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.

Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles / Nazemi, S. A.; Olesinska, M.; Pezzella, C.; Varriale, S.; Lin, C. -W.; Corvini, P. F. -X.; Shahgaldian, P.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 57:90(2021), pp. 11960-11963. [10.1039/d1cc04916j]

Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles

Pezzella C.;Varriale S.;
2021

Abstract

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.
2021
Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles / Nazemi, S. A.; Olesinska, M.; Pezzella, C.; Varriale, S.; Lin, C. -W.; Corvini, P. F. -X.; Shahgaldian, P.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 57:90(2021), pp. 11960-11963. [10.1039/d1cc04916j]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/877385
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