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Covalent organic frameworks for lipase adsorption: A multiscale simulation.

Daohui Zhao1, Yu Zhou1, Hangxing Wang1

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Covalent organic frameworks (COFs) effectively immobilize enzymes like Candida antarctica lipase B (CalB). Functionalized TpPa-AMCOOH COFs offer optimal enzyme orientation and accessibility for enhanced biocatalysis.

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Area of Science:

  • Materials Science
  • Biochemistry
  • Computational Chemistry

Background:

  • Covalent organic frameworks (COFs) are advanced porous materials with tunable properties.
  • Enzyme immobilization is critical for developing efficient biocatalysts.
  • Understanding enzyme-COF interactions is key to designing effective immobilization matrices.

Purpose of the Study:

  • To investigate the adsorption mechanisms of Candida antarctica lipase B (CalB) on functionalized TpPa-X COFs.
  • To evaluate the influence of COF functionalization on enzyme-substrate interactions.
  • To identify optimal COF materials for enhanced enzyme immobilization and activity.

Main Methods:

  • Utilized parallel tempered Monte Carlo simulations.
  • Employed molecular dynamics simulations.
  • Analyzed enzyme adsorption behavior and interaction energies on different TpPa-X COFs.

Main Results:

  • CalB adsorbs effectively onto TpPa-1, TpPa-AMC2NH2, and TpPa-AMCOOH COFs.
  • Adsorption strength follows the order: TpPa-AMC2NH2 > TpPa-AMCOOH > TpPa-1.
  • CalB's active site is oriented towards the solution on TpPa-AMCOOH, improving substrate accessibility.
  • Enzyme conformation remains stable, indicating good biocompatibility of TpPa-X COFs.

Conclusions:

  • Functionalized COFs, particularly TpPa-AMCOOH, are excellent candidates for CalB immobilization.
  • The study provides theoretical insights into COF-biomolecule interactions and biocompatibility.
  • Findings guide the development of tailored porous materials for enzyme immobilization and biocatalysis.