[Comparative role of exo-1,4-beta-glucosidase and cellobiase in the enzymatic hydrolysis of cellulose].

An inhibitory action of glucono-delta-lactone on individual components of cellulase complexes from Trichoderma reesei, T. longibrachiatum, T. lignorum and Aspergillus foetidus has been studied. It was shown that gluconolactone exerts an inhibiting effect on cellobiases only (the inhibition constants varied within the range of 0.03-0.1 mM) and does not influence the activities of endoglucanases, cellobiohydrolases and exoglucosidases of the complexes. This formed a basis for a new method for determination of the exoglucosidase activity in a mixture with other components of the cellulase complexes. The complete and selective inhibition of cellobiases by gluconolactone with exoglucosidases activity being intact allowed to evaluate the relative contribution of these enzymes in glucose formation in the course of enzymatic hydrolysis of cellulose (CM-cellulose, filter paper and Avicel). It was found that for most of the cellulase complexes studied the crucial role in glucose formation both from soluble and insoluble cellulose at early steps of hydrolysis belongs to exoglucosidase. On the other hand, the role of exoglucosidase (comparatively with cellobiase) progressively decreases in the course of cellulose hydrolysis. The latter effect does not presumably reflect the changes in the mechanism of cellulose conversion in the course of hydrolysis, but is due to a specific kinetic behaviour of the multienzyme cellulase system.