Cloning and Functional Expression of an α-Galactosidase from Yersinia pestis biovar Microtus str. 91001

Yanan CAO; Huoqing HUANG; Kun MENG; Peilong YANG; Pengjun SHI; Yaru WANG; Huiying LUO; Zhifang ZHANG; Ningfeng WU; Bin YAO

doi:10.1271/bbb.80145

Biochemistry & Molecular Biology Notes

Cloning and Functional Expression of an α-Galactosidase from Yersinia pestis biovar Microtus str. 91001

Yanan CAO, Huoqing HUANG, Kun MENG, Peilong YANG, Pengjun SHI, Yaru WANG, Huiying LUO, Zhifang ZHANG, Ningfeng WU, Bin YAO

Author information

Yanan CAO
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Huoqing HUANG
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Kun MENG
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Peilong YANG
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Pengjun SHI
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Yaru WANG
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Huiying LUO
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences
Zhifang ZHANG
Biotechnology Research Institute, Chinese Academy of Agricultural Sciences
Ningfeng WU
Biotechnology Research Institute, Chinese Academy of Agricultural Sciences
Bin YAO
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences

Keywords: α-galactosidase, glycoside hydrolase, Yersinia pestis biovar Microtus str. 91001, characterization

JOURNAL FREE ACCESS

2008 Volume 72 Issue 8 Pages 2203-2205

DOI https://doi.org/10.1271/bbb.80145

View "Advance Publication" version (August 7, 2008).

Details

Abstract

A gene encoding a glycoside hydrolase (GH) family 36 α-galactosidase was cloned from Yersinia pestis biovar Microtus str. 91001 and expressed in Escherichia coli. The purified recombinant α-galactosidase (Aga-Y) was optimally active at 37 °C and pH 6.8. The features of temperature profile, thermoliability, kinetics, and amino acid composition indicated that Aga-Y had properties of a cold-adapted enzyme.

Corresponding author

Register with J-STAGE for free!