Genetic Characterization and Heterologous Expression of Brochocin-C, an Antibotulinal, Two-Peptide Bacteriocin Produced by Brochothrix campestris ATCC 43754
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چکیده
منابع مشابه
Brochocin-C, a new bacteriocin produced by Brochothrix campestris.
Brochotrix campestris ATCC 43754 produces a bacteriocin inhibitory towards Brochothrix thermosphacta, lactobacilli, Listeria spp., and other gram-positive bacteria. This antimicrobial agent is heat stable, sensitive to proteases, catalase insensitive, and free of organic acids. No phage particles were detected by transmission electron microscopy. Muramidase activity was not detected in the prep...
متن کاملThe outer membrane of gram-negative bacteria inhibits antibacterial activity of brochocin-C.
Brochocin-C is a two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754 that has a broad activity spectrum comparable to that of nisin. Brochocin-C has an inhibitory effect on EDTA-treated gram-negative bacteria, Salmonella enterica serovar Typhimurium lipopolysaccharide mutants, and spheroplasts of Typhimurium strains LT2 and SL3600. Brochocin-C treatment of cells and spheroplas...
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The structural genes for the two-peptide bacteriocin enterocin 1071 (Ent1071) in Enterococcus faecalis FAIR-E 309 were cloned. DNA sequence analysis showed that the enterocin 1071A (Ent1071A) peptide of strain FAIR-E 309 differed by two amino acids from the Ent1071A reported for E. faecalis BFE 1071 (E. Balla, L. M. T. Dicks, M. Du Toit, M. J. van der Merwe, and W. H. Holzapfel, Appl. Environ. ...
متن کاملDetection and Characterization of Weissellicin 110, a Bacteriocin Produced by Weissella cibaria
Background: Weissellicin 110 is the only bacteriocin reported in Weissella cibaria up to now. This bacteriocin represents several unique features. This is the first report on the gene sequence that encodes for the bacteriocin. Objectives: Providing a rapid detection method to isolate the weissellicin 110 encoding gene and determination of the bacteriocin distribution were the objectives. Materi...
متن کاملHeterologous expression, purification and refolding of an anti-listerial peptide produced by Pediococcus acidilactici K7
The fusion protein, 6XHis-Xpress-PedA was constructed and expressed in Escherichia coli BL21 (DE3). The presence of a 12.8 kDa recombinant protein, localized in inclusion bodies (IBs) at high concentration, was confirmed by SDS-PAGE analysis and by western blotting using anti-His antibody. The rec-pediocin was purified by Nickel-nitrilotriacetic acid beads and refolded using 5 mM of β-mercaptoe...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1998
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.64.12.4757-4766.1998