Isolation, purification and partial characterization of ficin from Ficus carica latex

Abstract

This study aimed at the isolation, purification and characterization of fig latex ficin. Samples were collected from fruit joint with the fig tree. Supernatant was decanted from fig latex after centrifugation at 3000 rpm which represents crude enzyme extract. Latex content was concentrated by sucrose powder. Purification steps were carried out with ion-exchange and gel filtration using DEAE- cellulose and sephadex G-50 columns respectively. Enzyme yield and purification folds were 51.688% and 15.635 respectively with specific activity 148.336 U/mg. By using gel filtration, molecular weight of the purified enzyme was estimated to be 22.725 Da. The pH at which ficin showing activity ranged between 6-8.5. Ficin showed a good stability in pH ranging between 6-8. Optimum temperature for activity and stability were 50 C○ and 25-40 C○ respectively. Activation energy for substrate conversion of this enzyme was calculated to be 10.22 Kca/mol.