| dc.contributor.author |
Sanjay, G |
|
| dc.contributor.author |
Sugunan, S |
|
| dc.date.accessioned |
2011-09-30T11:47:47Z |
|
| dc.date.available |
2011-09-30T11:47:47Z |
|
| dc.date.issued |
2005 |
|
| dc.identifier.issn |
1566-7367 |
|
| dc.identifier.uri |
http://dyuthi.cusat.ac.in/purl/2312 |
|
| dc.description.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. |
en_US |
| dc.description.sponsorship |
Cochin University of Science & Technology |
en_US |
| dc.language.iso |
en |
en_US |
| dc.publisher |
Elsevier |
en_US |
| dc.subject |
Immobilisation |
en_US |
| dc.subject |
Immobilised enzymes |
en_US |
| dc.subject |
Montmorillonite |
en_US |
| dc.subject |
Adsorption |
en_US |
| dc.subject |
Microporous |
en_US |
| dc.subject |
Sucrose hydrolysis |
en_US |
| dc.title |
Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching |
en_US |
| dc.type |
Working Paper |
en_US |
| dc.contributor.faculty |
Science |
en_US |
| dc.identifier.url |
http://www.sciencedirect.com/science/article/pii/S1566736704002225 |
en_US |