<jats:p>The performance of <jats:italic>Candida antarctica</jats:italic> lipase B (CALB) has been evaluated in 1-butyl-3-methylimidazolium tetrafluoroborate (BMIMBF<jats:sub>4</jats:sub>)/water mixtures in a wide range of molar fractions (<jats:inline-formula><mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="m1"><mml:mrow><mml:msub><mml:mi mathvariant="normal">χ</mml:mi><mml:mrow><mml:mi>B</mml:mi><mml:mi>M</mml:mi><mml:mi>I</mml:mi><mml:mi>M</mml:mi><mml:mi>B</mml:mi><mml:mi>F</mml:mi><mml:mn>4</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math></jats:inline-formula>) with and without 1-dodecyl-3-methylimidazolium tetrafluoroborate (C<jats:sub>12</jats:sub>-MIMBF<jats:sub>4</jats:sub>), a surfactant derived from BMIMBF<jats:sub>4</jats:sub>. The main aim of this work is to evaluate the influence of <jats:inline-formula><mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="m2"><mml:mrow><mml:msub><mml:mi mathvariant="normal">χ</mml:mi><mml:mrow><mml:mi>B</mml:mi><mml:mi>M</mml:mi><mml:mi>I</mml:mi><mml:mi>M</mml:mi><mml:mi>B</mml:mi><mml:mi>F</mml:mi><mml:mn>4</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math></jats:inline-formula> over micellar aggregates to assess the activity of enzymatic reactions. The investigated reaction corresponds to the hydrolysis of the substrate <jats:italic>p</jats:italic>-nitrophenyl laureate in each <jats:inline-formula><mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="m3"><mml:mrow><mml:msub><mml:mi mathvariant="normal">χ</mml:mi><mml:mrow><mml:mi>B</mml:mi><mml:mi>M</mml:mi><mml:mi>I</mml:mi><mml:mi>M</mml:mi><mml:mi>B</mml:mi><mml:mi>F</mml:mi><mml:mn>4</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math></jats:inline-formula>. The kinetic study for <jats:inline-formula><mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="m4"><mml:mrow><mml:msub><mml:mi mathvariant="normal">χ</mml:mi><mml:mrow><mml:mi>B</mml:mi><mml:mi>M</mml:mi><mml:mi>I</mml:mi><mml:mi>M</mml:mi><mml:mi>B</mml:mi><mml:mi>F</mml:mi><mml:mn>4</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math></jats:inline-formula> at around 0.2 proved to be a border point in enzymatic activity. At <jats:inline-formula><mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="m5"><mml:mrow><mml:msub><mml:mi mathvariant="normal">χ</mml:mi><mml:mrow><mml:mi>B</mml:mi><mml:mi>M</mml:mi><mml:mi>I</mml:mi><mml:mi>M</mml:mi><mml:mi>B</mml:mi><mml:mi>F</mml:mi><mml:mn>4</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math></jats:inline-formula> = 0.1, the lipase activity increases in the presence of C<jats:sub>12</jats:sub>-MIMBF<jats:sub>4</jats:sub>. However, at higher concentrations, BMIMBF<jats:sub>4</jats:sub> has a negligible effect over the lipase activity. These results suggest specific interactions between water and BMIMBF<jats:sub>4</jats:sub> 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<jats:sub>4</jats:sub> 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.</jats:p>
