An Acidophilic beta-Galactosidase from Bispora sp MEY-1 with High Lactose Hydrolytic Activity under Simulated Gastric Conditions

文献类型： 外文期刊

第一作者： Wang, Hui

作者： Wang, Hui;Luo, Huiying;Bai, Yingguo;Wang, Yaru;Yang, Peilong;Shi, Pengjun;Yao, Bin;Zhang, Wei;Fan, Yunliu

作者机构：

关键词： Acidophilic;Bispora sp MEY-1;beta-galactosidase;simulated gastric fluid

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2009 年 57 卷 12 期

页码：

收录情况： SCI

摘要： BgalA, a full-length gene (3,009 bp) that encodes a beta-galactosidase, was cloned from the meso-acidophilic fungus Bispora sp. MEY-1 and expressed in Pichia pastoris. The deduced amino acid sequence of BgalA shares highest identity (55.5%) with the beta-galactosidase from Aspergillus phoenicis, which belongs to the glycoside hydrolyase family 35. Purified recombinant BgalA is acidophilic, exhibiting maximum activity at pH 1.5, which is lower than that reported for other beta-galactosidases. The enzyme has high pH and thermal stability and is resistant to proteases and cations found in milk. The K-m and V-max of BgalA for 2-nitrophenyl-beta-D-galactopyranoside and lactose are 5.22 mM and 120.8 mu mol/(min.mg), and 0.31 mM and 137.3 mu mol/(min.mg), respectively. Under simulated gastric conditions, BgalA has greater stability (similar to 100%) and hydrolysis ratio (>80%) toward milk lactose than the commercially available beta-galactosidase from Aspergillus oryzae (ATCC 20423). Thus, BgalA may be a better digestive supplement for alleviating symptoms associated with lactase deficiency.

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