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

Nguyen, Thuong; Lee, Hae; Hong, Soon; Jang, Ji-Ryang; Choe, Woo-Seok; Yoo, Ik-Keun

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 (OmpC) as an anchoring motif. The optimal induction period and arabinose concentration for the expression of peptide-fused OmpC were determined to be 2 h and 0.001 g/L, respectively. Selective adsorption of Pb onto recombinant cells was verified with individual or combinatory use of four metal ions, Pb, Ni, Co, and Cu; the amount of bound Pb onto the biosorbents was significantly higher than the other metal ions. The adsorption isotherm of recombinant cells for Pb followed the Langmuir isotherm with a maximum adsorption loading ( q) of 526 μmol/g dry cell weight.

ESCHERICHIA coli; PEPTIDES; CELL surface display; LEAD toxicology; COST effectiveness

Applied Biochemistry & Biotechnology, 2013, Vol 169, Issue 4, p1188

0273-2289

Academic Journal

10.1007/s12010-012-0073-2