Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of
phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial
uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or engineering
of enzymes to be stable and active in acidic or alkaline pHs, high temperatures, oxidative conditions and
tolerant to high salinity and/or organic solvents. Here we used a PCR-based screening to clone two novel
laccase coding sequences from the white-rot basidiomycete Trametes trogii. Recombinant expression of
lcc3 gene in Komagataella (=Pichia) pastoris showed that it encodes a thermo active and the... More
Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of
phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial
uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or engineering
of enzymes to be stable and active in acidic or alkaline pHs, high temperatures, oxidative conditions and
tolerant to high salinity and/or organic solvents. Here we used a PCR-based screening to clone two novel
laccase coding sequences from the white-rot basidiomycete Trametes trogii. Recombinant expression of
lcc3 gene in Komagataella (=Pichia) pastoris showed that it encodes a thermo active and thermostable
laccase with an optimum temperature of 50 ◦C and with a half-life of 45 min at 70 ◦C and a stability
higher than 3 h at 60 ◦C. Furthermore, recombinant LCC3 was capable of decolorizing between 50% and
100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural
redox mediator acetosyringone within 2 h of incubation at pH 6 and 70 ◦C.
