Rational Construction of Light‐Enzyme Hybrid System Driving Interfacial Electrons for Selective Degradation of Bisphenol A: Controlled Immobilization Strategy and Synergistic Catalytic Mechanism

Conventional enzyme immobilization often blocks active sites and disrupts electron transfer due to random binding. Here, a rational interface engineering strategy for laccase immobilization is reported. Laccase (LaC) is anchored onto amino/hydroxyl‐functionalized mesoporous carbon spheres (MCS) to form LaC‑MCS. Then, a hydrogen‑bonded organic framework (HOF‑101) shell is grown in situ to yield a core–shell photoenzyme hybrid (LaC‑MCS@HOF). The bifunctional MCS core provides rigid anchoring and flexible stabilization, maximizing active‑site exposure. The HOF shell selectively enriches bisphenol A (BPA) by 52.1% via static adsorption, and under light irradiation, photogenerated electrons are directionally injected into the T1 copper center of laccase, accelerating the rate‑limiting enzymatic cycle. The hybrid achieves 90.3% BPA degradation in light (75.1% in dark), with a 3.7‑fold activity enhancement over free laccase. Electron paramagnetic resonance confirms a cooperative multi‑ROS pathway (·O 2 − and ·OH). The system maintains >86.2% efficiency after 90 days (360 cycles) in a double‑straight‑channel microfluidic reactor. The platform's universality is demonstrated by immobilizing catalase and horseradish peroxidase, achieving >98.3% degradation within 30 min. This work provides a new conceptual framework for designing photoenzyme hybrids with interfacial electron transfer, selective enrichment, and exceptional stability for environmental remediation.