Ficus Enzymes. I. Separation of the Proteolytic Enzymes of Ficus Carica and Ficus Glabrata Latices.

Ficin is the name given to the proteolytic enzyme activity of the latex of trees of the genus Ficus (1). While this proteolytic activity has been utilized for centuries and Walti (2) crystallized a proteolytic enzyme from fig latex, little is known of the physical, chemical, and enzymatic properties of this activity. The information available on ficin indicates that it closely resembles papain with regard to substrate specificity, esterase activity, transpeptidation reactions, and activation by reducing agents (3). Bernhard and Gutfreund (4), Hammond and Gutfreund (5), and Liener (6) have partially purified ficin and have studied some of its properties. Cohen (7) reported work on some of the properties of crystallized ficin of undefined origin. The presence of more than one proteolytic enzyme component in ficin is indicated by studies on substrate specificity and heat stability (8), pH-activity curves (9), and by separation procedures (3, 10, 11). The present work led to the development of a procedure for the complete and reproducible separation of the proteolytic enzymes of ficin. It will be shown that the proteolytic enzymes of Ficus glabrata and Ficus carica latices differ chromatographitally and electrophoretically and that there are both qualitative and quantitative differences in the proteolytic enzyme components from different varieties of F. carica.