Characterization of a bacteriocin produced by Streptococcus thermophilus 81

Abstract

A new bacteriocin, produced by Streptococcus thermophilus 81 has been isolated, purified and characterized. By its heat sensitivity and broad inhibitory spectrum it does not resemble any other S. thermophilus bacteriocin. The mode of action is bacteriostatic. This peptide of 32 amino acids is efficient against several Bacillus species, Listeria monocytogenes, Salmonella typhimurium, Escherichia coli, Yersinia pseudotuberculosis and Yersinia enterocolitica. This bacteriocin is heat labile but its activity was not altered by pH variation from 3 to 10. Six months of storage at 40 degrees C did not influence the activity. The inactivation by detergents and the inability to resolve the protein in SDS-PAGE supposes a more complex structure or a possible stabilizing effect of other molecules. The low sensitivity of Lactobacillus delbrueckii subsp. bulgaricus to the isolated bacteriocin suggests that S. thermophilus 81 may be used in yoghurt starters.