Abstract
Tannin–tannin and tannin–protein interactions in water–ethanol solvent mixtures arestudied in the context of red wine tasting. While tannin self-aggregation is relevant for thevisual aspect of wine tasting (limpidity and related colloidal phenomena), tannin affinitiesfor salivary proline-rich proteins is fundamental for a wide spectrum of organolepticproperties related to astringency.Tannin–tannin interactions are analyzed in water–ethanol wine-like solvents and theprecipitation map is constructed for a typical grape tannin. The interaction betweentannins and human salivary proline-rich proteins (PRP) are investigated in the frameworkof the shell model for micellization, known for describing tannin-induced aggregation ofβ-casein. Tannin-assisted micellization and compaction of proteins observed by SAXS aredescribed quantitatively and discussed in the case of astringency.
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