Applied Microbiology and Biotechnology

, Volume 27, Issue 5–6, pp 451–456 | Cite as

Purification and properties of an acetyl specific carboxylesterase from Nocardia mediterranei

  • Hans-Peter Schär
  • Daniel Gygax
  • Gerardo M. Ramos Tombo
  • Oreste Ghisalba


An acetyl specific carboxylesterase has been purified from Nocardia mediterranei. The purified enzyme is homogeneous as shown by SDS polyacrylamide gel electrophoresis. The esterase has a molecular weight of 68,000 and is composed of two identical subunits. The enzyme exhibits optimal activity at pH 7.5 and at 35°C and is stable below 40°C. The enzyme activity is inhibited by several sulfhydryl reagents. The esterase hydrolyzes preferentially acetyl esters. Propionyl esters are cleaved very slowly whereas butyryl esters are no substrates at all. In addition, the esterase shows a pronounced regiospecificity. On the other hand the enantiospecificity is rather low as demonstrated by the hydrolysis of prochiral and racemic substrates.


Enzyme Ester Hydrolysis Electrophoresis Polyacrylamide 
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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • Hans-Peter Schär
    • 1
  • Daniel Gygax
    • 1
  • Gerardo M. Ramos Tombo
    • 1
  • Oreste Ghisalba
    • 1
  1. 1.Central Research Laboratories of Ciba-Geigy Ltd.BaselSwitzerland

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