Cloning, characterization, and antifungal activity of an endo-1,3-beta-d-glucanase from Streptomyces sp S27

文献类型： 外文期刊

第一作者： Shi, Pengjun

作者： Shi, Pengjun;Yao, Guoyu;Yang, Peilong;Li, Ning;Luo, Huiying;Bai, Yingguo;Wang, Yaru;Yao, Bin;Yao, Guoyu

作者机构：

关键词： Streptomyces sp S27;Endo-1,3-beta-D-glucanase;Antifungal protein

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2010 年 85 卷 5 期

页码：

收录情况： SCI

摘要： An endo-1,3-beta-d-glucanase gene, designated as bglS27, was cloned from Streptomyces sp. S27 and successfully expressed in Escherichia coli BL21 (DE3). The full-length gene contains 1,362 bp and encodes a protein of 453 amino acids with a calculated molecular mass of 42.7 kDa. The encoded protein comprises a catalytic module of glycosyl hydrolase family 16, a short glycine linker region, and a family 13 carbohydrate-binding module. The purified recombinant enzyme (BglS27) showed optimal activity at 65A degrees C and pH 5.5 and preferentially catalyzed the hydrolysis of glucans with a beta-1,3-linkage using an endolytic mode of action. The specific activity and K (m) value of BglS27 for laminarin were 236.0 U mg(-1) and 1.89 mg ml(-1), respectively. In antifungal assay, BglS27 had the ability to inhibit the growth of phytopathogenic fungi Rhizoctonic solani and Fusarium oxysporum and some mycotoxin-producing fungi Fusarium crookwellense and Paecilomyces variotii. These favorable properties make BglS27 a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation.

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