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AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
BACKGROUND: Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktail...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6420742/ https://www.ncbi.nlm.nih.gov/pubmed/30923563 http://dx.doi.org/10.1186/s13068-019-1394-y |
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author | Filiatrault-Chastel, Camille Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy |
author_facet | Filiatrault-Chastel, Camille Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy |
author_sort | Filiatrault-Chastel, Camille |
collection | PubMed |
description | BACKGROUND: Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. RESULTS: In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. CONCLUSIONS: Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-019-1394-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6420742 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-64207422019-03-28 AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes Filiatrault-Chastel, Camille Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy Biotechnol Biofuels Research BACKGROUND: Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. RESULTS: In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. CONCLUSIONS: Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-019-1394-y) contains supplementary material, which is available to authorized users. BioMed Central 2019-03-16 /pmc/articles/PMC6420742/ /pubmed/30923563 http://dx.doi.org/10.1186/s13068-019-1394-y Text en © The Author(s) 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Filiatrault-Chastel, Camille Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title | AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title_full | AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title_fullStr | AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title_full_unstemmed | AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title_short | AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
title_sort | aa16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6420742/ https://www.ncbi.nlm.nih.gov/pubmed/30923563 http://dx.doi.org/10.1186/s13068-019-1394-y |
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