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Improvement in the thermostability of chitosanase from Bacillus ehimensis by introducing artificial disulfide bonds

文献类型： 外文期刊

作者： Sheng, Jun 1 ; Ji, Xiaofeng 1 ; Zheng, Yuan 1 ; Wang, Zhipeng 1 ; Sun, Mi 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Lab Enzyme Engn, Qingdao 266071, Peoples R China

关键词： Bacillus ehimensis; Chitosanase; Disulfide bridge; Homology modeling; Kinetic parameters; Thermostability

期刊名称：BIOTECHNOLOGY LETTERS （ 2020影响因子：2.461； 五年影响因子：2.457 ）

ISSN： 0141-5492

年卷期： 2016 年 38 卷 10 期

页码：

收录情况： SCI

摘要： To determine the effects of artificial disulfide bridges on the thermostability and catalytic efficiency of chitosanase EAG1. Five artificial disulfide bridges were designed based on the structural information derived from the three-dimensional (3-D) model of chitosanase EAG1. Two beneficial mutants (G113C/D116C, A207C-L286C) were located in the flexible surface loop region, whereas the similar substitutions introduced in alpha-helices regions had a negligible effect. Mut5, the most active mutant, had a longer half-life at 50 A degrees C (from 10.5 to 69.3 min) and a 200 % higher catalytic efficiency (K (cat)/K (m)) than that of the original EAG1. The contribution of disulfide bridges to enzyme thermostability is mainly dependent on its location within the polypeptide chain. Strategical placement of a disulfide bridge in flexible regions provides a rigid support and creation of a protected microenvironment, which is effective in improving enzyme's thermostability and catalytic efficiency.

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