Assessment of Enzyme Functionality at Metal-Organic Framework Interfaces Developed through Molecular Simulations

Area of Science:

• Biocatalysis and enzyme engineering
• Materials science and nanotechnology
• Computational chemistry

Background:

• Enzymes offer high efficiency and selectivity for chemical transformations but suffer from poor reusability and denaturation in industrial settings.
• Enzyme immobilization is key to enhancing biocatalyst stability and enabling reuse in synthetic environments.
• Metal-organic frameworks (MOFs) are promising materials for enzyme immobilization due to their tunable properties and industrial applicability.

Purpose of the Study:

• To investigate the noncovalent interactions between model enzymes (carbonic anhydrase and myeloperoxidase) and selected MOFs (MIL-160 and ZIF-8).
• To evaluate the binding energies and interaction mechanisms for enzyme-MOF complexes using molecular dynamics simulations.
• To understand how MOF properties influence enzyme stability and functional viability for industrial applications.

Main Methods:

• Molecular dynamics (MD) simulations were employed to model enzyme-MOF interactions.
• The study focused on carbonic anhydrase (CA) and myeloperoxidase (MPO) as model enzymes.
• MIL-160 and ZIF-8 were selected as representative MOFs for assessing binding energies and interaction types.

Main Results:

• Carbonic anhydrase (CA) and myeloperoxidase (MPO) exhibited optimal binding energies of 201 and 501 kJ mol⁻¹, respectively, with MIL-160, driven by hydrogen bonding.
• Enzyme binding to ZIF-8 was influenced more by hydrophobic-hydrophobic interactions, yielding binding energies of 106 kJ mol⁻¹ for CA and 201 kJ mol⁻¹ for MPO.
• The findings highlight the differential binding mechanisms of enzymes to various MOFs, influenced by specific noncovalent interactions.

Conclusions:

• Metal-organic frameworks (MOFs) like MIL-160 and ZIF-8 can effectively immobilize enzymes, enhancing their stability and reusability.
• Hydrogen bonding plays a significant role in the binding of enzymes to MIL-160, while hydrophobic interactions dominate with ZIF-8.
• These insights are crucial for designing advanced biocatalysts for diverse industrial applications, including biomedical technology and chemical production.