4.8 Article

Self-Assembled Enzyme Nanoparticles for Carbon Dioxide Capture

Journal

NANO LETTERS
Volume 16, Issue 5, Pages 3379-3384

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.6b01121

Keywords

enzyme-peptide fusion; self-assembly; protein nanoparticles; carbon dioxide capture; carrier-free immobilization; recombinant enzyme

Funding

  1. Monash University
  2. CSIRO
  3. Faculty of Engineering, Monash University

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Enzyme-based processes have shown promise as a sustainable alternative to amine-based processes for carbon dioxide capture. In this work, we have engineered carbonic anhydrase nanoparticles that retain 98% of hydratase activity in comparison to their free counterparts. Carbonic anhydrase was fused with a self-assembling peptide that facilitates the noncovalent assembly of the particle and together were recombinantly expressed from a single gene construct in Escherichia coli. The purified enzymes, when subjected to a reduced pH, form 50-200 nm nanoparticles. The CO2 capture capability of enzyme nanoparticles was demonstrated at ambient (22 +/- 2 degrees C) and higher (50 degrees C) temperatures, under which the nanoparticles maintain their assembled state. The carrier-free enzymatic nanoparticles demonstrated here offer a new approach to stabilize and reuse enzymes in a simple and cost-effective manner.

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