Cloning, Expression and Characterization of a Novel Cold-adapted -galactosidase from the Deep-sea Bacterium Alteromonas sp. ML52

文献类型： 外文期刊

第一作者： Sun, Jingjing

作者： Sun, Jingjing;Yao, Congyu;Wang, Wei;Liu, Junzhong;Dai, Fangqun;Hao, Jianhua;Sun, Jingjing;Wang, Wei;Liu, Junzhong;Dai, Fangqun;Hao, Jianhua;Yao, Congyu;Zhuang, Zhiwei;Hao, Jianhua

作者机构：

关键词： Alteromonas; deep sea; cold-adapted enzyme; -galactosidase; lactose-free milk

期刊名称：MARINE DRUGS （ 影响因子：5.118； 五年影响因子：5.951 ）

ISSN： 1660-3397

年卷期： 2018 年 16 卷 12 期

页码：

收录情况： SCI

摘要： The bacterium Alteromonas sp. ML52, isolated from deep-sea water, was found to synthesize an intracellular cold-adapted -galactosidase. A novel -galactosidase gene from strain ML52, encoding 1058 amino acids residues, was cloned and expressed in Escherichia coli. The enzyme belongs to glycoside hydrolase family 2 and is active as a homotetrameric protein. The recombinant enzyme had maximum activity at 35 degrees C and pH 8 with a low thermal stability over 30 degrees C. The enzyme also exhibited a K-m of 0.14 mM, a V-max of 464.7 U/mg and a k(cat) of 3688.1 S-1 at 35 degrees C with 2-nitrophenyl--d-galactopyranoside as a substrate. Hydrolysis of lactose assay, performed using milk, indicated that over 90% lactose in milk was hydrolyzed after incubation for 5 h at 25 degrees C or 24 h at 4 degrees C and 10 degrees C, respectively. These properties suggest that recombinant Alteromonas sp. ML52 -galactosidase is a potential biocatalyst for the lactose-reduced dairy industry.

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