Secretory expression of organophosphorus hydrolase OPHC2 in Yarrowia lipolytica Polg
2015
Li, Meng | Yu, Xiaolan | Wang, Fei | Zhai, Chao | Shen, Wei | Yu, Xianhong | Wang, Xiaojuan | Ma, Lixin
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.
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