Laccase from Trametes versicolor was immobilized via the formation of interlinking enzyme aggregates (CLEA). Its free and immobilized enzymes were characterized, and its efficiency was tested via the removal of bisphenol A (BPA) in aqueous solution. The resistances against thermal denaturation and pH variations were improved upon immobilization. Although the optimal pH of the enzyme was not modified by immobilization, the latter considerably increased its stability in the pH range of 2.0 to 8.0. The immobilized form was still 50% active after 6 months of storage, while the free form took 1 month to suffer a similar drop in activity. Both free and immobilized T. versicolor laccases were efficient in removing 200 µM BPA from aqueous solutions. The free laccase removed 79% and 92.9% of the compound during the first hour of reaction when 0.1 and 0.2 U were used, respectively. The immobilized form, on the other hand, removed 72% and 94.1% of 200 µM BPA during the first hour of reaction when 0.2 and 0.5 U were used, respectively. The immobilized enzyme allowed seven reuse cycles in the oxidation of ABTS and up to four cycles in the degradation of BPA. The results suggest that the laccase from T. versicolor may be useful in biological strategies aiming at degrading endocrine disruptors, such as BPA.