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Purification, characterization, and biological effects of a second bacteriocin from Enterococcus faecalis ssp. liquefaciens S-48 and its mutant strain B-48-28.
Authors:I López-Lara  A Gálvez  M Martínez-Bueno  M Maqueda  E Valdivia
Institution:Departamento de Microbiología, Universidad de Granada, Facultad de Ciencias, Spain.
Abstract:Enterococcus faecalis ssp. liquefaciens S-48 (producer of the peptide antibiotic AS-48) and its mutant B-48-28 (AS-48-) secrete the bacteriocin Bc-48. This substance has been purified to homogeneity from culture supernatants of strain B-48-28; it consists of a protein (80 kDa) stable from pH. 5.5 to 9.0 and sensitive to temperatures above 45 degrees C and to proteases. Its inhibitory spectrum is restricted to strains of Enterococcus faecalis. Bc-48 inhibits protein synthesis but does not affect amino acid uptake. A partial reduction of cell viability, together with autolysis, is also observed. Bc-48 differs from peptide AS-48 in both its molecular properties and mode of action.
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