Improving the catalytic performance of Proteinase K from Parengyodontium album for use in feather degradation

文献类型： 外文期刊

第一作者： Ren, Yaxin

作者： Ren, Yaxin;Luo, Huiying;Huang, Huoqing;Wang, Yaru;Wang, Yuan;Su, Xiaoyun;Bai, Yingguo;Zhang, Jie;Yao, Bin;Tu, Tao;Ren, Yaxin;Wang, Guozeng;Hakulinen, Nina

作者机构：

关键词： Proteinase K; B-factor; Thermostability; Molecular modification; Feather degradation

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2020 年 154 卷

页码：

收录情况： SCI

摘要： Proteinase K (PROK) from Parengyodontium album hydrolyzes keratin, a major protein component of poultry feathers, which are an inexpensive and renewable protein resource. Based on structural studies for analysis of amino acid flexibility near the catalytic center, identification of highly conserved residues, and experimental screening, we obtained a mutant R218S with residual activity 1.6-fold higher than that of PROK after incubation at 60 degrees C for 1 h. Molecular dynamics simulation indicated that substitution of Arg218 with Ser leads to three hydrogen bonds being introduced into the structure, stabilizing the beta-sheet in which Ser218 is located, and thus improvement of thermostability. Additionally, the mutant R218S had a 15% increase in specific activity compared to PROK and improvement in the rate and thoroughness of feather degradation compared with PROK. We confirmed the positive effects of enhancing catalytic center rigidity on enzyme thermostability, a finding which may have broad applications. (C) 2019 Elsevier B.V. All rights reserved.

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