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 |
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Pages (from-to) | 929-934 |
Number of pages | 6 |
Journal | Tetrahedron-Asymmetry |
Volume | 11 |
Issue number | 4 |
DOIs | |
Publication status | Published - 10 Mar 2000 |
Keywords
- Lipases
- Enantioselectivity
- Lipase B