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Interfacial Stabilization through MOF-Polymer Core-Shell Design: Ultraefficient, Stable and Recyclable Enzymatic

Chengfu Zhang1,2,3, Jinxia Hu1,4, Ling Ma5

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We created a novel hybrid material that significantly enhances enzyme stability and catalytic efficiency. This breakthrough improves enzyme performance in challenging conditions, paving the way for advanced biocatalysis.

Keywords:
MOFenzyme immobilizationlipasepolyacrylic acid

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Area of Science:

  • Materials Science
  • Biochemistry
  • Chemical Engineering

Background:

  • Enzyme immobilization in metal-organic frameworks (MOFs) is hindered by framework instability under extreme conditions, leading to reduced enzymatic activity.
  • Developing robust enzyme-MOF composites is crucial for advancing biocatalysis, biosensing, and industrial applications.

Purpose of the Study:

  • To design a novel MOF-poly(acrylic acid) (PAA) hybrid material (MPHM) with an "active core-skeleton-shell" architecture to enhance enzyme stability and catalytic efficiency.
  • To investigate the structural and functional properties of the lipase-MPHM composite (lipase@MPHM).

Main Methods:

  • Fabrication of a hierarchical MOF-poly(acrylic acid) hybrid material with an "active core-skeleton-shell" structure.
  • Immobilization of lipase within the MOF-PAA hybrid material.
  • Characterization of enzyme activity, catalytic efficiency, and stability under various stress conditions (EDTA, pH 14, urea).
  • Assessment of reusability and storage stability.
  • Molecular docking simulations to elucidate stabilization mechanisms.

Main Results:

  • Lipase@MPHM demonstrated a 294% increase in activity and a 596% enhancement in catalytic efficiency compared to free lipase.
  • The hybrid material achieved high catalytic performance at ultralow enzyme loading (0.015 ng).
  • Lipase@MPHM retained significant activity (67.01% to 52.51%) after exposure to EDTA, pH 14, and urea treatments.
  • The composite exhibited stable activity over 11 reuse cycles and 11 weeks of storage.
  • Molecular docking revealed enhanced hydrophobic interactions stabilizing the lipase conformation.

Conclusions:

  • The developed MOF-PAA hybrid material provides a robust platform for enzyme immobilization, significantly improving enzyme stability and catalytic performance.
  • The "active core-skeleton-shell" architecture effectively protects the enzyme from degradation, enabling prolonged activity and reusability.
  • This strategy offers a promising approach for designing durable enzyme-MOF composites for diverse applications in biocatalysis and beyond.