Biological preparation of an optically activ alcohol. Part III. Enantioselective hydrolysis of .ALPHA.-cyano-3-phenoxybenzyl acetate with Arthrobacter lipase
| Autor: | Takeaki Umemura, Hideo Hirohara, Shigeyasu Nabeshima, Hidefumi Yamamoto, Satoshi Mitsuda |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
biology
Enantioselective synthesis Triacylglycerol lipase biology.organism_classification General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Hydrolysis chemistry Enzymatic hydrolysis Arthrobacter biology.protein Organic chemistry Lipase General Agricultural and Biological Sciences Triethylamine Racemization |
| Zdroj: | Agricultural and Biological Chemistry. 54:2907-2912 |
| ISSN: | 1881-1280 0002-1369 |
| DOI: | 10.1271/bbb1961.54.2907 |
| Popis: | Lipase-catalyzed enantioselective hydrolysis of the acetic ester of racemic α-cyano-3-phenoxybenzyl alcohol (CPBA) was examined to prepare (S)-CPBA. Most of the lipases tested hydrolyzed (S)-CPBA acetate preferentially, while Candida cylindracea lipase favored (R)-CPBA acetate. Enantioselective hydrolysis by Arthrobacter lipase gave the optically pure (S)-CPBA in the reaction mixture of pH 4.0. The kinetic studies showed that (R)-CPBA acetate reacted as a competitive inhibitor. The Arthrobacter lipase solution in the water/oil biphasic reaction system could be used repeatedly. The lipase immobilized to resins had insufficient activity or low operational stability for the repeated batch reaction. The unhydrolyzed (R)-CPBA acetate was racemized by heating with triethylamine and could be reused as the substrate of the enzymatic hydrolysis. A chemico-enzymatic process for the preparation of (S)-CPBA was developed based on these studies. |
| Databáze: | OpenAIRE |
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