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

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.
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https://hal.inrae.fr/hal-02674030
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Submitted on : Sunday, May 31, 2020 - 4:57:16 PM
Last modification on : Monday, April 4, 2022 - 2:30:04 PM

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Sandra Hélinck, P. Charbonnel, Catherine Foucaud-Scheunemann, J.C. Piard, Vincent Juillard. Charged casein-derived oligopeptides competitively inhibit the transport of a reporter oligopeptide by Lactococcus lactis. Journal of Applied Microbiology, Wiley, 2003, 94 (5), pp.900-907. ⟨10.1046/j.1365-2672.2003.01922.x⟩. ⟨hal-02674030⟩

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