The extent of the change in salivary protein characteristics after repeated stimulations was shown to be correlated to differences in perceived astringency. Salivary characteristics of 77 subjects were compared after masticatory (S1) and taste/masticatory (S2) stimulations. The variations (S2 minus S1) of protein concentration and saliva haze-forming capacity (HFC) were used to define 3 subject groups: low responding (LR, n = 20), medium responding (MR, n = 37), and high responding (HR, n = 20). Salivary protein concentration did not change in LR subjects; decreased a little, but significantly, in MR subjects; and strongly decreased in HR subjects. After S2, HFC increased in LR subjects, slightly decreased in MR subjects, and strongly decreased in HR subjects. Salivary protein electrophoresis patterns for HR and LR subjects were analyzed. No significant modifications of glycosylated proline-rich proteins (PRPs), PRPs, and amylases and a slight decrease in cystatins and histatins were found when S2 and S1 samples were compared in LR subjects, whereas HR subjects showed a strong decrease in all the above proteins after S2. Significant modifications of mucins were not found. Tannic acid (TA, 3 g/L) astringency ratings after S1 from HR subjects were significantly higher than those from the other 2 groups, whereas no differences were found comparing LR and MR ratings. The “carryover” effect due to 4 sequential exposures to TA samples (1.4 g/L) was observed in both HR and MR groups, whereas no significant astringency rating variation was found in the LR group. The results support the inhibiting role of proteins with strong phenol-binding activity on astringency elicitation. Individual physiological variations of parotid gland functionality might account for differences in sensitivity to astringent phenolic stimuli.

Fining treatments involve the addition of a substance or a mixture to wine, and are generally carried out in order to clarify, stabilize or modify the wine’s organoleptic characteristics. Usually these fining agents will bind the target compound(s) to form insoluble aggregates that are subsequently removed from the wine. The main reasons to perform wine fining treatments are to carry out wine clarification, stabilization and to remove phenolic compounds imparting unwanted sensory characteristics on the wine, which is an operation that often relies on the use of animal proteins, such as casein, gelatin, egg and fish proteins. However, due to the allergenic potential of these animal proteins, there is an increasing interest in developing alternative solutions including the use of fining proteins extracted from plants (e.g., proteins from cereals, grape seeds, potatoes, legumes, etc.), and non-proteinaceous plant-based substances (e.g., cell wall polysaccharides and pomace materials). In this article, the state of the art alternative fining agents of plant origins are reviewed for the first time, including considerations of their organoleptic and technological effects on wine, and of the allergenic risks that they can pose for consumers.

Background and Aims: Grape proteins are responsible for the appearance of haziness in white wines during storage after bottling. However, only a few studies have approached the analysis of the fate of must proteins throughout the alcoholic fermentation. This study aimed to systematically investigate the daily variations in protein type and content during the fermentation in order to understand its influence on hazing potential and to attain some basic information to improve the practical management of grape proteins involved in the hazing of white wines.\ud Methods and Results: The evolution of total soluble protein and individual protein fractions was studied in samples taken before, during and after alcoholic fermentation of a white grape must. The results were then related to variations in protein instability as measured by the heat test. Both the quantity of soluble protein and the protein instability increased during fermentation and then decreased after one month storage of the wine. Protein composition did not vary during fermentation as assessed by SDS-PAGE and anion exchange chromatography (AEC). However, variations in the relative proportions of the six protein fractions obtainable by AEC were noted in the different samples. The contribution of each AEC protein fraction to wine instability was determined by considering both the intrinsic instability and the relative quantity of each of the individual protein fractions in the wine. It was demonstrated that the grape thaumatin-like protein VVTL1, as identified by mass spectrometry, showed the largest increase during fermentation and accounted for almost 40% of the heat induced haze of the final wine. Moreover, the decreased protein instability noted after one month storage of the wine could be attributed to the stabilizing effect of polysaccharides released by the yeast cells.\ud Conclusions: The quantity and relative proportion of soluble proteins vary during and after the alcoholic fermentation, as does their heat instability in wine. Grape VVTL1, constituting a large proportion of the total proteins in wine, seems to play a major role in protein haze formation. The release of yeast polysaccharides is related to an increased heat-stability of total wine protein, despite the increase in the relative proportion of their most unstable component VVTL1. Therefore, the hazing potential of a white wine seems to be affected by variations in the relative proportions of its macromolecular components occurring in the early stages of winemaking.\ud Significance of the Study: This study addressed for the first time the issue of the protein changing during the fermentation of white wine. The results obtained here offer useful information to aid understanding of the contribution of individual proteins to white wine instability, which can in turn be applied for the improvement of the winemaking process