Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
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منابع مشابه
Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45.
Lactocin S, a bacteriocin produced by Lactobacillus sake L45, has been purified to homogeneity by ion exchange, hydrophobic interaction and reverse-phase chromatography, and gel filtration. The purification resulted in approximately a 40,000-fold increase in the specific activity of lactocin S and enabled the determination of a major part of the amino acid sequence. Judging from the amino acid ...
متن کاملUse of a bacteriocin produced by Pediococcus acidilactici to inhibit Listeria monocytogenes associated with fresh meat.
A bacteriocin produced by Pediococcus acidilactici had an inhibitory and bactericidal effect on Listeria monocytogenes associated with fresh meat. MICs were significantly lower than minimum killing concentrations. When meat was inoculated with L. monocytogenes, the bacteriocin reduced the number of attached bacteria in 2 min by 0.5 to 2.2 log cycles depending upon bacteriocin concentration. Mea...
متن کاملInhibition of Listeria monocytogenes by using bacteriocin PA-1 produced by Pediococcus acidilactici PAC 1.0.
The bacteriocin produced by Pediococcus acidilactici PAC 1.0, previously designated PA-1 bacteriocin, was found to be inhibitory and bactericidal for Listeria monocytogenes. A dried powder prepared from PAC 1.0 culture supernatant fortified with 10% milk powder was found to contain bacteriocin activity. An MIC against L. monocytogenes and lytic effects in broth cultures were determined. Inhibit...
متن کاملPurification, partial amino acid sequence and mode of action of pediocin PD-1, a bacteriocin produced by Pediococcus damnosus NCFB 1832.
Pediocin PD-1 is a ribosomally synthesized antimicrobial peptide produced by Pediococcus damnosus NCFB1832. It inhibits the growth of several food spoilage bacteria, including malolactic bacteria isolated from wine. Pediocin PD-1 is 2866.87+/-0.4 Da in size, has an isoelectric point (pI) of ca. 9.0 and, on amino acid composition, has partial homology to the lantibiotic plantaricin C. The highes...
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: Journal of General Microbiology
سال: 1992
ISSN: 0022-1287
DOI: 10.1099/00221287-138-9-1985