Lipase-catalyzed enantioselective acylation of 3-benzyloxypropane-1,2-diol in supercritical carbon dioxide
| Autor: | Ildikó Kmecz, J. Sawinsky, László Poppe, Viktória Bódai, Zoltán Juvancz, Csaba Csajági, Katalin Renner, Béla Simándi, Enikő R. Tőke |
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| Rok vydání: | 2006 |
| Předmět: |
Environmental Engineering
Supercritical carbon dioxide biology Chemistry Diol Biomedical Engineering Acetaldehyde Triacylglycerol lipase Bioengineering biology.organism_classification Acylation chemistry.chemical_compound biology.protein Organic chemistry Lipase Enantiomeric excess Trichoderma reesei Biotechnology |
| Zdroj: | Biochemical Engineering Journal. 28:275-280 |
| ISSN: | 1369-703X |
| DOI: | 10.1016/j.bej.2005.11.010 |
| Popis: | Lipase-catalyzed acylation of 3-benzyloxypropane-1,2-diol with vinyl acetate as acyl donor using different lipases [porcine pancreas lipase (PPL), Lipase AK “Amano”, Lipase PS “Amano”, and crude enzymes from Trichoderma reesei RUT-C30, Thermoascus thermophilus (NRRL5208), Talaromyces emersonii (NRLL3221)] was studied in supercritical carbon dioxide (scCO2). In the reactions catalyzed by different lipases different amounts of monoacetate and diacetate products along with minor amounts of cyclic acetals forming from the diol and acetaldehyde were obtained. Application of Lipase AK led to the highest conversion (84.7%) and the highest enantiomeric excess values (eemonoacetates = 38%, eediacetate = 85%). Effect of water content of scCO2 on the productivity and the enantiomer selectivity of the reactions with Lipase AK was also investigated. |
| Databáze: | OpenAIRE |
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