Kinetics of immobilized sucrose phosphorylase
- 1 February 1982
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 24 (2) , 317-328
- https://doi.org/10.1002/bit.260240206
Abstract
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°C to about 5 days at 40°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.This publication has 23 references indexed in Scilit:
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