Enzyme Encapsulation in a Porous Hydrogen-Bonded Organic Framework
| Autor: | Stephen Bell, Weibin Liang, Paolo Falcaro, Heinz Amenitsch, Marcello B. Solomon, Francesco Carraro, Christian J. Doonan, Christopher J. Sumby, Nicholas G. White |
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| Rok vydání: | 2019 |
| Předmět: |
Hydrogen
Surface Properties Carboxylic Acids Molecular Conformation chemistry.chemical_element Alcohol oxidoreductase 010402 general chemistry 01 natural sciences Biochemistry Catalysis Colloid and Surface Chemistry Particle Size Porosity chemistry.chemical_classification Hydrogen bond Biomolecule Imidazoles Water Hydrogen Bonding General Chemistry Hydrogen-Ion Concentration Amides 0104 chemical sciences Alcohol oxidase Alcohol Oxidoreductases chemistry Chemical engineering Biocatalysis Zeolites Zeolitic imidazolate framework |
| Zdroj: | Journal of the American Chemical Society. 141:14298-14305 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.9b06589 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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