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Spectroscopy reveals that ethyl esters interact with proteins in wine.

Identifieur interne : 000076 ( Main/Exploration ); précédent : 000075; suivant : 000077

Spectroscopy reveals that ethyl esters interact with proteins in wine.

Auteurs : Mattia Di Gaspero [Italie] ; Paolo Ruzza [Italie] ; Rohanah Hussain [Royaume-Uni] ; Simone Vincenzi [Italie] ; Barbara Biondi [Italie] ; Diana Gazzola [Italie] ; Giuliano Siligardi [Royaume-Uni] ; Andrea Curioni [Italie]

Source :

RBID : pubmed:27664648

Descripteurs français

English descriptors

Abstract

Impairment of wine aroma after vinification is frequently associated to bentonite treatments and this can be the result of protein removal, as recently demonstrated for ethyl esters. To evaluate the existence of an interaction between wine proteins and ethyl esters, the effects induced by these fermentative aroma compounds on the secondary structure and stability of VVTL1, a Thaumatin-like protein purified from wine, was analyzed by Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. The secondary structure of wine VVTL1 was not strongly affected by the presence of selected ethyl esters. In contrast, VVTL1 stability was slightly increased by the addition of ethyl-octanoate, -decanoate and -dodecanoate, but decreased by ethyl-hexanoate. This indicates the existence of an interaction between VVTL1 and at least some aroma compounds produced during fermentation. The data suggest that proteins removal from wine by bentonite can result in indirect removal of at least some aroma compounds associated with them.

DOI: 10.1016/j.foodchem.2016.08.133
PubMed: 27664648


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Impairment of wine aroma after vinification is frequently associated to bentonite treatments and this can be the result of protein removal, as recently demonstrated for ethyl esters. To evaluate the existence of an interaction between wine proteins and ethyl esters, the effects induced by these fermentative aroma compounds on the secondary structure and stability of VVTL1, a Thaumatin-like protein purified from wine, was analyzed by Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. The secondary structure of wine VVTL1 was not strongly affected by the presence of selected ethyl esters. In contrast, VVTL1 stability was slightly increased by the addition of ethyl-octanoate, -decanoate and -dodecanoate, but decreased by ethyl-hexanoate. This indicates the existence of an interaction between VVTL1 and at least some aroma compounds produced during fermentation. The data suggest that proteins removal from wine by bentonite can result in indirect removal of at least some aroma compounds associated with them. </div>
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