Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function

• Published in: Royal Society open science Vol. 6; no. 5; p. 190205
• Main Authors: Moses Phiri, Masauso, Wingrove Mulder, Danielle, Mason, Shayne, Christiaan Vorster, Barend
• Format: Journal Article
• Language: English
• Published: England The Royal Society 01.05.2019
• Subjects: bioconjugate; Chemistry; glucose oxidase; gold nanostars; immobilization; nanobiosensor; bioconjugate; gold nanostars; immobilization; nanobiosensor; glucose oxidase
• ISSN: 2054-5703; 2054-5703
• DOI: 10.1098/rsos.190205

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 -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.