The influence of temperature upon the hydrolysis of cellobiose by beta-1,4-glucosidases from Aspergillus niger.

We have made experimental studies into the enzymatic hydrolysis of cellobiose within the temperature range of 40 degrees C to 70 degrees C at pH 4.9, by using beta-1,4-glucosidase from Aspergillus niger. At 70 degrees C there was significant enzyme deactivation, which could be fitted to a potential deactivation model with values of n equal to 1.09 and k(d) to 0.1564 (g/l)(-0.09) min(-1), whereas the rate of hydrolysis could be fitted to the Michaelis-Menten equation. Between 40 degrees C and 60 degrees C we noted a substrate inhibition and that the CEC compound formed contributed to glucose production. The apparent activation energies had values of 4.66, 8.45, 4.82, and 3.99 kJ/mol for the kinetic constants k(a) and k(a2) the Michaelis constant and the substrate inhibition constant, respectively.