Effects of mixed reverse micellar structure on stability and activity of yeast alcohol dehydrogenase
β Scribed by Dong-Hwang Chen; Min-Hung Liao
- Book ID
- 114395771
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 117 KB
- Volume
- 18
- Category
- Article
- ISSN
- 1381-1177
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π SIMILAR VOLUMES
Yeast alcohol dehydrogenase (YADH) solubilized in reverse micelles of aerosol OT (i.e., AOT or sodium bis (2-ethyl hexyl) sulfosuccinate) in isooctane has been shown to be catalytically more active than that in aqueous buffer under optimum conditions of pH, temperature, and water content in reverse
## Abstract Remarkable increases in enzyme catalytic stability resulting from addition of charged waterβsoluble polymers have recently been reported, suggesting that use of these polymers may be an attractive general strategy for enzyme stabilization. To test the proposed hypothesis that coulombic