Artigo Revisado por pares

Interactions of tea tannins and condensed tannins with proteins

2009; Elsevier BV; Volume: 51; Issue: 2 Linguagem: Inglês

10.1016/j.jpba.2009.05.035

ISSN

1873-264X

Autores

Richard A. Frazier, E. R. Deaville, Rebecca Green, Elisabetta Stringano, Ian Willoughby, John Plant, I. Mueller‐Harvey,

Tópico(s)

Antioxidant Activity and Oxidative Stress

Resumo

Binding parameters for the interactions of four types of tannins: tea catechins, grape seed proanthocyanidins, mimosa 5-deoxy proanthocyanidins, and sorghum procyanidins (mDP=17), with gelatin and bovine serum albumin (BSA) have been determined from isothermal titration calorimetry data. Equilibrium binding constants determined for the interaction with gelatin were in the range 10(4) to 10(6) M(-1) and in the order: sorghum procyanidins > grape seed proanthocyanidins > mimosa 5-deoxy proanthocyanidins > tea catechins. Interaction with BSA was generally weaker, with equilibrium binding constants of < or =10(3)M(-1) for grape seed proanthocyanidins, mimosa 5-deoxy proanthocyanidins and tea catechins, and 10(4)M(-1) for the sorghum procyanidins. In all cases the interactions with proteins were exothermic and involved multiple binding sites on the protein. The data are discussed in relation to the structures and the known nutritional effects of the condensed tannins.

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