The loss of wine aroma is generally associated to a direct binding of aroma compounds with bentonite. Recently it has been demonstrated that ethyl esters removal by bentonite was increased in the presence of proteins, suggesting the existence of additional interactions. In order to understand if there is a direct association between ethyl esters and wine proteins, the effects induced by these volatile molecules on VVTL1 structure were analyzed by Synchrotron Radiation Circular Dichroism (SRCD) and fluorescence. Although VVTL1 was not strongly affected by ethyl esters and the tryptophan residues were not involved, the data indicate the existence of an interaction between ethyl esters and the proteins.
ARE THE ETHYL ESTERS ABLE TO INTERACT WITH WINE PROTEINS?
DI GASPERO, MATTIA;RUZZA, PAOLO;GAZZOLA, DIANA;BIONDI, BARBARA;VINCENZI, SIMONE;CURIONI, ANDREA;
2016
Abstract
The loss of wine aroma is generally associated to a direct binding of aroma compounds with bentonite. Recently it has been demonstrated that ethyl esters removal by bentonite was increased in the presence of proteins, suggesting the existence of additional interactions. In order to understand if there is a direct association between ethyl esters and wine proteins, the effects induced by these volatile molecules on VVTL1 structure were analyzed by Synchrotron Radiation Circular Dichroism (SRCD) and fluorescence. Although VVTL1 was not strongly affected by ethyl esters and the tryptophan residues were not involved, the data indicate the existence of an interaction between ethyl esters and the proteins.
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