Screening, Characterization, and Mechanistic Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Milk Fermented with Lactobacillus delbrueckii QS306 with and without Ultrahigh-Pressure Treatment.

Abstract

In this study, the peptides in milk fermented with Lactobacillus delbrueckii QS306 with and without ultrahigh-pressure treatment were identified using UPLC-Q-exactive-HF-X-MS/MS. In total, 27 novel pentapeptides with potential angiotensin converting enzyme inhibitory (ACEI) activity were screened via bioinformatic analysis, and the activities of seven novel pentapeptides were assessed. Among them, HLPLP, PYPQR, and VAPFP exhibited better IC50 values. Stability assessment via in vitro simulation revealed that the three pentapeptides were significantly reduced (P < 0.05) during digestion but exhibited 85% activity after digestion. HLPLP was a competitive inhibitor, while PYPQR and VAPFP were noncompetitive inhibitors of ACE. Molecular docking indicated that the three peptides could stably bind to ACE. Molecular dynamics (MD) simulation and activity verification indicated that PYPQR and VAPFP had better stability and activity. This study demonstrated that novel ACEI pentapeptides in milk fermented with L. delbrueckii QS306 with and without ultrahigh-pressure treatment could be considered promising candidates for controlling hypertension.