Isopropyl 2-ethoxyacetate—an efficient acylating agent for lipase-catalyzed kinetic resolution of amines in batch and continuous-flow modes
| Autor: | László Poppe, Gábor Hornyánszky, Zoltán Boros, Márk Oláh |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
biology
010405 organic chemistry Chemistry Organic Chemistry 010402 general chemistry biology.organism_classification 01 natural sciences Biochemistry 0104 chemical sciences Kinetic resolution Acylation Drug Discovery biology.protein Organic chemistry Candida antarctica Enantiomer Lipase Selectivity Enantiomeric excess Isopropyl |
| Zdroj: | Tetrahedron. 72:7249-7255 |
| ISSN: | 0040-4020 |
| DOI: | 10.1016/j.tet.2015.12.046 |
| Popis: | Productivity [conversion (c) and specific reaction rate (rbatch or rflow)] and enantiomer selectivity [enantiomeric ratio (E) and enantiomeric excess (ee) of the products] of ethyl and isopropyl esters of acetic, 2-methoxyacetic and 2-ethoxyacetic acids as acylating agents were compared in the N-acylation of (±)-1-phenylethanamine rac-1 catalyzed by variously immobilized forms of Candida antarctica lipase B (CaLB) using shake flasks and continuous-flow reactors. The effect of the temperature in the 0–80 °C range on productivity and enantiomer selectivity in KRs of rac-1 was investigated with the isopropyl esters in continuous-flow mode using CaLB-filled minireactors. Isopropyl 2-ethoxyacetate surpassed the performance of ethyl 2-methoxyacetate in terms of both productivity (1.9–2.9 times higher rate in batch mode) and enantiomeric selectivity (ee(R)-amide>99.9% compared to 99.8%) providing at 40 °C high volumetric productivity (2.22 kg L−1 h−1), specific reaction rate and enantiomeric excess (rflow=783 μmol min−1 g−1, ee(R)-2c>99.9%). |
| Databáze: | OpenAIRE |
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