Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 7, Issue 45, Pages 25270-25280Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.5b07290
Keywords
nzymatic biofuel cell; industrial biotechnology; laccase; multicopper oxidase; protein immobilization; protein-surface interactions
Funding
- UK's Engineering and Physical Sciences Research Council (EPSRC) [EP/G00434X/2]
- NOWNANO Centre for Doctoral Training
- University of Manchester's School of Materials' Doctoral Training Account
- Engineering and Physical Sciences Research Council [1231569, EP/G00434X/2] Funding Source: researchfish
- EPSRC [EP/G00434X/2] Funding Source: UKRI
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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 of up to 2 min. Both unmodified and carboxylate-functionalized gold-coated sensors showed that a deposition solution concentration of 10-25 mg mL(-1) gave the highest activity per mass of adsorbed enzyme with an effective catalytic rate constant (k(cat)) of about 60 s(-1). The densification of adsorbed layers observed by DPI correlated with reduced bioactivity observed by parallel E-QCM-D measurements. Postadsorption 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.
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