Angiotensin I converting enzyme-inhibitory activity of bovine, ovine, and caprine kappa-casein macropeptides and their tryptic hydrolysates.
This work evaluated the angiotensin-converting enzyme (ACE)-inhibitory activities of bovine, ovine, and caprine kappa-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis / Q000378:metabolism*; D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D058870:Food, Organic; D006041:Goats; D006868:Hydrolysis; D020128:Inhibitory Concentration 50; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism*; D012756:Sheep; D013997:Time Factors; D014357:Trypsin / Q000378:metabolism
D000806:Angiotensin-Converting Enzyme Inhibitors; D002364:Caseins; D010446:Peptide Fragments; D014357:Trypsin