Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein |
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Authors: | Tauzin Jérôme Miclo Laurent Gaillard Jean Luc |
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Institution: | Laboratoire des BioSciences de l'Aliment, UC 885 INRA, Faculté des Sciences et Techniques, Université Henri Poincaré Nancy 1, Vandoeuvre-lès-Nancy, France. |
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Abstract: | 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. |
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Keywords: | Bovine αS2-casein Angiotensin-I-converting enzyme inhibitor Tryptic hydrolysate Bioactive peptide Casokinin |
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