Oxidation of aromatic compounds and bioelectrocatalysis of peroxide by a novel white laccase from Myrothecium verrucaria NF-05

The enzymatic and electrochemical catalytic properties of a novel white laccase from Myrothecium verrucaria NF-05 were evaluated and compared with those of commercial oxidoreductases. NF-05 laccase effectively catalyzed the oxidation of several phenols and amines, indicating its wide substrate specificity. The cyclic voltammetry curves showed direct electron transfer on carbonous electrodes due to the direct absorption of NF-05 laccase. Peroxide was bioelectrochemically reduced more efficiently on NF-05 laccase-modified electrodes than on electrodes that were modified with commercial enzymes. The results demonstrate the potential applications of this enzyme in environmental bioremediation of aromatic pollutants and preparation of electronic devices.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Catalytical property of a novel white laccase was significantly better than control. ► The laccase alone significantly and effectively oxidized several aromatic compounds. ► The laccase showed great affinity to carbonous electrodes. ► DET was observed on carbonous electrodes directly absorbed by the laccase. ► Peroxide was electrochemically reduced on the laccase modified electrodes.