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

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  • 1Department of Chemical and Biomedical Engineering, West Virginia University, Morgantown, West Virginia 26506-6070, United States.

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Enzyme immobilization using metal-organic frameworks (MOFs) enhances biocatalyst stability and reusability. Molecular dynamics simulations reveal MOF interactions crucial for enzyme functional viability in industrial applications.

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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.