Eleven fungal isolates were screened for their ability to oxidize 2,2’-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid). The highest laccase activity levels (about 6 200 U l^–1) were obtained in Coriolopsis byrsina GRB13 liquid cultures in the presence of 4-dimethylaminobenzoic acid and oak leaf extract. The enzyme from Coriolopsis byrsina GRB13 purified to homogeneity had a molecular mass of 57.7 kDa and an absorption maximum at 604 nm that is characteristic of blue copper proteins. It oxidized various substrates including 2,2’-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid), syringaldazine, promazine, phenoxazines, p-hydroxyphenylacetic acid and caffeic acid as well as Phenol Red and potassium hexacyanoferrate(II) (apparent bimolecular constants covered a range of 0.0002–25 μM^–1 s^–1). The laccase catalyzed synthesis of various substituted quinones starting from the simple o- and hydroquinone. Enzymatic synthesis of 3H-phenothiazin-3-one and 10H-phenazin-2-one was achieved for the first time. Two synthesized quinones (2-(N-methylanilino)-1,4-benzoquinone and 2-(3-nitroanilino)-1,4-benzoquinone) were powerful redox mediators applicable for bioelectrocatalytic systems based on pyrroquinoline quinone-dependent glucose dehydrogenase.

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