Zone Electrophoresis of Myrothrecium Cellulose

Abstract

THE cellulase activity of culture filtrates of the mould Myrothecium verrucaria (Alb. and Schw.) Ditm. ex Fr. has been variously attributed to: (i) a single hydrolytic enzyme¹ which, inter alia, is homogeneous in free-boundary electrophoresis at pH 7; (ii) at least two and possibly three hydrolytic enzymes which migrate at different rates under the same conditions of electrophoresis²; and (iii) an enzyme, C ₁, of unspecified function which enables cellulose to be further degraded by C _x, a group of enzymes characterized by hydrolytic activity towards carboxymethylcellulose³, which can be resolved⁴ into at least eight components by zone electrophoresis at pH 7. Other controversies centre on the specificity of the enzyme(s) with respect to the chain-length of cellulose and its hydrolysis products and involve certain other enzymes as well. The need to resolve these controversies prompts us to report some procedures which enable the electrophoretic homogeneity and substrate specificity of cellulases to be tested simultaneously.