Bioaccessibility and Bioavailability of ACE Inhibitory Peptides from Fermented Milk with Lactococcus lactis NRRL B-50571 after an Ex Vivo Absorption Model

The present study aimed to determine the bioaccessibilityand bioavailabilityof peptide fractions with angiotensin-converting enzyme inhibition(ACEI) from fermented milk with Lactococcus lactis NRRL B-50571 (FM-571) after being subjected to simulated gastrointestinaldigestion (SGD) and an ex vivo absorption model. Results showed thatACEI increased (p < 0.05) after SGD and decreased(p < 0.05) after absorption. Conversely, the IC50 decreased (p < 0.05) after SGD and afterabsorption. Moreover, peptide abundance increased (p < 0.05) after SGD, indicating augmented bioaccessibility. Thereafter,peptide abundance decreased (p < 0.05) after absorption,resulting in 1.36 & PLUSMN; 0.1% of peptide bioavailability. Furthermore,RP-HPLC collected fractions from the serosal compartment exhibitedthe lowest IC50. 113 peptides were identified in the serosalcompartment, from which 14 bioavailable peptides showed high bindingpotential to ACE after in silico analysis. Henceforth, these resultssuggest that novel peptides derived from FM-571 with ACEI were bioavailable.