Kinetics of immobilized sucrose phosphorylase.

Sucrose phosphorylase was immobilized on porous ceramic beads with 3-aminopropyltriethoxysilane and glutaraldehyde. It was determined experimentally that under laboratory conditions there was no diffusional resistance to the enzyme-catalyzed reaction. The half-life of the immobilized enzyme varied from about 35 days at 30 degrees C to about 5 days at 40 degrees C. The pH optimum was found to be between 6.5 and 7.0. The activation energy for the reaction was found to be about 12.5 kcal/mol. Eleven independent kinetic constants in the complete rate equation for the previously proposed ping-pong mechanism were found to be in good agreement with those for the soluble enzyme.