Improved thermal performance of Thermomyces lanuginosus GH11 xylanase by engineering of an N-terminal disulfide bridge

文献类型： 外文期刊

第一作者： Wang, Yawei

作者： Wang, Yawei;Fu, Zheng;Xiong, Hairong;Wang, Yawei;Fu, Zheng;Huang, Huoqing;Yao, Bin;Zhang, Huashan;Turunen, Ossi

作者机构：

关键词： Disulfide bridge;GH11 xylanase;Protein engineering;Thermomyces lanuginosus DSM10635;Thermostability

期刊名称：BIORESOURCE TECHNOLOGY （ 影响因子：9.642； 五年影响因子：9.237 ）

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收录情况： SCI

摘要： In order to increase the stability of thermophilic. Thermomyces lanuginosus GH11 xylanase, TLX, a disulfide bridge Q1C-Q24C was introduced into the N-terminal region of the enzyme. The apparent temperature optimum shifted upwards at pH 6.5 by about 10. °C to 75. °C. The resistance to thermal inactivation also increased by about 10. °C. The melting temperature measured by CD spectroscopy increased from 66 to 74. °C. Therefore the N-terminal disulfide bridge increased both kinetic and thermodynamic stability almost equally. At pH 8 and 70. °C, the disulfide bridge increased the enzyme half-life 20-fold in the presence of substrate. In contrast to the situation in acidic-neutral pH, the substrate decreased the thermostability of xylanases in alkaline pH. The upper limit for the performance of the disulfide bridge mutant at pH 9 was 75. °C. This study showed that N-terminal disulfide bridges can stabilize even thermostable family GH11 xylanases.

分类号： Q

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