Nithianandam, V. S. ; Srinivasan, K. S. V. ; Thomas Joseph, K. ; Santappa, M. (1981) Preparation and properties of immobilized amyloglucosidase Biotechnology and Bioengineering, 23 (10). pp. 2273-2282. ISSN 0006-3592
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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/bit.260...
Related URL: http://dx.doi.org/10.1002/bit.260231010
Abstract
Amyloglucosidase was immobilized on a copolymer of methyl methacrylate and 2-dimethylaminoethyl methacrylate. The resulting immobilized amyloglucosidase has 19% of the soluble enzyme specific activity. The pH optimum of immobilized amyloglucosidase is shifted towards acidity by 1.9 units. The temperature optimum of immobilized enzyme is shifted upward by 5°C. The immobilized amyloglucosidase has the maximum stability at pH 4.6, whereas the soluble enzyme has maximum stability at pH 5.5. While soluble amyloglucosidase has a maximum thermal stability at 50°C, the stability of the immobilized amyloglucosidase steadily decreases with the increase in temperature.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons. |
ID Code: | 43304 |
Deposited On: | 11 Jun 2011 06:28 |
Last Modified: | 11 Jun 2011 06:28 |
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