Milchproteine zur Bereitstellung von Mikronährstoffen in Lebensmitteln
Polyphenol-Milchprotein-Konjugation
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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. Strukturelle Modelle zeigten, dass Polyphenolbindungen über hydrophile, hydrophobe und H-bindende Kontakte verlaufen, wobei Curcumin stabilere Konjugate bildet. Die Reihenfolge der Proteinbindungen war beta-LG>beta-casein> -casein. The loading efficacy was 30 to 50% for these polyphenol-protein conjugates. Polyphenol binding induced major alterations of protein ...
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. Strukturelle Modelle zeigten, dass Polyphenolbindungen über hydrophile, hydrophobe und H-bindende Kontakte verlaufen, wobei Curcumin stabilere Konjugate bildet. Die Reihenfolge der Proteinbindungen war 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. Milchproteine sind in der Lage, diese diätetischen Polyphenole in vitro abzugeben.
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