Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein.
Angiotensin-I-converting enzyme (ACE) inhibitory activity of a tryptic digest of bovine alpha(S2)-casein (alpha(S2)-CN) was extensively investigated. Forty-three peptide peaks were isolated and tested. Seven casokinins (i.e. CN-derived ACE inhibitory peptides) were identified and their IC50 values were determined. Four peptides exhibited an IC50 value lower than 20 microM. Peptides alpha(S2)-CN (f174-181) and alpha(S2)-CN (f174-179) had IC50 values of 4 microM. Surprisingly, deletion of the C-terminal dipeptide of two of these casokinins did not significantly alter their inhibitory activity.
Tauzin
Jérôme
J
Laboratoire des BioSciences de l'Aliment, UC 885 INRA, Faculté des Sciences et Techniques, Université Henri Poincaré Nancy 1, Vandoeuvre-lès-Nancy, France.
Miclo
Laurent
L
Gaillard
Jean Luc
JL
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004305:Dose-Response Relationship, Drug; D006868:Hydrolysis; D010455:Peptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism*
D000806:Angiotensin-Converting Enzyme Inhibitors; D002364:Caseins; D010455:Peptides; D014357:Trypsin