ISSN print edition: 0366-6352 ISSN electronic edition: 1336-9075 Registr. No.: MK SR 9/7 Published monthly

Acetylcholine Esterase — Dynamic Behaviour with Flow Calorimetry

F. Malík and V. Štefuca

Department of Chemical and Biochemical Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, SK-812 37 Bratislava

E-mail: malik@chelin.chtf.stuba.sk

Received: 28 March 2002

Abstract: The application of enzyme flow calorimetry for the monitoring of hysteresis behaviour of immobilized enzyme was investigated. The hysteresis of immobilized acetylcholine esterase induced by combination of mass transfer and substrate inhibition was considered. Theoretical analysis of the hysteresis was based on mathematical modelling using kinetic and di usion parameters from literature. The influence of Thiele modulus and the ratio of substrate inhibition and Michaelis constant (K_i/K_m) on the size and region of hysteresis was determined. It was shown that by increasing the value of Thiele modulus or K_i/K_m, the region of hysteresis was shifted towards higher substrate concentrations. On the basis of the simulation results it was concluded that a commercial preparation of acetylcholine esterase should give rise to hysteresis at value of Thiele modulus higher than 150. The considered particle diameter should be in the range from 0.1 to 1.0 mm.

Full paper in Portable Document Format: 566a406.pdf

Chemical Papers 56 (6) 406–411 (2002)