Abstract
Polycyclic aromatic hydrocarbons (PAHs) are recognized as a toxic, mutagenic and/or carcinogenic compounds, and their pollution of soil and aquifer is of increasing environmentally risk. Laccases (E.C. 1.10.3.2) are phenoloxidases catalyze the oxidation of PAHs in the presence of a mediator compound and hyacinth plant. In this study laccase from Trametes versicolor was immobilized into chitosan, and the potential to oxidize anthracene in the presence of 1-hydroxybenzotriazole (HBT) was examined. Results indicated that the immobilization enhanced the stability of laccase against temperature, pH, inhibitors and loading time compared with the other cases. The immobilized laccase-mediator system was as efficient as the free enzyme for oxidizing the tested PAHs. After 24h. of incubation, immobilized laccase–HBT showed a system oxidization more than immobilized laccase without (HBT) of PAHs; Chitosan with hyacinth plant and (HBT) resulted better conversion than chitosan with or without HBT. These results indicate a new chance for applying the immobilized laccase in bioremediation.
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