Lipase-Catalyzed Regioselective Acylation and Deacylation of Glucose Derivatives
| Autor: | Frederik Beck, Ture Damhus, Morten Würtz Christensen, Ole Kirk |
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| Rok vydání: | 1995 |
| Předmět: | |
| Zdroj: | Biocatalysis and Biotransformation. 12:91-97 |
| ISSN: | 1029-2446 1024-2422 |
| Popis: | In the development of an efficient synthesis of 1-O-decanoyl-2,3,4,6-tetra-O-acetyl-β-D-glucose (β-2) several lipase-based approaches have been explored. Among five immobilized Upases tested, the lipase from Candida antarctica proved particularly efficient for catalyzing selective hydrolysis in the 1-position of 1,2,3,4,6-penta-O-acetyl-β-D-glucose (β-1). Using triethylamine as catalyst, the hydrolysis product 2,3,4,6-tetra-O-acetyl-D-glucose (3) can be esterified with decanoyl chloride to form β-2 selectively, thereby providing an efficient chemo-enzymatic synthesis starting from readily available raw materials. Attempts to produce β-2 from β-1 by lipase-catalyzed interesterification or to esterify 3 with decanoic acid using a lipase as catalyst were unsuccessful. The latter finding was explained by the hemiacetal OH group of glucose being unable to act as nucleophile in the lysis of the lipase acyl-enzyme intermediate. Furthermore, β-2 was found to bee a too bulky substrate to fit into the active site o... |
| Databáze: | OpenAIRE |
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