| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10243395 | Catalysis Communications | 2005 | 6 Pages |
Abstract
Invertase was immobilised on microporous montmorillonite K-10 via adsorption and covalent binding. The immobilised enzymes were tested for sucrose hydrolysis activity in a batch reactor. Km for immobilised systems was greater than free enzyme. The immobilised forms could be reused for 15 continuous cycles without any loss in activity. After 25 cycles, 85% initial activity was retained. A study on leaching of enzymes showed that 100% enzyme was retained even after 15 cycles of reuse. Leaching increased with reaction temperature. Covalent binding resisted leaching even at temperatures of 70 °C.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
G. Sanjay, S. Sugunan,