Article Abstract:
The peptide bacteriocin, piscicolin 126, produced by the lactic acid bacterium Carnobacterium piscicola JG126, exhibits bactericidal activity against the food-borne human pathogen Listeria monocytogenes. Its molecular characterization reveals a unique amino acid sequence. Purification and structural analysis of piscicolin 126 reveals its class II bacteriocin status with 44 amino acid residues and one intrapeptide disulfide ring. The bactericidal activity of piscicolin 126 is neither affected by high pH values nor by catalase/lipase/lysozyme, but is destroyed by proteolytic enzymes.
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Article Abstract:
A new method to extract large amounts of bacteriocins from lactic acid bacteria was developed. The procedure involved manipulation of the culture broth pH to maximally adsorb bacteriocins to the cell surface, which were subsequently removed by centrifugation. The procedure was used to extract pediocin AcH, nisin, sakacin A and leuconocin Lcm1 from lactic acid bacteria. The resulting bacteriocins were potent and concentrated. This demonstrates the efficacy of the new method, which will be useful in producing biopreservatives.
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Article Abstract:
Transposon Tn917 knockout libraries are constructed for Listeria innocua strain Lin11 and screened for mutants that are resistant to pediocin AcH in order to identify genes that are important for class IIa bacteriocin interaction and resistance in L. species. The combined results show that the inactivation of lin0142 protein is responsible for pediocin AcH resistance in G7 mutant and that lin0142 is required for the transcription of the mpt operon.
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