Substrate protection of immobilized glucose isomerase
โ Scribed by Kuo-Cheng Chen; Juan-Yih Wu
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 623 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0006-3592
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โฆ Synopsis
Using commercial immobilized glucose isomerase (SWETASEa, Nagase Co.), the effect of substrate protection on enzyme deactivation has been studied in a batch manner. The data analysis was carried out based on Briggs-Haldane kinetics in which enzyme deactivation accompanying the protection of substrates was also considered. The protection factor was proposed to elucidate the dependence of the degree of substrate protection. The existence of the protection of glucose isomerase by the substrates has been verified experimentally. Also, the enzyme-substrate complex deactivates with a decay constant which is one-half that of the free enzyme. Theoretical analysis of enzyme deactivation with substrate protection offers an effective understanding which i s essential for enzyme replacement and process optimization.
๐ SIMILAR VOLUMES
## Abstract The immobilization of glucose isomerase (Dโxylose ketol isomerase, EC 5.3.1.5) by covalently bonding to various carriers and by adsorption to ion exchange resins was attempted in order to obtain a stable immobilized enzyme which can be used for continuous isomerization of glucose in a c