Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger

Christophe Morisseau, Alain Archelas, Carole Guitton, Didier Faucher, Roland Furstoss, Jacques C. Baratti

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The epoxide hydrolase from Aspergillus niger was purified to homogeneity using a four-step procedure and p-nitrostyrene oxide (pNSO) as substrate. The enzyme was purified 246-fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum activity was observed at 40 °C, pH 7.0, and with dimethylformamide as cosolvent to dissolve pNSO. Hydrolysis of pNSO was highly enantioselective, with an E value (i.e. enantiomeric ratio) of 40 and a high regioselectivity (97%) for the less hindered carbon atom of the epoxide. This enzyme may be a good biocatalyst for the preparation of enantiopure epoxides or diols.

Original languageEnglish (US)
Pages (from-to)386-395
Number of pages10
JournalEuropean Journal of Biochemistry
Issue number2
StatePublished - Jul 15 1999



  • Aspergillus niger
  • Diols
  • Enantioselectivity
  • Epoxide hydrolase
  • Regioselectivity

ASJC Scopus subject areas

  • Biochemistry

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