A Novel GH7 Endo-beta-1,4-Glucanase from Neosartorya fischeri P1 with Good Thermostability, Broad Substrate Specificity and Potential Application in the Brewing Industry

文献类型： 外文期刊

第一作者： Liu, Yun

作者： Liu, Yun;Xie, Xiangming;Liu, Yun;Shi, Pengjun;Ma, Rui;Luo, Huiying;Bai, Yingguo;Yao, Bin;Dun, Baoqing

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 9 期

页码：

收录情况： SCI

摘要： An endo-beta-1,4-glucanase gene, cel7A, was cloned from the thermophilic cellulase-producing fungus Neosartorya fischeri P1 and expressed in Pichia pastoris. The 1,410-bp fulllength gene encodes a polypeptide of 469 amino acids consisting of a putative signal peptide at residues 1-20, a catalytic domain of glycoside hydrolase family 7 (GH7), a short Thr/Ser-rich linker and a family 1 carbohydrate-binding module (CBM 1). The purified recombinant Cel7A had pH and temperature optima of pH 5.0 and 60 degrees C, respectively, and showed broad pH adaptability (pH 3.0-6.0) and excellent stability at pH3.0-8.0 and 60 degrees C. Belonging to the group of nonspecific endoglucanases, Cel7A exhibited the highest activity on barley beta-glucan (2020 +/- 9 Umg(-1)), moderate on lichenan and CMC-Na, and weak on laminarin, locust bean galactomannan, Avicel, and filter paper. Under simulated mashing conditions, addition of Cel7A (99 mu g) reduced the mash viscosity by 9.1% and filtration time by 24.6%. These favorable enzymatic properties make Cel7A as a good candidate for applications in the brewing industry.

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