The kinetics of cellobiose hydrolysis was studied using beta-glucosidase fr
om Penicillium Funiculosum, both free and immobilized on nylon powder, at d
ifferent temperatures, pH values, enzymatic activities and initial cellobio
se and glucose concentrations.
The experimental results were fitted to a kinetic model by considering the
substrate and product inhibitions as well as the thermal deactivation of be
ta-glucosidase with a mean deviation of less than 10%, The immobilization o
f beta-glucosidase led to an increase in the stability of the enzyme agains
t changes in the pH value.