Studying the purification of Enzyme Chymopapain in Vietnamese carica papaya l. fruit latex

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.