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Cloning, expression, and identification of a novel class IIa bacteriocin in the Escherichia coli cell-free protein expression system

The NB - C1 gene, acquired from the result of data mining of the lactic acid bacteria genome, is a novel potential class IIa bacteriocin gene with the characteristic YGNGVxC cluster. To produce soluble NB-C1 efficiently and overcome issues of protein toxicity, we adopted a GFP fusion strategy using... Full description

Journal Title: Biotechnology Letters 2012, Vol.34(2), pp.359-364
Main Author: Chen, Haiqin
Other Authors: Yan, Xie , Tian, Fengwei , Song, Yuanda , Chen, Yong , Zhang, Hao , Chen, Wei
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0141-5492 ; E-ISSN: 1573-6776 ; DOI: 10.1007/s10529-011-0779-1
Link: http://dx.doi.org/10.1007/s10529-011-0779-1
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recordid: springer_jour10.1007/s10529-011-0779-1
title: Cloning, expression, and identification of a novel class IIa bacteriocin in the Escherichia coli cell-free protein expression system
format: Article
creator:
  • Chen, Haiqin
  • Yan, Xie
  • Tian, Fengwei
  • Song, Yuanda
  • Chen, Yong
  • Zhang, Hao
  • Chen, Wei
subjects:
  • Antimicrobial activity
  • Bacteriocin
  • cell-free protein expression system
  • NB-C1 gene
ispartof: Biotechnology Letters, 2012, Vol.34(2), pp.359-364
description: The NB - C1 gene, acquired from the result of data mining of the lactic acid bacteria genome, is a novel potential class IIa bacteriocin gene with the characteristic YGNGVxC cluster. To produce soluble NB-C1 efficiently and overcome issues of protein toxicity, we adopted a GFP fusion strategy using an Escherichia coli cell-free protein expression system. We constructed the expression vector pIVEX2.4d-GFP-NB-C1, which was expressed in both the batch mode and the continuous exchange cell-free (CECF) systems. The amount of soluble fusion protein achieved from the CECF system (2.2 mg/ml) was approximately three times higher than that in the batch mode (0.73 mg/ml). The soluble fusion protein was purified via one-step Ni–NTA affinity chromatography, with a concentration of 0.26 mg/ml and a purity of 95%. The purified NB-C1 showed strong antimicrobial activity against the indicator bacteria Listeria monocytogenes .
language: eng
source:
identifier: ISSN: 0141-5492 ; E-ISSN: 1573-6776 ; DOI: 10.1007/s10529-011-0779-1
fulltext: fulltext
issn:
  • 1573-6776
  • 15736776
  • 0141-5492
  • 01415492
url: Link


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titleCloning, expression, and identification of a novel class IIa bacteriocin in the Escherichia coli cell-free protein expression system
creatorChen, Haiqin ; Yan, Xie ; Tian, Fengwei ; Song, Yuanda ; Chen, Yong ; Zhang, Hao ; Chen, Wei
ispartofBiotechnology Letters, 2012, Vol.34(2), pp.359-364
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subjectAntimicrobial activity ; Bacteriocin ; cell-free protein expression system ; NB-C1 gene
descriptionThe NB - C1 gene, acquired from the result of data mining of the lactic acid bacteria genome, is a novel potential class IIa bacteriocin gene with the characteristic YGNGVxC cluster. To produce soluble NB-C1 efficiently and overcome issues of protein toxicity, we adopted a GFP fusion strategy using an Escherichia coli cell-free protein expression system. We constructed the expression vector pIVEX2.4d-GFP-NB-C1, which was expressed in both the batch mode and the continuous exchange cell-free (CECF) systems. The amount of soluble fusion protein achieved from the CECF system (2.2 mg/ml) was approximately three times higher than that in the batch mode (0.73 mg/ml). The soluble fusion protein was purified via one-step Ni–NTA affinity chromatography, with a concentration of 0.26 mg/ml and a purity of 95%. The purified NB-C1 showed strong antimicrobial activity against the indicator bacteria Listeria monocytogenes .
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titleCloning, expression, and identification of a novel class IIa bacteriocin in the Escherichia coli cell-free protein expression system
descriptionThe NB - C1 gene, acquired from the result of data mining of the lactic acid bacteria genome, is a novel potential class IIa bacteriocin gene with the characteristic YGNGVxC cluster. To produce soluble NB-C1 efficiently and overcome issues of protein toxicity, we adopted a GFP fusion strategy using an Escherichia coli cell-free protein expression system. We constructed the expression vector pIVEX2.4d-GFP-NB-C1, which was expressed in both the batch mode and the continuous exchange cell-free (CECF) systems. The amount of soluble fusion protein achieved from the CECF system (2.2 mg/ml) was approximately three times higher than that in the batch mode (0.73 mg/ml). The soluble fusion protein was purified via one-step Ni–NTA affinity chromatography, with a concentration of 0.26 mg/ml and a purity of 95%. The purified NB-C1 showed strong antimicrobial activity against the indicator bacteria Listeria monocytogenes .
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abstractThe NB - C1 gene, acquired from the result of data mining of the lactic acid bacteria genome, is a novel potential class IIa bacteriocin gene with the characteristic YGNGVxC cluster. To produce soluble NB-C1 efficiently and overcome issues of protein toxicity, we adopted a GFP fusion strategy using an Escherichia coli cell-free protein expression system. We constructed the expression vector pIVEX2.4d-GFP-NB-C1, which was expressed in both the batch mode and the continuous exchange cell-free (CECF) systems. The amount of soluble fusion protein achieved from the CECF system (2.2 mg/ml) was approximately three times higher than that in the batch mode (0.73 mg/ml). The soluble fusion protein was purified via one-step Ni–NTA affinity chromatography, with a concentration of 0.26 mg/ml and a purity of 95%. The purified NB-C1 showed strong antimicrobial activity against the indicator bacteria Listeria monocytogenes .
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doi10.1007/s10529-011-0779-1
pages359-364
date2012-02