The properties of the AOx-based O2-scavenger make it theoretically suitable for all oxidasebased biosensors, with the exception of those targeting short-chain primary alcohols or formaldehyde, as these are substrates of AOx. To confirm this versatility, we tested two additional biosensors that use oxidases as biorecognition elements. We created a lactate biosensor by immobilizing lactate oxidase on a glassy carbon electrode using the same Oscomplex modified polymer as in the glucose biosensor. Similarly, we developed a creatinine biosensor by immobilizing sarcosine oxidase and combining it with creatininase and creatinase in solution. Similarly to glucose oxidase (Figure ), the sensing enzymes for lactate and creatine (lactate oxidase, sarcosine oxidase, creatinase and creatininase) in presence of paraformaldehyde do not lead to any catalytic current, demonstrating the absence of unwanted cross-reactions (Figure ). The effect of the O2-scavenger was tested for the lactate and creatinine biosensors (Figure ). In both cases, the O2-scavenger suppressed the oxygen reduction current and the addition of 1 mM of the respective analyte generated the catalytic wave for analyte oxidation. In presence of the scavenger, the catalytic currents measured at 0.8