In a classical amperometric experiment (e.g. chronoamperometry at a bare electrode), the analyte is consumed at the electrode–electrolyte interface, and the current is limited by mass transport. This leads to the formation of a diffusion layer.

However, I’m unsure whether the same concept of a diffusion layer applies in amperometric sensors based on immobilised enzymes, such as those using glucose oxidase (GOx).

Here’s my reasoning:

  • In regular electrochemistry, the interfacial charge transfer rate is described by the Butler–Volmer kinetics, and depends exponentially on the overpotential. These reactions can be quite fast under sufficient driving force.
  • In enzymatic sensors, the redox reaction occurs indirectly, mediated by the enzyme. I suspect that the enzyme kinetics is slower than the interfacial charge transfer in standard electrochemistry.
  • Therefore, I question whether a classical diffusion layer forms at the electrode in enzymatic sensors.

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