The hydrolysis of maltodextrins (10 DE) by glucoamylase was studied in a ba
tch reactor at temperatures between 40 and 80 degreesC and substrate concen
tration range from 17 to 300 kg/m(-3). The experimental data were fitted to
a model including thermal deactivation of the enzyme. In the model, the re
action rate was correlated with an extended Michaelis-Menten equation inclu
ding inhibition by product, and the thermal deactivation of glucoamylase wa
s fitted with a first-order reaction. The dependence of rate parameters on
temperature was correlated using the Arrhenius equation. The differential e
quation of the model was integrated and the optimal enzyme demand and tempe
rature were determined for isothermal operation. (C) 2001 John Wiley & Sons
, Inc.