Alcohol dehydrogenase (alcohol: NAD oxidoreductase, E. C. 1. 1. 1. 1.) from Thea sinensis seeds (variety: Zairai) was isolated and purified about 1, 500-fold using preparative disc electrophoresis. The specific activity was about 3.4units/mg protein against ethyl alcohol. Its s020. w value was 6.96S and its molecular weight was approximately 150, 000 using gel filtration on Sephadex G-200. The physical, chemical and catalytic properties of the enzyme are described. The oxidoreduction products formed by the enzyme were identified by gas chromatography, and for the unsaturated compounds the conversion of double bond and geometrical isomerization was observed. The substrate specificity of tea enzyme is discussed in comparison with the enzymes from Leuconostoc mesenteroides, and horse and human livers. Paticularly a tendency for reactivity in the oxidoreduction of unsaturated alcohols and aldehydes were discribed by comparing the effects of geometry, the position of the double bond and the length of chain in substrates.
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Hatanaka et al. (1974) studied this question.