Molecular Cloning and Expression of a Novel beta-Glucosidase Gene from Phialophora sp G5

文献类型： 外文期刊

第一作者： Li, Xuejun

作者： Li, Xuejun;Zhao, Junqi;Shi, Pengjun;Yang, Peilong;Wang, Yaru;Luo, Huiying;Yao, Bin;Li, Xuejun

作者机构：

关键词： Phialophora sp G5;Aryl beta-glucosidase;Pichia pastoris;Heterologous expression

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

ISSN： 0273-2289

年卷期： 2013 年 169 卷 3 期

页码：

收录情况： SCI

摘要： A novel beta-glucosidase gene, bgl1G5, was cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. Sequence analysis indicated that the gene consists of a 1,431-bp open reading frame encoding a protein of 476 amino acids. The deduced amino acid sequence of bgl1G5 showed a high identity of 85 % with a characterized beta-glucosidase from Humicola grisea of glycoside hydrolase family 1. Compared with other fungal counterparts, Bgl1G5 showed similar optimal activity at pH 6.0 and 50 A degrees C and was stable at pH 5.0-9.0. Moreover, Bgl1G5 exhibited good thermostability at 50 A degrees C (6 h half-life) and higher specific activity (54.9 U mg(-1)). The K (m) and V (max) values towards p-nitrophenyl beta-d-glucopyranoside (pNPG) were 0.33 mM and 103.1 mu mol min(-1) mg(-1), respectively. The substrate specificity assay showed that Bgl1G5 was highly active against pNPG, weak on p-nitrophenyl beta-d-cellobioside (pNPC) and p-nitrophenyl-beta-d-galactopyranoside (ONPG), and had no activity on cellobiose. This result indicated Bgl1G5 was a typical aryl beta-glucosidase.

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