PURIFICATION AND SOME PROPERTIES OF THERMOSTABLE INVERTASE FROM WINE

Abstract Invertase from a white table wine made from Semillon grapes was purified to homogeneity on polyacrylamide gel electrophoresis. The enzymatic and physicochemical properties of the enzyme were compared with those of invertase purified from Semillon grape juice. The invertases from the two sources showed similar properties, suggesting that the wine invertase originated from the juice and was stable during the vinification and aging processes.