Molecular Characterization of a New Alkaline-Tolerant Xylanase from Humicola insolens Y1

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

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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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