{"title":"Enantiospecificity of immobilized horse liver alcohol dehydrogenase.","authors":"H Görisch, W Boland, L Jaenicke","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>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%.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":"6 1-2","pages":"103-6"},"PeriodicalIF":0.0000,"publicationDate":"1984-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied biochemistry","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
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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