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A newly developed shearing device was used to study shear-induced inactivation of thermostable alpha-amylase in a plain shear field, under conditions comparable to extrusion. The results show that the inactivation can be described well with a first-order process, in which the inactivation energy largely depends on the shear stress, instead of specific mechanical energy or strain history. The resulting dependency of the rate of inactivation on the shear stress is very strong and nonlinear, which leads to the conclusion that in many cases the maximally applied shear stress determines the inactivation. Quantification of the inactivation rates gives design criteria for the application of enzymes in more viscous systems than conventionally used, provided that the reactor is designed such that no peak shear stresses occur.

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We have investigated the hydrolysis of maltodextrins in a high concentration (up to 70%), by means of enzymatic and acid catalysis. The study revealed that the equilibrium compositions of the catalyzed reactions were kinetically determined by the selectivity of the catalyst, the substrate concentration and the reaction time. A model comprising a set of two kinetic equations was used to describe the hydrolysis and condensation reactions of glucoamylase-catalyzed reactions, even to highly concentrated systems. Increased substrate concentration resulted in the formation of more condensation products. The enzyme inhibition was low and was found to be independent of the substrate concentration.