Isolation of lipase producer and its performance in enantioselective hydrolysis of glycidyl butyrate

Appl Biochem Biotechnol. 2003 Jan;104(1):69-79. doi: 10.1385/abab:104:1:69.

Abstract

A racemic glycidyl butyrate resolving strain, preliminarily identified as a Rhizopus sp., had been isolated from soil. Its extracellular lipase was found to enantioselectively hydrolyze the (S)-enantiomer of the chiral ester, with optimal activities at pH 5.3 and 42 degrees C. Higher enantioselectivity of the enzyme was observed at lower temperatures, while the best enantioselectivity was obtained at pH 5.5-6.0, with an E value (enantiomeric ratio) of 57.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Butyrates / metabolism*
  • Enzyme Activation
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Lipase / metabolism*
  • Mycelium / classification
  • Mycelium / metabolism
  • Reproducibility of Results
  • Rhizopus / classification*
  • Rhizopus / enzymology*
  • Sensitivity and Specificity
  • Soil Microbiology
  • Species Specificity
  • Stereoisomerism
  • Temperature

Substances

  • Butyrates
  • Lipase