A novel GH1 β-glucosidase from an Arctic bacterium: Characterization and secretory expression in Bacillus subtilis

文献类型： 外文期刊

第一作者： Sun, Jingjing

作者： Sun, Jingjing;Wang, Wei;Hao, Jianhua;Sun, Jingjing;Wang, Wei;Hao, Jianhua

作者机构：

关键词： Glycoside hydrolase; Devosia; Complex cellulases; Signal peptide; Secretory expression

期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：4.4； 五年影响因子：4.2 ）

ISSN： 1359-5113

年卷期： 2024 年 140 卷

页码：

收录情况： SCI

摘要： beta-Glucosidases are widely applied to biofuel production, food industry, and improvement in flavors. The novel beta-glucosidase gene debgl was identified from the Arctic bacterium Devosia sp. Arc12 and expressed in Escherichia coli BL21 (DE3). The putative gene, belonging to the glycoside hydrolase family 1, consists of 1311 nucleotides and encodes 437 amino acid residues. The optimal temperature and pH of the recombinant DeBgl were 55 degrees C and 7, respectively. The recombinant DeBgl displayed salt and ethanol tolerance, and the V-max, K-m, and k(cat) for the substrate cellobiose were 754 mu mol min(-1) mg(-1), 12.8 mM, and 661.4 s(-1), respectively. The concentration of glucose was reached 51.6 g L-1 after incubation at 40 degrees C for 8 h in 100 g L-1 cellobiose solution. It suggests that the recombinant DeBgl is a good candidate enzyme to degrade complex celluloses. The signal peptide (SP) citH has been proven to be the most suitable for the secretory expression of beta-glucosidase by screening the signal peptide library in Bacillus subtilis. The secretory activity of the SP citH fused DeBgl in the vector pMA5 was 9-fold higher than that of the DeBgl without signal peptide. This secretory expression system of beta-glucosidase may benefit its industrial application.

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