文献类型: 外文期刊
第一作者: Zhang, Fan
作者: Zhang, Fan;Shi, Pengjun;Bai, Yingguo;Luo, Huiying;Yuan, Tiezheng;Huang, Huoqing;Yang, Peilong;Yao, Bin;Zhang, Fan;Miao, Lihong
作者机构:
关键词: Phialophora sp G5;Xylanase;Thermostability;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: 2011 年 89 卷 6 期
页码:
收录情况: SCI
摘要: An endo-beta-1,4-xylanase gene, designated xyn10G5, was cloned from Phialophora sp. G5 and expressed in Pichia pastoris. The 1,197-bp full-length gene encodes a polypeptide of 399 amino acids consisting of a putative signal peptide at residues 1-20, a family 10 glycoside hydrolase domain, a short Gly/Thr-rich linker and a family 1 carbohydrate-binding module (CBM). The deduced amino acid sequence of XYN10G5 shares the highest identity (53.4%) with a putative xylanase precursor from Aspergillus terreus NIH2624. The purified recombinant XYN10G5 exhibited the optimal activity at pH 4.0 and 70 degrees C, remained stable at pH 3.0-9.0 (>70% of the maximal activity), and was highly thermostable at 70 degrees C (retaining similar to 90% of the initial activity for 1 h). Substrate specificity studies have shown that XYN10G5 had the highest activity on soluble wheat arabinoxylan (350.6 U mg(-1)), and moderate activity to various heteroxylans, and low activity on different types of cellulosic substrates. Under simulated gastric conditions, XYN10G5 was stable and released more reducing sugars from soluble wheat arabinoxylan; when combined with a glucanase (CelA4), the viscosity of barley-soybean feed was significantly reduced. These favorable enzymatic properties make XYN10G5 a good candidate for application in the animal feed industry.
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