Artículos de revistas
Improvement of enterocin P purification process
Fecha
2006-09Registro en:
Cuozzo, Sergio Antonio; Calvez, S.; Prévost, H.; Drider, D.; Improvement of enterocin P purification process; Springer; Folia Microbiologica; 51; 5; 9-2006; 401-405
0015-5632
1874-9356
CONICET Digital
CONICET
Autor
Cuozzo, Sergio Antonio
Calvez, S.
Prévost, H.
Drider, D.
Resumen
Purification and heterologous expression of enterocin P (EntP), a sec-dependent bacteriocin produced byEnterococcus faecium, inEscherichia coli is described. PCR-amplified product of the enterocin P structural geneentP was cloned into plasmid pET-32b under the control of the inducible T7/ac 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 ofE. coli harboring appropriate recombinant plasmid, characterized by ELISA and Western-blot analysis and purified by immunoaffinity chromatography. The use ofE. coli as heterologous host and pET-32b as expressing vector offers promising tools for heterologous production of class IIa bacteriocin.