Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Abstract Background To produce second-generation biofuels, enzymatic catalysis is required to convert cellulose from lignocellulosic biomass into fermentable sugars. β-Glucosidases finalize the process by hydrolyzing cellobiose into glucose, so the efficiency of cellulose hydrolysis largely depends...

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Bibliographic Details
Main Authors: Mu-Rong Kao, Hsion-Wen Kuo, Cheng-Chung Lee, Kuan-Ying Huang, Ting-Yen Huang, Chen-Wei Li, C. Will Chen, Andrew H. -J. Wang, Su-May Yu, Tuan-Hua David Ho
Format: Article
Language:English
Published: BMC 2019-11-01
Series:Biotechnology for Biofuels
Subjects:
Chaetomella raphigera
GH3
β-Glucosidase
Saccharification
O-Glycosylation
Lignocellulosic biomass
Online Access:http://link.springer.com/article/10.1186/s13068-019-1599-0

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http://link.springer.com/article/10.1186/s13068-019-1599-0

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