Sodium alginate-immobilized epoxide hydrolase: A multifaceted strategy for enhanced stability, reusability, and...

Immobilized macromolecular enzymes effectively address critical challenges including environmental sensitivity, thermal instability, and non-reusability, thereby establishing the fundamental and practical significance of enzyme immobilization research. This study employed sodium alginate (SA), ZIF-8, and Bi-EA materials to immobilize Aspergillus carlsbadensis-derived epoxide hydrolase (AcEH). Comparative analysis revealed SA's superior immobilization efficiency. Material characterization via SEM, FTIR, and XRD was performed, followed by optimization of SA immobilization parameters. The immobilized enzyme maintained activity over 6 reuse cycles. Incorporating 0.5 wt% carboxymethyl cellulose (CMC) extended AcEH@SA-CMC reusability to 8 cycles. Magnetic modification through Fe₃O₄ powder incorporation yielded AcEH@SA-CMC- Fe₃O₄ hydrogel with enhanced recoverability. Results demonstrate SA's exceptional biocompatibility underpins its immobilization efficacy, while CMC co-entanglement creates a porous network facilitating mass transfer and mechanical reinforcement. Fe₃O₄ powder plays a promoting role in improving enzyme activity. This methodology not only evaluates immobilization matrices but establishes an optimized protocol for macromolecular AcEH immobilization.