Abstract

Activities of several enzymes associated with cellulolysis were compared using as substrates cell-walls of Lolium multiflorum and cotton cellulose. Purified enzymes C 1 (see Ref. 1 for definition), C. x (CM-cellulase) and β-glucosidase were employed as well as culture filtrates containing C x . Activities were determined by ability to digest the substrates and to release H 2O-soluble phenolic compounds from the grass cell-walls. The culture filtrates most active on cotton cellulose were obtained using the fungi Trichoderma viride and Fusarium solani; with grass cell-walls the most active were from T. viride, Gliocladium roseum, a species of Basidiomycetes, and one strain of Myrothecium verrucaria (IMI Strain 25 291). For the crude enzyme preparations tested, there were highly significant correlations between the digestibility of grass cell-walls and the UV-absorption of the filtrate at λ max 290 nm and at λ max 324 nm but there was no significant correlation between the digestibility of grass cell-walls and that of cotton cellulose. Partially purified C 1 and C x from two different fungal sources showed activity on both substrates. Differences in MW of the H 2O-soluble phenolic compounds obtained by treatment of grass cell-walls with C 1 and C x components suggest that these enzymes could have different modes of action. Synergism between C 1 and C x from T. koningii occurred with both substrates but with C 1 and C x from F. solani synergism only occurred with cotton cellulose.

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