Shimazu Mark, Nguyen Anne, Mulchandani Ashok, Chen Wilfred
Department of Chemical and Environmental Engineering, University of California, Riverside, California 92521, USA.
Biotechnol Prog. 2003 Sep-Oct;19(5):1612-4. doi: 10.1021/bp0340640.
A surface anchor system derived from the ice-nucleation protein (INP) from Pseudomonas syringe was used to localize organophosphorus hydrolase (OPH) onto the surface of Pseudomonas putida KT2440. Cells harboring the shuttle vector pPNCO33 coding for the INP-OPH fusion were capable of targeting OPH onto the cell surface as demonstrated by whole cell ELISA. The whole cell activity of P. putida KT2440 was shown to be 10 times higher than those of previous efforts expressing the same fusion protein in Escherichia coli. The capability of expressing enzymes on the surface of a robust and environmentally benign P. putida KT2440 should open up new avenues for a wide range of applications such as in situ bioremediation.
一种源自丁香假单胞菌冰核蛋白（INP）的表面锚定系统被用于将有机磷水解酶（OPH）定位到恶臭假单胞菌KT2440的表面。携带编码INP-OPH融合蛋白的穿梭载体pPNCO33的细胞能够将OPH靶向到细胞表面，全细胞酶联免疫吸附测定（ELISA）证明了这一点。恶臭假单胞菌KT2440的全细胞活性比之前在大肠杆菌中表达相同融合蛋白的研究高出10倍。在健壮且环境友好的恶臭假单胞菌KT2440表面表达酶的能力应为原位生物修复等广泛应用开辟新途径。
