TY - JOUR
T1 - [FeFe]-Hydrogenase Encapsulated in Zeolitic Imidazolate Framework (ZIF)-8 Nanoparticles as a Robust Biocatalyst for Photocatalytic Hydrogen Production
AU - Kosem, Nuttavut
AU - Ohsaki, Yutaka
AU - Watanabe, Motonori
AU - Song, Jun Tae
AU - Ishihara, Tatsumi
N1 - Publisher Copyright:
© 2024 American Chemical Society.
PY - 2024/4/22
Y1 - 2024/4/22
N2 - [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.
AB - [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.
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U2 - 10.1021/acssuschemeng.3c08560
DO - 10.1021/acssuschemeng.3c08560
M3 - Article
AN - SCOPUS:85190174135
SN - 2168-0485
VL - 12
SP - 6300
EP - 6309
JO - ACS Sustainable Chemistry and Engineering
JF - ACS Sustainable Chemistry and Engineering
IS - 16
ER -