A Novel beta-mannanase with High Specific Activity from Bacillus circulans CGMCC1554: Gene Cloning, Expression and Enzymatic Characterization

文献类型： 外文期刊

第一作者： Yang, Peilong

作者： Yang, Peilong;Li, Yanan;Wang, Yaru;Meng, Kun;Luo, Huiying;Yuan, Tiezheng;Bai, Yingguo;Yao, Bin;Li, Yanan;Zhan, Zhichun

作者机构：

关键词： beta-Mannanase;Bacillus circulans;Expression;Characterization;High specific activity

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： 2009 年 159 卷 1 期

页码：

收录情况： SCI

摘要： A DNA fragment of 2,042 bp containing a novel beta-mannanase gene, man5A, was identified from the genome of the mannan-degrading bacterium Bacillus circulans CGMCC1554. The open reading frame of man5A comprised 978 bp encoding a protein of 326 amino acids with a predicted molecular weight of 32 kDa. The amino acid sequence of the encoded mannanase, MAN5A, showed the highest identity (78.5%) to beta-mannanases belonging to glycosyl hydrolases family 5. The gene man5A was efficiently expressed in Escherichia coli and Pichia pastoris with the highest activity of 541 U/ml in a 3-L fermenter. Recombinant MAN5A purified from E. coli had a high specific activity of 4,839 U/mg, which is much higher than that of enzymes that showed high sequence identity. The enzyme showed maximum activity at pH 7.6 and 60 A degrees C and resistance to trypsin. After hydrolysis of LBG, oligomannosides accounted for 76% of the hydrolysis products. All these properties collectively make MAN5A a better candidate than current mannanases for use in the food and feed industry.

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