A thermophilic endo-1,4-beta-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials

文献类型： 外文期刊

第一作者： Wang, Kun

作者： Wang, Kun;Luo, Huiying;Bai, Yingguo;Shi, Pengjun;Huang, Huoqing;Xue, Xianli;Yao, Bin

作者机构：

关键词： Talaromyces emersonii;Endo-1,4-beta-glucanase;Thermophilic;Broad substrate specificity

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2014 年 98 卷 16 期

页码：

收录情况： SCI

摘要： Thermophilic cellulases are of significant interest to the efficient conversion of plant cell wall polysaccharides into simple sugars. In this study, a thermophilic and thermostable endo-1,4-beta-glucanase, TeEgl5A, was identified in the thermophilic fungus Talaromyces emersonii CBS394.64 and functionally expressed in Pichia pastoris. Purified recombinant TeEgl5A exhibits optimal activity at pH 4.5 and 90 A degrees C. It is highly stable at 70 A degrees C and over a broad pH range of 1.0-10.0, and shows strong resistance to most metal ions, sodium dodecyl sulfate (SDS), and proteases. TeEgl5A has broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds (barley beta-glucan, laminarin, lichenan, CMC-Na, carob bean gum, and birchwood xylan). Under simulated mashing conditions, addition of 60 U TeEgl5A reduced more viscosity (10.0 vs.7.6 %) than 80 U of Ultraflo XL from Novozymes. These properties make TeEgl5A a good candidate for extensive application in the detergent, textile, feed, and food industries.

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