Purification, gene cloning and characterization of an acidic beta-1,4-glucanase from Phialophora sp G5 with potential applications in the brewing and feed industries

文献类型： 外文期刊

第一作者： Zhao, Junqi

作者： Zhao, Junqi;Shi, Pengjun;Yuan, Tiezheng;Huang, Huoqing;Li, Zhongyuan;Meng, Kun;Yang, Peilong;Yao, Bin

作者机构：

关键词： Phialophora sp G5;beta-1,4-Glucanase;Purification;Gene cloning;Animal feed;Brewing

期刊名称：JOURNAL OF BIOSCIENCE AND BIOENGINEERING （ 影响因子：2.894； 五年影响因子：2.746 ）

ISSN： 1389-1723

年卷期： 2012 年 114 卷 4 期

页码：

收录情况： SCI

摘要： An extracellular beta-1,4-glucanase (CelG5, similar to 55.0 kDa) was isolated from the culture filtrate of Phialophora sp. G5, and its encoding gene was cloned. The deduced amino acid sequence of CelG5 was at most 73.6% and 44.0%, respectively, identical with a hypothetical protein from Sordaria macrospora and an experimentally verified GH 7 endo-beta-1,4-glucanase of Neurospora tetrasperma FGSC 2508. Native CelG5 had pH and temperature optima of pH 4.5-5.0 and 55-60 degrees C. The enzyme showed some properties superior than most fungal beta-1,4-glucanases, such as high activity over a wide pH range (exhibiting >50% of the maximum activity at pH 2.0-7.0), excellent stability in extreme acidic to alkaline conditions (pH 2.0-9.0), and strong resistance against pepsin and trypsin (retaining 89% and 94% activity, respectively). Recombinant CelG5 produced in Pichia pastoris had a molecular mass and a pH optimum similar to native CelG5, but with maximal activity at 65 degrees C. Application tests showed that native CelG5 was stable under simulated gastric conditions (retaining >70% activity), and had capacity to decrease the viscosity of barley-bean feed (8.9% by 200 U CelG5) and mash (6.1% by 50 U CelG5) and increase the filtration rate of mash (18.4% by 50 U CelG5). These properties make CelG5 a good candidate for utilization in the animal feed and brewing industries. (c) 2012, The Society for Biotechnology, Japan. All rights reserved.

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