Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain

Detalhes bibliográficos
Autor(a) principal: Brenelli, Lívia B.
Data de Publicação: 2019
Outros Autores: Persinoti, Gabriela F., Cairo, João Paulo L. Franco, Liberato, Marcelo V., Gonçalves, Thiago Augusto, Otero, Igor V. R. [UNESP], Mainardi, Pedro H. [UNESP], Felby, Claus, Sette, Lara D. [UNESP], Squina, Fabio M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1038/s41598-019-53608-1
http://hdl.handle.net/11449/198199
Resumo: The repertoire of redox-active enzymes produced by the marine fungus Peniophora sp. CBMAI 1063, a laccase hyper-producer strain, was characterized by omics analyses. The genome revealed 309 Carbohydrate-Active Enzymes (CAZymes) genes, including 48 predicted genes related to the modification and degradation of lignin, whith 303 being transcribed under cultivation in optimized saline conditions for laccase production. The secretome confirmed that the fungus can produce a versatile ligninolytic enzyme cocktail. It secretes 56 CAZymes, including 11 oxidative enzymes classified as members of auxiliary activity families (AAs), comprising two laccases, Pnh_Lac1 and Pnh_Lac2, the first is the major secretory protein of the fungi. The Pnh_Lac1-mediator system was able to promote the depolymerization of lignin fragments and polymeric lignin removal from pretreated sugarcane bagasse, confirming viability of this fungus enzymatic system for lignocellulose-based bioproducts applications.
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spelling Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strainThe repertoire of redox-active enzymes produced by the marine fungus Peniophora sp. CBMAI 1063, a laccase hyper-producer strain, was characterized by omics analyses. The genome revealed 309 Carbohydrate-Active Enzymes (CAZymes) genes, including 48 predicted genes related to the modification and degradation of lignin, whith 303 being transcribed under cultivation in optimized saline conditions for laccase production. The secretome confirmed that the fungus can produce a versatile ligninolytic enzyme cocktail. It secretes 56 CAZymes, including 11 oxidative enzymes classified as members of auxiliary activity families (AAs), comprising two laccases, Pnh_Lac1 and Pnh_Lac2, the first is the major secretory protein of the fungi. The Pnh_Lac1-mediator system was able to promote the depolymerization of lignin fragments and polymeric lignin removal from pretreated sugarcane bagasse, confirming viability of this fungus enzymatic system for lignocellulose-based bioproducts applications.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Brazilian Biorenewables National Laboratory (LNBR) Brazilian Center for Research in Energy and Materials (CNPEM)Programa de Processos Tecnológicos e Ambientais Universidade de Sorocaba (UNISO)Universidade Estadual Paulista (UNESP) Instituto de BiociênciasDepartamento de Bioquímica e Biologia Tecidual Instituto de Biologia Universidade de Campinas (UNICAMP)University of Copenhagen Faculty of Science Department of Geosciences and Natural Resource ManagementUniversidade Estadual Paulista (UNESP) Instituto de BiociênciasCNPq: 159488/2014-1Brazilian Center for Research in Energy and Materials (CNPEM)Universidade de Sorocaba (UNISO)Universidade Estadual Paulista (Unesp)Universidade Estadual de Campinas (UNICAMP)Faculty of ScienceBrenelli, Lívia B.Persinoti, Gabriela F.Cairo, João Paulo L. FrancoLiberato, Marcelo V.Gonçalves, Thiago AugustoOtero, Igor V. R. [UNESP]Mainardi, Pedro H. [UNESP]Felby, ClausSette, Lara D. [UNESP]Squina, Fabio M.2020-12-12T01:06:19Z2020-12-12T01:06:19Z2019-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1038/s41598-019-53608-1Scientific Reports, v. 9, n. 1, 2019.2045-2322http://hdl.handle.net/11449/19819910.1038/s41598-019-53608-12-s2.0-85075621665Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reportsinfo:eu-repo/semantics/openAccess2021-10-23T09:55:28Zoai:repositorio.unesp.br:11449/198199Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T09:55:28Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
title Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
spellingShingle Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
Brenelli, Lívia B.
title_short Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
title_full Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
title_fullStr Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
title_full_unstemmed Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
title_sort Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
author Brenelli, Lívia B.
author_facet Brenelli, Lívia B.
Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R. [UNESP]
Mainardi, Pedro H. [UNESP]
Felby, Claus
Sette, Lara D. [UNESP]
Squina, Fabio M.
author_role author
author2 Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R. [UNESP]
Mainardi, Pedro H. [UNESP]
Felby, Claus
Sette, Lara D. [UNESP]
Squina, Fabio M.
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Brazilian Center for Research in Energy and Materials (CNPEM)
Universidade de Sorocaba (UNISO)
Universidade Estadual Paulista (Unesp)
Universidade Estadual de Campinas (UNICAMP)
Faculty of Science
dc.contributor.author.fl_str_mv Brenelli, Lívia B.
Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R. [UNESP]
Mainardi, Pedro H. [UNESP]
Felby, Claus
Sette, Lara D. [UNESP]
Squina, Fabio M.
description The repertoire of redox-active enzymes produced by the marine fungus Peniophora sp. CBMAI 1063, a laccase hyper-producer strain, was characterized by omics analyses. The genome revealed 309 Carbohydrate-Active Enzymes (CAZymes) genes, including 48 predicted genes related to the modification and degradation of lignin, whith 303 being transcribed under cultivation in optimized saline conditions for laccase production. The secretome confirmed that the fungus can produce a versatile ligninolytic enzyme cocktail. It secretes 56 CAZymes, including 11 oxidative enzymes classified as members of auxiliary activity families (AAs), comprising two laccases, Pnh_Lac1 and Pnh_Lac2, the first is the major secretory protein of the fungi. The Pnh_Lac1-mediator system was able to promote the depolymerization of lignin fragments and polymeric lignin removal from pretreated sugarcane bagasse, confirming viability of this fungus enzymatic system for lignocellulose-based bioproducts applications.
publishDate 2019
dc.date.none.fl_str_mv 2019-12-01
2020-12-12T01:06:19Z
2020-12-12T01:06:19Z
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/10.1038/s41598-019-53608-1
Scientific Reports, v. 9, n. 1, 2019.
2045-2322
http://hdl.handle.net/11449/198199
10.1038/s41598-019-53608-1
2-s2.0-85075621665
url http://dx.doi.org/10.1038/s41598-019-53608-1
http://hdl.handle.net/11449/198199
identifier_str_mv Scientific Reports, v. 9, n. 1, 2019.
2045-2322
10.1038/s41598-019-53608-1
2-s2.0-85075621665
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Scientific Reports
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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
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repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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