Two laccase isoenzymes (LacA and LacB) were isolated from a novelTrichoderma harzianumS7113 isolate employing ammonium sulfate precipitation, Sephadex G100, and DEAE Sepharose ion exchange chromatography. The molecular weights of the purified LacA and LacB laccases were estimated to be 63 and 48 kDa, respectively. The two isoenzymes had their optimum activities at the same temperature (50 °C), but at slightly different pH values (pH 3.0 for LacA and pH 2.5 for LacB). LacA and LacB had the same thermal stability at 40 °C and pH stability at pH 9.0. The two isoenzymes also showed a high level of specific activity toward ABTS, where theK_mvalues of LacA and LacB were 0.100 and 0.065 mM, whereas theirV_maxvalues were 0.603 and 0.182 µmol min⁻¹, respectively. LacA and LacB catalytic activity was stimulated by Mg²⁺, Zn²⁺, K⁺, and Ni²⁺, whereas it was inhibited by Hg²⁺and Pb²⁺, β-mercaptoethanol, EDTA, and SDS, and completely inhibited by sodium azide. Our findings indicate that purified laccase has a promising capacity for bisphenol A (BPA) bioremediation across a broad pH range. This finding opens up new opportunities for the commercialization of this technique in a variety of biotechnology-based applications, particularly for removing endocrine chemicals from the environment.