Article Abstract:
A bacteriocin activity which inhibited strains of Brocothrix thermosphacta and Listeria spp. was detected in cultures of Brochothrix campestris ATCC 43754. The antimicrobial agent, designated brochocin-C, was sensitive to protease, unaffected by the addition of catalase and did not exhibit lysozme or muramidase-like activity. Moreover, brochocin-C did not inhibit Gram-negative bacteria under standard assay conditions, indicating that it is similar to other bacteriocins from some Gram-positive bacteria.
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Article Abstract:
A study was conducted to analyze the biochemical and genetic properties of brochocin-C, a bacteriocin produced by Brochothrix campestris ATCC 43754. Automated Edman degradation was carried out with a gas-phase sequencer to determine the N-terminal amino acid sequence of purified brochocin-C. Experimental results indicated that the amino acid sequence of the purified BrcA peptide supported double-glycine-type leader peptides of class II bacteriocins.
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Article Abstract:
Results demonstrate that functional brochocin A and brochocin B are produced by Carnobacterium piscicola clones, whereas in Escherichia coli the brochocins are fragmented and weakly active or inactive. While brochocin A is expressed as a mature 59-amino acid peptide, brochocin B is produced as a fragment. Both brochocins show a high beta-sheet content in the secondary structure.
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