Gene Cloning, Overexpression, and Characterization of a Xylanase from Penicillium sp CGMCC 1669

文献类型： 外文期刊

第一作者： Liu, Wanli

作者： Liu, Wanli;Shi, Pengjun;Yang, Peilong;Wang, Guozeng;Wang, Yaru;Luo, Huiying;Yao, Bin;Liu, Wanli;Chen, Qiang

作者机构：

关键词： Xylanase;Penicillium sp F63 CGMCC 1669;Pichia pastoris;Overexpression

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

ISSN： 0273-2289

年卷期： 2010 年 162 卷 1 期

页码：

收录情况： SCI

摘要： A xylanase-encoding gene, xyn11F63, was isolated from Penicillium sp. F63 CGMCC1669 using degenerated polymerase chain reaction (PCR) and thermal asymmetric interlaced (TAIL)-PCR techniques. The full-length chromosomal gene consists of 724 bp, including a 73-bp intron, and encodes a 217 amino acid polypeptide. The deduced amino acid sequence of xyn11F63 shows the highest identity of 70% to the xylanase from Penicillium sp. strain 40, which belongs to glycosyl hydrolases family 11. The gene was overexpressed in Pichia pastoris, and its activity in the culture medium reached 516 U ml(-1). After purification to electrophoretic homogeneity, the enzyme showed maximal activity at pH 4.5 and 40A degrees C, was stable at acidic buffers of pH 4.5-9.0, and was resistant to proteases (proteinase K, trypsin, subtilisin A, and alpha-chymotrypsin). The specific activity, K (m), and V (max) for oat spelt xylan substrate was 7,988 U mg(-1), 22.2 mg ml(-1), and 15,105.7 mu mol min(-1) mg(-1), respectively. These properties make XYN11F63 a potential economical candidate for use in feed and food industrial applications.

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