Enzyme Encapsulation in a Porous Hydrogen-Bonded Organic Framework

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

Research output: Contribution to journalArticle

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
JournalJournal of the American Chemical Society
Publication statusPublished - 19 Aug 2019

Fingerprint Dive into the research topics of 'Enzyme Encapsulation in a Porous Hydrogen-Bonded Organic Framework'. Together they form a unique fingerprint.

  • Cite this