Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles
We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2021-11, Vol.57 (9), p.1196-11963 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica layer of controlled thickness is grown at the silica surface, entrapping the enzyme and thus avoiding enzyme leaching. We demonstrate that this approach results not only in high and durable activity retention but also enzyme stabilisation.
We report a method of glycosylated enzyme immobilisation and stabilisation based on the formation of boronate esters between a surface-attached boronate and the enzyme glycans, followed by the growth of an organosilica layer of controlled thickness. |
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ISSN: | 1359-7345 1364-548X |
DOI: | 10.1039/d1cc04916j |