Molecular Simulation of Enzyme Adsorption and Immobilization in MIL-53(Fe)-Based Covalent Organic Frameworks
DOI:
https://doi.org/10.64229/7n7qs610Keywords:
Molecular simulation, Enzyme immobilization, Covalent organic framework, Density functional theoryAbstract
This study investigates enzyme adsorption in covalent organic frameworks (COFs) using molecular simulations. Laccase was immobilized on MIL-53(Fe) and NH₂-MIL-53(Fe) frameworks to develop visible-light-responsive biocatalysts. Molecular dynamics (MD) and density functional theory (DFT) analyses revealed that enzyme immobilization significantly enhanced electron transfer (ET) between the photocatalyst and the enzyme’s active site, promoting efficient charge separation and interfacial electron mobility. Electron spin resonance spectroscopy and free energy calculations demonstrated that visible light improved photogenerated ET, increasing tetracycline degradation rate constant from 0.0062 to 0.0127 min⁻¹. Morphological analysis showed MIL-53(Fe) possessed a stable octahedral crystalline structure with ~400 nm border length, ideal for enzyme binding. The binding free energy of -356 kcal/mol indicated thermodynamically favorable and strong enzyme-framework interactions. Furthermore, covalent immobilization improved laccase’s structural stability and preserved its native conformation compared to physisorption, facilitating access to the active site. Overall, this work highlights that COF-based enzyme immobilization offers a stable and highly active platform for enhanced photocatalytic degradation and environmental remediation applications.
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