Collect. Czech. Chem. Commun.
1979, 44, 986-990
https://doi.org/10.1135/cccc19790986
Effect of pH and temperature on alcohol dehydrogenase
Sylva Leblová, Roman Lapka and Noemi Nováková
Department of Biochemistry, Charles University, 128 40 Prague 2
Abstract
Alcohol dehydrogenase isolated from germinating pea seeds catalyzes ethanol oxidation at pH 8.7 and acetaldehyde reduction at pH 7.0. The values of the Michaelis constants are the lowest in the range of pH-optimums. The effect of temperature on the reaction rate was investigated over the range 15-55 °C. The initial and maximal rates increase with the increasing temperature and attain a maximum at 40 °C. The values of the Michaelis constants are the lowest at 21 °C. Pea alcohol dehydrogenase looses its activity at 70 °C, the binary enzyme-NAD complex is more thermostable.
