Beta-glucosidase of Trichoderma: its biosynthesis and role in saccharification of cellulose

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Abstract
The extracellular .beta.-glucosidase of T. viride generally was present in low levels when the organism was cultured on cellulose because it was inactivated under the acid conditions which developed in the medium while the other enzymes of the cellulase complex were more stable. With the appropriate pH control, inactivation of .beta.-glucosidase was prevented and the activity of this enzyme increased during growth. In the saccharification of crystalline cellulose, or of cellulose at low concentrations, much of the glucose produced was the result of the cleavage of cellobiose by .beta.-glucosidase. When high concentrations (10%) of pretreated cellulose were saccharified, significant quantities of glucose were produced by action of enzymes other than .beta.-glucosidase.