Skip to main content
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1995 May;61(5):1847–1852. doi: 10.1128/aem.61.5.1847-1852.1995

Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium.

S Maisnier-Patin 1, J Richard 1
PMCID: PMC167446  PMID: 7646021

Abstract

An orange cheese coryneform bacterium isolated from the surface of Gruyère of Comté and identified as Brevibacterium linens produces an antimicrobial substance designated linenscin OC2. This compound inhibits gram-positive food-borne pathogens including Staphylococcus aureus and Listeria monocytogenes but is not active against gram-negative bacteria. Linenscin OC2 caused viability loss and lysis of the test organism, Listeria innocua. Electron microscopy showed that linenscin OC2 induces protoplast formation and cell lysis. The native substance is resistant to proteolytic enzymes, heat, and organic solvents and stable over a wide range of pH. The molecular weight of the native linenscin OC2 was estimated by gel chromatography to be over 285,000. Linenscin OC2 was purified by ammonium sulfate precipitation, 2-propanol extraction, and reverse-phase chromatography. Direct detection of antimicrobial activity on a sodium dodecyl sulfate-polyacrylamide gel suggested an apparent molecular mass under 2,412 Da. Molecular mass was determined to be 1,196.7 Da by mass spectrometry. Amino acid composition analysis indicated that linenscin OC2 may contain 12 residues.

Full Text

The Full Text of this article is available as a PDF (522.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barefoot S. F., Klaenhammer T. R. Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B. Antimicrob Agents Chemother. 1984 Sep;26(3):328–334. doi: 10.1128/aac.26.3.328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  3. Farber J. M., Peterkin P. I. Listeria monocytogenes, a food-borne pathogen. Microbiol Rev. 1991 Sep;55(3):476–511. doi: 10.1128/mr.55.3.476-511.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Garcerá M. J., Elferink M. G., Driessen A. J., Konings W. N. In vitro pore-forming activity of the lantibiotic nisin. Role of protonmotive force and lipid composition. Eur J Biochem. 1993 Mar 1;212(2):417–422. doi: 10.1111/j.1432-1033.1993.tb17677.x. [DOI] [PubMed] [Google Scholar]
  5. Harding C. D., Shaw B. G. Antimicrobial activity of Leuconostoc gelidum against closely related species and Listeria monocytogenes. J Appl Bacteriol. 1990 Nov;69(5):648–654. doi: 10.1111/j.1365-2672.1990.tb01558.x. [DOI] [PubMed] [Google Scholar]
  6. Harkness R. E., Olschläger T. The biology of colicin M. FEMS Microbiol Rev. 1991 Jul;8(1):27–41. doi: 10.1111/j.1574-6968.1991.tb04955.x. [DOI] [PubMed] [Google Scholar]
  7. Hastings J. W., Sailer M., Johnson K., Roy K. L., Vederas J. C., Stiles M. E. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J Bacteriol. 1991 Dec;173(23):7491–7500. doi: 10.1128/jb.173.23.7491-7500.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hastings J. W., Stiles M. E. Antibiosis of Leuconostoc gelidum isolated from meat. J Appl Bacteriol. 1991 Feb;70(2):127–134. doi: 10.1111/j.1365-2672.1991.tb04438.x. [DOI] [PubMed] [Google Scholar]
  9. Héchard Y., Dérijard B., Letellier F., Cenatiempo Y. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides. J Gen Microbiol. 1992 Dec;138(12):2725–2731. doi: 10.1099/00221287-138-12-2725. [DOI] [PubMed] [Google Scholar]
  10. Joerger M. C., Klaenhammer T. R. Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481. J Bacteriol. 1986 Aug;167(2):439–446. doi: 10.1128/jb.167.2.439-446.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Konisky J. Colicins and other bacteriocins with established modes of action. Annu Rev Microbiol. 1982;36:125–144. doi: 10.1146/annurev.mi.36.100182.001013. [DOI] [PubMed] [Google Scholar]
  12. Pucci M. J., Vedamuthu E. R., Kunka B. S., Vandenbergh P. A. Inhibition of Listeria monocytogenes by using bacteriocin PA-1 produced by Pediococcus acidilactici PAC 1.0. Appl Environ Microbiol. 1988 Oct;54(10):2349–2353. doi: 10.1128/aem.54.10.2349-2353.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ryser E. T., Maisnier-Patin S., Gratadoux J. J., Richard J. Isolation and identification of cheese-smear bacteria inhibitory to Listeria spp. Int J Food Microbiol. 1994 Feb;21(3):237–246. doi: 10.1016/0168-1605(94)90030-2. [DOI] [PubMed] [Google Scholar]
  14. STREHLER B. L., TOTTER J. R. Firefly luminescence in the study of energy transfer mechanisms. I. Substrate and enzyme determination. Arch Biochem Biophys. 1952 Sep;40(1):28–41. doi: 10.1016/0003-9861(52)90070-2. [DOI] [PubMed] [Google Scholar]
  15. Upreti G. C., Hinsdill R. D. Production and mode of action of lactocin 27: bacteriocin from a homofermentative Lactobacillus. Antimicrob Agents Chemother. 1975 Feb;7(2):139–145. doi: 10.1128/aac.7.2.139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Valdes-Stauber N., Götz H., Busse M. Antagonistic effect of coryneform bacteria from red smear cheese against Listeria species. Int J Food Microbiol. 1991 Jun;13(2):119–130. doi: 10.1016/0168-1605(91)90054-s. [DOI] [PubMed] [Google Scholar]
  17. Valdés-Stauber N., Scherer S. Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. Appl Environ Microbiol. 1994 Oct;60(10):3809–3814. doi: 10.1128/aem.60.10.3809-3814.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Venema K., Abee T., Haandrikman A. J., Leenhouts K. J., Kok J., Konings W. N., Venema G. Mode of Action of Lactococcin B, a Thiol-Activated Bacteriocin from Lactococcus lactis. Appl Environ Microbiol. 1993 Apr;59(4):1041–1048. doi: 10.1128/aem.59.4.1041-1048.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. van Belkum M. J., Kok J., Venema G., Holo H., Nes I. F., Konings W. N., Abee T. The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner. J Bacteriol. 1991 Dec;173(24):7934–7941. doi: 10.1128/jb.173.24.7934-7941.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES