Thermostability of alcohol dehydrogenase in the presence of sucrose
โ Scribed by Gyana R. Satpathy; Sunil Nath
- Book ID
- 104648448
- Publisher
- Springer-Verlag
- Year
- 1996
- Tongue
- English
- Weight
- 255 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0951-208X
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โฆ Synopsis
SUMIWARY
The influence of sucrose on the thermostability of pure alcohol dehydrogenase is investigated for various temperatures (50-70ยฐC) in the presence and absence of sucrose (0, 80 wt. X). The thermal inactivation clearly exhibits nonlinear biphasic behavior. The thermal inactivation rate constants and the magnitude of the heat-stable and -heat-labile fractions of the enzyme are quantified.
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Representatives of five allozymic classes of Drosophila alcohol dehydrogenase have been compared with respect to their activity levels on two alcohol substrates, quantities of ADH protein, and stability in crude extracts. Within each allozymic class, strains from widely diverse geographic locations