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- W3044277890 abstract "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" @default.
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- W3044277890 date "2020-10-01" @default.
- W3044277890 modified "2023-09-25" @default.
- W3044277890 title "Development of fenitrothion adsorbing recombinant Escherichia coli by cell surface display of pesticide-binding peptide" @default.
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- W3044277890 doi "https://doi.org/10.1016/j.jbiotec.2020.07.014" @default.
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