CAPILLARY ELECTROPHORETIC ANALYSIS OF WINE PROTEINS - MODIFICATIONS DURING THE MANUFACTURE OF SPARKLING WINES

This paper reports a new electrophoretic method for the analysis of wi ne proteins. The method used for protein isolation and concentration w as dialysis followed by lyophilization. Electrophoretic separation was carried out on an uncoated fused silica capillary of 57 cm total leng th, 50 cm effective length, and 75 mu m i.d., using 100 mM tris(hydrox ymethyl)aminomethane (Tris)-HCl, pH 8.0, at 12 kV. Detection was at 21 4 nm. The protein fractions of sparkling wines after 3, 6, 9, 12, 15, 18, and 24 months of aging on yeast lees and of the must and the base wine from which they originated were studied. Eight peaks were separat ed in the must. During the first fermentation, both the intensity and the number of peaks were lower. In the first months of aging with yeas t another reduction in the intensity of the peaks was observed, althou gh new peaks appeared, probably corresponding to polypeptide forms rel eased by the yeast. These results were compared with those achieved by native-PAGE.