Sophorose induction of an intracellular b-glucosidase in Trichoderma.

The disaccharide sophorose induces Trichoderma to increase a soluble intracellular b-glucosidase that hydrolyses cellobiose, sophorose, and p-nitrophenyl-b-D-glucopyranoside. Simultaneously, it depresses the activity of a similar insoluble enzyme that is associated with the mycelium. Gel electrophoresis indicates that a single enzyme is responsible for all the soluble intracellular b-glucosidase activity. Cycloheximide severely inhibits sophorose induction of this enzyme indicating that the increase in activity normally obtained with sophorose is due to the de novo formation of the enzyme. The same sugars that promote the formation and release of cellulase by Trichoderma induce an increase in the soluble intracellular b-glucosidase. A function of the soluble intracellular enzyme appears to be the hydrolysis of cellobiose, which would otherwise accumulate during cellulose degradation, and thus to prevent cellobiose inhibition of cellulase.