Abstract
Pig liver esterase (PLE) was physically immobilised in a polysulphone ultrafiltration hollow fibre membrane reactor and used for the repetitive batch two-phase hydrolysis and separation, on a multigram scale, of the meso-diester dimethyl cis-cycloxex-4-ene-1,2-dicarboxylate 1 to enantiomerically pure (1S,2R)-cyclohex-4-ene-1,2-dicarboxylic acid monomethyl ester 2. After 25 days, the enzyme still retained its initial activity, which corresponds to 62% of its activity in the free form, and the enantiomeric purity of monoester 2 was still higher than 97%. Simple experimental conditions were established for the large laboratory scale preparation of substrate 1 and isolation of product 2 from the aqueous phase. Copyright (C) 2000 Elsevier Science Ltd.
| Original language | English |
|---|---|
| Pages (from-to) | 929-934 |
| Number of pages | 6 |
| Journal | Tetrahedron-Asymmetry |
| Volume | 11 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 10 Mar 2000 |
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Keywords
- Lipases
- Enantioselectivity
- Lipase B
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Asymmetric hydrolysis of a meso-diester using pig liver esterase immobilised in hollow fibre ultrafiltration membrane. / Sousa, Helena A.; Crespo, João G.; Afonso, Carlos A. M.
In: Tetrahedron-Asymmetry, Vol. 11, No. 4, 10.03.2000, p. 929-934.Research output: Contribution to journal › Article
TY - JOUR
T1 - Asymmetric hydrolysis of a meso-diester using pig liver esterase immobilised in hollow fibre ultrafiltration membrane
AU - Sousa, Helena A.
AU - Crespo, João G.
AU - Afonso, Carlos A. M.
N1 - We would like to thank Fundação para a Ciência e Tecnologia (FCT, project PBIC/C/QUI/2360/95 and a Ph.D. grant for H.A.S.).
PY - 2000/3/10
Y1 - 2000/3/10
N2 - Pig liver esterase (PLE) was physically immobilised in a polysulphone ultrafiltration hollow fibre membrane reactor and used for the repetitive batch two-phase hydrolysis and separation, on a multigram scale, of the meso-diester dimethyl cis-cycloxex-4-ene-1,2-dicarboxylate 1 to enantiomerically pure (1S,2R)-cyclohex-4-ene-1,2-dicarboxylic acid monomethyl ester 2. After 25 days, the enzyme still retained its initial activity, which corresponds to 62% of its activity in the free form, and the enantiomeric purity of monoester 2 was still higher than 97%. Simple experimental conditions were established for the large laboratory scale preparation of substrate 1 and isolation of product 2 from the aqueous phase. Copyright (C) 2000 Elsevier Science Ltd.
AB - Pig liver esterase (PLE) was physically immobilised in a polysulphone ultrafiltration hollow fibre membrane reactor and used for the repetitive batch two-phase hydrolysis and separation, on a multigram scale, of the meso-diester dimethyl cis-cycloxex-4-ene-1,2-dicarboxylate 1 to enantiomerically pure (1S,2R)-cyclohex-4-ene-1,2-dicarboxylic acid monomethyl ester 2. After 25 days, the enzyme still retained its initial activity, which corresponds to 62% of its activity in the free form, and the enantiomeric purity of monoester 2 was still higher than 97%. Simple experimental conditions were established for the large laboratory scale preparation of substrate 1 and isolation of product 2 from the aqueous phase. Copyright (C) 2000 Elsevier Science Ltd.
KW - Lipases
KW - Enantioselectivity
KW - Lipase B
UR - http://www.scopus.com/inward/record.url?scp=0034629039&partnerID=8YFLogxK
U2 - 10.1016/S0957-4166(00)00009-4
DO - 10.1016/S0957-4166(00)00009-4
M3 - Article
VL - 11
SP - 929
EP - 934
JO - Tetrahedron-Asymmetry
JF - Tetrahedron-Asymmetry
SN - 0957-4166
IS - 4
ER -