engleski

Oxidation of N-Cbz-aminopropanol catalyzed by alcohol dehydrogenase

Alcohol dehydrogenases (ADHs) catalyze oxidoreduction reactions of a broad spectrum of substrates, i.e. alcohols, aldehydes and ketones [1]. Therefore they attract great scientific interest [2]. They play an important role in several physiological functions (in plants, microorganisms and animal tissues) including metabolism of alcohol where they catalyze the reversible oxidation of alcohols to corresponding aldehydes or ketones with the use of coenzymes [3]. In this work the oxidation of N-Cbz-3- aminopropanol (Scheme 1) was investigated. Scheme 1. The reaction scheme Two different enzymes were used for the oxidation of this alcohol, alcohol dehydrogenase isolated from Saccharomyces cerevisiae and alcohol dehydrogenase from horse liver. Since ADH requires coenzyme, NAD+, for its catalytic activity, two different NAD+ regeneration systems were investigated and compared: the addition of cosubstrate - acetone and the addition of NADH oxidase (NOX) isolated from Lactococcus lactis. The product of this reaction, N-Cbz-3- aminopropanal, is the substrate for the reaction of aldol addition catalyzed by D-fructose-6- phosphate aldolase (FSA), and these two reactions were coupled in order to avoid the isolation and purification of the aldehyde. All reactions were carried out in a batch reactor.

alcohol dehydrogenase; coenzyme regeneration; aldola addition

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