An alpha-galactosidase from an acidophilic Bispora sp MEY-1 strain acts synergistically with beta-mannanase

文献类型： 外文期刊

第一作者： Wang, Hui

作者： Wang, Hui;Luo, Huiying;Bai, Yingguo;Huang, Huoging;Shi, Pengjun;Yao, Bin;Li, Jiang;Fan, Yunliu

作者机构：

关键词： Acidophilic alpha-galactosidase;Bispora sp MEY-1;Synergistic enzyme action

期刊名称：BIORESOURCE TECHNOLOGY （ 影响因子：9.642； 五年影响因子：9.237 ）

ISSN： 0960-8524

年卷期： 2010 年 101 卷 21 期

页码：

收录情况： SCI

摘要： An alpha-galactosidase gene (AgalB) was cloned from the acidophilic fungus Bispora sp. MEY-1 and expressed in Pichia pastoris. The deduced amino acid sequence showed highest identity (35%) to the alpha-galactosidase from Penicillium simplicissimum, belonging to the glycosyl hydrolase family 27. The purified recombinant alpha-galactosidase (r-AgalB) exhibited optimal activity at pH 3.5 and 55 degrees C, was stable at pH 2.2-8.0, and showed higher hydrolytic activity towards galactomannan polysaccharides (guar gum and locust bean gum) than toward small galacto-oligosaccharides (melibiose, raffinose and stachyose). A synergistic (3-fold) increase in guar gum hydrolysis was observed when beta-mannanase Man5A from Bispora sp. MEY-1 and r-AgalB were combined. Further, an increase in the reaction time from 5 h to 12 h or increase of the temperature from 37 degrees C to 55 degrees C enhanced guar gum degradation by the enzyme combination. These properties make r-AgalB a good candidate for extensive application in the pulp/paper, food, and feed industries. (C) 2010 Elsevier Ltd. All rights reserved.

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