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In this book, the binding efficacies of several antioxidant polyphenols resveratrol, genistein and curcumin with milk proteins, beta-lactoglobulin, -casein and beta-casein were compared in aqueous solution at physiological conditions. Structural models showed that polyphenol bindings are via hydrophilic, hydrophobic and H-bonding contacts with curcumin forming more stable conjugates. The order of protein binding was beta-LG>beta-casein> -casein. The loading efficacy was 30 to 50% for these polyphenol-protein conjugates. Polyphenol binding induced major alterations of protein conformations.…mehr

Produktbeschreibung
In this book, the binding efficacies of several antioxidant polyphenols resveratrol, genistein and curcumin with milk proteins, beta-lactoglobulin, -casein and beta-casein were compared in aqueous solution at physiological conditions. Structural models showed that polyphenol bindings are via hydrophilic, hydrophobic and H-bonding contacts with curcumin forming more stable conjugates. The order of protein binding was beta-LG>beta-casein> -casein. The loading efficacy was 30 to 50% for these polyphenol-protein conjugates. Polyphenol binding induced major alterations of protein conformations. Milk proteins are capable of delivery of these dietary polyphenols in vitro.
Autorenporträt
H.A. Tajmir-Riahi : Professeur de recherche à l'Université du Québec à Trois-Rivières (UQTR), Canada. Il a été admis au Cercle d'excellence de l'Université du Québec en 2017. Il a publié 340 articles dans des revues internationales, 6 livres et 15 chapitres de livres. Intérêt de recherche : interactions des médicaments avec l'ADN, l'ARN et les protéines ; délivrance de médicaments.