Portal de Periódicos da CAPES

Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching

2004; Elsevier BV; Volume: 6; Issue: 1 Linguagem: Inglês

10.1016/j.catcom.2004.11.003

1873-3905

G. Sanjay, S. Sugunan,

Electrochemical sensors and biosensors

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.