Abstract
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][PF 6] 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 ee p (%) ( E value >1000) in just 2 h, whereas, the free lipase gave only 8% conversion.
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