Abstract
Purification of yeast invertase was attempted by means of chromatography using Duolite C-10, a sulfonic acid cation exchange resin, and some properties of the enzyme obtained thereby were investigated. The results obtained are as follows:
1. By this method a yeast invertase preparate can be purified to an extremely advanced state, especially in its polysaccharide content.
2. As a result of purification by the method, the pH-stability range of the enzyme migrates slightly towards the alkaline side. But, there occurs almost no change in the heat-stability of the enzyme.
3. Almost no change in transglycosylation activity of the enzyme is exhibited.
4. In ultraviolet absorption spectra, the absorption maximum of the enzyme shifts from about 270 mμ to 278 mμ, greatly increasing enzyme activity per unit of the extinction coefficient.
5. However, the purified enzyme was found to contain still two or more components, electrophoretically.
