Search Results (9)

The high cost of equipment is a significant entry barrier to research for smaller organisations in developing solutions to air pollution problems. Low-cost electrochemical sensors have shown sensitivity at parts-per-billion by volume (ppbV) mixing ratios but are subject to variations due to changing environmental conditions, particularly temperature. We have previously demonstrated that under isothermal/isohume conditions such as those found in kinetic studies, very stable electrochemical responses occur. In this paper, we demonstrate the utility of a low-cost IoT-based sensor system that employs four-electrode electrochemical sensors under isothermal/isohume conditions for studying the kinetics of the atmospheric oxidation of nitrogen oxides. The results suggest that reproducible results for NO and NO₂ kinetics can be achieved. The method produced oxidation rates of 7.95 × 10³ L² mol⁻² s⁻¹ (±1.3%), for NO and 7.99 × 10⁻⁴ s⁻¹ (±2.1%) for NO₂. This study suggests that the oxidation kinetics of nitrogen oxides can be assessed with low-cost sensors, which can support a wide range of industrial applications, such as designing biocatalytic coatings for air pollution remediation. Full article

In the present work, a biocatalytic glucose optical sensor produced by immobilizing glucose oxidase (GOD) as a recognition molecule over a PMMA (polymethylmethacrylate) optical fiber is introduced. An enzymatic encapsulation process was carried out using the sol–gel method, depositing a TEOS-based coating by immersion at the end of an optical fiber; the biosensor was characterized using different glucose levels. Finally, the best way to encapsulate the enzyme and prevent it from degrading is to perform the process at room temperature, and later implement the deposition of the coating on the fiber. The drying process was optimal below 8 °C. Full article

Fibrous membranes offer broad opportunities to deploy immobilized enzymes in new reactor and application designs, including multiphase continuous flow-through reactions. Enzyme immobilization is a technology strategy that simplifies the separation of otherwise soluble catalytic proteins from liquid reaction media and imparts stabilization and performance enhancement. Flexible immobilization matrices made from fibers have versatile physical attributes, such as high surface area, light weight, and controllable porosity, which give them membrane-like characteristics, while simultaneously providing good mechanical properties for creating functional filters, sensors, scaffolds, and other interface-active biocatalytic materials. This review examines immobilization strategies for enzymes on fibrous membrane-like polymeric supports involving all three fundamental mechanisms of post-immobilization, incorporation, and coating. Post-immobilization offers an infinite selection of matrix materials, but may encounter loading and durability issues, while incorporation offers longevity but has more limited material options and may present mass transfer obstacles. Coating techniques on fibrous materials at different geometric scales are a growing trend in making membranes that integrate biocatalytic functionality with versatile physical supports. Biocatalytic performance parameters and characterization techniques for immobilized enzymes are described, including several emerging techniques of special relevance for fibrous immobilized enzymes. Diverse application examples from the literature, focusing on fibrous matrices, are summarized, and biocatalyst longevity is emphasized as a critical performance parameter that needs increased attention to advance concepts from lab scale to broader utilization. This consolidation of fabrication, performance measurement, and characterization techniques, with guiding examples highlighted, is intended to inspire future innovations in enzyme immobilization with fibrous membranes and expand their uses in novel reactors and processes. Full article

High equipment cost is a significant entry barrier to research for small organizations in developing solutions to air pollution problems. Low-cost electrochemical sensors show sensitivity at parts-per-billion by volume mixing ratios but are subject to variation due to changing environmental conditions, in particular temperature. In this study, we demonstrate a low-cost Internet of Things (IoT)-based sensor system for nitric oxide analysis. The sensor system used a four-electrode electrochemical sensor exposed to a series of isothermal/isohume conditions. When deployed under these conditions, stable baseline responses were achieved, in contrast to ambient air conditions where temperature and humidity conditions may be variable. The interrelationship between working and auxiliary electrodes was linear within an environmental envelope of 20–40 °C and 30–80% relative humidity, with correlation coefficients from 0.9980 to 0.9999 when measured under isothermal/isohume conditions. These data enabled the determination of surface functions that describe the working to auxiliary electrode offsets and calibration curve gradients and intercepts. The linear and reproducible nature of individual calibration curves for stepwise nitric oxide (NO) additions under isothermal/isohume environments suggests the suitability of these sensors for applications aside from their role in air quality monitoring. Such applications would include nitric oxide kinetic studies for atmospheric applications or measurement of the potential biocatalytic activity of nitric oxide consuming enzymes in biocatalytic coatings, both of which currently employ high-capital-cost chemiluminescence detectors. Full article

Serotonin is a biogenic amine that has multiple roles in the human body and is mainly known as the happiness hormone. A new laccase (Lac)-based biosensor has been developed for the qualitative and quantitative determination of serotonin in three dietary supplements from three different manufacturers. The enzyme was immobilized on an organized mesoporous carbon-modified carbon screen-printed electrode (OMC-SPE) by the drop-and-dry method, the active surface being pretreated with glutaraldehyde. With the new biosensor, serotonin was selectively detected from different solutions. Square-wave voltammetry was the technique used for the quantitative determination of serotonin, obtaining a detection limit value of 316 nM and a quantification limit value of 948 nM in the linearity range of 0.1–1.2 µM. The pH for the determinations was 5.2; at this value, the biocatalytic activity of the laccase was optimal. At the same time, the electrochemical performance of the OMC-SPE/Lac biosensor was compared with that of the unmodified sensor, a performance that highlighted the superiority of the biosensor and the very important role of the enzyme in electrodetection. The results obtained from the quantitative determination of serotonin by square-wave voltammetry were compared with those from the FTIR method, revealing a very good correlation between the results obtained by the two quantitative determination methods. Full article

Incorporating enzymes with three-dimensional (3D) printing is an exciting new field of convergence research that holds infinite potential for creating highly customizable components with diverse and efficient biocatalytic properties. Enzymes, nature’s nanoscale protein-based catalysts, perform crucial functions in biological systems and play increasingly important roles in modern chemical processing methods, cascade reactions, and sensor technologies. Immobilizing enzymes on solid carriers facilitates their recovery and reuse, improves stability and longevity, broadens applicability, and reduces overall processing and chemical conversion costs. Three-dimensional printing offers extraordinary flexibility for creating high-resolution complex structures that enable completely new reactor designs with versatile sub-micron functional features in macroscale objects. Immobilizing enzymes on or in 3D printed structures makes it possible to precisely control their spatial location for the optimal catalytic reaction. Combining the rapid advances in these two technologies is leading to completely new levels of control and precision in fabricating immobilized enzyme catalysts. The goal of this review is to promote further research by providing a critical discussion of 3D printed enzyme immobilization methods encompassing both post-printing immobilization and immobilization by physical entrapment during 3D printing. Especially, 3D printed gel matrix techniques offer mild single-step entrapment mechanisms that produce ideal environments for enzymes with high retention of catalytic function and unparalleled fabrication control. Examples from the literature, comparisons of the benefits and challenges of different combinations of the two technologies, novel approaches employed to enhance printed hydrogel physical properties, and an outlook on future directions are included to provide inspiration and insights for pursuing work in this promising field. Full article

Enzymatic biosensors enjoy commercial success and are the subject of continued research efforts to widen their range of practical application. For these biosensors to reach their full potential, their selectivity challenges need to be addressed by comprehensive, solid approaches. This review discusses the status of enzymatic biosensors in achieving accurate and selective measurements via direct biocatalytic and inhibition-based detection, with a focus on electrochemical enzyme biosensors. Examples of practical solutions for tackling the activity and selectivity problems and preventing interferences from co-existing electroactive compounds in the samples are provided such as the use of permselective membranes, sentinel sensors and coupled multi-enzyme systems. The effect of activators, inhibitors or enzymatic substrates are also addressed by coupled enzymatic reactions and multi-sensor arrays combined with data interpretation via chemometrics. In addition to these more traditional approaches, the review discusses some ingenious recent approaches, detailing also on possible solutions involving the use of nanomaterials to ensuring the biosensors’ selectivity. Overall, the examples presented illustrate the various tools available when developing enzyme biosensors for new applications and stress the necessity to more comprehensively investigate their selectivity and validate the biosensors versus standard analytical methods. Full article

Integrating polypyrrole-cellulose nanocrystal-based composites with glucose oxidase (GOx) as a new sensing regime was investigated. Polypyrrole-cellulose nanocrystal (PPy-CNC)-based composite as a novel immobilization membrane with unique physicochemical properties was found to enhance biosensor performance. Field emission scanning electron microscopy (FESEM) images showed that fibers were nanosized and porous, which is appropriate for accommodating enzymes and increasing electron transfer kinetics. The voltammetric results showed that the native structure and biocatalytic activity of GOx immobilized on the PPy-CNC nanocomposite remained and exhibited a high sensitivity (ca. 0.73 μA·mM⁻¹), with a high dynamic response ranging from 1.0 to 20 mM glucose. The modified glucose biosensor exhibits a limit of detection (LOD) of (50 ± 10) µM and also excludes interfering species, such as ascorbic acid, uric acid, and cholesterol, which makes this sensor suitable for glucose determination in real samples. This sensor displays an acceptable reproducibility and stability over time. The current response was maintained over 95% of the initial value after 17 days, and the current difference measurement obtained using different electrodes provided a relative standard deviation (RSD) of 4.47%. Full article

Tyrosinase-based biosensors containing a phthalocyanine as electron mediator have been prepared by two different methods. In the first approach, the enzyme and the electron mediator have been immobilized in carbon paste electrodes. In the second method, they have been introduced in an arachidic acid Langmuir-Blodgett nanostructured film that provides a biomimetic environment. The sensing properties of non-nanostructured and nanostructured biosensors towards catechol, catechin and phenol have been analyzed and compared. The enzyme retains the biocatalytic properties in both matrixes. However, the nanostructured biomimetic films show higher values of maximum reaction rates and lowest apparent Michaelis-Menten constants. In both types of sensors, the sensitivity follows the decreasing order catechol > catechin > phenol. The detection limits observed are in the range of 1.8–5.4 μM for Langmuir-Blodgett biosensors and 8.19–8.57 μM for carbon paste biosensors. In summary, it has been demonstrated that the Langmuir-Blodgett films provide a biomimetic environment and nanostructured biosensors show better performances in terms of kinetic, detection limit and stability. Full article