Abstract
Collagen peptides (CP) have been used as functional foods for enhancing skin and joint health. Further degradation of CP results in peptide sizes small enough to enter the bloodstream following absorption in the small intestine. We examined the effects of food matrices on CP degradation into short chain peptides and absorption efficiency after ingestion. Changes to hydroxyproline (Hyp)-containing peptide levels in CP after yogurt fermentation and in human plasma by co-ingestion of CP and yogurt, with or without fermentation, were evaluated by liquid chromatography-mass spectrometry (LC-MS). The fermentation of CP with yogurt resulted in the significant degradation of CP into several Hyp-containing peptides such as Ala-Hyp, Leu-Hyp, Phe-Hyp, Ala-Hyp-Gly, and Leu-Hyp-Gly. CP ingestion after yogurt fermentation significantly increased the plasma concentrations of Phe-Hyp, cyclo(Ala-Hyp), and cyclo(Pro-Hyp) compared to water-based CP ingestion. The co-ingestion of CP and yogurt without fermentation significantly increased the plasma levels of Ala-Hyp, Phe-Hyp, Ala-Hyp-Gly, Leu-Hyp-Gly, Pro-Hyp-Gly, cyclo(Ala-Hyp), cyclo(Glu-Hyp), and cyclo(Pro-Hyp). Overall, the co-ingestion of CP and yogurt with or without fermentation significantly enhanced the absorption of CP-derived peptides, represented by the high Cmax and area under the curve per 1 h (AUC, nmol/h·mL) of Hyp-containing peptides. These results suggest that, in addition to increasing short chain Hyp-containing peptide levels via fermentation, yogurt matrices containing milk-derived peptides and/or lactic acid bacteria-derived peptidases may influence the efficient absorption of CP-derived peptides into human blood.
Highlights
Collagen is a major protein of the extracellular matrix in various connective tissues
The samples were reconstituted with 0.1 % formic acid, and the Hyp-containing peptides were analyzed by liquid chromatography-mass spectrometry (LC-MS) in multiple reaction monitoring (MRM) mode, as described above
We demonstrated that lactic acid bacteria in yogurt could produce short chain Hyp-containing peptides from Collagen peptides (CP) in “yogurt-fermented CP” samples and that yogurt enhanced the levels of CP-derived peptides in human blood
Summary
Collagen is a major protein of the extracellular matrix in various connective tissues. We showed that cyclo(Pro-Hyp), a major component of food-derived cyclic peptides, was more effective at enhancing the growth rate of mouse skin fibroblasts than Pro-Hyp [13] Based on these in vivo and in vitro studies, linear or cyclic Hyp-containing di- and tripeptides are expected to accumulate in the bloodstream after the ingestion of CP and subsequently regulate the functions of target cells in the skin and joint tissues. Walrand et al have demonstrated that the co-ingestion of fermented milk and CP could increase the plasma concentration of collagen-specific amino acids, especially proline (Pro) [17] They suggested that milk-derived peptides in fermented milk products might affect the absorption of collagen-derived amino acids in the small intestine. Hyp-containing peptides in mouse blood after oral administration [19] These studies suggest that food-derived enzymes can produce small peptides and enhance the absorption of food-derived peptides in human blood after ingestion. We evaluated the concentration of Hyp-containing di- and tripeptides in human blood after the co-ingestion of CP with or without yogurt fermentation
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