초록
<P>The enzymatic oxidation of amino alcohols was studied to address the long‐standing problem of product stability. Amino aldehydes, highly sought and unstable compounds, can be generated under mild conditions if they are immediately protected. Utilizing a range of alcohol dehydrogenases (ADHs) and semicarbazide as a scavenger, the enantioselective synthesis of protected amino aldehydes is possible. Glycerol dehydrogenase from <I>Gluconobacter oxydans</I> (<I>Go</I>GDH) displayed excellent enantioselectivity but limited substrate scope, whereas horse liver ADH catalyzed a broad range of conversions with low enantioselectivities.</P>