نبذة مختصرة : The performance of Candida antarctica lipase B (CALB) has been evaluated in 1-butyl-3-methylimidazolium tetrafluoroborate (BMIMBF 4 )/water mixtures in a wide range of molar fractions ( χ B M I M B F 4 ) with and without 1-dodecyl-3-methylimidazolium tetrafluoroborate (C 12 -MIMBF 4 ), a surfactant derived from BMIMBF 4 . The main aim of this work is to evaluate the influence of χ B M I M B F 4 over micellar aggregates to assess the activity of enzymatic reactions. The investigated reaction corresponds to the hydrolysis of the substrate p -nitrophenyl laureate in each χ B M I M B F 4 . The kinetic study for χ B M I M B F 4 at around 0.2 proved to be a border point in enzymatic activity. At χ B M I M B F 4 = 0.1, the lipase activity increases in the presence of C 12 -MIMBF 4 . However, at higher concentrations, BMIMBF 4 has a negligible effect over the lipase activity. These results suggest specific interactions between water and BMIMBF 4 molecules in relation to CALB. This research highlights the superactivity phenomenon driven by the reaction media and the micelle interface. In this interfacial interaction, BMIMBF 4 acts directly on the changes induced on the enzyme upon its interaction with the micellar interface. This study opens a green perspective toward the biocatalysis field.
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