Characterization of salt-adapted secreted lignocellulolytic enzymes from the mangrove fungus Pestalotiopsis sp
Yonathan Arfi (),
Didier Chevret,
Bernard Henrissat,
Jean-Guy Berrin,
Anthony Levasseur and
Eric Record
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Yonathan Arfi: INRA, UMR1163—Biotechnologie des Champignons Filamenteux, ESIL-Polytech, Aix-Marseille University
Didier Chevret: INRA, UMR1319 Micalis, Plateforme d’Analyse Protéomique de Paris Sud-Ouest
Bernard Henrissat: CNRS, UMR6098 Architecture et Fonction des Macromolécules Biologiques
Jean-Guy Berrin: INRA, UMR1163—Biotechnologie des Champignons Filamenteux, ESIL-Polytech, Aix-Marseille University
Anthony Levasseur: INRA, UMR1163—Biotechnologie des Champignons Filamenteux, ESIL-Polytech, Aix-Marseille University
Eric Record: INRA, UMR1163—Biotechnologie des Champignons Filamenteux, ESIL-Polytech, Aix-Marseille University
Nature Communications, 2013, vol. 4, issue 1, 1-9
Abstract:
Abstract Fungi are important for biomass degradation processes in mangrove forests. Given the presence of sea water in these ecosystems, mangrove fungi are adapted to high salinity. Here we isolate Pestalotiopsis sp. NCi6, a halotolerant and lignocellulolytic mangrove fungus of the order Xylariales. We study its lignocellulolytic enzymes and analyse the effects of salinity on its secretomes. De novo transcriptome sequencing and assembly indicate that this fungus possesses of over 400 putative lignocellulolytic enzymes, including a large fraction involved in lignin degradation. Proteomic analyses of the secretomes suggest that the presence of salt modifies lignocellulolytic enzyme composition, with an increase in the secretion of xylanases and cellulases and a decrease in the production of oxidases. As a result, cellulose and hemicellulose hydrolysis is enhanced but lignin breakdown is reduced. This study highlights the adaptation to salt of mangrove fungi and their potential for biotechnological applications.
Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2850
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DOI: 10.1038/ncomms2850
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