An acidic beta-mannanase from Penicillium sp C6: gene cloning and over-expression in Pichia pastoris

文献类型： 外文期刊

第一作者： Yao, Bin

作者： Yao, Bin;Cai, Hongying;Shi, Pengjun;Huang, Huoqing;Luo, Huiying;Bai, Yingguo;Yang, Peilong;Meng, Kun;Yao, Bin

作者机构：

关键词： Penicillium sp C6;beta-Mannanase;Pichia pastoris;Over-expression

期刊名称：WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.312； 五年影响因子：3.58 ）

ISSN： 0959-3993

年卷期： 2011 年 27 卷 12 期

页码：

收录情况： SCI

摘要： Using degenerate polymerase chain reaction (PCR), thermal asymmetric interlaced (TAIL)-PCR, and reverse transcription (RT)-PCR techniques, a new beta-mannanase gene, denoted as man5C6, was obtained from Penicillium sp. C6. The gene has an open reading frame of 1,155 bp, and codes for a polypeptide (Man5C6) of 384 amino acids including a putative 26-residue signal peptide. The deduced amino acid sequence showed highest identity (59.2%) with an experimentally verified beta-mannanase from Podospora anserine belonging to glycoside hydrolase family 5. Man5C6 was successfully expressed in Pichia pastoris, and secreted up to 2.5 g in 1 l medium. Recombinant Man5C6 was easily purified to electrophoretic homogeneity by a sing-step chromatography. The purified recombinant enzyme exhibited optimal activity at pH 4.5, and remained > 55% of its maximum activity at pH 3.0-7.0. The temperature optimum was found to be 70A degrees C. The specific activity, and K (m) and V (max) values were 226.5 U mg(-1), 12.3 mg ml(-1) and 2,400.2 mu mol min(-1) mg(-1), respectively, for locust bean gum, and 78.7 U mg(-1), 0.2 mg ml(-1) and 894.6 mu mol min(-1) mg(-1), respectively, for konjac flour. These properties make Man5C6 a potential candidate for high-level production of beta-mannanase with low cost and simple processing technology.

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