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

dc.contributor.authorBrenelli, Lívia B.
dc.contributor.authorPersinoti, Gabriela F.
dc.contributor.authorCairo, João Paulo L. Franco
dc.contributor.authorLiberato, Marcelo V.
dc.contributor.authorGonçalves, Thiago Augusto
dc.contributor.authorOtero, Igor V. R. [UNESP]
dc.contributor.authorMainardi, Pedro H. [UNESP]
dc.contributor.authorFelby, Claus
dc.contributor.authorSette, Lara D. [UNESP]
dc.contributor.authorSquina, Fabio M.
dc.contributor.institutionBrazilian Center for Research in Energy and Materials (CNPEM)
dc.contributor.institutionUniversidade de Sorocaba (UNISO)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionFaculty of Science
dc.date.accessioned2020-12-12T01:06:19Z
dc.date.available2020-12-12T01:06:19Z
dc.date.issued2019-12-01
dc.description.abstractThe 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.en
dc.description.affiliationBrazilian Biorenewables National Laboratory (LNBR) Brazilian Center for Research in Energy and Materials (CNPEM)
dc.description.affiliationPrograma de Processos Tecnológicos e Ambientais Universidade de Sorocaba (UNISO)
dc.description.affiliationUniversidade Estadual Paulista (UNESP) Instituto de Biociências
dc.description.affiliationDepartamento de Bioquímica e Biologia Tecidual Instituto de Biologia Universidade de Campinas (UNICAMP)
dc.description.affiliationUniversity of Copenhagen Faculty of Science Department of Geosciences and Natural Resource Management
dc.description.affiliationUnespUniversidade Estadual Paulista (UNESP) Instituto de Biociências
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdCNPq: 159488/2014-1
dc.identifierhttp://dx.doi.org/10.1038/s41598-019-53608-1
dc.identifier.citationScientific Reports, v. 9, n. 1, 2019.
dc.identifier.doi10.1038/s41598-019-53608-1
dc.identifier.issn2045-2322
dc.identifier.scopus2-s2.0-85075621665
dc.identifier.urihttp://hdl.handle.net/11449/198199
dc.language.isoeng
dc.relation.ispartofScientific Reports
dc.sourceScopus
dc.titleNovel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strainen
dc.typeArtigo
dspace.entity.typePublication
unesp.author.orcid0000-0002-0975-7283[2]
unesp.author.orcid0000-0002-5980-3786[9]

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