Development of fenitrothion adsorbing recombinant Escherichia coli by cell surface display of pesticide-binding peptide.

In this study, constructed Escherichia coli could efficiently adsorb fenitrothion by displaying a pesticide-binding peptide on it using the anchoring motif OmpC. A codon-optimized, pesticide-binding peptide was attached to the C-terminus of OmpC at loop 7 (993 bp). The efficiency of fenitrothion binding by the monomer peptide was evaluated under different temperatures, pH levels, and fenitrothion concentrations. To enhance fenitrothion adsorption, a dimer of pesticide-binding peptide was also constructed and displayed. Compared with the peptide monomer, the dimer-displaying strain showed superior fenitrothion-binding ability. The performance of the strains was evaluated in artificial polluted soil, and their morphology was analyzed by FE-SEM. The results showed that these two kinds of constructed strains can adsorb fenitrothion in contaminated environments with no cellular activity reduction. ARTICLE INFO.