Improvement of GH10 family xylanase thermostability by introducing of an extra alpha-helix at the C-terminal

文献类型： 外文期刊

第一作者： Li, Guangqi

作者： Li, Guangqi;Chen, Xiaojuan;Huang, Rong;Li, Lingbo;Miao, Youzhi;Liu, Dongyang;Zhang, Ruifu;Li, Guangqi;Zhang, Ruifu;Zhou, Xuan

作者机构：

关键词： GH10 family xylanase; Thermostability; Poly-threonine; Enzyme engineering

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

ISSN： 0006-291X

年卷期： 2019 年 515 卷 3 期

页码：

收录情况： SCI

摘要： Xylanase is an important enzyme in industrial applications, which usually require the enzyme to maintain activity in high-temperature condition. In this study, a GH10 family xylanase XynAFO from a thermophilic composting fungus, Aspergillus fumigatus Z5, was investigated to determine its thermostable mechanism. XynAFO showed excellent thermostability, which could maintain 50% relative activity after incubation for 1 h at 70 degrees C. The homologous modeling structure of XynAFO was constructed and an alpha-helix composed of poly-threonine has been found in the linker region between the catalytic domain and the carbohydrate-binding module domain. Both the molecular dynamics simulation and the biochemical experiments proved that the alpha-helix plays an important role in the thermostability of XynAFO. Introducing of this poly-threonine region to the C-terminus of another GH10 family xylanase improved its thermostability. Our results indicated that the poly-threonine alpha-helix at the C-terminus of the catalytic domain was important for improving the thermophilic of GH10 family xylanases, which provides a new strategy for the thermostability modification of xylanases. (C) 2019 Elsevier Inc. All rights reserved.

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