Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching


Autoria(s): Sanjay, G; Sugunan, S
Data(s)

30/09/2011

30/09/2011

2005

Resumo

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.

Cochin University of Science & Technology

Identificador

1566-7367

http://dyuthi.cusat.ac.in/purl/2312

http://www.sciencedirect.com/science/article/pii/S1566736704002225

Idioma(s)

en

Publicador

Elsevier

Palavras-Chave #Immobilisation #Immobilised enzymes #Montmorillonite #Adsorption #Microporous #Sucrose hydrolysis
Tipo

Working Paper