Purification and partial amino acid sequence of Brevicin 27, a bacteriocin produced by Lactobacillus brevis SB27

• Published in: Current microbiology Vol. 34; no. 3; pp. 173 - 179
• Main Authors: Benoit, V. (Ecole Nationale Superieure d'Agronomie et des Industries Alimentaires, Vandoeuvre les Nancy, France.), Lebrihi, A, Milliere, J.B, Lefebvre, G
• Format: Journal Article
• Language: English
• Published: New York, NY Springer 01.03.1997; Springer Nature B.V
• Subjects: ACIDE AMINE; Amino acid composition; Amino Acid Sequence; Amino acids; AMINOACIDOS; Bacteria; Bacteria - drug effects; BACTERIOCINAS; BACTERIOCINE; Bacteriocins - chemistry; Bacteriocins - isolation & purification; Bacteriocins - pharmacology; Bacteriology; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Fundamental and applied biological sciences. Psychology; Lactobacillus - chemistry; LACTOBACILLUS BREVIS; Microbiology; Mission oriented research; Molecular Sequence Data; Molecular Weight; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Physiology and metabolism; Proteins; Lactic acid bacteria; Purification; Lactobacillus brevis; Bacteriocin; Bacteria; Lactobacillaceae; Activity spectrum; Antibacterial agent; Biological activity; Aminoacid sequence
• ISSN: 0343-8651; 1432-0991
• DOI: 10.1007/s002849900164

Brevicin 27, a bacteriocin produced by Lactobacillus brevis SB27, is inhibitory mainly against closely related Lactobacillus brevis and Lactobacillus buchneri strains. It was purified from the culture supernatant by a four-step purification procedure including ammonium sulfate precipitation, cation exchange, hydrophobic interaction, and reverse-phase, high performance liquid chromatographies. The purified bacteriocin was subjected to mass spectrometry, amino acid composition analysis, and sequencing by Edman degradation. It was shown to be an about 5200-Da basic protein containing a high proportion of lysine and of hydrophobic amino acids. The partial N-terminal amino acid sequence (25 residues) was unique when compared with the Protein Data Bank (PDB), Swiss Prot, and Protein Information Resource (PIR) data banks and to the translated Gen Bank