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Fungal glycosyl hydrolases for sustainable plant biomass valorization: Talaromyces amestolkiae as a model fungus

期刊

INTERNATIONAL MICROBIOLOGY
卷 24, 期 4, 页码 545-558

出版社

SPRINGER
DOI: 10.1007/s10123-021-00202-z

关键词

Ascomycete; Cellulases; Xylanases; Bioethanol; Bioactive compounds

资金

  1. SusPlast-CSIC Interdisciplinary Platform

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Fungi play a crucial role in nature by secreting enzymes to degrade plant biomass, mobilizing organic carbon fixed by photosynthesis. Biotechnology can utilize lignocellulosic biomass and fungal enzymes to sustainably produce consumer goods. This study focuses on enzymes secreted by the filamentous ascomycete Talaromyces amestolkiae and their applications in biotechnology.
As the main decomposers and recyclers in nature, fungi secrete complex mixtures of extracellular enzymes for degradation of plant biomass, which is essential for mobilization of the organic carbon fixed by the photosynthesis in vegetal cells. Biotechnology can emulate the closed natural biological cycles, using lignocellulosic biomass as a renewable resource and lignocellulolytic fungal enzymes as catalysts to sustainably produce consumer goods. Cellulose and hemicellulose are the major polysaccharides on Earth, and the main enzymes involved in their hydrolytic depolymerization are cellulases (endoglucanases, cellobiohydrolases, and beta-glucosidases) and hemicellulases (mainly endoxylanases and beta-xylosidases). This work will focus on the enzymes secreted by the filamentous ascomycete Talaromyces amestolkiae and on some of their biotechnological applications. Their excellent hydrolytic activity was demonstrated by the partial degradation of xylans to prebiotic oligosaccharides by the endoxylanase XynN, or by the saccharification of lignocellulosic wastes to monosaccharides (fermentable to ethanol) either by the whole secretomes or by isolated enzymes used as supplements of commercial cocktails. However, apart from their expected hydrolytic activity, some of the beta-glycosidases produced by this strain catalyze the transfer of a sugar molecule to specific aglycons by transglycosylation. As the synthesis of customized glycoconjugates is a major goal for biocatalysis, mutant variants of the beta-xyloxidase BxTW1 and the ss-glucosidases BGL-1 and BGL-2 were obtained by directed mutagenesis, substantially improving the regioselective production yields of bioactive glycosides since they showed reduced or null hydrolytic activity.

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