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Fast-Disintegrating Oral Films Containing Nisin-Loaded Niosomes. [PDF]
MoleculesAmer AA +4 more
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<i>Lactococcus lactis</i> as a New Strategy for Oral Vaccination: Current Insights and Future Perspectives. [PDF]
PharmaceuticsGrossolli-Galvez J +3 more
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Biomedical applications of nisin [PDF]
Journal of Applied Microbiology, 2016 Nisin is a bacteriocin produced by a group of Gram-positive bacteria that belongs to Lactococcus and Streptococcus species. Nisin is classified as a Type A (I) lantibiotic that is synthesized from mRNA and the translated peptide contains several unusual amino acids due to post-translational modifications.
Alexander Rickard, J C Fenno
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Nisin induction without nisin secretion
Microbiology, 2006Nisin Z, a post-translationally modified antimicrobial peptide ofLactococcus lactis, is positively autoregulated by extracellular nisin via the two-component regulatory proteins NisRK. A mutation in the nisin NisT transporter renderedL. lactisincapable of nisin secretion, and nisin accumulated inside the cells.
Hanan T Abbas, Hilmi +3 more
openaire +2 more sources
2020
Nisin is a 34-amino acid peptide known as a bacteriocin. It belongs to class-Ia bacteriocins known as lantibiotics. It is the most characterized and commercially used antimicrobial peptide. It was commercialized in the 1950s for the prevention of late blowing in cheese by Clostridium.
Eghbal, Noushin +2 more
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Nisin is a 34-amino acid peptide known as a bacteriocin. It belongs to class-Ia bacteriocins known as lantibiotics. It is the most characterized and commercially used antimicrobial peptide. It was commercialized in the 1950s for the prevention of late blowing in cheese by Clostridium.
Eghbal, Noushin +2 more
openaire +2 more sources
Applications of the bacteriocin, nisin
Antonie van Leeuwenhoek, 1996Nisin was first introduced commercially as a food preservative in the UK approximately 30 years ago. First established use was as a preservative in processed cheese products and since then numerous other applications in foods and beverages have been identified. It is currently recognised as a safe food preservative in approximately 50 countries.
J, Delves-Broughton +3 more
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Analysis of nisin A, nisin Z and their degradation products by LCMS/MS
Food Chemistry, 2011The peptides nisin A and nisin Z belong to type-A lantibiotics applied as preservatives in cheese production. The present study optimised and validated a liquid chromatography-tandem mass spectrometry (LCMS/MS) method for the analysis of nisin A in cheese.
N, Schneider +2 more
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Identification and characterization of the lantibiotic nisin Z, a natural nisin variant
European Journal of Biochemistry, 1991Lactococcus lactis strain NIZO 22186 produces an extracellular, lanthinine‐containing 3.5‐kDa polypeptide with antimicrobial activity. Its retention time on reversed‐phase (RP) HPLC and its amino acid composition showed high similarities but no complete identity to nisin.
J W, Mulders +4 more
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The effect of nisin concentration and nutrient depletion on nisin production of Lactococcuslactis
Applied Microbiology and Biotechnology, 1997The kinetics of nisin production was studied in batch cultures using a construct of Lactococcus lactis subsp. lactis C2SmPrt-, containing a transposon (TnNip) that encodes nisin production. The introduction of TnNip into C2SmPrt- significantly lowered the specific growth rate and the maximum A620 reached was reduced from 15.2 to 11.0.
W S, Kim, R J, Hall, N W, Dunn
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The effect of nisin on murein synthesis
Archives of Microbiology, 1980Nisin inhibits murein synthesis with concomitant accumulation of undecaprenyl-pyrophospho-MurHAc(pentapeptide) (lipid intermediate I). This inhibition is caused by the formation of a complex between the antibiotic and lipid intermediate I. Undecaprenyl-pyrophospho-MurNAc(pentapeptide)-GlcNAc (lipid intermediate II) also forms a complex with nisin ...
REISINGER, P +3 more
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