0000000001063041
AUTHOR
M. Rammelsberg
Antibacterial polypeptides of Lactobacillus species
Twelve of 79 strains of the genus Lactobacillus, mainly isolated from plants or fermenting material, were found to inhibit at least one of the nine indicator strains of the species Lact. brevis, Pediococcus damnosus and Leucanostoc oenos. The antimicrobial activities from Lact. brevis B 37 and Lact. casei B 80 were caused by polypeptides detectable in the culture liquids. They are bacteriocins with a narrow antimicrobial spectrum. Brevicin 37 from Lact. brevis B 37 was active against many lactic acid bacteria and Nocardia corallina, whereas caseicin 80 from Lact. casei B 80 inhibits only one other strain of Lact. casei. Brevicin 37 is stable at 121dC, caseicin 80 is inactivated above 60dC, …
Caseicin 80: purification and characterization of a new bacteriocin from Lactobacillus casei
When grown in complex or synthetic media, Lactobacillus casei B 80 synthesizes a mitomycin C-inducible polypeptide with very specific bactericidal activity against the sensitive strain Lactobacillus casei B 109. The amount of secreted bacteriocin in the culture solution was low, about 1 mg/l. The bacteriocin which we called caseicin 80, was also detectable in cell extracts, although only 2% of the total activity was retained intracellularly. Caseicin 80 was concentrated by ultrafiltration and purified by cation exchange chromatography with Cellulose SE-23 and Superose. The molecular weight was in the range of M r=40,000–42,000 and the isoelectric point was pH 4.5.