Enzyme Encapsulation in a Porous Hydrogen-Bonded Organic Framework

Weibin Liang, Francesco Carraro, Marcello B. Solomon, Stephen G. Bell, Heinz Amenitsch, Christopher J. Sumby*, Nicholas G. White, Paolo Falcaro, Christian J. Doonan

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    209 Citations (Scopus)

    Abstract

    Protection of biological assemblies is critical to applications in biotechnology, increasing the durability of enzymes in biocatalysis or potentially stabilizing biotherapeutics during transport and use. Here we show that a porous hydrogen-bonded organic framework (HOF) constructed from water-soluble tetra-amidinium (1·Cl4) and tetracarboxylate (2) building blocks can encapsulate and stabilize biomolecules to elevated temperature, proteolytic and denaturing agents, and extend the operable pH range for catalase activity. The HOF, which readily retains water within its framework structure, can also protect and retain the activity of enzymes such as alcohol oxidase, that are inactive when encapsulated within zeolitic imidazolate framework (ZIF) materials. Such HOF coatings could provide valid alternative materials to ZIFs: They are metal free, possess larger pore apertures, and are stable over a wider, more biologically relevant pH range.

    Original languageEnglish
    Pages (from-to)14298-14305
    Number of pages8
    JournalJournal of the American Chemical Society
    Volume141
    Issue number36
    DOIs
    Publication statusPublished - 11 Sept 2019

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