Cloning and functional expression of an alpha-galactosidase from Yersinia pestis biovar Microtus str. 91001.
A gene encoding a glycoside hydrolase (GH) family 36 alpha-galactosidase was cloned from Yersinia pestis biovar Microtus str. 91001 and expressed in Escherichia coli. The purified recombinant alpha-galactosidase (Aga-Y) was optimally active at 37 degrees 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.
Cao
Yanan
Y
Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, PR China.
Huang
Huoqing
H
Meng
Kun
K
Yang
Peilong
P
Shi
Pengjun
P
Wang
Yaru
Y
Luo
Huiying
H
Zhang
Zhifang
Z
Wu
Ningfeng
N
Yao
Bin
B
D003001:Cloning, Molecular; D004795:Enzyme Stability; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature; D015010:Yersinia pestis / Q000201:enzymology* / Q000235:genetics; D000519:alpha-Galactosidase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D011994:Recombinant Proteins; D000519:alpha-Galactosidase