A detailed physicochemical and functional analysis of immobilized laccase on Cu-BDC material was carried out to evaluate its efficiency and stability in the removal of 17α-ethynylestradiol (EE2). Structural and morphological studies of Cu-BDC before and after laccase immobilization were conducted using SEM, CLSM, and AFM microscopy. Before immobilization, the material was characterized by a smooth structure with few defects, numerous free spaces, and open internal channels. After laccase immobilization, the MOF surface was coated with the enzyme, forming agglomerates of irregular shape, confirmed by an increase in particle number and a decrease in surface roughness. The immobilization process achieved an efficiency of more than 80%, with 88% retention of the enzyme's catalytic activity. The kinetic and thermodynamic parameters indicated higher stability of the immobilized laccase compared to the free enzyme, suggesting that MOF provides a suitable support for enzyme immobilization, enhancing its stability and efficiency. The fabricated biocatalytic systems also exhibited greater tolerance to varying pH and temperature conditions as compared to the free enzyme. These biocatalytic systems demonstrated high efficiency in the degradation of 17α-ethynylestradiol from model solutions and real wastewater. The results obtained indicate that the immobilization of laccase on a Cu-BDC carrier can be an effective solution for bioremediation processes of pollutants in wastewater, opening up prospects for the wide application of this technology in the water and wastewater industry.