Kinetic studies on insoluble cellulose-cellulase system

Enzymatic hydrolysis of insoluble amorphous cellulose by Trichoderma viride cellulase was investigated in a batch reactor at several substrate concentrations and three enzyme levels. The reactions were carried out at 50 degrees C and pH 4.8. Enzyme was rapidly adsorbed onto solids on contact, then gradually returned to the liquid phase as the reaction proceeded. A kinetic model that considered the fast adsorption which was followed by the slow reaction, and subsequent product inhibition was developed to interpret the experimental observations. The resulting equation successfully correlated the data for up to 70% conversion. The methods for determining the kinetic parameters are discussed.