Identification and Analysis of ACE-Inhibitory Peptides Derived from Milk Fermented by .

Inhibition of angiotensin I-converting enzyme (ACE) activity is an effective way to treat hypertension. In the present study, the ability to produce ACE-inhibitory peptides during fermentation of skimmed milk by the M3 strain was evaluated, and the inhibitory mechanism and stability were studied by bioinformatics analysis. The results showed that the ACE inhibition activity of fermented milk was 71.94 ± 1.39%. After digestion with gastric juice and pancreatic juice, the ACE inhibitory activities of the fermented milk were 78.40 ± 1.93 and 74.96 ± 1.73%, respectively. After the fermented milk was purified using ultrafiltration and gel chromatography, 11 peptides from milk proteins were identified and sequenced by Nano LC-MS/MS. Molecular docking displayed that peptide PWIQPK had a high affinity, with ACE showing a binding energy of -6.10 kcal/mol. Hydrogen bonds were formed between PWIQPK and Glu384 in the S1 active pocket of ACE and Asp358. In addition, van der Waals forces were observed. proteolysis suggested that PWIQPK could resist the digestion of pepsin and trypsin, indicating that it is relatively stable in the digestive tract. All results indicate that milk fermented by M3 has the potential to be used as a functional food having antihypertensive effects.