文献类型： 外文期刊
第一作者： Shi, Pengjun
作者： Shi, Pengjun;Du, Yanlong;Yang, Hong;Huang, Huoqing;Wang, Yaru;Yao, Bin;Zhang, Xiu
作者机构：
期刊名称：BIOMED RESEARCH INTERNATIONAL （ 影响因子：3.411； 五年影响因子：3.62 ）
ISSN： 2314-6133
年卷期： 2015 年
页码：
收录情况： SCI
摘要： An endo-1,4-beta-xylanase-encoding gene, xyn11B, was cloned fromthe thermophilic fungus Humicola insolensY1. The gene encodes a multimodular xylanase that consists of a typical hydrophobic signal sequence, a catalytic domain of glycoside hydrolase (GH) family 11, a glycine-rich linker, and a family 1 carbohydrate binding module (CBM1). Deduced Xyn11B shares the highest identity of 74% with a putative xylanase from Podospora anserina S mat+. Recombinant Xyn11B was successfully expressed in Pichia pastoris and purified to electrophoretic homogeneity. Xyn11B had a high specific activity of 382.0 U mg(-1) towards beechwood xylan and showed optimal activity at pH 6.0 and 50 degrees C. Distinct from most reported acidic fungal xylanases, Xyn11B was alkaline-tolerant, retaining 30.7% of the maximal activity at pH 9.0. The K-m and K-max values for beechwood xylanwere 2.2 mg mL(-1) and 462.8 mu mol min(-1) mg(-1), respectively. The enzyme exhibited a wider substrate specificity and produced a mixture of xylooligosaccharides. All these favorable enzymatic properties make Xyn11B attractive for potential applications in various industries.
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