Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers
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 o...
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MDPI AG
2022-01-01
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author | Melanie Welden Arshak Poghossian Farnoosh Vahidpour Tim Wendlandt Michael Keusgen Christina Wege Michael J. Schöning |
author_facet | Melanie Welden Arshak Poghossian Farnoosh Vahidpour Tim Wendlandt Michael Keusgen Christina Wege Michael J. Schöning |
author_sort | Melanie Welden |
collection | DOAJ |
description | 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, <i>tobacco mosaic virus</i> (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-SiO<sub>2</sub>-Ta<sub>2</sub>O<sub>5</sub> 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 Ta<sub>2</sub>O<sub>5</sub>-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an <b>XOR</b> (<b>Exclusive OR</b>) enzyme logic gate. |
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issn | 2079-6374 |
language | English |
last_indexed | 2024-03-10T01:48:54Z |
publishDate | 2022-01-01 |
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spelling | doaj.art-43085bd32d064a9490bf32b2309d5ddf2023-11-23T13:08:26ZengMDPI AGBiosensors2079-63742022-01-011214310.3390/bios12010043Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme NanocarriersMelanie Welden0Arshak Poghossian1Farnoosh Vahidpour2Tim Wendlandt3Michael Keusgen4Christina Wege5Michael J. Schöning6Institute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428 Jülich, GermanyMicroNanoBio, 40479 Düsseldorf, GermanyInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428 Jülich, GermanyInstitute of Biomaterials and Biomolecular Systems, University of Stuttgart, 70569 Stuttgart, GermanyInstitute of Pharmaceutical Chemistry, Philipps University Marburg, 35032 Marburg, GermanyInstitute of Biomaterials and Biomolecular Systems, University of Stuttgart, 70569 Stuttgart, GermanyInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428 Jülich, GermanyUtilizing 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, <i>tobacco mosaic virus</i> (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-SiO<sub>2</sub>-Ta<sub>2</sub>O<sub>5</sub> 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 Ta<sub>2</sub>O<sub>5</sub>-gate was analyzed by scanning electron microscopy. Additionally, the bi-enzyme EISCAP was applied to mimic an <b>XOR</b> (<b>Exclusive OR</b>) enzyme logic gate.https://www.mdpi.com/2079-6374/12/1/43<i>tobacco mosaic virus</i> (TMV)capacitive field-effect sensorbi-enzyme biosensorenzyme-logic gateureasepenicillinase |
spellingShingle | Melanie Welden Arshak Poghossian Farnoosh Vahidpour Tim Wendlandt Michael Keusgen Christina Wege Michael J. Schöning Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers Biosensors <i>tobacco mosaic virus</i> (TMV) capacitive field-effect sensor bi-enzyme biosensor enzyme-logic gate urease penicillinase |
title | Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers |
title_full | Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers |
title_fullStr | Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers |
title_full_unstemmed | Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers |
title_short | Towards Multi-Analyte Detection with Field-Effect Capacitors Modified with <i>Tobacco Mosaic Virus</i> Bioparticles as Enzyme Nanocarriers |
title_sort | towards multi analyte detection with field effect capacitors modified with i tobacco mosaic virus i bioparticles as enzyme nanocarriers |
topic | <i>tobacco mosaic virus</i> (TMV) capacitive field-effect sensor bi-enzyme biosensor enzyme-logic gate urease penicillinase |
url | https://www.mdpi.com/2079-6374/12/1/43 |
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