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 |
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Keywords
- Aspergillus niger
- Diols
- Enantioselectivity
- Epoxide hydrolase
- Regioselectivity
ASJC Scopus subject areas
- Biochemistry
Cite this
Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger. / Morisseau, Christophe; Archelas, Alain; Guitton, Carole; Faucher, Didier; Furstoss, Roland; Baratti, Jacques C.
In: European Journal of Biochemistry, Vol. 263, No. 2, 15.07.1999, p. 386-395.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger
AU - Morisseau, Christophe
AU - Archelas, Alain
AU - Guitton, Carole
AU - Faucher, Didier
AU - Furstoss, Roland
AU - Baratti, Jacques C.
PY - 1999/7/15
Y1 - 1999/7/15
N2 - 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.
AB - 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.
KW - Aspergillus niger
KW - Diols
KW - Enantioselectivity
KW - Epoxide hydrolase
KW - Regioselectivity
UR - http://www.scopus.com/inward/record.url?scp=0033565356&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033565356&partnerID=8YFLogxK
U2 - 10.1046/j.1432-1327.1999.00519.x
DO - 10.1046/j.1432-1327.1999.00519.x
M3 - Article
C2 - 10406946
AN - SCOPUS:0033565356
VL - 263
SP - 386
EP - 395
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 2
ER -