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Isolation and Purification of Two Bacteriocins 3D Produced by Enterococcus faecium with Inhibitory Activity Against Listeria monocytogenes

Author:
Bayoub, Kaoutar, Mardad, Ilham, Ammar, Emna, Serrano, Aurelio, Soukri, Abdelaziz
Source:
Current microbiology 2011 v.62 no.2 pp. 479-485
ISSN:
0343-8651
Subject:
Enterococcus faecium, Listeria monocytogenes, antibacterial properties, antimicrobial agents, bacteriocins, catalase, heat stability, mass spectrometry, pH, pepsin, peptides, reversed-phase high performance liquid chromatography, temperature, trypsin
Abstract:
Strain 3D, isolated from fermented traditional Moroccan dairy product, and identified as Enterococcus faecium, was studied for its capability to produce two bacteriocins acting against Listeria monocytogenes. Bacteriocins 3 Da and 3Db were heat stable inactivated by proteinase K, pepsin, and trypsin but not when treated with catalase. The evidenced bacteriocins were stable in a wide pH range from 2 to 11 and bactericidal activity was kept during storage at 4°C. However, the combination of temperature and pH exhibited a stability of the bacteriocins. RP-HPLC purification of the anti-microbial compounds shows two active fractions eluted at 16 and 30.5 min, respectively. Mass spectrometry analysis showed that E. faecium 3D produce two bacteriocins Enterocin 3 Da (3893.080 Da) and Enterocin 3Db (4203.350 Da). This strain is food-grade organism and its bacteriocins were heat-stable peptides at basic, neutral, and acid pH: such bacteriocins may be of interest as food preservatives.
Agid:
510891