This study presents a highly efficient and sustainable biocatalytic platform for bisphenol A (BPA) bioremediation through the covalent immobilization of laccase onto hierarchically functionalized cotton fibers. The immobilization strategy involved selective periodate oxidation of cellulose, grafting a hexamethylenediamine (HMDA) spacer arm, and glutaraldehyde activation, ensuring stable covalent attachment. Characterization via FTIR, SEM, and BET confirmed successful surface modification and high enzyme loading, achieving an immobilization yield of 90.5%. The immobilized laccase (CT-DA-HMD-Lac) exhibited significantly enhanced performance compared to the free enzyme, with a two-fold increase in maximum reaction velocity (Vmax) and a 75% improvement in catalytic efficiency of action (Vmax/Km). Furthermore, the biocatalyst demonstrated superior robustness, maintaining high activity across broader pH and temperature ranges, and retaining 75% of its initial activity after 15 consecutive reusability cycles. Storage stability was also markedly improved, with 83% activity retention after 60 days. Practical application in BPA degradation showed 85% removal efficiency within 300 min, a 2.4-fold increase in the degradation rate constant over the free enzyme. These results highlight functionalized cotton as a promising, cost-effective, and scalable support for advanced enzymatic wastewater treatment and the remediation of persistent endocrine-disrupting chemicals.
El‐Shishtawy et al. (Fri,) studied this question.