Chemo-enzymatic epoxidation of oleic acid and methyl oleate in solvent-free medium
Chemo-enzymatic epoxidation of oleic acid (OA) and its methyl ester has been performed using hydrogen peroxide and immobilized lipase from Candida antarctica (Novozym(R) 435). The purpose of the study was to characterize the reaction under solvent-free conditions. The reaction temperature had a sign...
| Published in: | Biocatalysis and Biotransformation |
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| Main Authors: | , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Taylor & Francis
2005
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| Subjects: | |
| Online Access: | https://lup.lub.lu.se/record/209766 https://doi.org/10.1080/10242420500389488 |
| Summary: | Chemo-enzymatic epoxidation of oleic acid (OA) and its methyl ester has been performed using hydrogen peroxide and immobilized lipase from Candida antarctica (Novozym(R) 435). The purpose of the study was to characterize the reaction under solvent-free conditions. The reaction temperature had a significant impact on epoxidation of OA. At lower temperatures, the substrate conversion was hindered by the formation of solid epoxystearic acid product. Nearly 90% conversion of OA to the epoxide product was obtained after 6 h at 50 degrees C. Longer reaction times at 40 degrees C and above resulted in by-product formation and eventually lowered the product yield. In contrast, the reaction with methyl oleate (MO) was less influenced by temperature. Almost complete epoxidation was achieved at 40-60 degrees C, the higher the temperature the shorter was the reaction time. The main epoxidation product obtained was epoxystearic acid methyl ester (EME), and the remaining was epoxystearic acid (EA) formed by the hydrolytic action of the lipase. Recycling of the lipase for epoxidation of MO at 50 degrees C indicated that the immobilized enzyme was prone to activity loss. |
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