Abstract
Model system experiments were carried out to determine if the binding of haze-active (HA) polyphenols to polyvinylpolypyrrolidone (PVPP) resembles the binding of HA polyphenols to HA proteins. Gallic acid and methyl gallate were shown to be “single-ended” polyphenols; these compounds can bind to one HA protein molecule, but they cannot cross-link to another to develop haze. Single-ended polyphenols can interfere with haze formation under certain conditions, apparently by blocking the access of an HA polyphenol to sites of attachment on HA proteins. Single-ended polyphenols were bound by PVPP and removed from solution. Single-ended polyphenols produced chromic shifts when they bound to polyproline and to soluble polyvinylpyrrolidone (PVP). Both polyproline (a model of an HA protein) and soluble PVP formed much more haze with catechin than with epicatechin under some conditions. These findings suggest that the mechanisms by which HA polyphenols attach to PVPP and HA protein are similar, but not identical.
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