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

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 degr...

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Autores principales: Brenelli, Lívia B., Persinoti, Gabriela F., Cairo, João Paulo L. Franco, Liberato, Marcelo V., Gonçalves, Thiago Augusto, Otero, Igor V. R., Mainardi, Pedro H., Felby, Claus, Sette, Lara D., Squina, Fabio M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6879535/
https://www.ncbi.nlm.nih.gov/pubmed/31772294
http://dx.doi.org/10.1038/s41598-019-53608-1
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author Brenelli, Lívia B.
Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R.
Mainardi, Pedro H.
Felby, Claus
Sette, Lara D.
Squina, Fabio M.
author_facet Brenelli, Lívia B.
Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R.
Mainardi, Pedro H.
Felby, Claus
Sette, Lara D.
Squina, Fabio M.
author_sort Brenelli, Lívia B.
collection PubMed
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.
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spelling pubmed-68795352019-12-05 Novel redox-active enzymes for ligninolytic applications revealed from multiomics analyses of Peniophora sp. CBMAI 1063, a laccase hyper-producer strain Brenelli, Lívia B. Persinoti, Gabriela F. Cairo, João Paulo L. Franco Liberato, Marcelo V. Gonçalves, Thiago Augusto Otero, Igor V. R. Mainardi, Pedro H. Felby, Claus Sette, Lara D. Squina, Fabio M. Sci Rep Article 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. Nature Publishing Group UK 2019-11-26 /pmc/articles/PMC6879535/ /pubmed/31772294 http://dx.doi.org/10.1038/s41598-019-53608-1 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Brenelli, Lívia B.
Persinoti, Gabriela F.
Cairo, João Paulo L. Franco
Liberato, Marcelo V.
Gonçalves, Thiago Augusto
Otero, Igor V. R.
Mainardi, Pedro H.
Felby, Claus
Sette, Lara D.
Squina, Fabio M.
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
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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6879535/
https://www.ncbi.nlm.nih.gov/pubmed/31772294
http://dx.doi.org/10.1038/s41598-019-53608-1
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