Improvement of enterocin P purification process
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17176759
DOI
10.1007/bf02931583
Knihovny.cz E-resources
- MeSH
- Bacteriocins biosynthesis genetics isolation & purification MeSH
- Enterococcus faecium genetics MeSH
- Escherichia coli genetics metabolism MeSH
- Genetic Vectors MeSH
- Cloning, Molecular MeSH
- Molecular Sequence Data MeSH
- Industrial Microbiology methods MeSH
- Gene Expression Regulation, Bacterial MeSH
- Recombinant Proteins biosynthesis genetics isolation & purification MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacteriocins MeSH
- enterocin P MeSH Browser
- Recombinant Proteins MeSH
Purification and heterologous expression of enterocin P (EntP), a sec-dependent bacteriocin produced by Enterococcus faecium, in Escherichia coli is described. PCR-amplified product of the enterocin P structural gene entP was cloned into plasmid pET-32b under the control of the inducible T7lac promoter. The neo-synthesized EntP was genetically modified by an addition of 3 extra amino acids, leading to recombinant EntRP. Active EntRP was recovered from the cytoplasmic soluble fraction of E. coli harboring appropriate recombinant plasmid, characterized by ELISA and Western-blot analysis and purified by immunoaffinity chromatography. The use of E. coli as heterologous host and pET-32b as expressing vector offers promising tools for heterologous production of class IIa bacteriocin.
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