Abstract A soluble enzyme which catalyses the NADPH-dependent reduction of the heterocyclic double bond of the isoflavone biochanin A (5, 7-dihydroxy-4′-methoxy- isoflavone) yielding the corresponding isoflavanone was isolated from the fungus Fusarium javanicum. The NADPH: biochanin A oxidoreductase was constitutively present in the mycelium with an extractable average activity of 4 pkat/g fresh weight. The enzyme was ...
