560 C. Santos-Buelga and V. de Freitas
Some studies have been made relating specifically to astringency. Some of these
studies have been focused directly on interactions between tannins and salivary
proteins, and in the changes in saliva protein composition after interaction with
tannins. Other studies have correlated the sensorial astringency with protein-tannin
interactions using several proteins as a model such as mucin, ovalbumin, gelatin,
BSA and salivary proteins. In fact, the astringency felt when sampling different
tannin solutions can be correlated with the ability of the same tannins to precipitate
proteins.
Apart from salivary proteins, other proteins have been used in the tannin-protein
interaction studies due to some characteristics that make them similar to PRPs,
like casein, gelatin, polyproline (Jobstl et al. 2004; Calderon et al. 1968; Luck
et al. 1994; Poncet-Legrand et al. 2006; Siebert et al. 1996). Although it is not a
protein, the polymer polyvinylpolypyrrolidone as also been used in these studies
(Hagerman and Butler 1981; Laborde etal. 2006). Recently, an electronic tongue
based on protein-tannin interactions has been developed to measure astringency
(Edelmann and Lendl 2002). Despite the unquestionable importance of all these
works to understand the interaction between tannins and proteins, extrapolation to
the real context of wine sensory should be done with care.
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