Contribution of a family 1 carbohydrate-binding module in thermostable glycoside hydrolase 10 xylanase from Talaromyces cellulolyticus toward synergistic enzymatic hydrolysis of lignocellulose
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- 作者：Hiroyuki Inoue ; Seiichiro Kishishita ; Akio Kumagai…
- 关键词：Enzymatic hydrolysis ; GH10 xylanase ; Cellulase ; Family 1 carbohydrate ; binding module ; Lignocellulosic biomass ; Rice straw ; Talaromyces cellulolyticus
- 刊名：Biotechnology for Biofuels
- 出版年：2015
- 出版时间：December 2015
- 年：2015
- 卷：8
- 期：1
- 全文大小：1,147 KB
- 刊物类别：Chemistry and Materials Science
- 刊物主题：Biotechnology
Plant Breeding/Biotechnology
Renewable and Green Energy
Environmental Engineering/Biotechnology - 出版者：BioMed Central
- ISSN：1754-6834
文摘
Background Enzymatic removal of hemicellulose components such as xylan is an important factor for maintaining high glucose conversion from lignocelluloses subjected to low-severity pretreatment. Supplementation of xylanase in the cellulase mixture enhances glucose release from pretreated lignocellulose. Filamentous fungi produce multiple xylanases in their cellulase system, and some of them have modular structures consisting of a catalytic domain and a family 1 carbohydrate-binding module (CBM1). However, the role of CBM1 in xylanase in the synergistic hydrolysis of lignocellulose has not been investigated in depth.