The rapid, field-ready detection of methamphetamine (MET) directly in sewage under flow remains a bottleneck for public health and law enforcement surveillance. We engineered a low-cost, 3D-printed flow-through electrochemical cell that houses a commercial screen-printed carbon electrode and operates in both non-flow and flow regimes. The platform was validated using the [Ru(NH3)6]3+/2+ couple, confirming negligible kinetic hindrance and suitability for voltammetric sensing under convective transport. Using square wave voltammetry and chronoamperometry, MET was quantified in filtered wastewater, with limits of detection of 15.9 µg L−1 in non-flow and 211.2 µg L−1 in flow conditions. Specificity tests yielded well-separated faradaic responses for the pre precursor α-phenylacetoacetonitrile (APAAN) and for MET, while amphetamine produced only a weak signal, enabling side-by-side discrimination in a single run. To our knowledge, this is the first demonstration of direct electrochemical sensing of MET in flowing wastewater using a 3D-printed flow-through platform. The simple, disposable design provides an actionable foundation for portable, near-real-time sewer surveillance and motivates antifouling/auto-cleaning strategies for long-term deployment.
The study presents a promising approach to enzymatic kinetics using Electrochemical Impedance Spectroscopy (EIS) to assess fundamental parameters of modified enteropeptidases. Traditional methods for determining these parameters, while effective, often lack versatility and convenience, especially under varying environmental conditions. The use of EIS provides a novel approach that overcomes these limitations. The enteropeptidase underwent genetic modification through the introduction of single amino acid modifications to assess their effect on enzyme kinetics. However, according to the one-sample t-test results, the difference between the engineered enzymes and hEKL was not statistically significant by conventional criteria. The kinetic parameters were analyzed using fluorescence spectroscopy and EIS, which was found to be an effective tool for the real-time measurement of enzyme kinetics. The results obtained through EIS were not significantly different from those obtained through traditional fluorescence spectroscopy methods (p value >> 0.05). The study validates the use of EIS for measuring enzyme kinetics and provides insight into the effects of specific amino acid changes on enteropeptidase function. These findings have potential applications in biotechnology and biochemical research, suggesting a new method for rapidly assessing enzymatic activity.