Isolation and characterization of two bacteriocins of Lactobacillus acidophilus LF221

Lactobacillus acidophilus LF221 produced bacteriocin-like activity against different bacteria including some pathogenic and food-spoilage species. Besides some lactic acid bacteria, the following species were inhibited: Bacillus cereus, Clostridium sp., Listeria innocua, Staphylococcus aureus, Strep...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1998-05, Vol.49 (5), p.606-612
Main Authors: Bogovic-Matijasic, B, Rogelj, I, Nes, I.F, Holo, H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Ammonium
Bacteria
Bacteriocins - chemistry
Bacteriocins - isolation & purification
Bacteriocins - pharmacology
Bacteriology
Biological and medical sciences
Chromatography, Gel
food preservatives
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Lactobacillus acidophilus
Lactobacillus acidophilus - chemistry
Microbiology
Molecular Sequence Data
Molecular Weight
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Peptides
probiotics
Sulfates
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Summary:Lactobacillus acidophilus LF221 produced bacteriocin-like activity against different bacteria including some pathogenic and food-spoilage species. Besides some lactic acid bacteria, the following species were inhibited: Bacillus cereus, Clostridium sp., Listeria innocua, Staphylococcus aureus, Streptococcus D. L. acidophilus LF221 produced at least two bacteriocins, acidocin LF221 A and acidocin LF221 B, which were purified by ammonium sulphate precipitation, ion-exchange chromatography, hydrophobic interaction and reverse-phase FPLC. The antibacterial substances were heat-stable, sensitive to proteolytic enzymes (trypsin, pepsin, pronase, proteinase K) and migrated as 3500- to 5000-Da proteins on sodium dodecyl sulphate/polyacrylamide gel electrophoresis. The sequences of 46 amino-terminal amino acid residues of peptide A and 35 of peptide B were determined. Among the residues identified, no modified amino acids were found. No significant homology was found between the amino acid sequences of acidocin LF221 A and other bacteriocins of lactic acid bacteria and 26% homology was found between acidocin LF221 B and brevicin 27. L. acidophilus LF221 may be of interest as a probiotic strain because of its human origin and inhibition of pathogenic bacteria, especially Clostridium difficile.
ISSN:0175-7598
1432-0614
DOI:10.1007/s002530051221