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

dc.accessRightsAnonymous*
dc.contributor.authorNazemi, Seyed
dc.contributor.authorOlesinska, Magdalena
dc.contributor.authorPezzella, Cinzia
dc.contributor.authorVarriale, Simona
dc.contributor.authorLin, Chia-Wei
dc.contributor.authorCorvini, Philippe
dc.contributor.authorShahgaldian, Patrick
dc.date.accessioned2022-03-28T06:40:40Z
dc.date.available2022-03-28T06:40:40Z
dc.date.issued2021
dc.description.abstractWe 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.en_US
dc.identifier.doi10.1039/d1cc04916j
dc.identifier.issn1359-7345
dc.identifier.issn1364-548X
dc.identifier.urihttps://irf.fhnw.ch/handle/11654/33396
dc.language.isoen_USen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.ispartofChemical Communicationsen_US
dc.titleImmobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticlesen_US
dc.type01A - Beitrag in wissenschaftlicher Zeitschrift
dc.volume57en_US
dspace.entity.typePublication
fhnw.InventedHereYesen_US
fhnw.IsStudentsWorknoen_US
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publicationen_US
fhnw.affiliation.hochschuleHochschule für Life Sciencesde_CH
fhnw.affiliation.institutInstitut für Ecopreneurshipde_CH
fhnw.openAccessCategoryCloseden_US
fhnw.pagination11960-11963en_US
fhnw.publicationStatePublisheden_US
relation.isAuthorOfPublicationb70a3a4f-d739-4ef3-84c8-cab8e28c05c7
relation.isAuthorOfPublication8884cd16-817b-4fba-a564-50a45970baa2
relation.isAuthorOfPublication.latestForDiscovery8884cd16-817b-4fba-a564-50a45970baa2
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