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Tuning the ph during the fermentation has a strong effect on the wine protein composition and the stability of the resulting white wines

3 Institut Agro, Montpellier SupAgro

Email contact:  celine.poncet-legrand[@]


AIM: Previous results have shown the impact of the pH on the stability of white wine proteins. In a context of global warming that implies increases in ethanol content and pH, we wanted to compare for the same initial must (given composition in polysaccharides, polyphenols, ions, ¼) the impact of the pH on the protein composition after fermentation. Several white wine varieties were considered.

METHODS: Vinifications were carried out using musts from Sauvignon, Muscat, Sylvaner, Riesling, Gewurztrminer , and Pinot Gris). The pH of the initial musts was adjusted to 3.0, 3.3, 3.6 and 3.9. For each wine thus obtained, heat tests (heating at 40°C for 4 hours) were carried out and proteins were analyzed and quantified by gel electrophoresis.

RESULTS: On the whole, protein concentrations in wines decreased during fermentation. However, this decrease was more marked for the lowest pH (3.0 and 3.3), as well as for some proteins (chitinases, b-glucanases). Thus the total concentration of proteins was higher at pH 3.9. The turbidity measured after heat tests evolved differently: a maximum was observed at pH 3.6 in the present experimental conditions (40°C- 4h).

CONCLUSIONS: This study confirms that the pH has a decisive impact on the protein composition in white wines, with higher pH favoring their conformational stability during winemaking. However, haze formation due to heat-induced denaturation of proteins is higher at high pH. This trend was observed whatever the studied variety, but with more or less haze intensities. This indicated also an impact of non-protein compounds, whose composition strongly depends on the grape variety.



Dufrechou, M., Poncet-Legrand, C., Sauvage, F.-X. X., & Vernhet, A. (2012). Stability of white wine proteins: combined effect of pH, ionic strength, and temperature on their aggregation. Journal of Agricultural and Food Chemistry, 60(5), 1308–1319.

Dufrechou, M., Vernhet, A., Roblin, P., Sauvage, F.-X., & Poncet-Legrand, C. (2013). White wine proteins: how does the pH affect their conformation at room temperature? Langmuir?: The ACS Journal of Surfaces and Colloids, 29(33), 10475–10482.

Vernhet, A., Meistermann, E., Cottereau, P., Charrier, F., Chemardin, P., & Poncet-Legrand, C. (2020). Wine Thermosensitive Proteins Adsorb First and Better on Bentonite during Fining: Practical Implications and Proposition of Alternative Heat Tests. Journal of Agricultural and Food Chemistry.

Published on 06/17/2018
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