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 degrees C the hydrolysis of cellobiose with Novozym 188, a commercial product with high beta-1,4-glucosidase activity derived from Aspergillus niger. We used wide variations in the conversion to be able to apply the integral method and thus determine that there is substrate and mixed product inhibition. Whether the SES triple compound contributes to the formation of glucose does not influence the fitting of the experimental results to the theoretical model to any significant extent. We have established how pH affects the kinetic parameters and ascertained that pH 4.3 is the optimum for the conversion of cellobiose into glucose.