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Molecular cloning and expression of a novel β-galactosidase from Bacillus coagulans
Author(s): 
Pages: 35-39
Year: Issue:  6
Journal: Journal of Nanjing Forestry University(Natural Science Edition)

Keyword:  Bacillus coagulansβ-galactosidaseexpression and purificationlactose hydrolysis;
Abstract: A novelβ-galactosidase gene was cloned from Bacillus coagulans NL01 which had ability to hydrolyze lactose into glucose and galactose in this study. The length of the β-galactosidase gene was 1 998 bp, and its coding sequence showed very low identity with other reported β-galactosidase. The gene was cloned into pETDuet-1 and expressed in Escherichia coli BL21( DE3) . The crude enzyme activity was 119.0 μmol/( min·mg) , and the purified enzyme activity was 666.4 μmol/( min·mg) after Ni-NTA purification. It was indicated from the analysis results of the hydrolysis prod?uct obtained by the purified β-galactosidase that this novel β-galactosidase presented high activity toward lactose con?version into glucose and galactose.
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