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Chemo-enzymatic epoxidation of oleic acid and methyl oleate in solvent-free medium

Orellana-Coca, C; Törnvall, Ulrika LU ; Adlercreutz, Dietlind LU ; Mattiasson, Bo LU and Hatti-Kaul, Rajni LU (2005) In Biocatalysis and Biotransformation 23(6). p.431-437
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
solvent-free, oleic acid methyl ester, oleic acid, epoxidation, lipase, process
in
Biocatalysis and Biotransformation
volume
23
issue
6
pages
431 - 437
publisher
Taylor & Francis
external identifiers
  • wos:000234678100006
  • scopus:30144435624
ISSN
1024-2422
DOI
10.1080/10242420500389488
language
English
LU publication?
yes
id
6ee7629a-961b-4400-a1a2-a4dc7415cc9c (old id 209766)
date added to LUP
2007-08-07 17:06:38
date last changed
2017-09-17 05:23:05
@article{6ee7629a-961b-4400-a1a2-a4dc7415cc9c,
  abstract     = {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.},
  author       = {Orellana-Coca, C and Törnvall, Ulrika and Adlercreutz, Dietlind and Mattiasson, Bo and Hatti-Kaul, Rajni},
  issn         = {1024-2422},
  keyword      = {solvent-free,oleic acid methyl ester,oleic acid,epoxidation,lipase,process},
  language     = {eng},
  number       = {6},
  pages        = {431--437},
  publisher    = {Taylor & Francis},
  series       = {Biocatalysis and Biotransformation},
  title        = {Chemo-enzymatic epoxidation of oleic acid and methyl oleate in solvent-free medium},
  url          = {http://dx.doi.org/10.1080/10242420500389488},
  volume       = {23},
  year         = {2005},
}