DataSheet1_Exploring the behavior of Candida antarctica lipase B in aqueous mixtures of an imidazolium ionic liquid and its surfactant analogue.PDF

• Main Authors: Paola R. Campodónico, Cristian Calderón, Jackson J. Alcázar, Belén Olivares, Limberg Jaldin, Cristian Suárez-Rozas
• Format: Dataset
• Language: unknown
• Published: 2024
• Subjects: Biochemistry; Environmental Chemistry; Geochemistry; Organic Chemistry; Inorganic Chemistry; Nuclear Chemistry; Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics); Medical Biochemistry and Metabolomics not elsewhere classified; Food Chemistry and Molecular Gastronomy (excl. Wine); Analytical Biochemistry; Cell Neurochemistry; Enzymes; Electroanalytical Chemistry; Analytical Chemistry not elsewhere classified; Organic Green Chemistry; Physical Organic Chemistry; Catalysis and Mechanisms of Reactions; Environmental Chemistry (incl. Atmospheric Chemistry); ionic liquids; enzyme; surfactant; catalysis; superactivity; Antarc*; Antarctica
• Online Access: https://doi.org/10.3389/fchem.2023.1289398.s001; https://figshare.com/articles/dataset/DataSheet1_Exploring_the_behavior_of_Candida_antarctica_lipase_B_in_aqueous_mixtures_of_an_imidazolium_ionic_liquid_and_its_surfactant_analogue_PDF/24971148

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 (χBMIMBF4) 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 χBMIMBF4 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 χBMIMBF4. The kinetic study for χBMIMBF4 at around 0.2 proved to be a border point in enzymatic activity. At χBMIMBF4 = 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.