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

• Published in: Frontiers in Chemistry
• Main Authors: Campodónico, Paola R., Calderón, Cristian, Alcázar, Jackson J., Olivares, Belén, Jaldin, Limberg, Suárez-Rozas, Cristian
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Frontiers Media SA 2024
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.3389/fchem.2023.1289398; https://www.frontiersin.org/articles/10.3389/fchem.2023.1289398/full

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.