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

doi:10.1046/j.1432-1327.1999.00519.x

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

Entomology

Research output: Contribution to journal › Article

58 Scopus citations

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 °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 language	English (US)
Pages (from-to)	386-395
Number of pages	10
Journal	European Journal of Biochemistry
Volume	263
Issue number	2
DOIs	https://doi.org/10.1046/j.1432-1327.1999.00519.x
State	Published - Jul 15 1999

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Keywords

Aspergillus niger
Diols
Enantioselectivity
Epoxide hydrolase
Regioselectivity

ASJC Scopus subject areas

Biochemistry

Cite this

Morisseau, C., Archelas, A., Guitton, C., Faucher, D., Furstoss, R., & Baratti, J. C. (1999). Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger. European Journal of Biochemistry, 263(2), 386-395. https://doi.org/10.1046/j.1432-1327.1999.00519.x

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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 °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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AU - Morisseau, Christophe

AU - Archelas, Alain

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AU - Faucher, Didier

AU - Furstoss, Roland

AU - Baratti, Jacques C.

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10.1046/j.1432-1327.1999.00519.x