Trypsin and pepsin are proteolytic enzymes secreted by the digestive system to digest proteins. Here, we examine the electrochemical behaviour and detection of trypsin and pepsin at a liquid/liquid (L|L) micro-interface array. For both proteins, aqueous phase of 10 mM hydrochloric acid was the only electrolyte solution in which they were electroactive. Neither protein was detected below 30 μM by cyclic voltammetry (CV) but stripping voltammetry following adsorption (AdSV) enabled the detection of sub-micromolar concentrations of both proteins. Although pepsin was electroactive at the micro-interface array in aqueous phase of 10 mM HCl, its behaviour was ill-defined and unsuitable for characterization by CV. It was found that pepsin easily blocked the micro-interfaces, as seen by greatly hampered ion transfer voltammetry of tetrapropylammonium ion (TPrA