Journal
PROCESS BIOCHEMISTRY
Volume 40, Issue 1, Pages 401-409Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2004.01.026
Keywords
immobilization; Candida rugosa lipase; Pseudomonas sp lipase; poly(ethylene oxide); enzymatic resolution
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Synthetic applications of lipases from Candida rugosa (CRL) and Pseudomonas sp. (PSL) immobilized on poly(ethylene oxide) (PEO) were studied. The morphology and thermal properties of the lipases immobilized on the support were analyzed by microscopy and thermal analysis techniques. To evaluate the efficiency of these systems, the esterification reaction of lauric acid (5 mmol) with n-pentanol (5 mmol) was studied. Reactional parameters such as time, temperature, enzyme concentration and organic media (n-hexane) were evaluated. The degree of esterification increased as a function of time, temperature and concentration. The influence of organic solvents (n-hexane, cyclohexane, n-heptane and acetone) was also considered for this reaction using a CRL/PEO system. The enzymatic resolutions of (R,S)-2-octanol, (R,S)-2-(4-chlorophenoxy) propionic and (R,S)-2-bromo hexanoic acids were also studied. The R-alcohol was obtained with enantiometric excess of product (eep) >98% (E = 180). For the resolution of racemic acids, the enantiomeric excess for the substrate (ees) values were in the range 1-76% and the eep values were in the range 6-96% (E = 1, 1-118). (C) 2004 Elsevier Ltd. All rights reserved.
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