Improvement on Thermostability of Pectate Lyase and Its Potential Application to Ramie Degumming

文献类型： 外文期刊

第一作者： Xu, Huan

作者： Xu, Huan;Feng, Xiangyuan;Yang, Qi;Zheng, Ke;Yi, Le;Duan, Shengwen;Cheng, Lifeng

作者机构：

关键词： Dickeya dadantii DCE-01; pectate lyase; ramie; degumming; site-directed mutation; thermostability

期刊名称：POLYMERS （ 影响因子：4.967； 五年影响因子：5.063 ）

ISSN：

年卷期： 2022 年 14 卷 14 期

页码：

收录情况： SCI

摘要： In order to obtain a thermostable pectate lyase for ramie degumming, a rational design based on structural analysis was carried out on a novel pectate lyase (Pel419) derived from the Dickeya Dadantii DCE-01 for high-efficiency ramie degumming. A total of five potential amino acid sites were chosen to replace residues. Then, the mutant enzymes were subjected to the heterologous expressions in Escherichia coli and their enzymatic characteristics were determined. The optimal reaction temperature for the five mutants kept consistent with that for the wild type. The enzyme activity and thermal stability of mutant V52A were significantly improved. Meanwhile, the weight loss rate obtained by V52A with the best enzymatic characteristics in the ramie degumming process at 50 degrees C is comparable with that obtained by commercial cotton-ramie processing pectinases, indicating that V52A was a potential industrial enzyme that could be applied to large-scale ramie degumming. In this study, the biological functions of conservative residues of Pel419 were preliminarily explored. The mutant V52A with both enzymatic activity and improved heat resistance was acquired, providing a superior material for developing enzyme preparations of ramie degumming, and rendering an effective method for the rational design aiming to improve the thermostability of pectate lyase.

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