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Purification, characterization and application of laccase from <i>Trametes versicolor</i> for colour and phenolic removal of olive mill wastewater in the presence of 1- hydroxybenzotriazole
Abstract
Laccase forms (L1 and L2) from Trametes versicolor CCT 4521 showed a molecular mass of 66 kDa and optimum temperature around 40oC. The optimum pH (4.0 and 5.0) and Km (28.6 and 5 ìM) values using
syringaldazine as substrate were found for L1 and L2, respectively. The enzymes were able to oxidize several compounds and were strongly inhibited by sodium azide, L-cysteine and dithiothreitol. The 75%
of the N-terminal sequences were identical in both forms and similarities around 40 - 60% of laccases from wood-degrading fungi were observed. The use of 1-hydroxybenzotriazole as a mediator increased the compounds oxidized by laccases in olive mill wastewater.
syringaldazine as substrate were found for L1 and L2, respectively. The enzymes were able to oxidize several compounds and were strongly inhibited by sodium azide, L-cysteine and dithiothreitol. The 75%
of the N-terminal sequences were identical in both forms and similarities around 40 - 60% of laccases from wood-degrading fungi were observed. The use of 1-hydroxybenzotriazole as a mediator increased the compounds oxidized by laccases in olive mill wastewater.
