Self-assembled enzyme nanoparticles for carbon dioxide capture

Bhuvana Kamath Shanbhag, Boyin Liu, Jing Fu, Victoria S. Haritos, Lizhong He

Research output: Contribution to journalArticleResearchpeer-review

17 Citations (Scopus)

Abstract

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 °C) and higher (50 °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.
Original languageEnglish
Pages (from-to)3379 - 3384
Number of pages6
JournalNano Letters
Volume16
Issue number5
DOIs
Publication statusPublished - 2016

Keywords

  • Carbon dioxide capture
  • Carrier-free immobilization
  • Enzyme-peptide fusion
  • Recombinant enzyme
  • Self-assembly
  • Protein nanoparticles

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