{"title":"固定化马肝醇脱氢酶的对映体特异性。","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":"{\"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}","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}
Enantiospecificity of immobilized horse liver alcohol dehydrogenase.
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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