ArticleBiosensors2022
Disposable Electrochemical Biosensor Based on the Inhibition of Alkaline Phosphatase Encapsulated in Acrylamide Hydrogels.
Article in Biosensors, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Confined Catalysis of Enzymes: Enhancement Strategies, Materials, and Biosensor Applications.Journal of functional biomaterials · 2026Review
- Non-invasive and user-friendly visual detection of salivary phosphate using enzymatic biosensor test strip for chronic kidney disease screening.Analytical and bioanalytical chemistry · 2026Article
- Fluorescent Nanocomposite Hydrogels Based on Conjugated Polymer Nanoparticles as Platforms for Alkaline Phosphatase Detection.Biosensors · 2023Article
- Portable Alkaline Phosphatase-Hydrogel Platform: From Enzyme Characterization to Phosphate Sensing.International journal of molecular sciences · 2023Article
- Electrochemistry and Spectroscopy-Based Biosensors.Biosensors · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The present work describes the development of an easy-to-use portable electrochemical biosensor based on alkaline phosphatase (ALP) as a recognition element, which has been immobilized in acrylamide-based hydrogels prepared through a green protocol over disposable screen-printed electrodes. To carry out the electrochemical transduction, an electroinactive substrate (hydroquinone diphosphate) was used in the presence of the enzyme and then it was hydrolyzed to an electroactive species (hydroquinone). The activity of the protein within the matrix was determined voltammetrically. Due to the adhesive properties of the hydrogel, this was easily deposited on the surface of the electrodes, greatly increasing the sensitivity of the biosensor. The device was optimized to allow the determination of phosphate ion, a competitive inhibitor of ALP, in aqueous media. Our study provides a proof-of-concept demonstrating the potential use of the developed biosensor for in situ, real-time measurement of water pollutants that act as ALP inhibitors.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.