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Modulating the Biofunctionality of Metal-Organic-Framework-Encapsulated Enzymes through Controllable Embedding

Guosheng Chen1, Xiaoxue Kou1, Siming Huang2

  • 1MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China.

Angewandte Chemie (International Ed. in English)
|November 22, 2019
PubMed
Summary

Enzyme@MOF stability and bioactivity depend on encapsulation. Rapid enzyme-triggered nucleation preserves enzyme activity, while slow coprecipitation leads to inactivity due to unfolding and ligand interference.

Keywords:
biocatalysisembedding patternsenzyme immobilizationenzyme-surface modificationmetal-organic frameworks

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Area of Science:

  • Biocatalysis
  • Materials Science
  • Nanotechnology

Background:

  • Enzyme encapsulation in Metal-Organic Frameworks (MOFs) enhances enzyme stability and imparts new MOF functionalities.
  • Limited understanding exists regarding how MOF embedding patterns influence enzyme bioactivity and functionality.

Purpose of the Study:

  • To investigate the impact of embedding patterns on the bioactivity of enzymes encapsulated within ZIF-8.
  • To elucidate the mechanisms behind activity loss or retention in enzyme@MOF systems.

Main Methods:

  • Controlled encapsulation of enzymes within ZIF-8 using two distinct methods: rapid enzyme-triggered nucleation and slow coprecipitation.
  • Chemical modification of enzyme amino acids to modulate encapsulation and bioactivity.

Main Results:

  • Enzyme@MOF retained high activity when ZIF-8 nucleation was rapid and enzyme-triggered.
  • Enzyme@MOF became inactive when encapsulation involved slow coprecipitation, leading to enzyme unfolding and ligand-induced coordination interference.

Conclusions:

  • The method of MOF encapsulation critically determines the bioactivity of embedded enzymes.
  • Enzyme biofunctionality can be modulated by controlling embedding patterns through chemical modification of enzyme amino acids.