Enzymatic resolution of (RS)-2-arylpropionic acid thioesters by Candida rugosa lipase-catalyzed thiotransesterification or hydrolysis in organic solvents |
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Institution: | 1. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan;2. Department of Bioresources and Environmental Science, Ishikawa Prefectural University, 1-308, Suematsu, Nonoichi, Ishikawa 921-8836, Japan |
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Abstract: | An enzymatic resolution process was developed to produce (S)-naproxen ester, (S)-naproxen or (S)-ibuprofen from the corresponding racemic thioesters by using lipase-catalyzed thiotransesterification or hydrolysis in organic solvents. Enzyme activity is greatly enhanced when activated naproxen thioesters containing an electron-withdrawing group are the substrates. Unlike other lipases, Candida rugosa lipase may discern the sulfur moiety of the thioesters, and yields lower enzyme activity when compared to the corresponding oxygen-containing analogues. Enzyme performances were further compared under various conditions, i.e. different combinations of reaction type (thiotransesterification or hydrolysis), solvent (isooctane or cyclohexane), substrate (naproxen or ibuprofen thioesters) and lipase sources. |
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