Characterization of a novel cold-adapted GH1 β-glucosidase from Psychrobacillus glaciei and its application in the hydrolysis of soybean isoflavone glycosides

文献类型： 外文期刊

第一作者： He, Jinjian

作者： He, Jinjian;Duan, Jiajing;Li, Yuying;Wang, Mansheng;Chen, Zishu;Shi, Pengjun;Yu, Pinglian;He, Jinjian;Duan, Jiajing;Zhang, Xiu

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关键词： Psychrobacillus glaciei; beta-Glucosidase; Cold adaptation; Sugar tolerance; Catalytic efficiency; Isoflavone glycosides

期刊名称：CURRENT RESEARCH IN FOOD SCIENCE （ 影响因子：6.2； 五年影响因子：6.2 ）

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年卷期： 2024 年 8 卷

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收录情况： SCI

摘要： The novel beta-glucosidase gene ( pgbgl1 ) of glycoside hydrolase (GH) family 1 from the psychrotrophic bacterium Psychrobacillus glaciei sp. PB01 was successfully expressed in Escherichia coli BL21 (DE3). The deduced PgBgl1 contained 447 amino acid residues with a calculated molecular mass of 51.4 kDa. PgBgl1 showed its maximum activity at pH 7.0 and 40 degrees C, and still retained over 10% activity at 0 degrees C, suggesting that the recombinant PgBgl1 is a cold -adapted enzyme. The substrate specificity, K m , V max , and K cat / K m for the p -Nitrophenyl-beta-D-glucopyr- anoside ( p NPG) as the substrate were 1063.89 U/mg, 0.36 mM, 1208.31 U/mg and 3871.92/s, respectively. Furthermore, PgBgl1 demonstrated remarkable stimulation of monosaccharides such as glucose, xylose, and galactose, as well as NaCl. PgBgl1 also demonstrated a high capacity to convert the primary soybean isoflavone glycosides (daidzin, genistin, and glycitin) into their respective aglycones. Overall, PgBgl1 exhibited high catalytic activity towards aryl glycosides, suggesting promising application prospects in the food, animal feed, and pharmaceutical industries.

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