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Area of Science:

  • Biomaterials Science
  • Enzyme Engineering
  • Nanotechnology

Background:

  • Virus-like particles (VLPs) and protein containers are valuable for nanomaterial synthesis.
  • Phosphotriesterase (PTE) is effective against insecticides and nerve agents but has limited practical application due to expression and stability issues.
  • Mesophilic enzymes like PTE exhibit low heat tolerance and are susceptible to proteolysis, hindering their use in bioremediation.

Purpose of the Study:

  • To enhance the stability and utility of phosphotriesterase (PTE) through encapsulation.
  • To investigate the use of bacteriophage P22 capsids as a delivery vehicle for PTE.
  • To develop a robust nanoparticle reactor for enzyme-based applications.

Main Methods:

  • Directed assembly and encapsulation of multiple PTE enzyme copies within bacteriophage P22 capsids.
  • Characterization of the thermal tolerance of encapsulated PTE.
  • Assessment of PTE stability against proteases and desiccation when encapsulated.

Main Results:

  • Encapsulated PTE demonstrated significantly enhanced thermal tolerance, retaining 50% activity at 60 °C.
  • The P22 capsid protected PTE from protease degradation.
  • Encapsulation also stabilized PTE against desiccation, improving its robustness.
  • The engineered system resulted in a stable and active nanoparticle reactor.

Conclusions:

  • Bacteriophage P22 capsids effectively enhance the stability of mesophilic phosphotriesterase.
  • Encapsulation overcomes key limitations of PTE, making it a more viable tool for bioremediation.
  • The engineered P22-PTE system represents a promising advancement in nanoparticle reactor technology.