Abstract
Purified and reconstituted quinohaemoprotein alcohol dehydrogenase (QH-EDH) from Comamonas testosteroni is shown to oxidize secondary alcohols enantioselectively. The products formed during the oxidation of secondary alcohols were positively identified as the corresponding ketones. In the oxidation of chiral secondary n-alkyl alcohols a preference of the enzyme for the S(+)alcohols was found. The apparent kinetic parameters (Km and Kmax) for a range of n-alkyl alcohols depend on the length of the alcohol chain and the location of the hydroxyl function in the chain. The enzyme is stable up to a temperature of 37 °C. Above this temperature the activity is irreversibly lost. The pH optimum of the enzyme in the conversion of secondary alcohols is 7.7.
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