Homogeneous esterification by lipase from Burkholderia cepacia in the fluorinated solvent.

The formation of noncovalent complexes between lipase from Burkholderia cepacia and the fluorinated ionic surfactant Kryto Development Product 4606 KDP was shown to promote the solubilization of the enzyme in the fluorinated solvent perfluoro(methylcyclohexane) (PFMC) and its operation as a catalyst in the fluorous PFMC/hexane biphasic system (FBS). In the reaction of esterification of 1-phenylethanol and vinyl acetate, the solubilized lipase showed high stereospecificity (ca. 99%) with a catalytic efficiency up to 56 nmol/(U h) with a high operational and storage stability. Temperature modulation of the FBS miscibility allowed the separation and recovery of the solubilized lipase for at least three times. The results are of practical importance for the development of recoverable biocatalysts soluble and active in the FBS.