Bacteriocin lactocin-S
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Bacteriocin lactocin-S

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Bacteriocin lactocin-S is an antimicrobial peptide produced by Lactobacillus sakei L45. It has antibacterial activity and inhibits the growth of selected species of the genera Lactobacillus, Pedicoccus, and Leuconostoc. It contains at least two lanthionines, which are probably formed between the serine in position 23 and the cysteine in position 28, and between the serine in position 32 and the cysteine in position 37.

Functional Peptides
Catalog number
CAS number
Ser-Thr-Pro-Val-Leu-Ala-Ser-Val-Ala-Val-Ser-Met-Glu-Leu-Leu-Pro-Thr-Ala-Ser-Val-Leu-Tyr-Ser-Asp-Val-Ala-Gly-Cys-Phe-Lys-Tyr-Ser-Ala-Lys-His-His-Cys; lasA; Lactocin S (Bacteriocin)
Lyophilized Powder or Liquid
Store at -20°C
1. Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45
C I Mørtvedt, J Nissen-Meyer, K Sletten, I F Nes Appl Environ Microbiol. 1991 Jun;57(6):1829-34. doi: 10.1128/aem.57.6.1829-1834.1991.
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 composition, lactocin S contained approximately 33 amino acid residues, of which about 50% were the nonpolar amino acids alanine, valine, and leucine. Amino acids were not detected upon direct N-terminal sequencing, indicating that the N-terminal amino acid was blocked. By cyanogen bromide cleavage at an internal methionine, the sequence of the 25 amino acids (including the methionine at the cleavage site) in the C-terminal part of the molecule was determined. The sequence was Met-Glu-Leu-Leu-Pro-Thr-Ala-Ala-Val-Leu-Tyr-Xaa-Asp-Val-Ala-Gly-Xaa-Phe- Lys-Tyr-Xaa-Ala-Lys-His-His, where Xaa represents unidentified residues. It is likely that the unidentified residues are modified forms of cysteine or amino acids associated with cysteine, since two cysteic acids per lactocin S molecule were found upon performic acid oxidation of lactocin S. The sequence was unique when compared to the SWISS-PROT data bank.
2. PCR detection of the lactocin S structural gene in bacteriocin-producing lactobacilli from meat
J M Rodríguez, L M Cintas, P Casaus, A Suárez, P E Hernández Appl Environ Microbiol. 1995 Jul;61(7):2802-5. doi: 10.1128/aem.61.7.2802-2805.1995.
The lactocin S structural gene (lasA) in seven bacteriocinogenic lactobacilli isolated from fermented sausages was studied. Two degenerate primers were synthesized to amplify a 75-bp fragment of the gene. Three strains amplified the fragment from their plasmid DNA, and hybridization analysis confirmed these results.
3. Enterococcus faecalis cytolysin and lactocin S of Lactobacillus sake
M S Gilmore, M Skaugen, I Nes Antonie Van Leeuwenhoek. 1996 Feb;69(2):129-38. doi: 10.1007/BF00399418.
Strains of Enterococcus faecalis and Lactobacillus sake have been found to express lantibiotics with unusual properties. The enterococcal lantibiotic is unusual in that it consists of two dissimilar subunits, both putatively containing modifications consistent with those found in other lantibiotics. The enterococcal lantibiotic is also unusual in the number of proteolytic steps involved in secretion signal removal and activation. Moreover, it has been observed to contribute to enterococcal disease in humans and in animal models. Structural studies of lactocin S, expressed by a strain of L. sake highlight unique properties including the presence of D-alanine within its structure, and a protease putatively responsible for lactocin S secretion signal peptide removal which, itself, lacks a signal or propeptide sequence. Despite the unusual properties of each of these lantibiotics, the operons encoding each, and accompanying auxiliary functions, are collinear suggesting a common ancestry. The accretion of interdigitating DNA sequences between genes encoded within the lactocin S determinant are unique to that determinant, however, and are of unknown function.
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