Development of a whole-cell biocatalyst/biosensor by display of multiple heterologous proteins on the escherichia coli cell surface for the detoxification and detection of organophosphates

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[1] Liu, Ruihua
[2] Yang, Chao
[3] Xu, Yingming
[4] Xu, Ping
[5] Jiang, Hong
[6] Qiao, Chuanling
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Xu, P. (pingxu@sjtu.edu.cn) | 1600年 / American Chemical Society卷 / 61期
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This paper reports the codisplay of organophosphorus hydrolase (OPH) and methyl parathion hydrolase (MPH)-green fluorescent protein (GFP) fusion on the cell surface of Escherichia coli using the truncated ice nucleation protein (INPNC) and Lpp-OmpA as the anchoring motifs. The surface localization of both OPH and MPH-GFP was demonstrated by cell fractionation; Western blot analysis; protease accessibility experiment; and immunofluorescence microscopy. Anchorage of the foreign proteins on the outer membrane neither inhibits cell growth nor affects cell viability. The recombinant strain can be used as a whole-cell biocatalyst and showed a broader substrate range than strains expressing either OPH or MPH. A mixture of six organophosphorus pesticides (OPs) (0.2 mM each) could be degraded completely within 5 h. The broader substrate specificity in combination with the rapid degradation rate makes the recombinant strain a promising candidate for detoxification of OPs. The fluorescence of surface-displayed GFP is very sensitive to environmental pH change. Because hydrolysis of OPs by OPH or MPH generates protons; the recombinant E. coli could be used as a whole-cell biosensor for the rapid detection of OPs by evaluating fluorescence changes as a function of OP concentrations. © 2013 American Chemical Society;
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