Two neutral thermostable cellulases from Phialophora sp G5 act synergistically in the hydrolysis of filter paper
文献类型: 外文期刊
第一作者: Zhao, Junqi
作者: Zhao, Junqi;Shi, Pengjun;Li, Zhongyuan;Yang, Peilong;Luo, Huiying;Bai, Yingguo;Wang, Yaru;Yao, Bin
作者机构:
关键词: Phialophora sp G5;Thermostability;Cellobiohydrolase;Endoglucanase;Synergism
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 121 卷
页码:
收录情况: SCI
摘要: Two novel cellulase genes, cbh6A and egGH45, were cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. The putative polypeptide of CBH6A consists of a family 1 CBM and a catalytic domain of glycosyl hydrolase family 6 cellobiohydrolases, while deduced EgGH45 only contains a catalytic domain of family 45 endoglucanases. CBH6A and EgGH45 were optimally active at pH 7.0 and 65 degrees C, and pH 6.0 and 60 degrees C, respectively. Both enzymes exhibited high activities and stabilities over a wide pH range and had good thermostability at 70 degrees C. CBH6A and EgGH45 had significant resistance to SOS (10 mM), remaining 35% and 54% activities, respectively. These enzymes had synergic effect on the hydrolysis of filter paper, showing the highest efficiency in the ratio of CBH6A to EgGH45 at 80:20. The properties make this enzyme combination potential for application in textile and detergents industries. (C) 2012 Elsevier Ltd. All rights reserved.
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