Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 beta-xylosidase: Activity and instability at high neutral salt concentrations

文献类型： 外文期刊

第一作者： Zhang, Rui

作者： Zhang, Rui;Li, Na;Liu, Yu;Han, Xiaowei;Shen, Jidong;Xu, Shujing;Wu, Qian;Zhou, Junpei;Huang, Zunxi;Zhang, Rui;Li, Na;Liu, Yu;Han, Xiaowei;Shen, Jidong;Xu, Shujing;Wu, Qian;Zhou, Junpei;Huang, Zunxi;Zhang, Rui;Li, Na;Liu, Yu;Han, Xiaowei;Shen, Jidong;Wu, Qian;Zhou, Junpei;Huang, Zunxi;Tu, Tao

作者机构：

关键词： beta-Xylosidase; Activity; Stability; Low temperature; Salt; Crystal structure; Glycoside hydrolase

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2019 年 301 卷

页码：

收录情况： SCI

摘要： beta-Xylosidase, of the glycoside hydrolase family 43 from Bacillus sp. HJ14, was expressed in Escherichia coli. Recombinant beta-xylosidase (rHJ14GH43) exhibited maximum activity at 25 degrees C, approximately 15, 45, and 88% of maximum activity at 0, 10, and 20 degrees C, respectively, and poor stability at temperatures over 20 degrees C. rHJ14GH43 showed moderate or high activity, but poor stability, in NaCl, KCl, NaNO3, KNO3, Na2SO4, and (NH4)(2)SO4 at concentrations from 3.0 to 30.0% (w/v). The crystal structure of rHJ14GH43 was resolved and showed higher structural flexibility due to fewer salt bridges and hydrogen bonds compared to mesophilic and thermophilic beta-xylosidases. High structural flexibility is presumed to be a key factor for catalytic adaptations to low temperatures and high salt concentrations. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments.

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