Improvement of enterocin P purification process
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
17176759
DOI
10.1007/bf02931583
Knihovny.cz E-zdroje
- MeSH
- bakteriociny biosyntéza genetika izolace a purifikace MeSH
- Enterococcus faecium genetika MeSH
- Escherichia coli genetika metabolismus MeSH
- genetické vektory MeSH
- klonování DNA MeSH
- molekulární sekvence - údaje MeSH
- průmyslová mikrobiologie metody MeSH
- regulace genové exprese u bakterií MeSH
- rekombinantní proteiny biosyntéza genetika izolace a purifikace MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriociny MeSH
- enterocin P MeSH Prohlížeč
- rekombinantní proteiny 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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