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 | |
| State | Published - Jul 15 1999 |
Keywords
- Aspergillus niger
- Diols
- Enantioselectivity
- Epoxide hydrolase
- Regioselectivity
ASJC Scopus subject areas
- Biochemistry
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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