Significant changes in the transesterification activity of free and mesoporous-immobilized Rhizopus oryzae lipase in ionic liquids.

We examined the activity of free Rhizopus oryzae lipase (ROL) and ROL immobilized on mesoporous materials in transesterification reactions in various dialkylimidazolium-cation based ionic liquids. For free ROL, the highest activity (0.39 U/mg protein) was obtained in [OMIm][PF(6)] followed by that (0.28 U/mg protein) in [BMIm][PF(6)]. Specific activities of ROL immobilized on mesocellular foam (MCF) were only 0.47 and 0.43 U/mg protein in [OMIm][PF(6)] and [BMIm][PF(6)], respectively. However, the specific activities of ROL immobilized on octadecyl functionalized MCF (C(18)-MCF) increased significantly to 15.64 and 14.84 U/mg protein in [OMIm][PF(6)] and [BMIm][PF(6)], respectively. Consequently, ROL immobilized on C(18)-MCF is a promising biocatalyst for biotransformation reactions in ionic liquids.