[Conversion of polychlorophenols by laccases with 1-hydroxybenzotriazole as a mediator].

The action of purified laccase from the basidial fungi Cerrena unicolor and Trametes sp. on 2,4,6-trichlorophenol (2,4,6-TCP) and pentachlorophenol (PCP) was studied, including reactions involving I-hydroxybenzotriazole as a mediator. Oxidation of 2,4,6-TCP by laccase without the mediator yielded 2,6-dichlorobenzoquinone as a primary conversion product, whereas PCP was not oxidized.

[Laccase of the lignolytic fungus Trametes hirsuta: purification and characterization of the enzyme, and cloning and primary structure of the gene].

The main physicochemical characteristics of the major isoform of the laccase secreted by the fungu, Trametes hirsuta 072 were studied. The enzyme belongs to the group of high redox potential laccases (E(T1) = 790 +/- 5), and it oxidizes with high efficiency various substrates of phenolic nature. The gene of this isoform was cloned, and its nucleotide sequence was determined.