ABSTRACT
Pleurotus ostreatus degrades polychlorinated biphenyls (PCBs) with an increase of laccase activity. Laccases are well known for their detoxifying activity. We show, using reverse transcription polymerase chain reaction and a biochemical assay, that reduction in PCBs (di, tri, tetra, and penta) levels are correlated with an increase in laccase activity. P. ostreatus cultures were obtained from 0 to 30 days in the presence or absence of 7,100 mg/L PCBs (from transformer oil) and a surfactant. After each selected time cultures were withdrawn and remaining PCBs were determined, a maximal removal percentage of PCBs was obtained at 20 (63.5 ± 2.0) and 30 days (63.8 ± 4.6) post-induction. Also, the activity of the enzyme was analyzed and it was found to increase at 10 (6.9-fold) and 20 (6.77-fold) days post-induction in the presence of PCBs, as determined by its activity. Taken together, these data suggest that PCBs induce laccase expression and that laccase catalyzes PCBs removal.
