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Biofonctionnalités de peptides issus de caséines [alpha]s bovines : Cinétique d'hydrolyse trypsique de la caséine [alpha]s2 et activité inhibitrice de l'ECA des peptides

Abstract : [Alpha]s2-Casein is the less studied substrate to obtain bioactive peptides among the major milk proteins. After its purification by ion exchange chromatography followed by hydrophobic interactions chromatography, it was hydrolysed by trypsin and resulting peptides were identified. Their release kinetics revealed three areas having different susceptibility to proteolysis. These data and secondary structure prediction helped to define a hypothetical model of protein organisation in solution. Four tryptic peptides inhibited angiotensin-I converting enzyme (CEI) with IC50 values comprised between 4 and 15 micro M. Their sequences were confronted with others inhibitors to discuss sequence-activity relationships.
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Submitted on : Thursday, March 29, 2018 - 10:44:52 AM
Last modification on : Monday, September 14, 2020 - 2:30:57 PM

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Jérôme Tauzin. Biofonctionnalités de peptides issus de caséines [alpha]s bovines : Cinétique d'hydrolyse trypsique de la caséine [alpha]s2 et activité inhibitrice de l'ECA des peptides. Biochimie [q-bio.BM]. Université Henri Poincaré - Nancy 1, 2003. Français. ⟨NNT : 2003NAN10224⟩. ⟨tel-01746789⟩

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