Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching

G, Sanjay and S., Sugunan (2006) Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching. Catalysis Communications , 6 (1). pp. 81-86.

PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
156Kb

Official URL: http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6W7K-4F0GBGS-2&_user=518931&_coverDate=01%2F01%2F2005&_alid=581573275&_rdoc=33&_fmt=full&_orig=search&_cdi=6629&_sort=d&_docanchor=&view=c&_ct=51&_acct=C000025838&_version=1&_urlVersion=0&_userid=5

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.

Item Type:	Article
Subjects:	Science > Chemistry
ID Code:	752
Deposited By:	Prof Balasubramanian Viswanathan
Deposited On:	27 May 2007 11:28
Last Modified:	27 May 2007 11:28

Repository Staff Only: item control page