The influence of pH upon the kinetic parameters of the enzymatic hydrolysis of cellobiose with Novozym 188

We have studied experimentally within the pH range of 3.65-5.5 at 50 degree sC the hydrolysis of cellobiose with Novozym 188, a commercial product with high beta -1,4-glucosidase activity derived from Aspergillus niger. We use d wide variations in the conversion to be able to apply the integral method and thus determine that there is substrate and mixed product inhibition. W hether the SES triple compound contributes to the formation of glucose does not influence the fitting of the experimental results to the theoretical m odel to any significant extent. We have established how pH affects the kine tic parameters and ascertained that pH 4.3 is the optimum for the conversio n of cellobiose into glucose.