Purification and Partial Amino Acid Sequence of Brevicin 27, a Bacteriocin Produced by Lactobacillus brevis SB27 |
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Authors: | Valérie Benoit Ahmed Lebrihi Jean-Bernard Millière Gérard Lefebvre |
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Institution: | (1) 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 , FR |
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Abstract: | Brevicin 27, a bacteriocin produced by Lactobacillus
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.
Received: 24 July 1996 / Accepted: 10 September 1996 |
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