Novel bicomponent microfibrous mats containing targeted amount of reactive maleic anhydride groups were prepared by electrospinning of mixed solutions of poly(styrene-alt-maleic anhydride) and poly(styrene-co-maleic anhydride). Then, amino-functionalized P(St-alt-MA)/P(St-co-MA) mats were obtained by reaction with p-phenylenediamine. ATR-FTIR and XPS spectroscopy were used to characterize pristine and modified P(St-alt-MA)/P(St-co-MA) mats. On the next step, laccase from Trametes versicolor was covalently attached onto the modified mats; the average amount of immobilized enzyme was 40 +/- 0.7 mg/g mat. The catalytic activity of the immobilized enzyme was studied in respect to bisphenol A (BPA) endocrine disruptor. The optimum activity of the immobilized enzyme was reached at maximum flow rate of 1.3 mL/s. After 90 min the BPA concentration was reduced by 60% and the catalytic activity of microfibrous mats remained stable for about 30 successive reuses. In addition, the relative activity of laccase immobilized on the microfibrous mats was displayed in a broader pH range as compared to that of the free one. (C) 2009 Elsevier Ltd. All rights reserved.