Probing Interactions between Metal-Organic Frameworks and Freestanding Enzymes in a Hollow Structure

Sheng Yu Chen, Wei Shang Lo, Yi Da Huang, Xiaomeng Si, Fu Siang Liao, Shang Wei Lin, Benjamin P. Williams, Ting Qian Sun, Hao Wei Lin, Yuanyuan An, Tu Sun, Yanhang Ma, Hsiao Ching Yang, Lien Yang Chou, Fa Kuen Shieh, Chia Kuang Tsung

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41 Scopus citations


It has been reported that the biological functions of enzymes could be altered when they are encapsulated in metal-organic frameworks (MOFs) due to the interactions between them. Herein, we probed the interactions of catalase in solid and hollow ZIF-8 microcrystals. The solid sample with confined catalase is prepared through a reported method, and the hollow sample is generated by hollowing the MOF crystals, sealing freestanding enzymes in the central cavities of hollow ZIF-8. During the hollowing process, the samples were monitored by small-angle X-ray scattering (SAXS) spectroscopy, electron microscopy, powder X-ray diffraction (PXRD), and nitrogen sorption. The interfacial interactions of the two samples were studied by infrared (IR) and fluorescence spectroscopy. IR study shows that freestanding catalase has less chemical interaction with ZIF-8 than confined catalase, and a fluorescence study indicates that the freestanding catalase has lower structural confinement. We have then carried out the hydrogen peroxide degradation activities of catalase at different stages and revealed that the freestanding catalase in hollow ZIF-8 has higher activity.

Original languageEnglish
Pages (from-to)6630-6635
Number of pages6
JournalNano Letters
Issue number9
StatePublished - 9 Sep 2020


  • enzyme immobilization
  • hollow MOF
  • interface
  • metal-organic frameworks
  • small-angle X-ray scattering


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