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Lipase catalyzed esterification of glycidol in organic solvents

Journal Article · · Biotechnology and Bioengineering; (United States)
; ;  [1]
  1. Univ. Nova de Lisboa, Oeiras (Portugal). Centro de Tecnologia Quimica e Biologica

The authors studied the resolution of racemic glycidol through esterification with butyric acid catalyzed by porcine pancreatic lipase in organic media. A screening of seven solvents (log P values between 0.49 and 3.0, P being the n-octanol-water partition coefficient of the solvent) showed that neither log P nor the logarithm of the molar solubility of water in the solvent provides good correlations between enantioselectivity and the properties of the organic media. Chloroform was one of the best solvents as regards the enantiometic purity (e.p.) of the ester produced. In this solvent, the optimum temperature for the reaction was determined to be 35C. The enzyme exhibited maximum activity at a water content of 13 [plus minus] 2% (w/w). The enantiomeric purity obtained was 83 [plus minus] 2% of (S)-glycidol butyrate and did not depend on the alcohol concentration or the enzyme water content for values of these parameters up to 200 mM and 25% (w/w), respectively. The reaction was found to follow a BiBi mechanism.

OSTI ID:
6279685
Journal Information:
Biotechnology and Bioengineering; (United States), Journal Name: Biotechnology and Bioengineering; (United States) Vol. 42:4; ISSN BIBIAU; ISSN 0006-3592
Country of Publication:
United States
Language:
English