Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , , |
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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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 |
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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1799965576316059648 |