Enzymatic electrochemical biosensor for glyphosate detection based on acid phosphatase inhibition
| Autor: | Gamolwan Tumcharern, Preeyanut Butmee, Margaret Kerr, Marie-José Durand, Anchalee Samphao, Kurt Kalcher, Gérald Thouand, Chomphunuch Songsiriritthigul |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Acid Phosphatase
Glycine Biosensing Techniques Spectrum Analysis Raman Biochemistry Silver nanoparticle Analytical Chemistry chemistry.chemical_compound Limit of Detection chemistry.chemical_classification biology Herbicides Chemistry Acid phosphatase Reproducibility of Results Electrochemical Techniques Chronoamperometry Enzymes Immobilized Molecular Docking Simulation Kinetics Enzyme Docking (molecular) Glyphosate biology.protein Glutaraldehyde Biosensor Nuclear chemistry |
| Zdroj: | Analytical and Bioanalytical Chemistry. 413:5859-5869 |
| ISSN: | 1618-2650 1618-2642 |
| Popis: | A novel enzymatic electrochemical biosensor was fabricated for the indirect detection of glyphosate-based acid phosphatase inhibition. The biosensor was constructed on a screen-printed carbon electrode modified with silver nanoparticles, decorated with electrochemically reduced graphene oxide, and chemically immobilized with acid phosphatase via glutaraldehyde cross-linking. We measured the oxidation current by chronoamperometry. The current arose from the enzymatic reaction of acid phosphatase and the enzyme-substrate disodium phenyl phosphate. The biosensing response is a decrease in signal resulting from inhibition of acid phosphatase in the presence of glyphosate inhibitor. The inhibition of acid phosphatase by glyphosate was investigated as a reversible competitive-type reaction based on the Lineweaver-Burk equation. Computational docking confirmed that glyphosate was the inhibitor bound in the substrate-binding pocket of acid phosphatase and that it was able to inhibit the enzyme efficiently. Additionally, the established method was applied to the selective analysis of glyphosate in actual samples with satisfactory results following a standard method. |
| Databáze: | OpenAIRE |
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