Biochemical characterization of a novel thermophilic alpha-galactosidase from Talaromyces leycettanus JCM12802 with significant transglycosylation activity
文献类型: 外文期刊
第一作者: Wang, Caihong
作者: Wang, Caihong;Wang, Huimin;Ma, Rui;Shi, Pengjun;Niu, Canfang;Luo, Huiying;Yang, Peilong;Yao, Bin;Ma, Rui;Yang, Peilong
作者机构:
关键词: Talaromyces leycettanus JCM12802;alpha-Galactosidase;Thermophilic;Transglycosylation;Galactose tolerance
期刊名称:JOURNAL OF BIOSCIENCE AND BIOENGINEERING ( 影响因子:2.894; 五年影响因子:2.746 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: Thermophilic alpha-galactosidases have great potentials in biotechnological and medicinal applications due to their high temperature activity and specific stability. In this study, a novel alpha-galactosidase gene of glycoside hydrolase family 27 (aga27A) was cloned from Talaromyces leycettanus JCM12802 and successfully expressed in Pichia pastoris GS115. Purified recombinant Aga27A (rAga27A) was thermophilic and thermotolerant, exhibiting the maximum activity at 70 degrees C and retaining stability at 65 degrees C. Like most fungal alpha-galactosidases, rAga27A had an acidic pH optimum (pH 4.0) but retained stability over a boarder pH range (pH 3.0-11.0) at 70 degrees C. Moreover, the enzyme exhibited strong resistance to most metal ions and chemicals tested (except for Ag+ and SDS) and great tolerance to galactose (19 mM). The preferable transglycosylation capacity of rAga27A with various substrates further widens its application spectrum. Thus rAga27A with excellent enzymatic properties will be ideal for applications in various industries, especially for the synthesis of galactooligosaccharides. (C) 2015, The Society for Biotechnology, Japan. All rights reserved.
分类号: Q5`Q81`TS26
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