The present work illustrates a new method: soft landed protein voltammetry (SLPV); this experimental procedure is based on the coupling of ion soft landing with a voltammetric technique and allows the electrode surface to be functionalized with biologically active molecules, thus opening up numerous new perspectives ranging from molecular electronics to protein chips.

One of the main drawbacks affecting first-generation electrochemical biosensors in the analysis of real matrices is the interference of electroactive species present in the sample under investigation. Several approaches have been attempted to overcome this problem in the past ten years but the best results were achieved by using mediated based electrochemical biosensors. Despite this, the kinetic of the redox mediators-enzymatic proteins interaction has not been studied deeply enough. In this work we have developed a theoretical-methodological approach for the characterization of the kinetic of interaction between redox enzymes and substrates and/or redox mediators. Particularly, the interaction of glucose oxidase (GOx) with several commercially available redox mediators has been studied by means of amperometry and cyclic voltammetry. The main kinetic parameters for different mediators were exploited and discussed with the aim of finding the best mediator for a glucose biosensor to be used on real samples.