Production of nisin-like bacteriocins by Lactococcus lactis strains isolated from vegetables

J Basic Microbiol. 1997;37(3):187-96. doi: 10.1002/jobm.3620370307.

Abstract

Four bacteriocin producing lactic acid bacteria isolated from vegetables were identified as Lactococcus lactis strains on the basis of physiological and biochemical characteristics, carbohydrate fermentation patterns and analysis of total soluble protein pattern by SDS PAGE. The bacteriocins had a wide spectrum of activity as antagonism was detected not only towards a variety of lactic acid bacteria, but also to Staphylococcus aureus and Listeria monocytogenes. These bacteriocins were resistant to heating at 121 degree C for 15 minutes and showed highest activity at low pH (<5.0). They were inactivated by the proteolytic enzymes alpha-chymotrypsin and proteinase K, but not by lipase, alpha-amylase, catalase or lysozyme. These bacteriocinogenic Lactococcus strains were all immune to the bacteriocins produced as well as to commercial nisin. Bacteriocin producer culture supernatants showed a high degree (70 or 100%) of cross-reactivity in the nisin ELISA, suggesting similarity of the produced bacteriocins to nisin. The potential application of bacteriocin producing lactococci of vegetable origin for safety assurance of vegetable foods and controlling vegetable fermentations is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / biosynthesis*
  • Antibiosis
  • Bacterial Typing Techniques
  • Bacteriocins / biosynthesis*
  • Culture Media
  • Endopeptidases / metabolism
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Lactococcus lactis / isolation & purification
  • Lactococcus lactis / metabolism*
  • Microbial Sensitivity Tests
  • Nisin / biosynthesis*
  • Vegetables / microbiology*

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Culture Media
  • Nisin
  • Endopeptidases