Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles. Issue 90 (27th October 2021)

• Record Type: Journal Article
• Authors: Nazemi, Seyed Amirabbas; Olesińska, Magdalena; Pezzella, Cinzia; Varriale, Simona; Lin, Chia-Wei; Corvini, Philippe F.-X.; Shahgaldian, Patrick
• Is Part Of: Chemical communications. Volume 57:Issue 90(2021)
• Page Start: 11960
• Page End: 11963
• Publication Date: 2021-10-27
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d1cc04916j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : 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. 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.