Scaffolding of Enzymes on Virus Nanoarrays: Effects of Confinement and Virus Organization on Biocatalysis

Organizing active enzyme molecules on nanometer‐sized scaffolds is a promising strategy for designing highly efficient supported catalytic systems for biosynthetic and sensing applications. This is achieved by designing model nanoscale enzymatic platforms followed by thorough analysis of the catalytic activity. Herein, the virus fd bacteriophage is considered as an enzyme nanocarrier to study the scaffolding effects on enzymatic activity. Nanoarrays of randomly oriented, or directionally patterned, fd bacteriophage virus are functionalized with the enzyme glucose oxidase (GOx), using an immunological assembly strategy, directly on a gold electrode support. The scaffolding process on the virus capsid is monitored in situ by AFM (atomic force microscopy) imaging, while cyclic voltammetry is used to interrogate the catalytic activity of the resulting functional GOx‐fd nanoarrays. Kinetic analysis reveals the ability to modulate the activity of GOx via nanocarrier patterning. The results evidence, for the first time, enhancement of the enzymatic activity due to scaffolding on a filamentous viral particle. Glucose oxidase scaffolded virus nanoarrays with tunable catalytic properties are directly organized onto electrode supports using immunodecoration for assembly. Structural and catalytic characterization reveals the effect of enzyme confinement on kinetic activity as a function of virus organization. Enhanced catalysis for glucose oxidase is found for randomly oriented GOx‐fd nanoarrays compared to aligned nanoarrays and reference nonscaffolded enzyme molecules.