Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching
Data(s) |
30/09/2011
30/09/2011
2005
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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 |