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Updated: Jul 31, 2026

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger
C Morisseau1, A Archelas, C Guitton
1Biocatalysis and Fine Chemistry Group, Université de la Méditerranée, ESA CNRS 6111, Faculté des Sciences de Luminy, Marseille, France.
Abstract:
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 degrees 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.
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