Highly Enantioselective Catalysis by Enzyme Encapsulated in Metal Azolate Frameworks with Micelle-Controlled Pore...

Area of Science:

• Materials Science
• Biocatalysis
• Nanotechnology

Background:

• Metal-organic frameworks (MOFs) offer enhanced stability for encapsulated enzymes.
• Small MOF apertures limit enzyme accessibility to small molecules, hindering broader applications.
• Enzyme immobilization in MOFs is crucial for developing efficient biocatalysts.

Purpose of the Study:

• To develop a novel MOF with large pores for enzyme encapsulation.
• To enable enzyme-catalyzed asymmetric synthesis of larger chiral molecules.
• To enhance the catalytic efficiency of encapsulated enzymes.

Main Methods:

• Aqueous synthesis of MAF-6 using visible linker micelles.
• Encapsulation of enzyme BCL within MAF-6.
• Optimization of surfactant effects (e.g., sodium dodecyl sulfate - SDS) during synthesis.
• Characterization of MAF-6 pore size (7.6 Å) and comparison with ZIF-8 (3.4 Å).

Main Results:

• MAF-6 exhibits a significantly larger pore aperture than ZIF-8.
• Enzyme BCL encapsulated in MAF-6 (BCL@MAF-6-SDS) showed 420 times greater catalytic efficiency than BCL@ZIF-8.
• The biocomposite efficiently synthesized drug precursors with 94-99% enantioselectivity and high yields.

Conclusions:

• Visible linker micelle-directed synthesis enables the creation of large-aperture MOFs for enzyme encapsulation.
• Enzyme@MAF-6 biocomposites are highly effective for the asymmetric synthesis of chiral molecules and pharmaceuticals.
• This work advances the understanding of enzyme encapsulation in MOFs for catalytic applications.