Kinetic study on thermal stability of immobilized invertase
- 1 October 1980
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 22 (10) , 2169-2178
- https://doi.org/10.1002/bit.260221013
Abstract
The kinetic study of the thermal stability of three kinds of invertases: native, immobilized on porous glass covalently, and on ion-exchange resin ionically, has been carried out, measuring their enzymatic activity for sucrose hydrolysis. Thermal deactivations of all invertases obeyed first-order kinetics, being independent of substrate concentration, with kd and ΔEd, ΔSd* as shown in Tables I and II, respectively. Based on these parameter values, the effects of immobilization and pH at deactivation on the stability have been considered, and it was suggested that the ionic bond gives a more loosely deformed enzyme than the covalent bond.Keywords
This publication has 5 references indexed in Scilit:
- Characteristics of immobilized invertaseBiotechnology & Bioengineering, 1980
- Amino acid- and sugar composition of invertase of Candida utilis.Agricultural and Biological Chemistry, 1978
- Preparation of immobilized invertaseBiotechnology & Bioengineering, 1973
- Invertase covalently coupled to porous glass: Preparation and characterizationBiotechnology & Bioengineering, 1972
- Studies on the Water-Insoluble Enzyme Hydrolysis of Sucrose by Insoluble Yeast InvertaseAgricultural and Biological Chemistry, 1966