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Updated: Mar 14, 2026

Free Radicals in Chemical Biology: from Chemical Behavior to Biomarker Development
Published on: April 15, 2013
Spectroscopy reveals that ethyl esters interact with proteins in wine
Mattia Di Gaspero1, Paolo Ruzza2, Rohanah Hussain3
1Department of Land, Environment, Agriculture and Forestry (TESAf), University of Padua, Viale dell'Università, 16, 35020 Legnaro (PD), Italy.
Bentonite fining in winemaking can reduce wine aroma by removing proteins. This study shows wine proteins interact with aroma compounds, suggesting indirect aroma loss during fining.
Area of Science:
- Oenology
- Food Chemistry
- Protein Chemistry
Background:
- Wine aroma is crucial for quality and can be negatively impacted by fining agents like bentonite.
- Bentonite treatment can lead to protein removal, potentially affecting aroma compounds like ethyl esters.
- Understanding protein-aroma compound interactions is key to preserving wine quality.
Purpose of the Study:
- To investigate the interaction between wine proteins and ethyl esters.
- To determine the effect of ethyl esters on the secondary structure and stability of a wine Thaumatin-like protein (VVTL1).
Main Methods:
- Purification of VVTL1 protein from wine.
- Analysis of VVTL1 secondary structure and stability using Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy.
- Assessment of the impact of selected ethyl esters on VVTL1.
Main Results:
- The secondary structure of VVTL1 was not significantly altered by the presence of ethyl esters.
- VVTL1 stability was enhanced by ethyl-octanoate, ethyl-decanoate, and ethyl-dodecanoate.
- VVTL1 stability was reduced by ethyl-hexanoate, indicating specific interactions.
Conclusions:
- Wine proteins, such as VVTL1, interact with certain ethyl esters.
- These interactions suggest that bentonite's protein removal can indirectly lead to the loss of associated aroma compounds.
- This finding provides insight into aroma impairment during wine processing.
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