Biochemical characterization of a bacteriocin-like inhibitory substance produced by Enterococcus faecium MXVK29, isolated from Mexican traditional sausage

J Sci Food Agric. 2010 Nov;90(14):2475-81. doi: 10.1002/jsfa.4109.

Abstract

Background: Enterococci are lactic acid bacteria that can produce bacteriocins, which may offer an additional hurdle to control the growth of food-borne pathogens; moreover, these bacteriocins may have great potential as natural biopreservatives. The aim of this work was to characterize a bacteriocin-like inhibitory substance (BLIS) with antilisterial activity produced by an enterococcal strain.

Results: The bacteriogenic strain was isolated from Mexican fermented sausages and identified as Enterococcus faecium with 99% sequence similarity. Maximal activity was detected at 16 h, where bacterial growth was in middle of the stationary phase. The producer strain was not inhibited by its own antimicrobial peptide. BLIS showed a strong anti-Listeria activity and was inactivated by proteinase K. Heating (121 °C for 15 min) induced some inactivation, but thermotolerance was higher at acid pH values. The yield obtained with a pH-mediated purification process was 32.7%, showing a band with an estimated molecular weight of 3.5 kDa. Automated N-terminal Edman degradation showed the following sequence: YYGNGVTCGSHHCSVD.

Conclusion: Biochemical characteristics of BLIS produced by E. faecium MXVK29 suggested that it belongs to Class IIa of the Klaenhammer classification and could be considered as a natural food preservative, although further studies need to be performed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological
  • Amino Acid Sequence
  • Antibiosis*
  • Bacteriocins / biosynthesis*
  • Endopeptidase K / pharmacology
  • Enterococcus faecium / growth & development
  • Enterococcus faecium / metabolism*
  • Food Microbiology*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Listeria / drug effects*
  • Meat Products / microbiology*
  • Molecular Sequence Data
  • Molecular Structure
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Peptides / pharmacology*

Substances

  • Bacteriocins
  • Peptides
  • Endopeptidase K