Abstract
Lipase-catalyzed alcoholysis was investigated in three different ionic liquids. Lyophilized native lipase had a low activity in all the ionic liquids but a poly(ethylene glycol) (PEG)-lipase complex (with a molar ratio of the polymer/enzyme of 10:1) had an increased activity of over 14-fold. Of several lipases tested, PEG-lipase PS (from Pseudomonas cepacia) exhibited the highest activity (1.07 mmol/(h g−1 protein)) in 1-octyl-3-methylimidazolium hexafluorophosphate.
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