Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function. Issue 5 (1st May 2019)

• Record Type: Journal Article
• Authors: Moses Phiri, Masauso; Wingrove Mulder, Danielle; Mason, Shayne; Christiaan Vorster, Barend
• Is Part Of: Royal Society open science. Volume 6:Issue 5(2019)
• Publication Date: 2019-05-01
• Subjects: immobilization -- bioconjugate -- gold nanostars -- glucose oxidase -- nanobiosensor; Science -- Periodicals; 500
• DOI: 10.1098/rsos.190205
• Languages: English
• ISSNs: 2054-5703

Abstract

Abstract : Gold 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 applications.