Enantioselective resolution of 2-arylpropionic acid derivatives employing immobilization of lipase from Bacillus subtilis strain Kakrayal_1 (BSK-L)
| Autor: | Pankaj Gupta, Rashmi Saraswat, Indu Bhushan, Bhahwal Ali Shah |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
Environmental Engineering Immobilized enzyme Silica Gel Bioengineering Bacillus subtilis 01 natural sciences chemistry.chemical_compound 010608 biotechnology Enzyme Stability Lipase Fourier transform infrared spectroscopy Enantiomeric excess Waste Management and Disposal chemistry.chemical_classification Chromatography biology 010405 organic chemistry Renewable Energy Sustainability and the Environment Silica gel Temperature Enantioselective synthesis Stereoisomerism General Medicine Enzymes Immobilized biology.organism_classification 0104 chemical sciences Enzyme chemistry biology.protein Propionates |
| Zdroj: | Bioresource Technology. 269:581-585 |
| ISSN: | 0960-8524 |
| DOI: | 10.1016/j.biortech.2018.08.123 |
| Popis: | This work studied the enantioselective resolution of 2-arylpropionic acid derivatives employing immobilization of lipase produced by Bacillus subtilis strain Kakrayal_1 (BSK-L). The efficient immobilization of lipase on modified silica gel was confirmed by Fourier transform infrared spectroscopy. Tethering of lipase facilitated the enhancement of physiochemical properties and stability of enzyme. Covalently immobilized enzyme retained 85% of residual activity even on reuse after 10th reaction cycle. Validation of immobilized lipase for enantioselective resolution of 2-arylpropionic acid derivatives led to 47.8% conversion efficiency with 87% enantiomeric excess (ee) for ketoprofen, and 27.3% conversion efficiency with 75% ee for flurbiprofen. The enantioselective resolution using immobilized lipase (BSK-L) was superior to free and commercially procured lipase, which suggest a potential application of immobilized lipase in the pharmaceutical/chemical industry. |
| Databáze: | OpenAIRE |
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