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A New beta-Galactosidase from the Antarctic Bacterium Alteromonas sp. ANT48 and Its Potential in Formation of Prebiotic Galacto-Oligosaccharides

文献类型： 外文期刊

作者： Li, Shangyong 1 ; Zhu, Xiangjie 2 ; Xing, Mengxin 2 ;

作者机构： 1.Qingdao Univ, Sch Basic Med, Dept Pharmacol, Qingdao 266071, Shandong, Peoples R China

2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Shandong, Peoples R China

关键词： beta-galactosidase; galactooligosaccharides; daily industry

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

ISSN：

年卷期： 2019 年 17 卷 11 期

页码：

收录情况： SCI

摘要： As an important medical enzyme, beta-galactosidases catalyze transgalactosylation to form prebiotic Galacto-Oligosaccharides (GOS) that assist in improving the effect of intestinal flora on human health. In this study, a new glycoside hydrolase family 2 (GH2) beta-galactosidase-encoding gene, galA, was cloned from the Antarctic bacterium Alteromonas sp. ANT48 and expressed in Escherichia coli. The recombinant beta-galactosidase GalA was optimal at pH 7.0 and stable at pH 6.6-7.0, which are conditions suitable for the dairy environment. Meanwhile, GalA showed most activity at 50 degrees C and retained more than 80% of its initial activity below 40 degrees C, which makes this enzyme stable in normal conditions. Molecular docking with lactose suggested that GalA could efficiently recognize and catalyze lactose substrates. Furthermore, GalA efficiently catalyzed lactose degradation and transgalactosylation of GOS in milk. A total of 90.6% of the lactose in milk could be hydrolyzed within 15 min at 40 degrees C, and the GOS yield reached 30.9%. These properties make GalA a good candidate for further applications.

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