A Neutral Thermostable beta-1,4-Glucanase from Humicola insolens Y1 with Potential for Applications in Various Industries

文献类型： 外文期刊

第一作者： Xu, Xinxin

作者： Xu, Xinxin;Li, Jinyang;Zhang, Wei;Liu, Bo;Zhang, Yuhong;Zhang, Zhifang;Fan, Yunliu;Huang, Huoqing;Shi, Pengjun;Luo, Huiying;Yao, Bin

作者机构：

期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）

ISSN： 1932-6203

年卷期： 2015 年 10 卷 4 期

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收录情况： SCI

摘要： We cloned a new glycoside hydrolase family 6 gene, Hicel6C, from the thermophilic fungus Humicola insolens Y1 and expressed it in Pichia pastoris. Using barley beta-glucan as a substrate, recombinant HiCel6C protein exhibited neutral pH (6.5) and high temperature (70 degrees C) optima. Distinct from most reported acidic fungal endo-beta-1,4-glucanases, HiCel6C was alkali- tolerant, retaining greater than 98.0, 61.2, and 27.6% of peak activity at pH 8.0, 9.0, and 10.0, respectively, and exhibited good stability over a wide pH range (pH 5.0-11.0) and at temperatures up to 60 degrees C. The Km and V-max values of HiCel6C for barley beta-glucan were 1.29 mg/mL and 752 mu mol/min.mg, respectively. HiCel6C was strictly specific for the beta-1,4-glucoside linkage exhibiting activity toward barley beta-glucan, lichenan, and carboxy methylcellulose sodium salt (CMC-Na), but not toward laminarin (1,3-beta-glucan). HiCel6C cleaved the internal glycosidic linkages of cellooligosaccharides randomly and thus represents an endo-cleaving enzyme. The predominant product of polysaccharide hydrolysis by HiCel6C was cellobiose, suggesting that it functions by an endo-processive mechanism. The favorable properties of HiCel6C make it a good candidate for basic research and for applications in the textile and brewing industries.

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