Secretory expression of organophosphorus hydrolase OPHC2 in Yarrowia lipolytica Polg.
In the present study, recombinant organophosphorus hydrolase OPHC2 was successfully produced by Yarrowia lipolytica and purified. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western blot analyses showed a major polypeptide band of 36 kDa. The purified enzyme was optimally active at 65°C and pH 8.5 and also displayed good thermal and pH stability using methyl parathion (O,O-dimethyl-O-4-p-nitrophenyl phosphorothioate) as a substrate. Moreover, as Y. lipolytica is a non-pathogenic, generally regarded as safe (GRAS) yeast, the cell culture supernatant can be used directly on vegetables and fruits that are contaminated by organophosphorus pesticides.
a Hubei Collaborative Innovation Center for Green Transformation of Bio-resources, Hubei Key Laboratory of Industrial Biotechnology, College of Life Sciences, Hubei University , Wuhan , Hubei Province , P. R. China.
Meng
M
Li
Xiaolan
X
Yu
Fei
F
Wang
Chao
C
Zhai
Wei
W
Shen
Xianhong
X
Yu
Xiaojuan
X
Wang
Lixin
L
Ma
D043303:Aryldialkylphosphatase / Q000235:genetics* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D052918:Environmental Restoration and Remediation; D008743:Methyl Parathion / Q000378:metabolism*; D025062:Yarrowia / Q000201:enzymology* / Q000235:genetics*
D008743:Methyl Parathion; D043303:Aryldialkylphosphatase
GRAS; Yarrowia lipolytica; organophosphorus hydrolase; organophosphorus pesticide