Selective lead adsorption by recombinant Escherichia coli Displaying a Lead-Binding Peptide

Thuong T.L. Nguyen; Hae Ryong Lee; Soon Ho Hong; Ji Ryang Jang; Woo Seok Choe; Ik Keun Yoo

doi:10.1007/s12010-012-0073-2

Selective lead adsorption by recombinant Escherichia coli Displaying a Lead-Binding Peptide

Thuong T.L. Nguyen
, Hae Ryong Lee
, Soon Ho Hong
, Ji Ryang Jang
, Woo Seok Choe
, Ik Keun Yoo

Department of Chemical Engineering

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

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 _t) as an anchoring motif. The optimal induction period and arabinose concentration for the expression of peptide-fused OmpC_t 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⁺, Ni2²⁺, Co ²⁺, 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.

Original language	English
Pages (from-to)	1188-1196
Number of pages	9
Journal	Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume	169
Issue number	4
DOIs	https://doi.org/10.1007/s12010-012-0073-2
State	Published - Feb 2013

Keywords

Biosorbent
Biosorption
Cell surface display
E. coli
Lead-binding peptide

Access to Document

10.1007/s12010-012-0073-2

Cite this

@article{cd2934cd6bbe4a40b30e0f3c207bc9ed,

title = "Selective lead adsorption by recombinant Escherichia coli Displaying a Lead-Binding Peptide",

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 t) 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+, Ni22+, Co 2+, 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.",

keywords = "Biosorbent, Biosorption, Cell surface display, E. coli, Lead-binding peptide",

author = "Nguyen, \{Thuong T.L.\} and Lee, \{Hae Ryong\} and Hong, \{Soon Ho\} and Jang, \{Ji Ryang\} and Choe, \{Woo Seok\} and Yoo, \{Ik Keun\}",

year = "2013",

month = feb,

doi = "10.1007/s12010-012-0073-2",

language = "English",

volume = "169",

pages = "1188--1196",

journal = "Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology",

issn = "0273-2289",

publisher = "Springer",

number = "4",

}

TY - JOUR

T1 - Selective lead adsorption by recombinant Escherichia coli Displaying a Lead-Binding Peptide

AU - Nguyen, Thuong T.L.

AU - Lee, Hae Ryong

AU - Hong, Soon Ho

AU - Jang, Ji Ryang

AU - Choe, Woo Seok

AU - Yoo, Ik Keun

PY - 2013/2

Y1 - 2013/2

N2 - 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 t) 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+, Ni22+, Co 2+, 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.

AB - 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 t) 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+, Ni22+, Co 2+, 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.

KW - Biosorbent

KW - Biosorption

KW - Cell surface display

KW - E. coli

KW - Lead-binding peptide

UR - https://www.scopus.com/pages/publications/84882945027

U2 - 10.1007/s12010-012-0073-2

DO - 10.1007/s12010-012-0073-2

M3 - Article

C2 - 23306894

AN - SCOPUS:84882945027

SN - 0273-2289

VL - 169

SP - 1188

EP - 1196

JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

JF - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

IS - 4

ER -

Selective lead adsorption by recombinant Escherichia coli Displaying a Lead-Binding Peptide

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this