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

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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 (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 (q max) of 526 μmol/g dry cell weight.

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Acknowledgments

This work was supported by a Korea Research Foundation grant funded by the Korean Government (KRF-2008-521-D00230).

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Authors and Affiliations

  1. School of Chemical Engineering and Bioengineering, University of Ulsan, Ulsan, 680-749, South Korea

    Thuong T. L. Nguyen, Hae Ryong Lee, Soon Ho Hong & Ik-Keun Yoo

  2. SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University, Suwon, 440-746, South Korea

    Ji-Ryang Jang & Woo-Seok Choe

  3. School of Chemical Engineering, Sungkyunkwan University, Suwon, 440-746, South Korea

    Woo-Seok Choe

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  1. Thuong T. L. Nguyen
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  2. Hae Ryong Lee
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  6. Ik-Keun Yoo
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Correspondence to Ik-Keun Yoo.

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Nguyen, T.T.L., Lee, H.R., Hong, S.H. et al. Selective Lead Adsorption by Recombinant Escherichia coli Displaying a Lead-Binding Peptide. Appl Biochem Biotechnol 169, 1188–1196 (2013). https://doi.org/10.1007/s12010-012-0073-2

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  • DOI: https://doi.org/10.1007/s12010-012-0073-2

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