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dc.contributor.authorPhiri, Masauso Moses
dc.contributor.authorMulder, Danielle Wingrove
dc.contributor.authorMason, Shayne
dc.contributor.authorVorster, Barend Christiaan
dc.date.accessioned2019-10-11T11:37:35Z
dc.date.available2019-10-11T11:37:35Z
dc.date.issued2019
dc.identifier.citationPhiri, M.M. et al. 2019. Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function. Royal Society open science, 6(5): Article no 190205. [https://doi.org/10.1098/rsos.190205]en_US
dc.identifier.issn2054-5703 (Online)
dc.identifier.urihttp://hdl.handle.net/10394/33428
dc.identifier.urihttps://royalsocietypublishing.org/doi/pdf/10.1098/rsos.190205
dc.identifier.urihttps://doi.org/10.1098/rsos.190205
dc.description.abstractGold nanoparticles provide a user-friendly and efficient surface for immobilization of enzymes and proteins. In this paper, we present a novel approach for enzyme bioconjugation to gold nanostars (AuNSs). AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs–Cys–GOx bioconjugate complex. Such a strategy has the potential for increased attachment affinity without protein adsorption onto the AuNSs surface. Good dispersity in buffer suspension was observed, as well as stability in high ionic environments. Using the AuNSs–Cys–GOx bioconjugates showed greater sensitivity in the measuring of low concentrations of glucose based on plasmonic and colorimetric detection. Such a novel approach for enzyme immobilization can lead to AuNSs–Cys–GOx bioconjugate complexes that can be used as catalytic nanodevices in nanobiosensors based on oxidases in biomedical applicationsen_US
dc.language.isoenen_US
dc.publisherRoyal Societyen_US
dc.titleFacile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal functionen_US
dc.typeArticleen_US
dc.contributor.researchID25264834 - Phiri, Masauso Moses
dc.contributor.researchID26718944 - Mulder, Danielle Wingrove
dc.contributor.researchID21487855 - Mason, Shayne William
dc.contributor.researchID22713077 - Vorster, Barend Christiaan


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