Charged casein-derived oligopeptides competitively inhibit the transport of a reporter oligopeptide by Lactococcus lactis

J Appl Microbiol. 2003;94(5):900-7. doi: 10.1046/j.1365-2672.2003.01922.x.

Abstract

Aim: To study the effect of casein-derived peptides, accumulated during growth of Lactococcus lactis in milk, on its oligopeptide transport (Opp) function.

Methods and results: This effect was estimated by analysing the ability of casein-derived peptides to compete for the transport of a reporter peptide by whole L. lactis cells. The transport of the reported peptide was monitored by determining the intracellular concentrations of the corresponding amino acids by means of reverse-phase high-performance liquid chromatography (HPLC). Uptake of the reporter peptide was competitively inhibited by casein-derived peptides. The competition was only because of charged casein-derived peptides, including anionic peptides. The design of specific pure peptides made it possible to evidence for a positive (or negative) influence exerted by the positively (or negatively) charged side chain of the N-terminal amino acid on the competition.

Conclusions: Charged casein-derived peptides impaired the oligopeptide transport function of L. lactis.

Significance and impact of the study: These results demonstrate an inhibition of Opp when too many peptides are produced by the proteinase. Peptide transport by Opp therefore represents a bottleneck for increasing the growth rate of L. lactis in milk.

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Bacteriological Techniques / methods
  • Binding, Competitive
  • Biological Transport
  • Carrier Proteins / metabolism
  • Caseins / metabolism*
  • Food Microbiology
  • Lactococcus lactis / growth & development
  • Lactococcus lactis / metabolism*
  • Lipoproteins / metabolism
  • Milk / microbiology*
  • Oligopeptides / metabolism*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Caseins
  • Lipoproteins
  • Oligopeptides
  • oligopeptide-binding protein, bacteria