Interaction of phenolic compounds with bovine serum albumin (BSA) and α-amylase and their relationship to astringency perception

The ability of grape seed extracts to bind to bovine serum albumin (BSA) and α-amylase was studied by fluorescence quenching of protein intrinsic fluorescence and nephelometry. The influence of grape seed ripeness on astringency was also evaluated. From the spectra obtained, the modified Sterm–Volmer (Kapp) and the bimolecular quenching constants were calculated. Results showed that grape seed extracts had good affinity for proteins. The association strength of tannin–protein interactions varied with changes in tannin structure associated with the degree of ripeness affecting the binding/quenching process. In all cases studied, higher values of Kapp were obtained in samples at harvest which have greater ability to bind to proteins than have samples at post-veraison time. Nephelometric assays show the same trend as do fluorescence quenching studies. A possible explanation for this is that, as seeds ripen, their tannins increase in molecular mass, which relates to an increase in hydrophobicity of the molecules, and this increases protein affinity. However, that is contrary to the reported decrease in astringency of grape seeds during maturity. This indicates that tannin–protein interactions are not the only explanation for the complex sensations of astringency of grape seeds.

► Grape seed extracts present good affinity to bind to proteins. ► Association strength of tannin–protein interactions changes with tannin structure. ► Samples at harvest have higher ability to bind to proteins than at post-veraison. ► Tannin–protein interactions are not the only explanation for the astringency.