Shielding against Unfolding by Embedding Enzymes in Metal-Organic Frameworks via a de Novo Approach

Fu Siang Liao, Wei Shang Lo, Yu Shen Hsu, Chang Cheng Wu, Shao Chun Wang, Fa Kuen Shieh, Joseph V. Morabito, Lien Yang Chou, Kevin C.W. Wu, Chia Kuang Tsung

Research output: Contribution to journalArticlepeer-review

176 Scopus citations

Abstract

We show that an enzyme maintains its biological function under a wider range of conditions after being embedded in metal-organic framework (MOF) microcrystals via a de novo approach. This enhanced stability arises from confinement of the enzyme molecules in the mesoporous cavities in the MOFs, which reduces the structural mobility of enzyme molecules. We embedded catalase (CAT) into zeolitic imidazolate frameworks (ZIF-90 and ZIF-8), and then exposed both embedded CAT and free CAT to a denature reagent (i.e., urea) and high temperatures (i.e., 80 °C). The embedded CAT maintains its biological function in the decomposition of hydrogen peroxide even when exposed to 6 M urea and 80 °C, with apparent rate constants kobs (s-1) of 1.30 × 10-3 and 1.05 × 10-3, respectively, while free CAT shows undetectable activity. A fluorescence spectroscopy study shows that the structural conformation of the embedded CAT changes less under these denaturing conditions than free CAT.

Original languageEnglish
Pages (from-to)6530-6533
Number of pages4
JournalJournal of the American Chemical Society
Volume139
Issue number19
DOIs
StatePublished - 17 May 2017

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