Electrochemical biosensor on disposable electrodes for the detection of alkaline phosphatase inhibitors in seawater
[EN] A disposable electrochemical biosensor for the detection of alkaline phosphatase (ALP) inhibitors in seawater was developed by immobilizing ALP within sol-gel silica and organically modified silica matrices deposited onto screen-printed carbon electrodes. Hydroquinone diphosphate, an electroina...
| Authors: | , , |
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| Format: | article |
| Publication Date: | 2026 |
| Country: | España |
| Institution: | Universitat Politècnica de València (UPV) |
| Repository: | RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
| Language: | English |
| OAI Identifier: | oai:dnet:riunet______::897f0bb7d07740d7949e23358cee7e8e |
| Online Access: | https://riunet.upv.es/handle/10251/235970 |
| Access Level: | Open access |
| Keyword: | Electrochemical biosensor Sol-gel silica ORMOSIL Alkaline phosphatase Phosphate ion inhibitor Synthetic seawater 14.- Conservar y utilizar de forma sostenible los océanos, mares y recursos marinos para lograr el desarrollo sostenible |
| Summary: | [EN] A disposable electrochemical biosensor for the detection of alkaline phosphatase (ALP) inhibitors in seawater was developed by immobilizing ALP within sol-gel silica and organically modified silica matrices deposited onto screen-printed carbon electrodes. Hydroquinone diphosphate, an electroinactive substrate, enabled amperometric quantification of enzymatic activity through the electrochemical detection of the hydrolysis product, hydroquinone. Fluorescence spectroscopy confirmed that ALP retained its structural integrity after immobilization, although restricted rotational mobility and microenvironmental polarity shifts were observed depending on the silica modifier. All matrices allowed substrate and product diffusion, although reduced apparent activity is detected relative to the free enzyme, because of diffusional constraints. Among the materials tested, isobutylmodified silica provided the optimal balance between structural stabilization and catalytic accessibility, yielding the highest apparent activity. Inhibition assays using phosphate ion demonstrated a clear dosedependent suppression of enzymatic activity, with a linear response from 1 to 10 mu M and a limit of detection of 0.38 mu M. The biosensor exhibits rapid response, portability, and suitability for in situ assessment of phosphate and other ALP-inhibiting contaminants in marine environments. |
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