Purification, characterization, and biological effects of a second bacteriocin from Enterococcus faecalis ssp. liquefaciens S-48 and its mutant strain B-48-28.
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.
López-Lara
I
I
Departamento de Microbiología, Universidad de Granada, Facultad de Ciencias, Spain.
Gálvez
A
A
Martínez-Bueno
M
M
Maqueda
M
M
Valdivia
E
E
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D001430:Bacteriocins / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D013293:Enterococcus faecalis / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D010710:Phosphates / Q000494:pharmacology
D001426:Bacterial Proteins; D001430:Bacteriocins; D010710:Phosphates; C065279:bacteriocin Bc 48; C018279:sodium phosphate