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.
- Lipase B