Improvement of the catalytic performance of a hyperthermostable GH10 xylanase from Talaromyces leycettanus JCM12802
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- 作者：Xiaoyu Wanga ; b ; 1 ; Huoqing Huanga ; 1 ; Xiangming Xieb ; Rui Maa ; Yingguo Baia ; Fei Zhenga ; b ; Shuai Youa ; Bingyu Zhanga ; Huifang Xiea ; Bin Yaoa ; Huiying Luoa ; luohuiying@caas.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Talaromyces leycettanus ; Glycoside hydrolase family 10 (GH10) ; Xylanase ; Hyperthermostable ; Catalysis improvement
- 刊名：Bioresource Technology
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：222
- 期：Complete
- 页码：277-284
- 全文大小：1857 K
文摘
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An acidic thermostable xylanase of GH10 (TlXyn10A) was identified in T.leycettanus.
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Sequence analysis revealed seven residues probably involved in substrate contacting.
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Mutant TlXyn10A_P with modifications at subsites +2 to +4 showed improved properties.
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TlXyn10_P in combination with cellulase released the most reducing sugar form wheat straw.