nisin-z and lacticin-481

nisin-z has been researched along with lacticin-481* in 3 studies

Other Studies

3 other study(ies) available for nisin-z and lacticin-481

ArticleYear
Nisin Z and lacticin 3147 improve efficacy of antibiotics against clinically significant bacteria.
    Future microbiology, 2019, Volume: 14

    Topics: Animals; Anti-Bacterial Agents; Antibiosis; Bacteria; Bacteriocins; Drug Synergism; Methicillin; Microbial Sensitivity Tests; Nisin; Skin; Swine

2019
Technological characterization of bacteriocin producing Lactococcus lactis strains employed to control Listeria monocytogenes in cottage cheese.
    International journal of food microbiology, 2012, Feb-01, Volume: 153, Issue:1-2

    In recent years, there has been a particular focus on the application of antimicrobial compounds produced by lactic acid bacteria (LAB) as natural preservatives to control the growth of spoilage and pathogenic bacteria in food. Bacteriocins are antimicrobial peptides which can be added to foods in concentrated forms as food preservatives, e.g. additives, or they can be produced in situ by starters or protective cultures. In this study, twenty Lactococcus lactis bacteriocin producers previously isolated from Italian fermented foods were subjected to a variety of physical and biochemical tests in order to identify those with the greatest potential as starter cultures in cheese production. Of these, four strains isolated from cheese (one nisin Z producer, one nisin A producer and two lacticin 481 producers) which fulfilled the desired technological criteria were assessed for their ability to control Listeria monocytogenes. The subsequent application of these bacteriocinogenic strains as starter cultures in Cottage cheese established that the nisin A producing Lact. lactis 40FEL3, and to a lesser extent the lacticin 481 producers 32FL1 and 32FL3, successfully controlled the growth of the pathogen. This is the first study to directly compare the ability of nisin A, nisin Z and lacticin 481 producing strains to control listerial growth during the manufacture and storage of Cottage cheese.

    Topics: Anti-Bacterial Agents; Bacteriocins; Cheese; Dairying; Food Preservatives; Lactococcus lactis; Listeria monocytogenes; Nisin

2012
Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study.
    European journal of biochemistry, 1996, Jan-15, Volume: 235, Issue:1-2

    Monomolecular layers of lipids at the air/water interface have been used as a model membrane to study membrane interactions of the lantibiotic nisin. The natural lantibiotics nisin A and nisin Z proved to have a high affinity for the anionic lipids phosphatidylglycerol and bis(phosphatidyl)glycerol (cardiolipin). The interaction with zwitterionic phopholipids or neutral lipids is very low at surface pressures higher than 32 mN/m. Nisin, nisin mutants and lacticin 481 show a remarkable correlation between anti-microbial activity and anionic lipid interaction. The results indicate that primarily the N-terminal part (residues 1-22) penetrates into the lipid phase. Reduction of the flexibility at positions 20-21 has a negative effect on monolayer interaction and activity. The C-terminal part is probably responsible for ionic interactions of nisin in monomeric or oligomeric form with anionic lipids. In mixtures of anionic and zwitterionic lipids maximal interactions are found at approximately 70 mol/100 mol anionic lipid. Gram-positive bacteria, which form the main target for nisin, are characterized by a high content of anionic lipids in the membrane. Monolayers formed of lipid extracts of bacteria sensitive to nisin were more strongly penetrated than those of bacteria relatively insensitive to nisin.

    Topics: Amino Acid Sequence; Anti-Bacterial Agents; Bacteria; Bacterial Proteins; Bacteriocins; Base Sequence; DNA Primers; Drug Resistance, Microbial; Escherichia coli; In Vitro Techniques; Lactococcus lactis; Membrane Lipids; Membranes, Artificial; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nisin

1996