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- W4206502135 abstract "Utilizing an appropriate enzyme immobilization strategy is crucial for designing enzyme-based biosensors. Plant virus-like particles represent ideal nanoscaffolds for an extremely dense and precise immobilization of enzymes, due to their regular shape, high surface-to-volume ratio and high density of surface binding sites. In the present work, tobacco mosaic virus (TMV) particles were applied for the co-immobilization of penicillinase and urease onto the gate surface of a field-effect electrolyte-insulator-semiconductor capacitor (EISCAP) with a p-Si-SiO2-Ta2O5 layer structure for the sequential detection of penicillin and urea. The TMV-assisted bi-enzyme EISCAP biosensor exhibited a high urea and penicillin sensitivity of 54 and 85 mV/dec, respectively, in the concentration range of 0.1-3 mM. For comparison, the characteristics of single-enzyme EISCAP biosensors modified with TMV particles immobilized with either penicillinase or urease were also investigated. The surface morphology of the TMV-modified Ta2O5-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an XOR (Exclusive OR) enzyme logic gate." @default.
- W4206502135 created "2022-01-25" @default.
- W4206502135 creator A5023099021 @default.
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- W4206502135 creator A5073021286 @default.
- W4206502135 date "2022-01-14" @default.
- W4206502135 modified "2023-10-02" @default.
- W4206502135 title "Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with Tobacco Mosaic Virus Bioparticles as Enzyme Nanocarriers" @default.
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- W4206502135 doi "https://doi.org/10.3390/bios12010043" @default.
- W4206502135 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35049671" @default.
- W4206502135 hasPublicationYear "2022" @default.