Heterogenous Gene Expression of Methyl Parathion Hydrolase and Analysis of the Enzyme Activity
- VernacularTitle:甲基对硫磷水解酶基因的高效表达及酶活性分析
- Author:
Lu-Lu LIU
;
Ya-Feng ZHOU
;
Zhi-Ping ZHANG
;
Hong LIU
;
Xian-En ZHANG
;
- Publication Type:Journal Article
- Keywords:
Organophosphorus degrading enzyme, Thioredoxin, Fusion expression
- From:
Microbiology
1992;0(06):-
- CountryChina
- Language:Chinese
-
Abstract:
Methyl parathion hydrolase (MPH, E.C.3.1.8.1) coding gene mph from Pseudomonas sp. WBC-3, isolated and identified by our lab, was successfully expressed in E. coli AD494 (DE3)/ pET32a(+) system as soluble fusion form at high level. The recombinant MPH showed nearly 4～5 fold higher specific activity to parathion than the enzyme from Pseudomonas sp. WBC-3. In addition, the thermal stability of the recombinant enzyme was improved comparing with the wild type enzyme.
