Characterization and Application of a New beta-Galactosidase Gal42 From Marine Bacterium Bacillus sp. BY02

文献类型： 外文期刊

第一作者： Zhou, Zihan

作者： Zhou, Zihan;He, Ningning;Han, Qi;Liu, Songshen;Xue, Ruikun;Li, Shangyong;Hao, Jianhua;Hao, Jianhua

作者机构：

关键词： beta-galactosidase; glycoside hydrolase family 42; Bacillus sp. BY02; lactose hydrolysis; zinc ion

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：6.064； 五年影响因子：6.843 ）

ISSN：

年卷期： 2021 年 12 卷

页码：

收录情况： SCI

摘要： beta-Galactosidase plays an important role in medicine and dairy industry. In this study, a new glycoside hydrolase family 42 (GH42) beta-galactosidase-encoding gene, gal42, was cloned from a newly isolated marine bacterium Bacillus sp. BY02 and expressed in Escherichia coli. Structural characterization indicated that the encoding beta-galactosidase, Gal42, is a homotrimer in solution, and homology modeling indicated that it retains the zinc binding sites of the Cys cluster. The reaction activity of Gal42 was significantly increased by Zn2+ (229.6%) and other divalent metal ions (Mn2+, Mg2+, and Co2+), while its activity was inhibited by EDTA (53.9%). Meanwhile, the thermo-stability of the Gal42 was also significantly enhanced by 5 and 10 mM of zinc ion supplement, which suggested that the "Cys-Zn" motif played important roles in both structural stability and catalytic function. Furthermore, Gal42 showed effective lactose hydrolysis activity, which makes the enzyme hydrolyze the lactose in milk effectively. These properties make Gal42 a potential candidate in food technology.

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