Kinetic study of the cellobiase activity of Trichoderma reesei cellulase complex at high substrate concentrations

At high cellobiose concentrations, the cellobiase activity of a Trichoderma reesei cellulase preparation does not follow Michaelis-Menten kinetics and shows substrate inhibition. Several rate equations were fitted to the initial rate-cellobiose concentration data. The best fit is obtained for a rate equation corresponding to partial substrate inhibition of cellobiase. In this case, the K-m, V(m)ax and K-I values obtained are 1.1 mM, 16 IU ml(-1) and 26 mM, respectively.