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Sakacins are bacteriocins produced by Lactobacillus sakei. They are often clustered with the other lactic acid bacteriocins.[1] The best known sakacins are sakacin A, G, K, P, and Q. In particular, sakacin A and P have been well characterized.

List of named sakacins[edit]

  • Sakacin A[2] is a small, 41 amino acid (the precursor is 90 aa), heat-stable polypeptide. It has been characterized genetically.[3] The regulation of sakacin A has been shown to be related to pheromones (possibly quorum sensing) and temperature changes.[4] It is identical to curvacin/curvaticin A.
  • Sakacin B is a heat and pH stable protein.[5]
  • Sakacin G is a 37 amino acid long (small) polypeptide.[6]
  • Sakacin K is closely related to Sakacin A (and curvacin A), sharing the first 30 N-terminal amino acids.[7] It has been studied extensively for its industrial applications.[8][9][10]
  • Sakacin M is a heat-resistant protein, MW = 4640.[11]
  • Sakacin P is a small, heat-stable, ribosomally synthesized polypeptide. Its genetics has been well-characterized.[12][13]
  • Sakacin Q was discovered in a strain producing Sakacin P.[14]
  • Sakacin R is very similar to sakacin P.[15] It is 43 amino acids long, and is also known as sakacin 674.
  • Sakacin T is a class II bacteriocin. It is produced from a single operon with sakacin X; there are three distinct promoters in the operon, the two sakacins are chemically distinct, though similar.[16][17] Sakacin T
  • Sakacin X is a class IIa bacteriocin. It appears in the references with Sakacin T (above).
  • Sakacin Z was apparently never published and is known from a reference to unpublished data (refers to B. Ray, under Table 6, page 551) [18]

The conventions governing the naming of sakacins are somewhat confused. Sakacin Z was named because it is produced by L. sakei Z, just as Sakacin 670 was named because it was produced by L. sakei 670; but the remaining naming convention uses letters A-Z, of which few are unambiguously available. Worse yet, many strains produce several sakacins [19] so that naming them by strain is ambiguous.

Applications of the Sakacins[edit]

Many of the sakacins have been tested for industrial applications[20] and inserted into other lactic acid bacteria.[21] Some have been engineered for production in food environments as well. Many were actually discovered in food contexts, like Greek dry cured sausage (sakacin B). In modern food chemistry, the sakacins have been studied for their use against Listeria in the production of sausages (like Portuguese lingüiça) and cured meat products (such as ham[22] and cold cuts[23]), cheeses, and other lactic acid fermented products. They are also used to repress unwanted bacterial growth that might cause ropiness, sliminess, malodor and other product defects.


  1. ^ Sablon E, Contreras B, Vandamme E (2000). "Antimicrobial peptides of lactic acid bacteria: mode of action, genetics and biosynthesis". Adv. Biochem. Eng. Biotechnol. 68: 21–60. PMID 11036685. 
  2. ^ Holck A, Axelsson L, Birkeland SE, Aukrust T, Blom H (1992). "Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706". J. Gen. Microbiol. 138 (12): 2715–20. PMID 1487735. 
  3. ^ Axelsson L, Holck A (1995). "The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706". J. Bacteriol. 177 (8): 2125–37. PMC 176857Freely accessible. PMID 7721704. 
  4. ^ Diep DB, Axelsson L, Grefsli C, Nes IF (2000). "The synthesis of the bacteriocin sakacin A is a temperature-sensitive process regulated by a pheromone peptide through a three-component regulatory system". Microbiology (Reading, Engl.). 146 (9): 2155–60. PMID 10974103. 
  5. ^ Samelis J, Roller S, Metaxopoulos J (1994). "Sakacin B, a bacteriocin produced by Lactobacillus sake isolated from Greek dry fermented sausages". Journal of applied bacteriology. 76 (5): 475–486. 
  6. ^ Simon L, Fremaux C, Cenatiempo Y, Berjeaud JM (2002). "Sakacin g, a new type of antilisterial bacteriocin". Appl. Environ. Microbiol. 68 (12): 6416–6420. PMC 134399Freely accessible. PMID 12450870. doi:10.1128/AEM.68.12.6416-6420.2002. 
  7. ^ Aymerich MT, Garriga M, Monfort JM, Nes I, Hugas M (2000). "Bacteriocin-producing lactobacilli in Spanish-style fermented sausages : characterization of bacteriocins". Food Microbiology. 17 (1): 33–45. doi:10.1006/fmic.1999.0275. 
  8. ^ Leroy F, de Vuyst L (1999). "Temperature and pH conditions that prevail during fermentation of sausages are optimal for production of the antilisterial bacteriocin sakacin K". Appl. Environ. Microbiol. 65 (3): 974–81. PMC 91131Freely accessible. PMID 10049850. 
  9. ^ Leroy F, de Vuyst L (1999). "The presence of salt and a curing agent reduces bacteriocin production by Lactobacillus sakei CTC 494, a potential starter culture for sausage fermentation". Appl. Environ. Microbiol. 65 (12): 5350–6. PMC 91728Freely accessible. PMID 10583988. 
  10. ^ Leroy F, Degeest B, De VL (2002). "A novel area of predictive modelling: describing the functionality of beneficial microorganisms in foods". Int. J. Food Microbiol. 73 (2–3): 251–259. PMID 11934033. doi:10.1016/S0168-1605(01)00657-2. 
  11. ^ Sobrino OJ, Rodríguez JM, Moreira WL, Cintas LM, Fernández MF, Sanz B, Hernández PE (1992). "Sakacin M, a bacteriocin-like substance from Lactobacillus sake 148". Int. J. Food Microbiol. 16 (3): 215–225. PMID 1445768. doi:10.1016/0168-1605(92)90082-E. 
  12. ^ Hühne K, Axelsson L, Holck A, Kröckel L (1996). "Analysis of the sakacin P gene cluster from Lactobacillus sake Lb674 and its expression in sakacin-negative Lb. sake strains". Microbiology (Reading, Engl.). 142 (6): 1437–48. PMID 8704983. 
  13. ^ Tichaczek PS, Vogel RF, Hammes WP (1994). "Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673". Microbiology (Reading, Engl.). 140 (2): 361–7. PMID 8180701. 
  14. ^ Mathiesen G, Huehne K, Kroeckel L, Axelsson L, Eijsink VG (2005). "Characterization of a new bacteriocin operon in sakacin P-producing Lactobacillus sakei, showing strong translational coupling between the bacteriocin and immunity genes". Appl. Environ. Microbiol. 71 (7): 3565–3574. PMC 1169027Freely accessible. PMID 16000763. doi:10.1128/AEM.71.7.3565-3574.2005. 
  15. ^ Holck AL, Axelsson L, Hühne K, Kröckel L (1994). "Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sake Lb674". FEMS Microbiol. Lett. 115 (2–3): 143–149. PMID 8138128. doi:10.1111/j.1574-6968.1994.tb06629.x. 
  16. ^ Vaughan A, O' Mahony J, Eijsink VG, O' Connell-Motherway M, van Sinderen D (2004). "Transcriptional analysis of bacteriocin production by malt isolate Lactobacillus sakei 5". FEMS Microbiol. Lett. 235 (2): 377–384. PMID 15183888. doi:10.1016/j.femsle.2004.05.011. 
  17. ^ Vaughan A, Eijsink VG, Van Sinderen D (2003). "Functional characterization of a composite bacteriocin locus from malt isolate Lactobacillus sakei 5". Appl. Environ. Microbiol. 69 (12): 7194–7203. PMC 309959Freely accessible. PMID 14660366. doi:10.1128/AEM.69.12.7194-7203.2003. 
  18. ^ Ray B, Miller KW (2000). "Pediocin". In Naidu AS. Natural Food Antimicrobial Systems. Boca Raton, Florida: CRC Press. ISBN 0-8493-2047-X. 
  19. ^ Héquet A, Laffitte V, Simon L, De Sousa-Caetano D, Thomas C, Fremaux C, Berjeaud JM (2007). "Characterization of new bacteriocinogenic lactic acid bacteria isolated using a medium designed to simulate inhibition of Listeria by Lactobacillus sakei 2512 on meat". Int. J. Food Microbiol. 113 (1): 67–74. PMID 16997410. doi:10.1016/j.ijfoodmicro.2006.07.016. 
  20. ^ Aasen IM, Markussen S, Møretrø T, Katla T, Axelsson L, Naterstad K (2003). "Interactions of the bacteriocins sakacin P and nisin with food constituents". Int. J. Food Microbiol. 87 (1–2): 35–43. PMID 12927705. doi:10.1016/S0168-1605(03)00047-3. 
  21. ^ Cocolin L, Rantsiou K (2007). "Sequencing and expression analysis of sakacin genes in Lactobacillus curvatus strains". Appl. Microbiol. Biotechnol. 76 (6): 1403–1411. PMID 17690878. doi:10.1007/s00253-007-1120-8. 
  22. ^ Jofré A, Garriga M, Aymerich T (2007). "Inhibition of Listeria monocytogenes in cooked ham through active packaging with natural antimicrobials and high-pressure processing". J. Food Prot. 70 (11): 2498–502. PMID 18044426. 
  23. ^ Katla T, Møretrø T, Sveen I, Aasen IM, Axelsson L, Rørvik LM, Naterstad K (2002). "Inhibition of Listeria monocytogenes in chicken cold cuts by addition of sakacin P and sakacin P-producing Lactobacillus sakei". J. Appl. Microbiol. 93 (2): 191–196. PMID 12147066. doi:10.1046/j.1365-2672.2002.01675.x.