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Optimizing the mass-specific activity of bilirubin oxidase adlayers through combined electrochemical quartz crystal microbalance and dual polarization interferometry analyses
Trevor McArdle, Thomas P. McNamara, Fan Fei, Kulveer Singh, Christopher F. Blanford
A C S Applied Materials and Interfaces. 2015;7(45):25270-25280.
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Abstract
Two surface analysis techniques, dual polarization interferometry (DPI) and analysis by an electrochemical quartz crystal microbalance with dissipation capability (E-QCM-D), were paired to find the deposition conditions that give the highest and most stable electrocatalytic activity per adsorbed mass of enzyme. Layers were formed by adsorption from buffered solutions of bilirubin oxidase from Myrothecium verrucaria at pH 6.0 to planar surfaces, under high enzyme loading (≥ 1 mg ml–1) for contact periods up to 2 min. Both unmodified and carboxylate-functionalized gold-coated sensors showed that a deposition solution concentration of between 10–25 mg ml–1 gave the highest activity per mass of adsorbed enzyme with an effective catalytic rate constant (kcat) of about 60 s–1. The densification of adsorbed layers observed by DPI correlated with reduced bioactivity observed by parallel E-QCM-D measurements. Post-adsorption changes in thickness and density observed by DPI were incorporated into Kelvin–Voigt models of the QCM-D response. The modeled response matched experimental observations when the adlayer viscosity tripled after adsorption.
Keyword(s)
industrial biotechnology; enzymatic biofuel cell; laccase; multicopper oxidase; protein immobilization; protein−surface interactions
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- EPSRC - RESEPSRC