Enzyme Surface Residues Direct Encapsulation into Metal-Organic Frameworks for Performance Regulation

Area of Science:

• Materials Science
• Biotechnology
• Catalysis

Background:

• Protein functionalization is key for advanced biomaterials.
• Metal-organic frameworks (MOFs) offer tunable structures for various applications.
• Controlling MOF topology and protein integration remains a challenge.

Purpose of the Study:

• To investigate the role of nitrogen-enriched protein surface groups in directing MOF topology.
• To develop a modified-protein-directed MOFs template synthesis (mDTS) strategy for ZIF-L formation.
• To enhance the catalytic performance and loading of proteins within MOFs.

Main Methods:

• Utilized a modified-protein-directed MOFs template synthesis (mDTS) strategy.
• Employed surface modifications on cytochrome c (Cyt c) to induce ZIF-L formation.
• Varied surface modifier concentrations to tune protein activity.

Main Results:

• Demonstrated selective induction of leaf-like zeolitic imidazolate frameworks (ZIF-L) using modified Cyt c.
• Achieved a structural transition from ZIF-8 to ZIF-L, enhancing protein loading and catalytic activity.
• Showcased tunable enzyme activity by adjusting surface modifier concentration.

Conclusions:

• Protein surface nitrogen groups effectively direct MOF topological transformations.
• The mDTS method facilitates broad applicability for protein-MOF composite development.
• This approach holds significant promise for industrial catalysis and biotechnological applications.