Kinetic resolution of (±)-1-phenylethanol in [Bmim][PF6] using high activity preparations of lipases

Lipases from two different sources Candida rugosa (CRL) and Burkholderia cepacia (BCL) were formulated as enzyme precipitated and rinsed with organic solvents, organic solvent rinsed enzyme preparation, cross-linked enzyme aggregates (CLEAs) and protein coated micro-crystals (PCMCs). These various enzyme formulates were evaluated for the kinetic resolution of (±)-1-phenylethanol in ionic liquid [Bmim][PF6] by transesterification with vinyl acetate. Of all the enzyme forms evaluated EPRP and PCMC in the case of CRL showed the best results with 26 % (E value = 153) and 53% (E value = 79) conversion, respectively, at 35 °C in 24 h. Carrying out this conversion with PCMC at lower temperature of 25 °C further improved the E value to 453 (with 44% conversion in 12 h). For BCL the acetone-rinsed enzyme preparation (AREP), CLEA and PCMC performed equally well with % conversion of 50 and 99 eep (%) (E value >1000) in just 2 h, whereas, the free lipase gave only 8% conversion.

Graphical abstractIt is shown that high activity preparations of the lipases are far superior to the lyophilized powders in kinetic resolution of (±)-1-phenylethanol in [Bmim][PF6].Figure optionsDownload full-size imageDownload as PowerPoint slide