A novel family 9 beta-1,3(4)-glucanase from thermoacidophilic Alicyclobacillus sp A4 with potential applications in the brewing industry

文献类型： 外文期刊

第一作者： Bai, Yingguo

作者： Bai, Yingguo;Wang, Jianshe;Shi, Pengjun;Luo, Huiying;Huang, Huoqing;Luo, Chunliang;Yao, Bin;Zhang, Zhifang

作者机构：

关键词： beta-1,3(4)-glucanase;Alicyclobacillus sp.;Malting and brewing;Glycoside hydrolase family 9

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 87 卷 1 期

页码：

收录情况： SCI

摘要： An endo-beta-1,3(4)-glucanase gene, Agl9A, was cloned from Alicyclobacillus sp. A4 and expressed in Pichia pastoris. Its deduced amino acid sequence shared the highest identity (48%) with an endo-beta-1,4-glucansae from Alicyclobacillus acidocaldarius that belongs to family 9 of the glycoside hydrolases. The purified recombinant Agl9A exhibited relatively wide substrate specificity, including lichenan (109%), barley beta-glucan (100%), CMC-Na (15.02%), and laminarin (6.19%). The optimal conditions for Agl9A activity were pH 5.8 and 55A degrees C. The enzyme was stable over a broad pH range (> 60% activity retained after 1-h incubation at pH 3.8-11.2) and at 60A degrees C (> 70% activity retained after 1-h incubation). Agl9A was highly resistant to various neutral proteases (e.g., trypsin, alpha-chymotrypsin, and collagenase) and Neutrase 0.8L (Novozymes), a protease widely added to the mash. Under simulated mashing conditions, addition of Agl9A (20 U/ml) or a commercial xylanase (200 U/ml) reduced the filtration rate (26.71% and 20.21%, respectively) and viscosity (6.12% and 4.78%, respectively); furthermore, combined use of Agl9A (10 U/ml) and the xylanase (100 U/ml) even more effectively reduced the filtration rate (31.73%) and viscosity (8.79%). These characteristics indicate that Agl9A is a good candidate to improve glucan degradation in the malting and brewing industry.

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