Henrique-Silva, F., Kimura, E. T., Leoni, S. G., Macedo, C., Malnic, B., Manzini, C. V., Marie, SKN, Martinez-Rossi, N. M., Menossi, M., Miracca, E. C., Nagai, M. A., Nobrega, F. G., Nobrega, M. P., Oba-Shinjo, S. M., Oliviera, M. K., Orabona, G. M., Otsuke, A. Y., Paco-Larson, M. L., Paixao, BMC, Pandolfi, JRC, Pardini, MIMC, Passos-Bueno, M. R., Passos, GAS, Pesquero, J. B., Pessoa, J. G., Rahal, Paula [UNESP], Rainho, C. A., Reis, C. P., Ricca, T. I., Rodriguez, V, Rogatto, Silvia Regina [UNESP], Romano, C. M., Romeiro, J. G., Rossi, A., Sa, R. G., Sales, M. M., SantAnna, S. C., Santarosa, P. L., Segato, F., Silva, W. A., Silva, IDCG, Silva, N. P., Soares-Costa, A., Sonati, M. F., Strauss, B. E., Tajara, E. H., Valentini, Sandro Roberto [UNESP], Villanova, F. E., Ward, L. S., Zanette, D. L., Universidade de São Paulo (USP), Ludwig Inst Canc Res, Univ Ribeirao Preto, Inst Ludwig, Universidade Federal de São Paulo (UNIFESP), Universidade Estadual de Campinas (UNICAMP), Universidade Estadual Paulista (Unesp), Universidade Federal de São Carlos (UFSCar), and Univ Vale Paraiba

Subjects
Transcription, Genetic, Software Validation, Molecular Sequence Data, Biology, Cell Line, Open Reading Frames, Exon, Software Design, Cell Line, Tumor, Complementary DNA, Consensus Sequence, Databases, Genetic, Methods, Genetics, Consensus sequence, Humans, Gene, Genetics (clinical), Expressed Sequence Tags, Expressed sequence tag, Genome, Human, Alternative splicing, Computational Biology, DNA, Neoplasm, U937 Cells, HISTOLOGIA, Alternative Splicing, Open reading frame, Genes, Human genome, Software, HeLa Cells
Abstract

Submitted by Guilherme Lemeszenski (guilherme@nead.unesp.br) on 2014-02-26T17:19:33Z No. of bitstreams: 1 WOS000222434200023.pdf: 392582 bytes, checksum: eb50adacff00ab5cc37867f0de853492 (MD5) Made available in DSpace on 2014-02-26T17:19:33Z (GMT). No. of bitstreams: 1 WOS000222434200023.pdf: 392582 bytes, checksum: eb50adacff00ab5cc37867f0de853492 (MD5) Previous issue date: 2004-07-01 Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-20T13:50:12Z No. of bitstreams: 1 WOS000222434200023.pdf: 392582 bytes, checksum: eb50adacff00ab5cc37867f0de853492 (MD5) Made available in DSpace on 2014-05-20T13:50:12Z (GMT). No. of bitstreams: 1 WOS000222434200023.pdf: 392582 bytes, checksum: eb50adacff00ab5cc37867f0de853492 (MD5) Previous issue date: 2004-07-01 We report the results of a transcript finishing initiative, undertaken for the purpose of identifying and characterizing novel human transcripts, in which RT-PCR was used to bridge gaps between paired EST Clusters, mapped against the genomic sequence. Each pair of EST Clusters selected for experimental validation was designated a transcript finishing unit (TFU). A total of 489 TFUs were selected for validation, and an overall efficiency of 43.1% was achieved. We generated a total of 59,975 bp of transcribed sequences organized into 432 exons, contributing to the definition of the structure of 211 human transcripts. The structure of several transcripts reported here was confirmed during the course of this project, through the generation of their corresponding full-length cDNA sequences. Nevertheless, for 21% of the validated TFUs, a full-length cDNA sequence is not yet available in public databases, and the structure of 69.2% of these TFUs was not correctly predicted by computer programs. The TF strategy provides a significant contribution to the definition of the complete catalog of human genes and transcripts, because it appears to be particularly useful for identification of low abundance transcripts expressed in a restricted Set of tissues as well as for the delineation of gene boundaries and alternatively spliced isoforms. Univ São Paulo, Inst Quim, BR-05513970 São Paulo, Brazil Ludwig Inst Canc Res, BR-01509010 São Paulo, Brazil Univ São Paulo, Dept Epidemiol, Sch Publ Hlth, BR-01246904 São Paulo, SP, Brazil Univ Ribeirao Preto, Dept Quim Informat Bioinformat, BR-14096380 Ribeirao Preto, Brazil Univ São Paulo, Fac Med Ribeirao Preto, Centro Terapia Celular, Hemocentro, BR-14051140 Ribeirao Preto, SP, Brazil Univ São Paulo, Fac Med Ribeirao Preto, Dept Clin Med, BR-14051140 Ribeirao Preto, SP, Brazil Inst Ludwig, Lab Biol Computacional, BR-01509010 São Paulo, SP, Brazil Univ São Paulo, Lab Genet Cardiol Mol, Inst Coracao, BR-05403000 São Paulo, SP, Brazil Univ Fed São Paulo, Bioinform Lab, Hlth Informatics Dept, BR-04039032 São Paulo, Brazil Univ Estad Campinas, Dept Clin Med, Fac Ciências Med, BR-13083970 Campinas, SP, Brazil Univ Fed São Paulo, Rheumatol Div, BR-04113001 São Paulo, Brazil Univ São Paulo, Dept Histol Embriol, Inst Ciências Biomed, BR-05508900 São Paulo, Brazil Univ Fed São Paulo, Dept Microbiol Immunol Parasitol, BR-04023062 São Paulo, Brazil Univ São Paulo, Lab Cellular Mol Endocrinol, Sch Med, BR-01246903 São Paulo, Brazil Univ Fed São Paulo, Dept Med, Disciplina Endocrinol, Lab Endocrinol Mol, BR-04039002 São Paulo, Brazil Univ São Paulo, Inst Ciências Biomed, Lab Transferencia Genica, BR-05508900 São Paulo, Brazil Univ São Paulo, Fac Med Ribeirao Preto, Dept Biol Celular Mol Bioagentes Patogenicas, BR-14049900 Ribeirao Preto, SP, Brazil Univ Estadual Paulista, Lab Biol Mol, Hemocentro, Fac Med, BR-18618970 Botucatu, SP, Brazil Univ Fed Sao Carlos, Dept Genet Evol, BR-13565905 Sao Carlos, SP, Brazil Univ São Paulo, Fac Ciências Farmaceuticas Ribeirao Preto, BR-14040903 Ribeirao Preto, SP, Brazil Univ São Paulo, Fac Filosofia Ciências Letras Ribeirao Preto, Ribeirao Preto, SP, Brazil Univ São Paulo, Dept Patol, Fac Med Vet Zootecnia, BR-05508000 São Paulo, Brazil Univ Estadual Campinas, Dept Genet Med, Fac Ciências Med, BR-13081970 Campinas, SP, Brazil Univ São Paulo, Fac Med Ribeirao Preto, Dept Genet, BR-14040900 Ribeirao Preto, SP, Brazil Univ São Paulo, Dept Bioquim, Inst Quim, BR-05599970 São Paulo, Brazil Univ São Paulo, Dept Neurol, Fac Med, BR-01246903 São Paulo, Brazil Univ Estadual Campinas, Lab Genoma Funcional, Centro Biol Mol Engenharia Genet, BR-13083970 Campinas, SP, Brazil Univ Estadual Campinas, Dept Genet Evol, Inst Biol, Campinas, SP, Brazil Univ São Paulo, Dept Radiol, Disciplina Oncol, Fac Med, BR-01246903 São Paulo, Brazil Univ Vale Paraiba, Inst Pesquisa Desenvolvimento, BR-12244000 Sao Jose Dos Campos, SP, Brazil Univ São Paulo, Inst Biociencias, Centro Estudios Genoma Humano, Dept Biol, BR-055508900 São Paulo, Brazil Univ Fed São Paulo, Lab Mol Gynecol, Dept Gynecol, BR-04039001 São Paulo, Brazil São Paulo State Univ, Sch Pharmacol, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil Univ São Paulo, Discipl Genet, Fac Odontol, BR-14040900 Ribeirao Preto, SP, Brazil Univ Fed São Paulo, Dept Biofisica, BR-04023062 São Paulo, Brazil Univ Estadual Paulista, Dept Biol, Inst Biociencias Letras Ciências Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil Univ Estadual Paulista, Dept Genet, Inst Biociencias, BR-18618000 Botucatu, SP, Brazil Univ São Paulo, Dept Bioquim Imunol, Fac Med Ribeirao Preto, BR-14049900 Ribeirao Preto, SP, Brazil Univ Estadual Campinas, Lab Genet Mol Cancer, Dept Clin Med, Fac Ciências Med, BR-13083970 Campinas, SP, Brazil Univ Estadual Campinas, Dept Patol Clin, Fac Ciências Med, BR-13083970 Campinas, SP, Brazil Univ São Paulo, Setor Vetores Virals, Lab Cardiol Mol, Inst Coracao, BR-15403000 São Paulo, Brazil Univ Estadual Paulista, Lab Biol Mol, Hemocentro, Fac Med, BR-18618970 Botucatu, SP, Brazil São Paulo State Univ, Sch Pharmacol, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil Univ Estadual Paulista, Dept Biol, Inst Biociencias Letras Ciências Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil Univ Estadual Paulista, Dept Genet, Inst Biociencias, BR-18618000 Botucatu, SP, Brazil

Published
2004

20. Erbium doping LiNbO3 by the ion exchange process

Author

Sada, C., Borsella, E., Caccavale, F., Gonella, Francesco, Segato, F., Korkishko, Y. u. N., Fedorov, V. A., Morozova, T. M., Battaglin, Giancarlo, and Polloni, Riccardo

Published
1998

35. Erbium doping of LiNbO3 by the ion exchange process

Author

Sada, C., primary, Borsella, E., additional, Caccavale, F., additional, Gonella, F., additional, Segato, F., additional, Korkishko, Yu. N., additional, Fedorov, V. A., additional, Morozova, T. M., additional, Battaglin, G., additional, and Polloni, R., additional

Published
1998
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39. Characterization of alpha-phase soft proton-exchanged LiNbO_3 optical waveguides

Author

Korkishko, Yu. N., Fedorov, V. A., Baranov, E. A., Proyaeva, M. V., Morozova, T. V., Caccavale, F., Segato, F., Sada, C., and Kostritskii, S. M.

Abstract

Waveguides in LiNbO_3 are realized by a soft proton exchange (SPE) process with use of a melt of stearic acid highly diluted by lithium stearate. No phase transitions are formed when -phase waveguides are obtained by SPE. The alpha-phase presents the same crystalline structure as that of pure LiNbO_3 crystal, and it maintains the excellent nonlinear and electro-optical properties of the bulk material. The kinetics of the SPE method is studied by the use of secondary-ion mass spectrometry and prism-coupling techniques. The hydrogen effective diffusion coefficient as well as the self-diffusion coefficients of H^+ and Li^+ ions are determined as a function of the proton-exchange temperature for X-cut LiNbO_3 .

Published
2001

40. Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber

Author

Segato Fernando, Damasio André R L, Gonçalves Thiago, Murakami Mario T, Squina Fabio M, Polizeli MariadeLourdesTM, Mort Andrew J, and Prade Rolf A

Subjects
Cellobiohydrolase, Cellobiohydrolase I, Cellobiohydrolase D, Aspergillus niveus, Aspergillus fumigatus, Crystalline cellulose breakdown, Biofuels, Cellulases, Biomass decomposition, Fuel, TP315-360, Biotechnology, TP248.13-248.65
Abstract

Abstract Background Cellulose consisting of arrays of linear beta-1,4 linked glucans, is the most abundant carbon-containing polymer present in biomass. Recalcitrance of crystalline cellulose towards enzymatic degradation is widely reported and is the result of intra- and inter-molecular hydrogen bonds within and among the linear glucans. Cellobiohydrolases are enzymes that attack crystalline cellulose. Here we report on two forms of glycosyl hydrolase family 7 cellobiohydrolases common to all Aspergillii that attack Avicel, cotton cellulose and other forms of crystalline cellulose. Results Cellobiohydrolases Cbh1 and CelD have similar catalytic domains but only Cbh1 contains a carbohydrate-binding domain (CBD) that binds to cellulose. Structural superpositioning of Cbh1 and CelD on the Talaromyces emersonii Cel7A 3-dimensional structure, identifies the typical tunnel-like catalytic active site while Cbh1 shows an additional loop that partially obstructs the substrate-fitting channel. CelD does not have a CBD and shows a four amino acid residue deletion on the tunnel-obstructing loop providing a continuous opening in the absence of a CBD. Cbh1 and CelD are catalytically functional and while specific activity against Avicel is 7.7 and 0.5 U.mg prot-1, respectively specific activity on pNPC is virtually identical. Cbh1 is slightly more stable to thermal inactivation compared to CelD and is much less sensitive to glucose inhibition suggesting that an open tunnel configuration, or absence of a CBD, alters the way the catalytic domain interacts with the substrate. Cbh1 and CelD enzyme mixtures on crystalline cellulosic substrates show a strong combinatorial effort response for mixtures where Cbh1 is present in 2:1 or 4:1 molar excess. When CelD was overrepresented the combinatorial effort could only be partially overcome. CelD appears to bind and hydrolyze only loose cellulosic chains while Cbh1 is capable of opening new cellulosic substrate molecules away from the cellulosic fiber. Conclusion Cellobiohydrolases both with and without a CBD occur in most fungal genomes where both enzymes are secreted, and likely participate in cellulose degradation. The fact that only Cbh1 binds to the substrate and in combination with CelD exhibits strong synergy only when Cbh1 is present in excess, suggests that Cbh1 unties enough chains from cellulose fibers, thus enabling processive access of CelD.

Published
2012
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41. Transcriptional profiling reveals the expression of novel genes in response to various stimuli in the human dermatophyte Trichophyton rubrum

Author

Aquino-Ferreira Roseli, Cursino-Santos Jeny R, Mazucato Mendelson, Cazzaniga Rodrigo A, Segato Fernando, Gras Diana E, Maranhão Fernanda CA, Paião Fernanda G, Silveira Henrique CS, Falcão Juliana P, Sanches Pablo R, Peres Nalu TA, Rossi Antonio, and Martinez-Rossi Nilce M

Subjects
Microbiology, QR1-502
Abstract

Abstract Background Cutaneous mycoses are common human infections among healthy and immunocompromised hosts, and the anthropophilic fungus Trichophyton rubrum is the most prevalent microorganism isolated from such clinical cases worldwide. The aim of this study was to determine the transcriptional profile of T. rubrum exposed to various stimuli in order to obtain insights into the responses of this pathogen to different environmental challenges. Therefore, we generated an expressed sequence tag (EST) collection by constructing one cDNA library and nine suppression subtractive hybridization libraries. Results The 1388 unigenes identified in this study were functionally classified based on the Munich Information Center for Protein Sequences (MIPS) categories. The identified proteins were involved in transcriptional regulation, cellular defense and stress, protein degradation, signaling, transport, and secretion, among other functions. Analysis of these unigenes revealed 575 T. rubrum sequences that had not been previously deposited in public databases. Conclusion In this study, we identified novel T. rubrum genes that will be useful for ORF prediction in genome sequencing and facilitating functional genome analysis. Annotation of these expressed genes revealed metabolic adaptations of T. rubrum to carbon sources, ambient pH shifts, and various antifungal drugs used in medical practice. Furthermore, challenging T. rubrum with cytotoxic drugs and ambient pH shifts extended our understanding of the molecular events possibly involved in the infectious process and resistance to antifungal drugs.

Published
2010
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42. Erbium doping of LiNbO[sub 3] by the ion exchange process.

Author

Sada, C., Borsella, E., Caccavale, F., Gonella, F., Segato, F., Korkishko, Yu. N., Fedorov, V. A., Morozova, T. M., Battaglin, G., and Polloni, R.

Subjects
SEMICONDUCTOR doping, ERBIUM, ION exchange (Chemistry), MASS spectrometry, MICROSTRUCTURE
Abstract

Erbium-doped LiNbO[sub 3] slides are fabricated by the ion exchange process. Compositional in-depth profiles of the species involved in the exchange are obtained by secondary ion mass spectrometry. Spectroscopic properties of Er[sup 3+] ions in the matrix are determined by photoluminescence spectroscopy. Structural and spectroscopic analyses suggest the formation of two different microstructures in the exchanged region. The potential of ion exchange for a controlled doping of LiNbO[sub 3] is outlined. © 1998 American Institute of Physics. [ABSTRACT FROM AUTHOR]

Published
1998
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43. A global metagenomic map of urban microbiomes and antimicrobial resistance

Author

Nadine Farhat, Tomoki Takeda, Astred Castro, Ken McGrath, Khaliun Sanchir, Iman Hajirasouliha, Eunice So, Laraib Zafar, Diana N. Nunes, Harun Mustafa, Amy Zhang, Priscilla Lisboa, Christian Schori, Marisano James, Jasna Chalangal, Sebastien Halary, Shahryar Rana, Yunmi Lee, Oli Schacher, Liliana Godoy, David A. Coil, Phanthira Pugdeethosal, Michelle D. Williams, German Marchandon, Angela Cantillo, Naoya Takahashi, Christopher Mozsary, Juana Gonzalez, Patrick K. H. Lee, Gerardo de Lamotte, Alessandro Robertiello, Steven Du, Fabienne Velter, Stefan G. Stark, Miguel Carbajo, Vincent Matthys, David A. Westfall, Julia Boeri, Irène Mauricette Mendy, Jonathan Cedillo, Francesco Oteri, Robert W. Crawford, Takayuki Ito, Tina Wunderlin, Maureen Muscat, David Paez-Espino, Carmen Urgiles, Aida Nesimi, Steffen Schaaf, Adan Ramirez-Rojas, Kunihiko Miyake, Christopher E. Mason, Anais Cardenas, Sharah Islam, Diego Benítez, Melissa Pool Pizzi, Kianna Ciaramella, Ciro Borrelli, Riham Islam, Dorottya Nagy-Szakal, Abd-Manaaf Bakere, Ait-hamlat Adel, Olha Lakhneko, Badamnyambuu Iderzorig, Ana Valeria Castro, Adam Phillips, Robert A. Petit, Flavia Corsi, Romain Conte, Krista Ryon, Soojin Jang, Joseph Benson, Fernanda de Souza Gomes Kehdy, Cindy Wang, Nicole Mathews, Jenn-Wei Chen, Rachel Paras, Paulina Pastuszek, Abigail Lyons, Paul Roldán, Muntaha Munia, Pierre Nicolas, Cassie L. Ettinger, Kyrylo Pyrshev, Katterinne N. Mendez, Eduardo Castro-Nallar, Valeriia Dotsenko, Michelle Tuz, Krizzy Mallari, Eileen Png, Yuya Sonohara, Tanja Miketic, Stéphane Delmas, Shu Zhang, Masaki Sato, Yuanting Zheng, Jifeng Zhu, Roland Häusler, Lucie Bittner, Savlatjon Rahmatulloev, Jonathan Foox, Bruno D'Alessandro, Alketa Plaku, Faisal Alquaddoomi, Yang Zhang, Kern Rei Chng, Juliana Lago, Allaeddine Chettouh, Tamera Henry, Houtan Noushmehr, Tranette Gregory, Sara Abdul Majid, Frank J. Kelly, Benjamin Pulatov, Laurie Casalot, Takema Kajita, Lennard Epping, Thais Fernanda Bartelli, Eftar Moniruzzaman, Renee Vivancos-Koopman, Thirumalaisamy P. Velavan, Tracy W. Liu, Yelyzaveta Tymoshenko, Alma Plaku, Nika Gurianova, Ambar Mendez, Anna Tomaselli, Sonia Dorado, Donato Giovannelli, Hira Choudhry, Synti Ng, Sheelta S. Kumar, Jennifer Q. Lu, Weijun Liang, Ellen Koag, Dennis Gankin, Maria João Amorim, Gwenola Simon, Kiyoshi Suganuma, Mikhail Karasikov, Christos A. Ouzounis, Madelyn May, Eran Elhaik, Stephan Ossowski, Kevin Bolzli, Matthew Arthur, Yuya Oto, Jananan Pathmanathan, Salah Mahmoud, Kou Takahashi, Brunna Marques, Kelly French, Felipe Sepúlveda, Shusei Yoshikawa, Paulo Thiago de Souza Santos, Andrew N. Gray, Juliana S Bernardes, Felipe Segato, Björn Brindefalk, George C. Yeh, Jhovana L. Velasco Flores, Jill Sullivan, Silva Baburyan, Denisse Flores, Russell Y. Neches, Sabrina Persaud, Rasheena Wright, Takumi Togashi, Verónica Antelo, Nao Kato, Skye Felice, Tatjana Mustac, Daisy Donnellan, Katerine Carrillo, Anna Litskevitch, Catalina García, Sota Ito, Naya Eady, Andrew Wan, Irene Meng, Sophie Guasco, Danilo Ercolini, Francesca De Filippis, Vincent Lemaire, Luice Fan, Lothar H. Wieler, Mariia Rybak, Jorge Sanchez, Jonathan S. Gootenberg, Itsuki Tomita, Maritza S Mosella, Laura Garcia, Natalka Makogon, Daisy Cheung, Hitler Francois Vasquez Arevalo, Freddy Asenjo, Gabriela P. Branco, Erika Cifuentes, Chloé Dequeker, Aspassia D. Chatziefthimiou, Alexis Terrero, Roy Meoded, Isabelle de Oliveira Moraes, Shaleni K. Singh, Orgil-Erdene Molomjamts, Karishma Miah, Laurent David, Wolfgang Haehr, Dao Phuong Giang, Romain Lannes, Prashanthi Ratnanandan, Ryota Yamanaka, Riccardo Vicedomini, Sadaf Ayaz, Oluwatosin M. Osuolale, Laura E. Vann, Gregory Chem, Andrea Gonzalez, Aszia Burrell, Ariel Chernomoretz, Sakura Ishizuka, Michelle Rivera, Avigdor Nosrati, Michelle B. Chen, Juliette Auvinet, Nils Ordioni, Tomoro Warashina, Guillaume Blanc, Tomislav Ivankovic, Christina Black, Lauren E. Hittle, David Hess-Homeier, Michael Kozhar, Hamood Suliman, Karobi Moitra, Saher Rahiel, Spyridon Gkotzis, Jenny Arevalo, Shaikh B. Iqbal, Beth Mutai, Mohammed Mohsin, Scott Tighe, Sylvie Collin, Yoshitaka Saito, Wayne Menary, Youping Deng, Lucy Lee, Esmeralda Jiminez, Ayuki Watanabe, Nikos C. Kyrpides, Natasha Mohan, Angelika Pupiec, Dedan Githae, Simone Cawthorne, Jonathan A. Eisen, Tomoki Iwashiro, Chiaki Homma, Thomas Saw Aung, Laura Molina, Marcus H. Y. Leung, Ophélie Da Silva, Yan Ling Wong, Hosna Noorzi, Mario Moreno, Alina Butova, Leming Shi, Brian W. Wong, Sarah S. Jackson, Moses Lin, Annabelle Meagher, Pujita Das, Catherine Burke, Mitsuki Ota, Maria Domenica Moccia, Nicolas Sprinsky, Catherine E. Pugh, David C. Green, Fazlina Fauzi, Erdenetsetseg Batdelger, Annie Geiger, Valeria Ventorino, Tolulope Oluwadare, Delisia Cuebas, Catalina Truong, Leonardo Posada, Michael Angelov, Tathiane M. Malta, Amanda Ng, Francesca Nadalin, Arya Hawkins-Zafarnia, Yuh Shiwa, Athena Mitsios, Milton Ozório Moraes, Manolo Laiola, Kalyn Ali, Jaden J.A. Hastings, Ikuto Saito, Maheen Shakil, Chisato Suzuki, Elena M. Vayndorf, Hubert Rehrauer, Ajay Menon, Kaitlan Russell, Aliyah Shari, Rebecca Smith, Gregorio Iraola, Max Priestman, Alan Briones, Silver A. Wolf, Camila Gonzalez-Poblete, Eleonora De Lazzari, Shirley Chiu, Michelle Ki, Irene Hoxie, Marianne Jaubert, Ayantu Jinfessa, Ryan J. King, Nghiem Xuan Hoan, Jalia Bynoe, Jacob Friedman, Aneisa Ramcharan, Pablo Fresia, Cristina Muñoz, Muhammad Afaq, Anyi Tang, Médine Benchouaia, Isabella Kuniko T. Takenaka, Anastasia Chasapi, Areeg Naeem, Hannah Benisty, Cecilia N. Cossio, Nathalie Hüsser, Mahfuza Sabina, Thais S. Sabedot, JoAnn Jacobs, Camila P. E. de Souza, Manuela Oliveira, Jean-Pierre Bouly, Mariko Usui, Wilson Miranda, Natalia Marciniak, Hiram Caballero, Samuel Weekes, Alexandra B. Graf, Emily Leong, Tatyana Nikolayeva, Dominique Thomas, Charlotte Greselle, Cecilia Salazar, Sreya Ray Chaudhuri, Kevin Becher, Sandra Roth, Ryusei Miura, Kari Oline Bøifot, Dimitri Manoir, Oliver Toth, Chandrima Bhattacharya, Manuel Perez, Isha Lamba, Takafumi Tsurumaki, Timothy D. Read, Anna-Lena M. Schinke, Ryan Sankar, Le Huu Song, Narasimha Rao Nedunuri, Emmanuel Dias-Neto, Ana Flávia Costa, Adiell Melamed, Christelle Desnues, Natalie R. Davidson, Aaron E. Darling, Hyung Jun Kim, Josephine Galipon, Jacqueline Orrego, Dimitar Vassilev, Michael Huber, Nur Hazlin Hazrin-Chong, Gaston H. Gonnet, Kaymisha Knights, Osman U. Sezerman, Dmitry Meleshko, Eunice Thambiraja, Jingcheng Yang, Aubin Fleiss, Gloria Nguyen, Katelyn Jackson, Nuria Aventin, Stephanie L. Hyland, Andrea Hässig, Catharine Aquino, Simona Lysakova, Israel O. Osuolale, Kasia Sluzek, Rania Siam, Alina Frolova, Samuel Hernandez, Yui Him Lo, Bazartseren Boldgiv, Ben Young, Maryna Korshevniuk, Majelia Ampadu, Yuk Man Tang, Amanda L. Muehlbauer, Sade Thomas, Gabriel Figueroa, Alexis Rivera, Lisbeth Pineda, Alexandra Dutan, Jennifer M. Tran, Chris K. Deng, Vedbar S. Khadka, Paola Florez de Sessions, Elizabeth Humphries, Hugues Richard, Hiba Naveed, Nora C. Toussaint, Mahshid Khavari, Maria del Mar Vivanco Ruiz, Antonin Thiébaut, Nicolás Rascovan, Marius Dybwad, Orhan Özcan, Lawrence Kwong, David Danko, Shaira Khan, Andrea Tassinari, Silvia Beurmann, Tsoi Ying Lai, Nanami Kubota, Tieliu Shi, Diana Chicas, Evan E. Afshin, Hirokazu Yano, Jonas Krebs, Mayuko Nakagawa, Hyun Jung Lee, Irene González Navarrete, Rachid Ounit, Lucia E. Alvarado-Arnez, Masaki Nasu, Allison Chan, Harilanto Andrianjakarivony, Jennifer Amachee, Mahdi Taye, Wan Chiew Ng, Kathryn O’Brien, Shino Ishikawa, Tristan Bitard-Feildel, Sora Takagi, Felix Hartkopf, Niamh B. O’Hara, Marcos A. S. Fonseca, Subhamitra Pakrashi, Amrit Kaur, Eva Hell, Patricia Vera-Wolf, Naimah Munim, Luiza Ferreira de Araújo, Mizuki Igarashi, Brianna Pompa-Hogan, Alessandra Carbone, Anne-Sophie Benoiston, Eric Helfrich, Michael A. Suarez-Villamil, Omar O. Abudayyeh, Natasha Abdullah, Jaime J. Fuentes, Juan Carlos Forero, Tetiana Yeskova, Denis Bertrand, Sambhawa Priya, Denisse Maldonado, Agier Nicolas, Ana Valeria B Castro, Starr Chatziefthimiou, André Kahles, Aaishah Francis, Fernanda Arredondo, Emilio Tarcitano, Irvind Buttar, Alex Alexiev, Jennifer Molinet, Sarah Shalaby, Itunu A. Oluwadare, Jason Sperry, Katrin Bakhl, Ana M. Cañas, Sofia Ahsanuddin, Miar Elaskandrany, Elodie Laine, Sven Bönigk, Johannes Werner, Stephen Eduard Boja Ruiz, Gargi Dayama, Paulina Buczansla, Brandon Valentine, Bharath Prithiviraj, Toni Bode, Stas Zubenko, Jake Cohen, Guilllaume Jospin, Zulena Saravi, Per O. Ljungdahl, Inderjit Kaur, Mauricio Moldes, Giuseppe KoLoMonaco, Denise Syndercombe Court, Sonia Bouchard, Sonia Losim, Sookwon Moon, Heba Shaaban, Suraj Patel, Sibo Zhu, Sarh Aly, Arif Asyraf Md Supie, LaShonda Dorsey, Juan Guerra, François Baudon, Rantimi A. Olawoyin, Alexia Bordigoni, Iqra Faiz, Mathilde Garcia, Gabriella Mason-Buck, María Gabriela Portilla, Niranjan Nagarajan, Fumie Takahara, Nancy Merino, Watson Andrew, Gina Kim, Yuma Sato, Hyenah Shim, Marie-Laure Jerier, Affifah Saadah Ahmad Kassim, Katerina Kuchin, Daniel Butler, Paweł P. Łabaj, Nadezhda Kobko-Litskevitch, Emmanuel F. Mongodin, Yuto Togashi, Paula Rodríguez, Pilar Lopez Hernandez, Xiaoqing Chen, Maria A. Sierra, Olga Nikolayeva, Manon Loubens, Colleen Conger, Hikaru Shirahata, Chenhao Li, Timothy Donahoe, Youngja Park, Lucia Elena Alvarado Arnez, Salama Chaker, Francisco Chavez, Alessandra Breschi, Jorge L. Sanchez, Kaung Myat San, Nayra Aguilar Rojas, Marcos Abraao, Kai Sasaki, Bryan Nazario, Olena Yemets, Klas I. Udekwu, Lynn M. Schriml, Anisia Peters, Aliaksei Holik, Mark Hernandez, Emile Faure, Malay Bhattacharyya, Josef W. Moser, Núria Andreu Somavilla, María Mercedes Zambrano, Kannan Rajendran, Gabriela E. Albuquerque, Tao Qing, Kazutoshi Tsuda, Ymke De Jong, Princess Osma, Mayra Arauco Livia, Javier Quilez Oliete, Carl Chrispin, Hyun Woo Joo, Ingrid Lafontaine, Nala An, Seisuke Sato, Felipe Segato Dezem, Andrew Maltez Thomas, Alexandre Desert, Xiao Wen Cai, O. Osuolale, Jun Wu, Coral Pardo-Esté, Courtney Robinson, Yuri Matsuzaki, Marina Nieto-Caballero, Cem Meydan, Ralph Schlapbach, Mark Menor, Sofia Castro, Rachel Kwong, Brittany Blyther, Olexandr Lykhenko, Jason R. Schriml, Christian Brion, Jenessa Orpilla, Juan A. Ugalde, Elsy Mankah Ngwa, Álvaro Aranguren, Lauren Mak, Matías Giménez, Ashanti Narce, Torsten Semmler, Stefan I. Tsonev, Abdollahi Nika, Katherine E. Dahlhausen, Monika Devi, Gunnar Rätsch, Oasima Muner, Carla Bello, Muhammad Al-Fath Amran, Anyelic Rosario, Melissa Ortega, Andrea Patrignani, Ante Peros, Elias McComb, Ryo Sato, Ireen Alam, Clara N. Dias, Soma Tanaka, Dayana Calderon, Ran Blekhman, Mathilde Mignotte, Alicia Boyd, Jochen Hecht, Thomas Neff, Xinzhao Tong, Josue Alicea, Kiara Olmeda, Sonia Marinovic, Carme Arnan, Kohei Ito, Samantha L. Goldman, Marianna S. Serpa, Renee Richer, Kaisei Sato, Jordana M. Silva, Akash Keluth Chavan, Sangwan Kim, Laís Pereira Ferreira, Sophie Vacant, Nowshin Sayara, Haruo Suzuki, Madeline Leahy, Juan C. Severyn, Sierra Vincent, Masaru Tomita, Maliha Mamun, Lucinda B. Davenport, Gabriella Oken, Dagmara Lewandowska, Gustavo Adolfo Malca Salas, Andrii Kuklin, Tyler Wong, Charlie Feigin, Eric Minwei Liu, Sonia L. Ghose, Daniela Bezdan, Antonietta La Storia, Juan P. Escalera-Antezana, Nuno Rufino de Sousa, Samuel M. Gerner, Weill Cornell Medicine [New York], Icahn School of Medicine at Mount Sinai [New York] (MSSM), Genome Institute of Singapore (GIS), Centre for Genomic Regulation [Barcelona] (CRG), Universitat Pompeu Fabra [Barcelona] (UPF)-Centro Nacional de Analisis Genomico [Barcelona] (CNAG), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Lawrence Berkeley National Laboratory [Berkeley] (LBNL), AUTRES, Massachusetts Institute of Technology (MIT), Indian Statistical Institute [Kolkata], University of Minnesota System, Universidad Andrés Bello [Santiago] (UNAB), California State University [Sacramento], University of Naples Federico II, University of Hawaii, Institut méditerranéen d'océanologie (MIO), Institut de Recherche pour le Développement (IRD)-Aix Marseille Université (AMU)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Toulon (UTLN), Medical Genomics Group, University College of London [London] (UCL)-UCL Cancer Institute, Norwegian Defence Research Establishment (FFI), Lund University [Lund], Institute of Molecular Biology and Genetics of National Academy of Sciences of Ukraine, University of Vienna [Vienna], King‘s College London, University of Colorado [Boulder], Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP), Institut Pasteur Korea - Institut Pasteur de Corée, Fudan University [Shanghai], City University of Hong Kong [Hong Kong] (CUHK), Stockholm University, University of Maryland School of Medicine, University of Maryland System, Fundação Oswaldo Cruz (FIOCRUZ), University of São Paulo (USP), Instituto de Patologia e Imunologia Molecular da Universidade do Porto (IPATIMUP), Barcelona Institute of Science and Technology (BIST), Elizade University, Acibadem Mehmet Ali Aydınlar University, Paléogénomique microbienne - Microbial paleogenomics, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU), Robert Koch Institute [Berlin] (RKI), East China Normal University [Shangaï] (ECNU), Cairo University, Vietnamese-German Center for Medical Research, Keio University, Université du Vermont, Universidad del Desarrollo, University of Sofia, University of Alaska [Fairbanks] (UAF), Universitätsklinikum Tübingen - University Hospital of Tübingen, Eberhard Karls Universität Tübingen = Eberhard Karls University of Tuebingen, Corporación Corpogen-Research Center, Biologie Computationnelle et Quantitative = Laboratory of Computational and Quantitative Biology (LCQB), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Weill Cornell Medicine [Cornell University], Cornell University [New York], University of Naples Federico II = Università degli studi di Napoli Federico II, Institut de Recherche pour le Développement (IRD)-Aix Marseille Université (AMU)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Toulon (UTLN)-Centre National de la Recherche Scientifique (CNRS), Fundação Oswaldo Cruz / Oswaldo Cruz Foundation (FIOCRUZ), Universidade de São Paulo = University of São Paulo (USP), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Софийски университет = Sofia University, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universidad Andrés Bello - UNAB (CHILE), Acibadem University Dspace, Danko, D., Bezdan, D., Afshin, E. E., Ahsanuddin, S., Bhattacharya, C., Butler, D. J., Chng, K. R., Donnellan, D., Hecht, J., Jackson, K., Kuchin, K., Karasikov, M., Lyons, A., Mak, L., Meleshko, D., Mustafa, H., Mutai, B., Neches, R. Y., Ng, A., Nikolayeva, O., Nikolayeva, T., Png, E., Ryon, K. A., Sanchez, J. L., Shaaban, H., Sierra, M. A., Thomas, D., Young, B., Abudayyeh, O. O., Alicea, J., Bhattacharyya, M., Blekhman, R., Castro-Nallar, E., Canas, A. M., Chatziefthimiou, A. D., Crawford, R. W., De Filippis, F., Deng, Y., Desnues, C., Dias-Neto, E., Dybwad, M., Elhaik, E., Ercolini, D., Frolova, A., Gankin, D., Gootenberg, J. S., Graf, A. B., Green, D. C., Hajirasouliha, I., Hastings, J. J. A., Hernandez, M., Iraola, G., Jang, S., Kahles, A., Kelly, F. J., Knights, K., Kyrpides, N. C., Labaj, P. P., Lee, P. K. H., Leung, M. H. Y., Ljungdahl, P. O., Mason-Buck, G., Mcgrath, K., Meydan, C., Mongodin, E. F., Moraes, M. O., Nagarajan, N., Nieto-Caballero, M., Noushmehr, H., Oliveira, M., Ossowski, S., Osuolale, O. O., Ozcan, O., Paez-Espino, D., Rascovan, N., Richard, H., Ratsch, G., Schriml, L. M., Semmler, T., Sezerman, O. U., Shi, L., Shi, T., Siam, R., Song, L. H., Suzuki, H., Court, D. S., Tighe, S. W., Tong, X., Udekwu, K. I., Ugalde, J. A., Valentine, B., Vassilev, D. I., Vayndorf, E. M., Velavan, T. P., Wu, J., Zambrano, M. M., Zhu, J., Zhu, S., Mason, C. E., Abdullah, N., Abraao, M., Adel, A. -H., Afaq, M., Al-Quaddoomi, F. S., Alam, I., Albuquerque, G. E., Alexiev, A., Ali, K., Alvarado-Arnez, L. E., Aly, S., Amachee, J., Amorim, M. G., Ampadu, M., Amran, M. A. -F., An, N., Andrew, W., Andrianjakarivony, H., Angelov, M., Antelo, V., Aquino, C., Aranguren, A., Araujo, L. F., Vasquez Arevalo, H. F., Arevalo, J., Arnan, C., Alvarado Arnez, L. E., Arredondo, F., Arthur, M., Asenjo, F., Aung, T. S., Auvinet, J., Aventin, N., Ayaz, S., Baburyan, S., Bakere, A. -M., Bakhl, K., Bartelli, T. F., Batdelger, E., Baudon, F., Becher, K., Bello, C., Benchouaia, M., Benisty, H., Benoiston, A. -S., Benson, J., Benitez, D., Bernardes, J., Bertrand, D., Beurmann, S., Bitard-Feildel, T., Bittner, L., Black, C., Blanc, G., Blyther, B., Bode, T., Boeri, J., Boldgiv, B., Bolzli, K., Bordigoni, A., Borrelli, C., Bouchard, S., Bouly, J. -P., Boyd, A., Branco, G. P., Breschi, A., Brindefalk, B., Brion, C., Briones, A., Buczansla, P., Burke, C. M., Burrell, A., Butova, A., Buttar, I., Bynoe, J., Bonigk, S., Boifot, K. O., Caballero, H., Cai, X. W., Calderon, D., Cantillo, A., Carbajo, M., Carbone, A., Cardenas, A., Carrillo, K., Casalot, L., Castro, S., Castro, A. V., Castro, A., Castro, A. V. B., Cawthorne, S., Cedillo, J., Chaker, S., Chalangal, J., Chan, A., Chasapi, A. I., Chatziefthimiou, S., Chaudhuri, S. R., Chavan, A. K., Chavez, F., Chem, G., Chen, X., Chen, M., Chen, J. -W., Chernomoretz, A., Chettouh, A., Cheung, D., Chicas, D., Chiu, S., Choudhry, H., Chrispin, C., Ciaramella, K., Cifuentes, E., Cohen, J., Coil, D. A., Collin, S., Conger, C., Conte, R., Corsi, F., Cossio, C. N., Costa, A. F., Cuebas, D., D'Alessandro, B., Dahlhausen, K. E., Darling, A. E., Das, P., Davenport, L. B., David, L., Davidson, N. R., Dayama, G., Delmas, S., Deng, C. K., Dequeker, C., Desert, A., Devi, M., Dezem, F. S., Dias, C. N., Donahoe, T. R., Dorado, S., Dorsey, L., Dotsenko, V., Du, S., Dutan, A., Eady, N., Eisen, J. A., Elaskandrany, M., Epping, L., Escalera-Antezana, J. P., Ettinger, C. L., Faiz, I., Fan, L., Farhat, N., Faure, E., Fauzi, F., Feigin, C., Felice, S., Ferreira, L. P., Figueroa, G., Fleiss, A., Flores, D., Velasco Flores, J. L., Fonseca, M. A. S., Foox, J., Forero, J. C., Francis, A., French, K., Fresia, P., Friedman, J., Fuentes, J. J., Galipon, J., Garcia, M., Garcia, L., Garcia, C., Geiger, A., Gerner, S. M., Ghose, S. L., Giang, D. P., Gimenez, M., Giovannelli, D., Githae, D., Gkotzis, S., Godoy, L., Goldman, S., Gonnet, G. H., Gonzalez, J., Gonzalez, A., Gonzalez-Poblete, C., Gray, A., Gregory, T., Greselle, C., Guasco, S., Guerra, J., Gurianova, N., Haehr, W., Halary, S., Hartkopf, F., Hawkins-Zafarnia, A., Hazrin-Chong, N. H., Helfrich, E., Hell, E., Henry, T., Hernandez, S., Hernandez, P. L., Hess-Homeier, D., Hittle, L. E., Hoan, N. X., Holik, A., Homma, C., Hoxie, I., Huber, M., Humphries, E., Hyland, S., Hassig, A., Hausler, R., Husser, N., Petit, R. A., Iderzorig, B., Igarashi, M., Iqbal, S. B., Ishikawa, S., Ishizuka, S., Islam, S., Islam, R., Ito, K., Ito, S., Ito, T., Ivankovic, T., Iwashiro, T., Jackson, S., Jacobs, J., James, M., Jaubert, M., Jerier, M. -L., Jiminez, E., Jinfessa, A., De Jong, Y., Joo, H. W., Jospin, G., Kajita, T., Ahmad Kassim, A. S., Kato, N., Kaur, A., Kaur, I., de Souza Gomes Kehdy, F., Khadka, V. S., Khan, S., Khavari, M., Ki, M., Kim, G., Kim, H. J., Kim, S., King, R. J., Kolomonaco, G., Koag, E., Kobko-Litskevitch, N., Korshevniuk, M., Kozhar, M., Krebs, J., Kubota, N., Kuklin, A., Kumar, S. S., Kwong, R., Kwong, L., Lafontaine, I., Lago, J., Lai, T. Y., Laine, E., Laiola, M., Lakhneko, O., Lamba, I., de Lamotte, G., Lannes, R., De Lazzari, E., Leahy, M., Lee, H., Lee, Y., Lee, L., Lemaire, V., Leong, E., Lewandowska, D., Li, C., Liang, W., Lin, M., Lisboa, P., Litskevitch, A., Liu, E. M., Liu, T., Livia, M. A., Lo, Y. H., Losim, S., Loubens, M., Lu, J., Lykhenko, O., Lysakova, S., Mahmoud, S., Majid, S. A., Makogon, N., Maldonado, D., Mallari, K., Malta, T. M., Mamun, M., Manoir, D., Marchandon, G., Marciniak, N., Marinovic, S., Marques, B., Mathews, N., Matsuzaki, Y., Matthys, V., May, M., Mccomb, E., Meagher, A., Melamed, A., Menary, W., Mendez, K. N., Mendez, A., Mendy, I. M., Meng, I., Menon, A., Menor, M., Meoded, R., Merino, N., Miah, K., Mignotte, M., Miketic, T., Miranda, W., Mitsios, A., Miura, R., Miyake, K., Moccia, M. D., Mohan, N., Mohsin, M., Moitra, K., Moldes, M., Molina, L., Molinet, J., Molomjamts, O. -E., Moniruzzaman, E., Moon, S., de Oliveira Moraes, I., Moreno, M., Mosella, M. S., Moser, J. W., Mozsary, C., Muehlbauer, A. L., Muner, O., Munia, M., Munim, N., Muscat, M., Mustac, T., Munoz, C., Nadalin, F., Naeem, A., Nagy-Szakal, D., Nakagawa, M., Narce, A., Nasu, M., Navarrete, I. G., Naveed, H., Nazario, B., Nedunuri, N. R., Neff, T., Nesimi, A., Ng, W. C., Ng, S., Nguyen, G., Ngwa, E., Nicolas, A., Nicolas, P., Nika, A., Noorzi, H., Nosrati, A., Nunes, D. N., O'Brien, K., O'Hara, N. B., Oken, G., Olawoyin, R. A., Oliete, J. Q., Olmeda, K., Oluwadare, T., Oluwadare, I. A., Ordioni, N., Orpilla, J., Orrego, J., Ortega, M., Osma, P., Osuolale, I. O., Osuolale, O. M., Ota, M., Oteri, F., Oto, Y., Ounit, R., Ouzounis, C. A., Pakrashi, S., Paras, R., Pardo-Este, C., Park, Y. -J., Pastuszek, P., Patel, S., Pathmanathan, J., Patrignani, A., Perez, M., Peros, A., Persaud, S., Peters, A., Phillips, A., Pineda, L., Pizzi, M. P., Plaku, A., Pompa-Hogan, B., Portilla, M. G., Posada, L., Priestman, M., Prithiviraj, B., Priya, S., Pugdeethosal, P., Pugh, C. E., Pulatov, B., Pupiec, A., Pyrshev, K., Qing, T., Rahiel, S., Rahmatulloev, S., Rajendran, K., Ramcharan, A., Ramirez-Rojas, A., Rana, S., Ratnanandan, P., Read, T. D., Rehrauer, H., Richer, R., Rivera, A., Rivera, M., Robertiello, A., Robinson, C., Rodriguez, P., Rojas, N. A., Roldan, P., Rosario, A., Roth, S., Ruiz, M., Boja Ruiz, S. E., Russell, K., Rybak, M., Sabedot, T. S., Sabina, M., Saito, I., Saito, Y., Malca Salas, G. A., Salazar, C., San, K. M., Sanchez, J., Sanchir, K., Sankar, R., de Souza Santos, P. T., Saravi, Z., Sasaki, K., Sato, Y., Sato, M., Sato, S., Sato, R., Sato, K., Sayara, N., Schaaf, S., Schacher, O., Schinke, A. -L. M., Schlapbach, R., Schori, C., Schriml, J. R., Segato, F., Sepulveda, F., Serpa, M. S., De Sessions, P. F., Severyn, J. C., Shakil, M., Shalaby, S., Shari, A., Shim, H., Shirahata, H., Shiwa, Y., Da Silva, O., Silva, J. M., Simon, G., Singh, S. K., Sluzek, K., Smith, R., So, E., Andreu Somavilla, N., Sonohara, Y., Rufino de Sousa, N., Souza, C., Sperry, J., Sprinsky, N., Stark, S. G., La Storia, A., Suganuma, K., Suliman, H., Sullivan, J., Supie, A. A. M., Suzuki, C., Takagi, S., Takahara, F., Takahashi, N., Takahashi, K., Takeda, T., Takenaka, I. K., Tanaka, S., Tang, A., Man Tang, Y., Tarcitano, E., Tassinari, A., Taye, M., Terrero, A., Thambiraja, E., Thiebaut, A., Thomas, S., Thomas, A. M., Togashi, Y., Togashi, T., Tomaselli, A., Tomita, M., Tomita, I., Toth, O., Toussaint, N. C., Tran, J. M., Truong, C., Tsonev, S. I., Tsuda, K., Tsurumaki, T., Tuz, M., Tymoshenko, Y., Urgiles, C., Usui, M., Vacant, S., Vann, L. E., Velter, F., Ventorino, V., Vera-Wolf, P., Vicedomini, R., Suarez-Villamil, M. A., Vincent, S., Vivancos-Koopman, R., Wan, A., Wang, C., Warashina, T., Watanabe, A., Weekes, S., Werner, J., Westfall, D., Wieler, L. H., Williams, M., Wolf, S. A., Wong, B., Wong, Y. L., Wong, T., Wright, R., Wunderlin, T., Yamanaka, R., Yang, J., Yano, H., Yeh, G. C., Yemets, O., Yeskova, T., Yoshikawa, S., Zafar, L., Zhang, Y., Zhang, S., Zhang, A., Zheng, Y., and Zubenko, S.

Subjects
Urban Population, Drug Resistance, Sequence assembly, Microbiologia, microbiome, global health, computer.software_genre, Medical and Health Sciences, shotgun sequencing, BGC, 0302 clinical medicine, Databases, Genetic, 11. Sustainability, Global health, AMR, 11 Medical and Health Sciences, ComputingMilieux_MISCELLANEOUS, 0303 health sciences, built environment, metagenome, antimicrobial resistance, NGS, de novo assembly, biology, Shotgun sequencing, Microbiota, built Environment, Bacterial, Biodiversity, Biological Sciences, 3. Good health, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Infection, Biotechnology, Geospatial analysis, [SDV.BID]Life Sciences [q-bio]/Biodiversity, Article, General Biochemistry, Genetics and Molecular Biology, Databases, 03 medical and health sciences, Antibiotic resistance, Genetic, Drug Resistance, Bacterial, International MetaSUB Consortium, Genetics, Humans, Microbiome, 030304 developmental biology, Human Genome, 06 Biological Sciences, 15. Life on land, biology.organism_classification, Resistènica als medicaments antiinfecciosos, SAÚDE PÚBLICA, Genòmica, 13. Climate action, Evolutionary biology, Metagenomics, Antimicrobial Resistance, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, computer, 030217 neurology & neurosurgery, Archaea, Developmental Biology
Abstract

Summary We present a global atlas of 4,728 metagenomic samples from mass-transit systems in 60 cities over 3 years, representing the first systematic, worldwide catalog of the urban microbial ecosystem. This atlas provides an annotated, geospatial profile of microbial strains, functional characteristics, antimicrobial resistance (AMR) markers, and genetic elements, including 10,928 viruses, 1,302 bacteria, 2 archaea, and 838,532 CRISPR arrays not found in reference databases. We identified 4,246 known species of urban microorganisms and a consistent set of 31 species found in 97% of samples that were distinct from human commensal organisms. Profiles of AMR genes varied widely in type and density across cities. Cities showed distinct microbial taxonomic signatures that were driven by climate and geographic differences. These results constitute a high-resolution global metagenomic atlas that enables discovery of organisms and genes, highlights potential public health and forensic applications, and provides a culture-independent view of AMR burden in cities., Graphical abstract, Highlights • Cities possess a consistent “core” set of non-human microbes • Urban microbiomes echo important features of cities and city-life • Antimicrobial resistance genes are widespread in cities • Cities contain many novel bacterial and viral species, This systematic, worldwide catalog of urban microbiomes represents a metagenomic atlas important for understanding the ecology, virulence, and antibiotic resistance of city-specific microbial communities.

Published
2021

44. Light-driven lytic polysaccharide monooxygenase catalysis mediated by Type I photosensitizers.

Author

Sepulchro AGV, Vacilotto MM, Dias LD, Pellegrini VOA, Velasco J, Inada NM, Segato F, and Polikarpov I

Abstract

The use of light as abundant, renewable, and clean energy source to boost lytic polysaccharide monooxygenase (LPMO) reactions represents an exciting and yet under-explored opportunity. Herein we demonstrated that photosensitizers, commonly used in photodynamic therapy, which act through the photocatalytic Type I mechanism can drive the oxidation of PASC by LPMOs, whereas Type II photosensitizers are not capable of promoting the LPMO activity. We analyzed Type I and Type II photosensitizers (methylene blue and tetraiodide salt of meso-tetrakis-(4-N-methylpyridyl) porphyrin, respectively) and demonstrated that, even without an addition of external reductant, Type I was capable of boosting Thermothelomyces thermophila MtLPMO9A activity in the presence of light. We also evaluated the photobiosystem in the presence and/or absence of molecular oxygen (O2) and hydrogen peroxide (H2O2), and investigated the role of superoxide radical in the methylene blue fueled reactions. Furthermore, we demonstrated that sodium bisulfite (NaHSO3), a chemical scavenger of H2O2, acts by safeguarding the enzyme from oxidative damage caused by accumulation of H2O2 early in photosensitizer-driven LPMO reactions. Finally, the results of the present work demonstrated that light-driven LPMO reactions mediated photodynamic therapy (PDT) Type I photosensitizers, which also includes molecules such as curcumin and riboflavin, is a general phenomenon., (© 2024 Wiley‐VCH GmbH.)

Published
2024
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45. Thermothelomyces thermophilus exo- and endo-glucanases as tools for pathogenic E. coli biofilm degradation.

Author

Samaniego LVB, Scandelau SL, Silva CR, Pratavieira S, de Oliveira Arnoldi Pellegrini V, Dabul ANG, Esmerino LA, de Oliveira Neto M, Hernandes RT, Segato F, Pileggi M, and Polikarpov I

Subjects
Hydrolysis, Cellulase metabolism, Cellulase chemistry, Hypocreales enzymology, Biofilms growth & development, Biofilms drug effects, Escherichia coli
Abstract

The escalating prevalence of drug-resistant pathogens not only jeopardizes the effectiveness of existing treatments but also increases the complexity and severity of infectious diseases. Escherichia coli is one the most common pathogens across all healthcare-associated infections. Enzymatic treatment of bacterial biofilms, targeting extracellular polymeric substances (EPS), can be used for EPS degradation and consequent increase in susceptibility of pathogenic bacteria to antibiotics. Here, we characterized three recombinant cellulases from Thermothelomyces thermophilus: a cellobiohydrolase I (TthCel7A), an endoglucanase (TthCel7B), and a cellobiohydrolase II (TthCel6A) as tools for hydrolysis of E. coli and Gluconacetobacter hansenii biofilms. Using a design mixture approach, we optimized the composition of cellulases, enhancing their synergistic activity to degrade the biofilms and significantly reducing the enzymatic dosage. In line with the crystalline and ordered structure of bacterial cellulose, the mixture of exo-glucanases (0.5 TthCel7A:0.5 TthCel6A) is effective in the hydrolysis of G. hansenii biofilm. Meanwhile, a mixture of exo- and endo-glucanases is required for the eradication of E. coli 042 and clinical E. coli biofilms with significantly different proportions of the enzymes (0.56 TthCel7B:0.44 TthCel6A and 0.6 TthCel7A:0.4 TthCel7B, respectively). X-ray diffraction pattern and crystallinity index of E. coli cellulose are comparable to those of carboxymethyl cellulose (CMC) substrate. Our results illustrate the complexity of E. coli biofilms and show that successful hydrolysis is achieved by a specific combination of cellulases, with consistent recurrence of TthCel7B endoglucanase., (© 2024. The Author(s).)

Published
2024
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46. Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans.

Author

Alves GS, de Andrades D, Salgado JCS, Mariano CB, Berto GL, Segato F, Ayub MAZ, Ward RJ, Alnoch RC, and Polizeli MLTM

Abstract

Acetylxylan esterases (AXEs) are essential enzymes that break down the acetyl groups in acetylated xylan found in plant cell walls polysaccharides. They work synergistically with backbone-depolymerizing xylanolytic enzymes to accelerate the degradation of complex polysaccharides. In this study, we cloned the gene axeA, which encodes the acetylxylan esterase from Aspergillus nidulans FGSC A4 (AxeAN), into the pEXPYR expression vector and introduced it into the high protein-producing strain A. nidulans A773. The purified AxeAN, with a molecular weight of 33.5 kDa as confirmed by SDS-PAGE, was found to be active on ρ-nitrophenyl acetate (ρNPA), exhibiting a remarkably high specific activity (170 U mg -1 ) at pH 7.0 and 55 °C. AxeAN demonstrated stability over a wide pH range (5.5-9.0), retaining >80% of its initial activity after 24 h. The K M and V max were 0.098 mmol L -1 and 320 U mg -1 , respectively, using ρNPA as a substrate. We also evaluated the synergistic effect of AxeAN with an endo-1,4-β-xylanase from Malbranchea pulchella (MpXyn10) in the hydrolysis of four different xylans (Birchwood, Beechwood, Oat spelt, and Arabinoxylan) to produce xylooligosaccharides (XOS). The best results were obtained using Birchwood xylan as substrate and MpXyn10-AxeAN as biocatalysts after 24 h of reaction (50 °C), with a XOS-yield of 91%, value 41% higher when compared to MpXyn10 (XOS-yield of 63%). These findings showed the potential of the application of AxeAN, together with other xylanases, to produce xylooligosaccharides with high purity and other products with high added value in the field of lignocellulosic biorefinery., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Published
2024
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47. Recombinant GH3 β-glucosidase stimulated by xylose and tolerant to furfural and 5-hydroxymethylfurfural obtained from Aspergillus nidulans.

Author

de Andrades D, Alnoch RC, Alves GS, Salgado JCS, Almeida PZ, Berto GL, Segato F, Ward RJ, Buckeridge MS, and Polizeli MLTM

Abstract

The β-glucosidase gene from Aspergillus nidulans FGSC A4 was cloned and overexpressed in the A. nidulans A773. The resulting purified β-glucosidase, named AnGH3, is a monomeric enzyme with a molecular weight of approximately 80 kDa, as confirmed by SDS-PAGE. Circular dichroism further validated its unique canonical barrel fold (β/α), a feature also observed in the 3D homology model of AnGH3. The most striking aspect of this recombinant enzyme is its robustness, as it retained 100% activity after 24 h of incubation at 45 and 50 ºC and pH 6.0. Even at 55 °C, it maintained 72% of its enzymatic activity after 6 h of incubation at the same pH. The kinetic parameters V max , K M , and Kcat/K M for ρ-nitrophenyl-β-D-glucopyranoside (ρNPG) and cellobiose were also determined. Using ρNPG, the enzyme demonstrated a V max of 212 U mg  - 1 , K M of 0.0607 mmol L  - 1 , and K cat /K M of 4521 mmol L  - 1  s  - 1 when incubated at pH 6.0 and 65 °C. The K M , V max , and K cat /K M using cellobiose were 2.7 mmol L  - 1 , 57 U mg  - 1 , and 27 mmol  -1  s  - 1 , respectively. AnGH3 activity was significantly enhanced by xylose and ethanol at concentrations up to 1.5 mol L  - 1 and 25%, respectively. Even in challenging conditions, at 65 °C and pH 6.0, the enzyme maintained its activity, retaining 100% and 70% of its initial activity in the presence of 200 mmol L  - 1 furfural and 5-hydroxymethylfurfural (HMF), respectively. The potential of this enzyme was further demonstrated by its application in the saccharification of the forage grass Panicum maximum, where it led to a 48% increase in glucose release after 24 h. These unique characteristics, including high catalytic performance, good thermal stability in hydrolysis temperature, and tolerance to elevated concentrations of ethanol, D-xylose, furfural, and HMF, position this recombinant enzyme as a promising tool in the hydrolysis of lignocellulosic biomass as part of an efficient multi-enzyme cocktail, thereby opening new avenues in the field of biotechnology and enzymology., (© 2024. The Author(s).)

Published
2024
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48. Analysis of Aureobasidium pullulans LB83 secretome reveals distinct carbohydrate active enzymes for biomass saccharification.

Author

Vieira MM, Valadares FL, Velasco J, da Silva SS, Segato F, and Chandel AK

Subjects
Saccharum chemistry, Chromatography, Liquid, Aureobasidium enzymology, Secretome enzymology, Carbohydrate Metabolism, Cellulase metabolism, Fermentation, Cellulose chemistry, Cellulose metabolism
Abstract

Aureobasidium pullulans LB83 is a versatile biocatalyst that produces a plethora of bioactive products thriving on a variety of feedstocks under the varying culture conditions. In our last study using this microorganism, we found cellulase activity (FPase, 2.27 U/ml; CMCase, 7.42 U/ml) and other plant cell wall degrading enzyme activities grown on sugarcane bagasse and soybean meal as carbon source and nitrogen, respectively. In the present study, we provide insights on the secretome analysis of this enzymatic cocktail. The secretome analysis of A. pullulans LB83 by Liquid Chromatography coupled to Mass Spectroscopy (LC-MS/MS) revealed 38 classes of Carbohydrate Active enZymes (CAZymes) of a total of 464 identified proteins. These CAZymes consisted of 21 glycoside hydrolases (55.26%), 12 glycoside hydrolases harboring carbohydrate-binding module (31.58%), 4 carbohydrate esterases (10.53%) and one glycosyl transferase (2.63%). To the best of our knowledge, this is the first report on the secretome analysis of A. pullulans LB83.

Published
2024
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49. Using low-shear aerated and agitated bioreactor for producing two specific laccases by trametes versicolor cultures induced by 2,5-xylidine: Process development and economic analysis.

Author

Fernandes AJ, Shibukawa VP, Prata AMR, Segato F, Dos Santos JC, Ferraz A, and Milagres AMF

Subjects
Trametes enzymology, Polyporaceae, Laccase metabolism, Laccase biosynthesis, Bioreactors
Abstract

Laccase isoforms from basidiomycetes exhibit a superior redox potential compared to commercially available laccases obtained from ascomycete fungi, rendering them more reactive toward mono-substituted phenols and polyphenolic compounds. However, basidiomycetes present limitations for large-scale culture in liquid media, restraining the current availability of laccases from this fungal class. To advance laccase production from basidiomycetes, a newly designed 14-L low-shear aerated and agitated bioreactor provided enzyme titers up to 23.5 IU/mL from Trametes versicolor cultures. Produced enzymes underwent ultrafiltration and LC/MS-MS characterization, revealing the predominant production of only two out of the ten laccases predicted in the T. versicolor genome. Process simulation and economic analysis using SuperPro designer® suggested that T. versicolor laccase could be produced at US$ 3.60/kIU in a 200-L/batch enterprise with attractive economic parameters and a payback period of 1.7 years. The study indicates that new bioreactors with plain design help to produce low-cost enzymes from basidiomycetes., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Published
2024
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50. Recombinant cellobiose dehydrogenase from Thermothelomyces thermophilus: Its functional characterization and applicability in cellobionic acid production.

Author

Oliva B, Velasco J, Leila Berto G, Polikarpov I, Cristante de Oliveira L, and Segato F

Subjects
Hydrogen-Ion Concentration, Disaccharides biosynthesis, Disaccharides metabolism, Temperature, Cellobiose metabolism, Sordariales enzymology, Hydrolysis, Eurotiales enzymology, Carbohydrate Dehydrogenases metabolism, Recombinant Proteins metabolism
Abstract

The fungus Thermothelomyces thermophilus is a thermotolerant microorganism that has been explored as a reservoir for enzymes (hydrolytic enzymes and oxidoreductases). The functional analysis of a recombinant cellobiose dehydrogenase (MtCDHB) from T. thermophilus demonstrated a thermophilic behavior, an optimal pH in alkaline conditions for inter-domain electron transfer, and catalytic activity on cellooligosaccharides with different degree of polymerization. Its applicability was evaluated to the sustainable production of cellobionic acid (CBA), a potential pharmaceutical and cosmetic ingredient rarely commercialized. Dissolving pulp was used as a disaccharide source for MtCDHB. Initially, recombinant exoglucanases (MtCBHI and MtCBHII) from T. thermophilus hydrolyzed the dissolving pulp, resulting in 87% cellobiose yield, which was subsequently converted into CBA by MtCDHB, achieving a 66% CBA yield after 24 h. These findings highlight the potential of MtCDHB as a novel approach to obtaining CBA through the bioconversion of a plant-based source., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Published
2024
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