Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass

Detalhes bibliográficos
Autor(a) principal: dos Santos, H�vila Brognaro
Data de Publicação: 2016
Outros Autores: Bezerra, Tha�s Milena Souza [UNESP], Pradella, Jos� G. C., Delabona, Priscila, Lima, Deise, Gomes, Eleni [UNESP], Hartson, Steve D., Rogers, Janet, Couger, Brian, Prade, Rolf
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1186/s13568-016-0276-y
http://hdl.handle.net/11449/173728
Resumo: Biomass is abundant, renewable and useful for biofuel production as well as chemical priming for plastics and composites. Deconstruction of biomass by enzymes is perceived as recalcitrant while an inclusive breakdown mechanism remains to be discovered. Fungi such as Myceliophthora thermophila M77 appear to decompose natural biomass sources quite well. This work reports on this fungus fermentation property while producing cellulolytic enzymes using natural biomass substrates. Little hydrolytic activity was detected, insufficient to explain the large amount of biomass depleted in the process. Furthermore, this work makes a comprehensive account of extracellular proteins and describes how secretomes redirect their qualitative protein content based on the nature and chemistry of the nutritional source. Fungus grown on purified cellulose or on natural biomass produced secretomes constituted by: cellobiohydrolases, cellobiose dehydrogenase, β-1,3 glucanase, β-glucosidases, aldose epimerase, glyoxal oxidase, GH74 xyloglucanase, galactosidase, aldolactonase and polysaccharide monooxygenases. Fungus grown on a mixture of purified hemicellulose fractions (xylans, arabinans and arabinoxylans) produced many enzymes, some of which are listed here: xylosidase, mixed β-1,3(4) glucanase, β-1,3 glucanases, β-glucosidases, β-mannosidase, β-glucosidases, galactosidase, chitinases, polysaccharide lyase, endo β-1,6 galactanase and aldose epimerase. Secretomes produced on natural biomass displayed a comprehensive set of enzymes involved in hydrolysis and oxidation of cellulose, hemicellulose-pectin and lignin. The participation of oxidation reactions coupled to lignin decomposition in the breakdown of natural biomass may explain the discrepancy observed for cellulose decomposition in relation to natural biomass fermentation experiments.
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spelling Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomassBiomassCellulose degradationCellulose hydrolysisCellulose oxidationMyceliophthora thermophilaSecretome compositionBiomass is abundant, renewable and useful for biofuel production as well as chemical priming for plastics and composites. Deconstruction of biomass by enzymes is perceived as recalcitrant while an inclusive breakdown mechanism remains to be discovered. Fungi such as Myceliophthora thermophila M77 appear to decompose natural biomass sources quite well. This work reports on this fungus fermentation property while producing cellulolytic enzymes using natural biomass substrates. Little hydrolytic activity was detected, insufficient to explain the large amount of biomass depleted in the process. Furthermore, this work makes a comprehensive account of extracellular proteins and describes how secretomes redirect their qualitative protein content based on the nature and chemistry of the nutritional source. Fungus grown on purified cellulose or on natural biomass produced secretomes constituted by: cellobiohydrolases, cellobiose dehydrogenase, β-1,3 glucanase, β-glucosidases, aldose epimerase, glyoxal oxidase, GH74 xyloglucanase, galactosidase, aldolactonase and polysaccharide monooxygenases. Fungus grown on a mixture of purified hemicellulose fractions (xylans, arabinans and arabinoxylans) produced many enzymes, some of which are listed here: xylosidase, mixed β-1,3(4) glucanase, β-1,3 glucanases, β-glucosidases, β-mannosidase, β-glucosidases, galactosidase, chitinases, polysaccharide lyase, endo β-1,6 galactanase and aldose epimerase. Secretomes produced on natural biomass displayed a comprehensive set of enzymes involved in hydrolysis and oxidation of cellulose, hemicellulose-pectin and lignin. The participation of oxidation reactions coupled to lignin decomposition in the breakdown of natural biomass may explain the discrepancy observed for cellulose decomposition in relation to natural biomass fermentation experiments.Office of ScienceConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Instituto de F�sica de S�o Carlos Universidade de S�o PauloLaborat�rio de Microbiologia e Bioqu�mica Aplicada Departamento de Biologia IBILCE/UNESP, Rua Cristov�o Colombo, 2265 Bairro Jd. NazarethLaborat�rio Nacional de Ci�ncia e Tecnologia do Bioetanol, Rua Giuseppe M�ximo Scolfaro, 10.000, Bairro Guar�Laborat�rio de Enzimologia Instituto de Qu�mica UNESPDepartment of Microbiology and Molecular Genetics Oklahoma State UniversityDepartment of Biochemistry and Molecular Biology Oklahoma State UniversityLaborat�rio de Microbiologia e Bioqu�mica Aplicada Departamento de Biologia IBILCE/UNESP, Rua Cristov�o Colombo, 2265 Bairro Jd. NazarethLaborat�rio de Enzimologia Instituto de Qu�mica UNESPOffice of Science: 06103-OKLCNPq: 201319/2012-8Office of Science: 403090/2012-1Office of Science: ZDJ-7-77608-01Universidade de S�o PauloUniversidade Estadual Paulista (Unesp)Laborat�rio Nacional de Ci�ncia e Tecnologia do BioetanolOklahoma State Universitydos Santos, H�vila BrognaroBezerra, Tha�s Milena Souza [UNESP]Pradella, Jos� G. C.Delabona, PriscilaLima, DeiseGomes, Eleni [UNESP]Hartson, Steve D.Rogers, JanetCouger, BrianPrade, Rolf2018-12-11T17:07:28Z2018-12-11T17:07:28Z2016-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1186/s13568-016-0276-yAMB Express, v. 6, n. 1, 2016.2191-0855http://hdl.handle.net/11449/17372810.1186/s13568-016-0276-y2-s2.0-849943583832-s2.0-84994358383.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAMB Express0,574info:eu-repo/semantics/openAccess2023-10-13T06:10:35Zoai:repositorio.unesp.br:11449/173728Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-10-13T06:10:35Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
title Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
spellingShingle Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
dos Santos, H�vila Brognaro
Biomass
Cellulose degradation
Cellulose hydrolysis
Cellulose oxidation
Myceliophthora thermophila
Secretome composition
title_short Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
title_full Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
title_fullStr Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
title_full_unstemmed Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
title_sort Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass
author dos Santos, H�vila Brognaro
author_facet dos Santos, H�vila Brognaro
Bezerra, Tha�s Milena Souza [UNESP]
Pradella, Jos� G. C.
Delabona, Priscila
Lima, Deise
Gomes, Eleni [UNESP]
Hartson, Steve D.
Rogers, Janet
Couger, Brian
Prade, Rolf
author_role author
author2 Bezerra, Tha�s Milena Souza [UNESP]
Pradella, Jos� G. C.
Delabona, Priscila
Lima, Deise
Gomes, Eleni [UNESP]
Hartson, Steve D.
Rogers, Janet
Couger, Brian
Prade, Rolf
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de S�o Paulo
Universidade Estadual Paulista (Unesp)
Laborat�rio Nacional de Ci�ncia e Tecnologia do Bioetanol
Oklahoma State University
dc.contributor.author.fl_str_mv dos Santos, H�vila Brognaro
Bezerra, Tha�s Milena Souza [UNESP]
Pradella, Jos� G. C.
Delabona, Priscila
Lima, Deise
Gomes, Eleni [UNESP]
Hartson, Steve D.
Rogers, Janet
Couger, Brian
Prade, Rolf
dc.subject.por.fl_str_mv Biomass
Cellulose degradation
Cellulose hydrolysis
Cellulose oxidation
Myceliophthora thermophila
Secretome composition
topic Biomass
Cellulose degradation
Cellulose hydrolysis
Cellulose oxidation
Myceliophthora thermophila
Secretome composition
description Biomass is abundant, renewable and useful for biofuel production as well as chemical priming for plastics and composites. Deconstruction of biomass by enzymes is perceived as recalcitrant while an inclusive breakdown mechanism remains to be discovered. Fungi such as Myceliophthora thermophila M77 appear to decompose natural biomass sources quite well. This work reports on this fungus fermentation property while producing cellulolytic enzymes using natural biomass substrates. Little hydrolytic activity was detected, insufficient to explain the large amount of biomass depleted in the process. Furthermore, this work makes a comprehensive account of extracellular proteins and describes how secretomes redirect their qualitative protein content based on the nature and chemistry of the nutritional source. Fungus grown on purified cellulose or on natural biomass produced secretomes constituted by: cellobiohydrolases, cellobiose dehydrogenase, β-1,3 glucanase, β-glucosidases, aldose epimerase, glyoxal oxidase, GH74 xyloglucanase, galactosidase, aldolactonase and polysaccharide monooxygenases. Fungus grown on a mixture of purified hemicellulose fractions (xylans, arabinans and arabinoxylans) produced many enzymes, some of which are listed here: xylosidase, mixed β-1,3(4) glucanase, β-1,3 glucanases, β-glucosidases, β-mannosidase, β-glucosidases, galactosidase, chitinases, polysaccharide lyase, endo β-1,6 galactanase and aldose epimerase. Secretomes produced on natural biomass displayed a comprehensive set of enzymes involved in hydrolysis and oxidation of cellulose, hemicellulose-pectin and lignin. The participation of oxidation reactions coupled to lignin decomposition in the breakdown of natural biomass may explain the discrepancy observed for cellulose decomposition in relation to natural biomass fermentation experiments.
publishDate 2016
dc.date.none.fl_str_mv 2016-12-01
2018-12-11T17:07:28Z
2018-12-11T17:07:28Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1186/s13568-016-0276-y
AMB Express, v. 6, n. 1, 2016.
2191-0855
http://hdl.handle.net/11449/173728
10.1186/s13568-016-0276-y
2-s2.0-84994358383
2-s2.0-84994358383.pdf
url http://dx.doi.org/10.1186/s13568-016-0276-y
http://hdl.handle.net/11449/173728
identifier_str_mv AMB Express, v. 6, n. 1, 2016.
2191-0855
10.1186/s13568-016-0276-y
2-s2.0-84994358383
2-s2.0-84994358383.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv AMB Express
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dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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