Expression and characterization of a cold-active and xylose-stimulated beta-glucosidase from Marinomonas MWYL1 in Escherichia coli
文献类型： 外文期刊
作者： Zhao, Wei 1 ; Peng, Rihe 1 ; Xiong, Aisheng 1 ; Fu, Xiaoyan 1 ; Tian, Yongsheng 1 ; Yao, Quanhong 1 ;
作者机构： 1.Shanghai Acad Agr Sci, Biotechnol Res Inst, Shanghai 201106, Peoples R China
关键词： β-Glucosidase;Glycoside hydrolase family 1;Marinomonas MWYL1;Cold-active;Xylose-stimulated
期刊名称：MOLECULAR BIOLOGY REPORTS （ 影响因子：2.316； 五年影响因子：2.357 ）
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年卷期：
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收录情况： SCI
摘要： The gene encoding a cold-active and xylose-stimulated beta-glucosidase of Marinomonas MWYL1 was synthesized and expressed in Escherichia coli. The recombinant enzyme (reBglM1) was purified and characterized. The molecular mass of the purified reBglM1 determined by SDS-PAGE agree with the calculated values (50.6 Da). Optima of temperature and pH for enzyme activity were 40 degrees C and 7.0, respectively. The enzyme exhibited about 20% activity at 5 degrees C and was stable over the range of pH 5.5-10.0. The presence of xylose significantly enhanced enzyme activity even at higher concentrations up to 600 mM, with maximal stimulatory effect (about 1.45-fold) around 300 mM. The enzyme is active with both glucosides and galactosides and showed high catalytic efficiency (k(cat) = 500.5 s(-1)) for oNPGlc. These characterizations enable the enzyme to be a promising candidate for industrial applications.
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