With respect to bioreactors and biosensors, it has to be noted that injector nozzles, communication pipes, and thermal stabilization tubing pipes in flow-based systems are often fabricated not only from metal, but also from various polymeric materials [1; 2]. In this way, polydimethyl siloxane [27; 28; 29; 30], polytetrafluoroethylene (Teflon [31]), polymethyl metacrylate [32], and nylon [33] represent typical polymers used for the fabrication of biosensor fluidic sections. Upon the motion of glycerol-containing solutions through polymeric fluidic lines, a charge is expected to be generated at the expense of the above-mentioned triboelectric effect, similar to the case with aqueous solutions. The second factor is that glycerol-containing liquids can be employed as heat-transfer agents for thermal stabilization of biosensor measurement systems [34]. This is particularly important in the instrumentation of systems operating in extreme field conditions in a wide range of temperatures (from negative to positive ones), depending only on the glycerol content. This is possible due to the unique properties of glycerol, since the freezing point of such a heat-transfer fluid can be varied in a very broad range, from \(-43.5\)\({}^{\circ}\)C (for \(66.7\%\)\(w/w\) glycerol solution [35]) to \(17\)\({}^{\circ}\)C (100% glycerol) [36]. As was mentioned above, the flowing of glycerol-containing solutions through the pipes of thermal stabilization systems is expected to cause a triboelectric effect, i.e., a generation of an electric charge. The latter, in its turn, should induce an electric field that can extend well beyond these communications, influencing protein solutions in biosensor systems or bioreactors. The present study is aimed at determining the influence of the flow of glycerol through a coiled polymeric pipe on the physicochemical properties of the HRP solution in the measuring cell, which is located in the vicinity of the coiled pipe. The HRP enzyme was employed as a model object, since this protein was comprehensively characterized in the literature [37; 38; 39; 40; 41; 42; 43; 44; 45; 46; 47]. The molecular weight of HRP, which represents a heme-containing enzyme glycoprotein [37; 38], is known to be 40 to 44 kDa [38; 39]. The HRP molecule contains 18-27% carbohydrate chains, stabilizing its structure [38; 40; 41]. It is known that many enzymes, including peroxidase [42], form aggregates. Similar to our previous studies [16; 48], atomic force microscopy (AFM) has been employed for the visualization of the effect of an electromagnetic field on proteins with the example of HRP macromolecules, which were adsorbed from the analyzed solution onto the atomically smooth surface of a mica substrate. AFM allows one to register a signal from even single-surface-adsorbed macromolecules, and this extremely high sensitivity has allowed us to detect minor changes in the properties of HRP macromolecules. In the present study, using AFM, it was found that the flow of glycerol (similar to water flow [16]) through the flow-based system influences the physicochemical properties of HRP macromolecules; namely, it induces changes in the HRP aggregation state and in its adsorbability onto the mica surface. The data obtained herein can be used in the development of biosensor systems intended for the diagnosis of socially relevant diseases (such as oncological and infectious ones). Our results can also be useful for the development of biosensors operating in a broad temperature range for the registration of changes in physiochemical properties of target proteins associated with these diseases. The effects observed in our experiments can also be taken into account for the development of models of fluid dynamics.