Selective Lead Adsorption by Recombinant Escherichia coli Displaying a Lead-Binding Peptide

A highly specific lead-binding peptide ThrAsnThrLeuSerAsnAsn was displayed on Escherichia coli, and lead adsorption characteristics of the recombinant bacteria were investigated. Cell surface-displayed peptide was expressed under the control of an arabinose promoter using outer membrane protein C (OmpCt) as an anchoring motif. The optimal induction period and arabinose concentration for the expression of peptide-fused OmpCt were determined to be 2 h and 0.001 g/L, respectively. Selective adsorption of Pb2+ onto recombinant cells was verified with individual or combinatory use of four metal ions, Pb2+, Ni2+, Co2+, and Cu2+; the amount of bound Pb2+ onto the biosorbents was significantly higher than the other metal ions. The adsorption isotherm of recombinant cells for Pb2+ followed the Langmuir isotherm with a maximum adsorption loading (qmax) of 526 μmol/g dry cell weight.

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