Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 181-186 |
| Seitenumfang | 6 |
| Fachzeitschrift | Enzyme and microbial technology |
| Jahrgang | 19 |
| Ausgabenummer | 3 |
| Publikationsstatus | Veröffentlicht - 15 Aug. 1996 |
Abstract
The lipase-catalyzed kinetic resolution of different 3-hydroxy esters in organic solvents and supercritical carbon dioxide (SCCO2) was studied. Similar enantiomeric excesses (ee, up to 99%) as found for transesterifications in organic solvents were achieved also in SCCO2. The influence of various reaction parameters was investigated for the resolution of 3-hydroxy octanoic acid methyl esters with lipase from Pseudomonas cepacia in SCCO2. Optimum conditions have been found at 11O bar, 40°C, and in the presence of 1.5 g molecular sieve by using vinyl acetate as acyl donor. The addition of different cosolvents had only a small effect on the reaction. Immobilization of the lipase on VA-epoxy resulted in similar optical purities as found for the elude lipase, but at halved reaction times. The effect of supercritical conditions on the stability of the lipase was also investigated.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biotechnologie
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Immunologie und Mikrobiologie (insg.)
- Angewandte Mikrobiologie und Biotechnologie
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in: Enzyme and microbial technology, Jahrgang 19, Nr. 3, 15.08.1996, S. 181-186.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Lipase-catalyzed kinetic resolution of 3-hydroxy esters in organic solvents and supercritical carbon dioxide
AU - Capewell, A.
AU - Wendel, V.
AU - Bornscheuer, Uwe T.
AU - Meyer, H. H.
AU - Scheper, T.
N1 - Funding information: This work was financially supportedb y the EEC BRIDGE program (Grant BIOT-CT-90-0176). The authors are grateful to Merck (Darmstadt,G ermany) for kindly providing us with chemicals and Amano PharmaceuticalsL td., Nagoya, Japan for the gift of lipase.
PY - 1996/8/15
Y1 - 1996/8/15
N2 - The lipase-catalyzed kinetic resolution of different 3-hydroxy esters in organic solvents and supercritical carbon dioxide (SCCO2) was studied. Similar enantiomeric excesses (ee, up to 99%) as found for transesterifications in organic solvents were achieved also in SCCO2. The influence of various reaction parameters was investigated for the resolution of 3-hydroxy octanoic acid methyl esters with lipase from Pseudomonas cepacia in SCCO2. Optimum conditions have been found at 11O bar, 40°C, and in the presence of 1.5 g molecular sieve by using vinyl acetate as acyl donor. The addition of different cosolvents had only a small effect on the reaction. Immobilization of the lipase on VA-epoxy resulted in similar optical purities as found for the elude lipase, but at halved reaction times. The effect of supercritical conditions on the stability of the lipase was also investigated.
AB - The lipase-catalyzed kinetic resolution of different 3-hydroxy esters in organic solvents and supercritical carbon dioxide (SCCO2) was studied. Similar enantiomeric excesses (ee, up to 99%) as found for transesterifications in organic solvents were achieved also in SCCO2. The influence of various reaction parameters was investigated for the resolution of 3-hydroxy octanoic acid methyl esters with lipase from Pseudomonas cepacia in SCCO2. Optimum conditions have been found at 11O bar, 40°C, and in the presence of 1.5 g molecular sieve by using vinyl acetate as acyl donor. The addition of different cosolvents had only a small effect on the reaction. Immobilization of the lipase on VA-epoxy resulted in similar optical purities as found for the elude lipase, but at halved reaction times. The effect of supercritical conditions on the stability of the lipase was also investigated.
KW - 3-hydroxy esters
KW - Kinetic resolution
KW - Lipase
KW - Organic solvents
KW - Pseudomonas cepacia
KW - Supercritical carbon dioxide
UR - http://www.scopus.com/inward/record.url?scp=0030586805&partnerID=8YFLogxK
U2 - 10.1016/0141-0229(95)00229-4
DO - 10.1016/0141-0229(95)00229-4
M3 - Article
AN - SCOPUS:0030586805
VL - 19
SP - 181
EP - 186
JO - Enzyme and microbial technology
JF - Enzyme and microbial technology
SN - 0141-0229
IS - 3
ER -