[FeFe]-Hydrogenase Encapsulated in Zeolitic Imidazolate Framework (ZIF)-8 Nanoparticles as a Robust Biocatalyst for Photocatalytic Hydrogen Production

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

[FeFe]-hydrogenase (HydA) is an active biocatalytic enzyme for solar-to-hydrogen (H2) conversion. However, stability is a main challenge that limits practical applications. This work aims to encourage the efficiency of HydA by encapsulating it in the zeolitic imidazolate framework-8 (ZIF-8) as a synthetic protective shield. The construction of HydA@ZIF-8 nanoparticles, with an average diameter of 700-1000 nm, at ambient conditions can preserve HydA activity within a spatially confined microenvironment, as characterized by scanning electron microscopy and X-ray diffraction analysis. Based on MV•+-dependent H2 production activity and kinetic analysis, both the stability and efficiency of HydA@ZIF-8 surpass those of free HydA and whole-cell biocatalysts over a wider range of pH and temperature. The achievement of robust HydA@ZIF-8 construction represents a significant step forward in the development of biocatalysts for various future applications.

Original languageEnglish
Pages (from-to)6300-6309
Number of pages10
JournalACS Sustainable Chemistry and Engineering
Volume12
Issue number16
DOIs
Publication statusPublished - Apr 22 2024

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Environmental Chemistry
  • General Chemical Engineering
  • Renewable Energy, Sustainability and the Environment

Fingerprint

Dive into the research topics of '[FeFe]-Hydrogenase Encapsulated in Zeolitic Imidazolate Framework (ZIF)-8 Nanoparticles as a Robust Biocatalyst for Photocatalytic Hydrogen Production'. Together they form a unique fingerprint.

Cite this