Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger.
Eur J Biochem
; 263(2): 386-95, 1999 Jul.
Article
en En
| MEDLINE
| ID: mdl-10406946
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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Base de datos:
MEDLINE
Asunto principal:
Aspergillus niger
/
Epóxido Hidrolasas
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Eur J Biochem
Año:
1999
Tipo del documento:
Article