Introduction & Objective: Ficin is a member of plant cystein proteases that is abundant in fig. This enzyme has many pharmacological and industrial uses. In the present study, the enzyme was purified by a simple procedure and its proteolytic activity was assayed on several plant and animal proteins.

Materials & Methods: Ficin was extracted from unripe fig, precipitated by ammonium sulfate and purified using ion-exchange chromatography on a Carboxymethyl Sepharose column. Proteolytic activities of the purified enzyme were determined in 4 buffering conditions on casein, alpha lactalbumin, beta lactoglobulin and gelatin proteins.

Results: Purified enzymes include two bands with molecular mass of 24 and 26 KDa. Results of proteolytic activity showed that ficin can digest casein. It has moderate hydrolytic activity on beta lactoglobulin and gelatin but ficin can not hydrolyze alpha lactalbumin.

Conclusion: It seems ficin has selective effects on some proteins so it can be a good candi-date for digestion of casein and making related drugs.