Lipase B from Candida antarctica in Highly Saline AOT-Water-Isooctane Reverse Micelle Systems for Enhanced Esterification Reaction

• Published in: Catalysts Vol. 13; no. 3; p. 492
• Main Authors: Márquez-Villa, José Martín, Mateos-Díaz, Juan Carlos, Rodríguez, Jorge A., Camacho-Ruíz, Rosa María
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.03.2023
• Subjects: Biocatalysts; Butyl oleate; Catalysts; Chemical reactions; Chemical synthesis; Enzymes; Esterification; Isooctane; Lipase; Mass transport; Microorganisms; Morphology; Nanoemulsions; Photon correlation spectroscopy; Reverse micelles; Solvents; Surfactants; Transport phenomena
• ISSN: 2073-4344; 2073-4344
• DOI: 10.3390/catal13030492

Butyl oleate synthesis by the lipase B from Candida antarctica (CalB) under extreme halophilic conditions was investigated in the present research through the AOT/Water/Isooctane reverse micellar system. The impact of aqueous content (Wo=H2OSurfactant) and NaCl variation on the enzymatic activity of CalB in the butyl oleate reaction in reverse micelles was explored. The results indicated that, based on the increase of NaCl, it is remarkable to achieve higher enzymatic activity up to 444.85 μmolmin at 5 M NaCl and Wo = 10, as the best esterification conditions at pH 7.2 and 30 °C. However, it was clear that butyl oleate synthesis by lipase CalB increased based on the reduction in the average reverse micelle size, where reverse micelle sizes were determined by dynamic light scattering (DLS). This increase in butyl oleate synthesis demonstrated the potential of reverse micelles as systems that enhance mass transport phenomena in heterogeneous biocatalysis. Furthermore, reverse micelles are promising systems for extreme halophilic lipases research.