Milk proteins for delivery of food micronutrients
Polyphenol-milk protein conjugation
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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. Mil...
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.
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