CERELA   05438
CENTRO DE REFERENCIA PARA LACTOBACILOS
Unidad Ejecutora - UE
artículos
Título:
Short peptides derived from NH2-terminus of subClass IIa bacteriocin enterocin CRL35 show antimicrobial activity.
Autor/es:
SALVUCCI E.; SAAVEDRA L; SESMA F.
Revista:
JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY
Editorial:
Oxford University Press
Referencias:
Año: 2007 vol. 59 p. 1102 - 1102
ISSN:
0305-7453
Resumen:
Enterocin CRL35 is a 43-aa heat stable peptide with antilisterial activity. It belongs tosubclass IIa bacteriocins characterized by a hydrophilic N-terminal domain which shares anYGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Short syntheticpeptides derived from the N-terminal half of divercin V41, enterocin A and enterocin CRL35were evaluated for antimicrobial properties. A 15-mer peptide fragment derived fromenterocin CRL35 inhibited the growth of Listeria innocua and Listeria monocytogenes insinthetical/minimal media and dissipated the membrane potential of sensitive cells.