Asymmetric hydrolysis of a meso-diester using pig liver esterase immobilised in hollow fibre ultrafiltration membrane

Helena A. Sousa, João G. Crespo, Carlos A. M. Afonso

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 languageEnglish
Pages (from-to)929-934
Number of pages6
JournalTetrahedron-Asymmetry
Volume11
Issue number4
DOIs
Publication statusPublished - 10 Mar 2000

Fingerprint

Dicarboxylic Acids
Polysulfones
swine
Ultrafiltration
Esterases
liver
Liver
hydrolysis
Hydrolysis
hollow
Esters
Enzymes
membranes
Membranes
fibers
Acids
Fibers
dicarboxylic acids
Substrates
enzymes

Keywords

  • Lipases
  • Enantioselectivity
  • Lipase B

Cite this

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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.",
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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 journalArticle

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.).

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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.

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