Purification and physico-chemical properties of laccase

Laccase of Rhus vernicifera was purified by column chromatography on an ion-exchange resin and zone electrophoresis. The purity was confirmed by sedimentation and electrophoresis. It was revealed that the enzyme molecule has a molecular weight of 120,000 and carries four atoms of cupric copper per molecule. The oxidation-reduction potential of the enzyme was measured spectrophotometrically in the presence of ferrocyanide-ferricyanide system. The E0′ value found was + 415 mV at 25° and pH 7.0. The purified enzyme showed two absorption maxima at 280 mμ and 615 mμ with a shoulder at 330 mμ.