Improved activity of lipase immobilized in microemulsion-based organogels for (R, S)-ketoprofen ester resolution: Long-term stability and reusability

• Published in: Biotechnology reports (Amsterdam, Netherlands) Vol. 7; no. C; pp. 1 - 8
• Main Authors: Zhang, Wei-Wei, Jia, Jun-Qi, Wang, Na, Hu, Cheng-Li, Yang, Sheng-Yong, Yu, Xiao-Qi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2015; Elsevier
• Subjects: Enzyme Biocatalysis; Immobilization; Kinetic resolution; Lipase; Microemulsion-based organogels; Stability; Enzyme Biocatalysis; Immobilization; Stability; Lipase; Kinetic resolution; Microemulsion-based organogels
• ISSN: 2215-017X; 2215-017X
• DOI: 10.1016/j.btre.2015.04.003

[Display omitted] Microemulsion-based organogels (MBGs) were effectively employed for the immobilization of four commonly used lipases. During the asymmetric hydrolysis of ketoprofen vinyl ester at 30°C for 24h, lipase from Rhizomucor miehei and Mucor javanicus immobilized in microemulsion-based organogels (RML MBGs and MJL MBGs) maintained good enantioselectivities (eep were 86.2% and 99.2%, respectively), and their activities increased 12.8-fold and 7.8-fold, respectively, compared with their free forms. They gave higher yields compared with other lipase MBGs and exhibited better enantioselectivity than commercial immobilized lipases. Immobilization considerably increased the tolerance to organic solvents and high temperature. Both MJL MBGs and RML MBGs showed excellent reusability during 30 cycles of repeated 24h reactions at 30°C (over 40 days). The system maintained yields of greater than 50%, while the ees values of RML MBGs and MJL MBGs remained nearly constant at 95% and 88%, respectively.