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  • Title: Enantiospecificity of immobilized horse liver alcohol dehydrogenase.
    Author: Görisch H, Boland W, Jaenicke L.
    Journal: J Appl Biochem; 1984; 6(1-2):103-6. PubMed ID: 6386789.
    Abstract:
    Horse liver alcohol dehydrogenase (EC 1.1.1.1) accepts a wide structural range of substrates but exhibits a well-defined and predictable stereospecificity. The enzyme was immobilized on CNBr-activated Sepharose 4B. The immobilized preparation was used to oxidize the enantiomeric pair of cis-1,2-bis(hydroxymethyl)-3-cyclopentene enantioselectively to a mixture of two diastereoisomeric chiral lactones. The two diastereoisomeric products are readily separated and each was isolated with an optical yield of greater than 99%.
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