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Journal of Environmental and Public Health
Volume 2010, Article ID 986460, 8 pages
Research Article

Partial Purification and Characterization of the Mode of Action of Enterocin S37: A Bacteriocin Produced by Enterococcus faecalis S37 Isolated from Poultry Feces

1ONIRIS. Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique, Rue de la Géraudière, BP 82225, 44322 Nantes Cedex 3, France
2UR 1268 Biopolymères Interactions Assemblages, équipe Fonctions et Interactions des Protéines Laitières, INRA, BP 71627, 44316 Nantes Cedex 3, France
3Department of Research into Sanitary Risks and Biotechnology of Reproduction, UPSP 5301 DGER, Nantes-Atlantic National College of Veterinary Medicine, Food Science and Engineering (ONIRIS), ONIRIS La Chantrerie, BP 40706, 44307 Nantes Cedex 03, France

Received 12 May 2010; Accepted 22 June 2010

Academic Editor: David O. Carpenter

Copyright © 2010 Y. Belguesmia et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The aim of this research was to purify and characterize the mode of action of enterocin S37, a bacteriocin produced by Enterococcus faecalis S37, a strain recently isolated from the chicken feces. Enterocin S37 has a molecular weight comprised between 4 and 5 kDa. It remained active after 1 h at 8 0 o C and at pH values ranging from 4.0 to 9.0. Furthermore, cell-free supernatant of Enterococcus faecalis S37 and purified enterocin S37 were active against Gram-positive bacteria including Listeria monocytogenes EGDe, L. innocua F, Enterococcus faecalis JH2-2, and Lactobacillus brevis F145. The purification of enterocin S37 was performed by ammonium sulfate precipitation followed up by hydrophobic-interaction chromatography procedures. Treatment of enterocin S37 with proteinase K, 𝛼 -chymotrypsin, and papain confirmed its proteinaceous nature, while its treatment with lysozyme and lipase resulted in no alteration of activity. Enterocin S37 is hydrophobic, anti-Listeria and likely acting by depletion of intracellular K+ ions upon action on K A T P channels. This study contributed to gain more insights into the mode of action of enterocins.