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- Title
Selective Lead Adsorption by Recombinant Escherichia coli Displaying a Lead-Binding Peptide.
- Authors
Nguyen, Thuong; Lee, Hae; Hong, Soon; Jang, Ji-Ryang; Choe, Woo-Seok; Yoo, Ik-Keun
- Abstract
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.
- Subjects
ESCHERICHIA coli; PEPTIDES; CELL surface display; LEAD toxicology; COST effectiveness
- Publication
Applied Biochemistry & Biotechnology, 2013, Vol 169, Issue 4, p1188
- ISSN
0273-2289
- Publication type
Academic Journal
- DOI
10.1007/s12010-012-0073-2