Purification and partial amino acid sequence of brevicin 27, a bacteriocin produced by Lactobacillus brevis SB27.
Brevicin 27, a bacteriocin produced by Lacto bacillus brevis SB27, is inhibitory mainly against closely related Lactobacillus brevis and Lactobacillus büchneri 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.
Benoit
V
V
Laboratoire de Microbiologie Industrielle et Alimentaire, Ecole Nationale Supérieure d'Agronomie et des Industries Alimentaires, Institut National Polytechnique de Lorraine, 2, Avenue de la Forêt de Haye, 54500 Vandoeuvre les Nancy, France.
Lebrihi
A
A
Millière
J B
JB
Lefebvre
G
G
D000595:Amino Acid Sequence; D001419:Bacteria / Q000187:drug effects; D001430:Bacteriocins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D007778:Lactobacillus / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight
D001430:Bacteriocins