AUTHOR=Campodónico Paola R. , Calderón Cristian , Alcázar Jackson J. , Olivares Belén , Jaldin Limberg , Suárez-Rozas Cristian 

TITLE=Exploring the behavior of Candida antarctica lipase B in aqueous mixtures of an imidazolium ionic liquid and its surfactant analogue

JOURNAL=Frontiers in Chemistry

VOLUME=11

YEAR=2024

URL=https://www.frontiersin.org/journals/chemistry/articles/10.3389/fchem.2023.1289398

DOI=10.3389/fchem.2023.1289398

ISSN=2296-2646

ABSTRACT=<p>The performance of <italic>Candida antarctica</italic> lipase B (CALB) has been evaluated in 1-butyl-3-methylimidazolium tetrafluoroborate (BMIMBF<sub>4</sub>)/water mixtures in a wide range of molar fractions (<inline-formula id="inf1"><mml:math id="m1" xmlns:mml="http://www.w3.org/1998/Math/MathML"><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></inline-formula>) with and without 1-dodecyl-3-methylimidazolium tetrafluoroborate (C<sub>12</sub>-MIMBF<sub>4</sub>), a surfactant derived from BMIMBF<sub>4</sub>. The main aim of this work is to evaluate the influence of <inline-formula id="inf2"><mml:math id="m2" xmlns:mml="http://www.w3.org/1998/Math/MathML"><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></inline-formula> over micellar aggregates to assess the activity of enzymatic reactions. The investigated reaction corresponds to the hydrolysis of the substrate <italic>p</italic>-nitrophenyl laureate in each <inline-formula id="inf3"><mml:math id="m3" xmlns:mml="http://www.w3.org/1998/Math/MathML"><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></inline-formula>. The kinetic study for <inline-formula id="inf4"><mml:math id="m4" xmlns:mml="http://www.w3.org/1998/Math/MathML"><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></inline-formula> at around 0.2 proved to be a border point in enzymatic activity. At <inline-formula id="inf5"><mml:math id="m5" xmlns:mml="http://www.w3.org/1998/Math/MathML"><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></inline-formula> = 0.1, the lipase activity increases in the presence of C<sub>12</sub>-MIMBF<sub>4</sub>. However, at higher concentrations, BMIMBF<sub>4</sub> has a negligible effect over the lipase activity. These results suggest specific interactions between water and BMIMBF<sub>4</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<sub>4</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.</p>