• biocatalysis;
  • biosensors;
  • electron transfer;
  • immobilization;
  • metalloenzymes


Typically, the use of heterogeneous enzyme catalysis is aimed at sustainability, reusability, or enhanced functionality of the biocatalyst and is achieved by immobilizing enzymes onto a support matrix or at a defined interface. Controlled enzyme immobilization is particularly important in bioelectrocatalysis because the catalyst must be effectively connected to a transducer to exploit its activity. This Review discusses what must be addressed for coupling biocatalysts to an electrode and the toolbox of methods that are available for achieving this outcome. As an illustration, we focus on the immobilization and stabilization of laccases at electronic interfaces. Historically, laccases have been used for the decolorization of dyes and for the synthesis of bio-organic compounds; however, more recently, they have been applied to the fields of sensing and energy harvesting.13 There is an ever-increasing focus on the development of new energy technologies, in which laccases find application (e.g., as cathodic catalysts in enzymatic fuel cells). Herein, we discuss the heterogeneous laccase biocatalysts that have been reported over the past 10–15 years and discuss why laccases continue to be biotechnologically relevant enzymes. Various methods for the immobilization of laccases are described, including the use of nanoscale supports and a range of encapsulation and cross-linking chemistries. We consider the application of immobilized laccases to the food industry, in the synthesis of pharmaceuticals, and in environmental applications, specifically in cases in which stabilization through heterogenization of the enzyme is critical to the application. We also include a consideration of electrochemical biosensors and the specific incorporation of laccases on the surfaces of transducers.