A protease-resistant exo-polygalacturonase from Klebsiella sp Y1 with good activity and stability over a wide pH range in the digestive tract

文献类型： 外文期刊

第一作者： Yuan, Peng

作者： Yuan, Peng;Meng, Kun;Wang, Yaru;Luo, Huiying;Shi, Pengjun;Huang, Huoqing;Bai, Yingguo;Yang, Peilong;Yao, Bin

作者机构：

关键词： Exo-polygalacturonase;Klebsiella sp;Feed and food additive;PF00295 family

期刊名称：BIORESOURCE TECHNOLOGY （ 影响因子：9.642； 五年影响因子：9.237 ）

ISSN： 0960-8524

年卷期： 2012 年 123 卷

页码：

收录情况： SCI

摘要： Polygalacturonases are important feed and food additives. In the present study an exo-polygalacturonase gene (pgu B) was cloned from Klebsiella sp. Y1 CGMCC 4433 and expressed in Escherichia coli BL21 (DE3). pgu B encodes a 658-amino acid polypeptide belonging to Glycoside Hydrolase Family 28. The optimal pH and temperature of exo-PGU B activity were 6.0 and 40-50 degrees C, respectively. The enzyme exhibited >35% of maximum activity within the pH range of 2.0-12.0. Exo-PGU B or an exo-PGU B/ endo-polygalacturonase mixture reduced the viscosity of polygalacturonic acid (1.0%, w/v) by 15.6 and 39.4%, respectively. Under simulated alimentary tract conditions, exo-PGU B was very stable (>25% activity from pH 1.5 to 6.8) and active, releasing 53.7 and 109.6 mu g of galacturonic acid from 400 to 800 mu g of polygalacturonic acid, respectively. These properties make exo-PGU B a potentially valuable additive for applications in feed and food. (C) 2012 Elsevier Ltd. All rights reserved.

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