Abstract

Studying the compositions of the individual enzymes in the fresh fruit papaya latex through the different growing periods of the fruit by CM-Cellulose ion exchange chromatography revealed that chymopapain is always the most abundant protease for the portion and the activity in total. The result was the same with the freezed-dried papaya latex. The purification of chymopapain from the freezed-dried papaya latex in the ammonium sulfate fraction step showed that chymopapain is still contaminated with peptidase. Continuing to next ion exchange chromatography step and then examining by SDS-PAGE electrophoresis shows that this enzyme can preliminarily be isolated.