A thermophilic alpha-galactosidase from Neosartorya fischeri P1 with high specific activity, broad substrate specificity and significant hydrolysis ability of soymilk

文献类型: 外文期刊

第一作者: Wang, Huimin

作者: Wang, Huimin;Shi, Pengjun;Luo, Huiying;Huang, Huoqing;Yang, Peilong;Yao, Bin

作者机构:

关键词: Neosartorya fischeri;alpha-Galactosidase;Thermophilic;Broad substrate specificity

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: 2014 年 153 卷

页码:

收录情况: SCI

摘要: An extracellular alpha-galactosidase (Gal27A) with high specific activity of 423 U mg (1) was identified in thermophilic Neosartorya fischeri P1. Its coding gene (1680 bp) was cloned and functionally expressed in Pichia pastoris. Sequence analysis indicated that deduced Gal27A contains a catalytic domain of glycoside hydrolase family 27. The native and recombinant enzymes shared some similar properties, such as pH optima at 4.5, temperature optima at 60-70 degrees C, resistance to most chemicals and saccharides, and great abilities to degrade raffinose and stachyose in soymilk. Considering the high yield (3.1 g L (1)) in P. pastoris, recombinant rGal27A is more favorable for industrial applications. This is the first report on purification and gene cloning of Neosartorya alpha-galactosidase. (C) 2013 Elsevier Ltd. All rights reserved.

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