Isolation, Purification and Characterization of Ethyl Earbamate Degrading Enzyme from Metschnikowia and Its Effect on Wine Aroma

In order to study the properties of Ethyl Carbamate (EC) enzyme produced by Metschnikowia, the EC enzyme was separated and purified by ammonium sulfate salting out and ion exchange chromatography, and the enzymatic properties of the purified EC enzyme were analyzed. The results showed that the activity of EC enzyme after purification was about 1.2 times higher than that before purification. The optimal reaction temperature of the purified EC enzyme was 35 ℃, and the thermal stability was strong between 25 and 45 ℃. The optimal pH was 5.5, and the enzyme had strong stability at pH5~6, that was, the acid stability was strong, and the alkali stability was poor. When the volume fraction of ethanol was 12%~14%, EC enzyme still had some enzyme activity. The substrate specificity results showed that the EC enzyme had a high degradation ability on EC and its precursor (urea), and had no significant effect on the volatile flavor substances of the finished wine.