Overexpression and characterization of a novel endo-beta-1,3(4)-glucanase from thermophilic fungus Humicola insolens Y1

文献类型： 外文期刊

第一作者： Li, Jinyang

作者： Li, Jinyang;Xu, Xinxin;Liu, Bo;Zhang, Yuhong;Zhang, Wei;Shi, Pengjun

作者机构：

关键词： Humicola insolens Y1;beta-1,3(4)-Glucanase;Glycosyl hydrolase family 16

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

ISSN： 1046-5928

年卷期： 2017 年 138 卷

页码：

收录情况： SCI

摘要： A novel endo-beta-1,3(4)-glucanase gene, cel16A, was cloned from the fungus Humicola insolens Y1. The 988-bp full-length gene encoded a 286-residue polypeptide consisting of a putative signal peptide of 20 residues and a catalytic domain belonging to glycosyl hydrolase family 16. It was successfully overexpressed in Pichia pastoris GS115. The purified recombinant Cel16A exhibited highest specific activity toward barley beta-glucan, followed by lichenan and laminarin, but not toward CMC-Na, birchwood xylan, Avicel and filter paper, indicating that Cel16A is an endo-beta-1,3(4)-glucanases. Recombinant Cel16A had a pH optimum at 5.5 and a temperature optimum at 55 degrees C with a specific activity of 693 U/mg toward barley beta-glucan. It exhibited good stability over pH 5.0-9.0 and at temperatures up to 50 degrees C, retaining over 80% maximum activity. The K-m and V-max values of Cel16A for barley beta-glucan were 0.91 mg ml(-1) and 1530 mol min(-1).mg(-1), respectively. All these favorable enzymatic properties of Cel16A make it a good candidate for applications in various industries. (C) 2017 Elsevier Inc. All rights reserved.

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