Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger

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...

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Veröffentlicht in:	European journal of biochemistry 1999-07, Vol.263 (2), p.386-395
Hauptverfasser:	Morisseau, C, Archelas, A, Guitton, C, Faucher, D, Furstoss, R, Baratti, J.C
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - chemistry Aspergillus niger Aspergillus niger - enzymology Base Sequence diols Dose-Response Relationship, Drug enantioselectivity epoxide hydrolase Epoxide Hydrolases - chemistry Epoxide Hydrolases - isolation & purification Epoxy Compounds - metabolism Hydrogen-Ion Concentration Kinetics Models, Chemical Molecular Sequence Data plant biochemistry plant physiology regioselectivity Temperature Time Factors
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