Kinetics of the reaction catalysed by rape alcohol dehydrogenase |
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Authors: | Marie Stiborová Sylva Leblová |
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Affiliation: | Department of Biochemistry, Charles University, Faculty of Natural Sciences, Prague, Czechoslovakia |
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Abstract: | The kinetics of the enzyme reaction of ethanol oxidation and acetaldehyde reduction catalysed by alcohol dehydrogenase (ADH) (EC 1.1.1.1) isolated from germinating rape seeds obeys the bi-bi ordered mechanism of Theorell and Chance. The enzyme reaction depends on the pH and temperature. The Km values for the basic substrates have the lowest values around the pH optimum of the reaction. The enzyme is most stable at pH 6.5–7. The Km values for ethanol and NAD increase with increasing temperature. The maximum rate of the ethanol oxidation satisfies the Arrhenius equation. The activation energy for the given temperature range is 40.11 kJ/mol. The rape ADH is denatured by heating above 60° but the enzyme-NAD complex is thermally more stable than the enzyme alone. |
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Keywords: | Cruciferae alcohol dehydrogenase coenzyme enzyme kinetics. |
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