276614 Immobilization and Stabilization of Lipase in Polyaniline Nanofibers for Esterification of Racemic Ibuprofen

Tuesday, October 30, 2012
Hall B (Convention Center )
Sung-Gil Hong1, Hansol Kim1 and Jungbae Kim2, (1)Chemical and biological engineering, Korea University, Seoul, South Korea, (2)Chemical and Biological Engineering, Korea University, Seoul, South Korea

Lipase (LP) is one of useful enzymes in various fields such as food, oil and fat, detergent, cosmetics and pharmaceutical industries. We immobilized and stabilized lipase into polyaniline nanofibers (PANFs) via a three-step process of enzyme adsorption, precipitation and crosslinking (EAPC). EAPC-LP/PANFs resulted in high enzyme loading/activity and stability. EAPC showed 5.1 and 5.9 times higher activity than enzyme adsorption (EA) and enzyme adsorption/crosslinking (EAC), respectively. After incubation under shaking at room temperature for 84 days, EA, EAC and EAPC retained 11%, 24% and 74% of initial activities, respectively. The EAPC approach successfully increased both stability and loading/activity of enzymes, which can be employed in various fields of enzyme applications. As a potential application, EAPC-LP/PANFs were employed for the resolution of racemic ibuprofen via esterification with n-propanol and water in isooctane including AOT. For 102 hours under 100mM AOT, EAPC showed 42% conversion of racemic ibuprofen, whereas EA and EAC showed 1.2% and 1.4% of conversion, respectively.

Extended Abstract: File Not Uploaded
See more of this Session: Poster Session: Nanoscale Science and Engineering
See more of this Group/Topical: Nanoscale Science and Engineering Forum