Influence of the reducing environment in the misfolding of wine proteins.

Abstract

While proteins are present in wine at low concentration, and are largely associated with undesirable haze formation in white wines, certain types or fractions make direct and indirect contributions to sensory quality and physical stability. The proteins found in wine represent a small subclass of the total pool of grape proteins that remain soluble in the non-physiological conditions of the wine matrix which is characterised by the presence of alcohol, high acidity, and relatively high levels of phenolic compounds. Although initially stable in these conditions, during storage of white and rosé wines proteins undergo changes leading to haze formation which is considered one of the most relevant non-microbiological defects, and which makes the wine commercially unacceptable. This phenomenon involves the two most abundant proteins present in wines: thaumatin-like proteins and chitinases, both belonging to pathogenesis-related proteins of the grape berry. Haze formation is often triggered by thermal fluctuations occurring during storage of white wines, although the presence of other non-protein-related factors seems to be necessary. Here, we review the characteristics of these two protein families and the factors that influence their solubility with a focus on the disulfide bonds reduction as a possible trigger for the onset of their aggregation.