Relevant bibliographies by topics / Enzyme-based biosensor

Academic literature on the topic 'Enzyme-based biosensor'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Enzyme-based biosensor"

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Turdean, Graziella L. "Design and Development of Biosensors for the Detection of Heavy Metal Toxicity." International Journal of Electrochemistry 2011 (2011): 1–15. http://dx.doi.org/10.4061/2011/343125.

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Many compounds (including heavy metals, HMs) used in different fields of industry and/or agriculture act as inhibitors of enzymes, which, as consequence, are unable to bind the substrate. Even if it is not so sensitive, the method for detecting heavy metal traces using biosensors has a dynamic trend and is largely applied for improving the “life quality”, because of biosensor's sensitivity, selectivity, and simplicity. In the last years, they also become more and more a synergetic combination between biotechnology and microelectronics. Dedicated biosensors were developed for offline and online analysis, and also, their extent and diversity could be called a real “biosensor revolution”. A panel of examples of biosensors: enzyme-, DNA-, imuno-, whole-cell-based biosensors were systematised depending on the reaction type, transduction signal, or analytical performances. The mechanism of enzyme-based biosensor and the kinetic of detection process are described and compared. In this context, is explainable why bioelectronics, nanotechnology, miniaturization, and bioengineering will compete for developing sensitive and selective biosensors able to determine multiple analytes simultaneously and/or integrated in wireless communications systems.
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Bravo, Iria, Cristina Gutiérrez-Sánchez, Tania García-Mendiola, Mónica Revenga-Parra, Félix Pariente, and Encarnación Lorenzo. "Enhanced Performance of Reagent-Less Carbon Nanodots Based Enzyme Electrochemical Biosensors." Sensors 19, no. 24 (December 17, 2019): 5576. http://dx.doi.org/10.3390/s19245576.

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This work reports on the advantages of using carbon nanodots (CNDs) in the development of reagent-less oxidoreductase-based biosensors. Biosensor responses are based on the detection of H2O2, generated in the enzymatic reaction, at 0.4 V. A simple and fast method, consisting of direct adsorption of the bioconjugate, formed by mixing lactate oxidase, glucose oxidase, or uricase with CNDs, is employed to develop the nanostructured biosensors. Peripherical amide groups enriched CNDs are prepared from ethyleneglycol bis-(2-aminoethyl ether)-N,N,N′,N′-tetraacetic acid and tris(hydroxymethyl)aminomethane, and used as precursors. The bioconjugate formed between lactate oxidase and CNDs was chosen as a case study to determine the analytical parameters of the resulting L-lactate biosensor. A linear concentration range of 3.0 to 500 µM, a sensitivity of 4.98 × 10−3 µA·µM−1, and a detection limit of 0.9 µM were obtained for the L-lactate biosensing platform. The reproducibility of the biosensor was found to be 8.6%. The biosensor was applied to the L-lactate quantification in a commercial human serum sample. The standard addition method was employed. L-lactate concentration in the serum extract of 0.9 ± 0.3 mM (n = 3) was calculated. The result agrees well with the one obtained in 0.9 ± 0.2 mM, using a commercial spectrophotometric enzymatic kit.
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Alvarado-Ramírez, Lynette, Magdalena Rostro-Alanis, José Rodríguez-Rodríguez, Juan Eduardo Sosa-Hernández, Elda M. Melchor-Martínez, Hafiz M. N. Iqbal, and Roberto Parra-Saldívar. "Enzyme (Single and Multiple) and Nanozyme Biosensors: Recent Developments and Their Novel Applications in the Water-Food-Health Nexus." Biosensors 11, no. 11 (October 21, 2021): 410. http://dx.doi.org/10.3390/bios11110410.

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The use of sensors in critical areas for human development such as water, food, and health has increased in recent decades. When the sensor uses biological recognition, it is known as a biosensor. Nowadays, the development of biosensors has been increased due to the need for reliable, fast, and sensitive techniques for the detection of multiple analytes. In recent years, with the advancement in nanotechnology within biocatalysis, enzyme-based biosensors have been emerging as reliable, sensitive, and selectively tools. A wide variety of enzyme biosensors has been developed by detecting multiple analytes. In this way, together with technological advances in areas such as biotechnology and materials sciences, different modalities of biosensors have been developed, such as bi-enzymatic biosensors and nanozyme biosensors. Furthermore, the use of more than one enzyme within the same detection system leads to bi-enzymatic biosensors or multi-enzyme sensors. The development and synthesis of new materials with enzyme-like properties have been growing, giving rise to nanozymes, considered a promising tool in the biosensor field due to their multiple advantages. In this review, general views and a comparison describing the advantages and disadvantages of each enzyme-based biosensor modality, their possible trends and the principal reported applications will be presented.
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Batista, Erica, Marx Pereira, Isaac Macêdo, Fabio Machado, Emily Moreno, Elgia Diniz, Italo Frazão, Lorrayne Bernardes, Severino Oliveira, and Eric Gil. "Electroanalytical Enzyme Biosensor Based on Cordia superba Enzyme Extract for the Detection of Phytomarkers in Kombucha." Biosensors 12, no. 12 (December 1, 2022): 1112. http://dx.doi.org/10.3390/bios12121112.

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Antioxidants are responsible for many beneficial health effects and are highly present in natural products, such as kombucha. Biosensors’ development targeting antioxidants and phytomarkers are an active research field. This work aimed to propose a voltammetric polyphenolxidase (Cordia superba) biosensor for catechin and total phenolic compounds quantification in kombucha samples. Optimizations were performed on the biosensor of Cordia superba to improve the accuracy and selectivity, such as enzyme–substrate interaction time, analytical responses for different patterns and signal differences with the carbon paste and modified carbon paste electrode. Kombucha probiotic drink samples were fermented for 7 to 14 days at a controlled temperature (28 ± 2 °C). A linear curve was made for catechin with a range of 10.00 to 60.00 µM, with a limit of detection of 0.13 µM and limit of quantification of 0.39 µM. The biosensor proposed in this work was efficient in determining the patterns of phenolic compounds in kombucha.
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Khan, Marya, Vandana Nagal, Sakeena Masrat, Talia Tuba, Nirmalya Tripathy, Mohammad K. Parvez, Mohammed S. Al-Dosari, et al. "Wide-Linear Range Cholesterol Detection Using Fe2O3 Nanoparticles Decorated ZnO Nanorods Based Electrolyte-Gated Transistor." Journal of The Electrochemical Society 169, no. 2 (February 1, 2022): 027512. http://dx.doi.org/10.1149/1945-7111/ac51f6.

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Electrolyte-gated transistor (EGT)-based biosensors are created with nanomaterials to harness the advantages of miniaturization and excellent sensing performance. A cholesterol EGT biosensor based on iron oxide (Fe2O3) nanoparticles decorated ZnO nanorods is proposed here. ZnO nanorods are directly grown on the seeded channel using a hydrothermal method, keeping in mind the stability of nanorods on the channel during biosensor measurements in an electrolyte. Most importantly, ZnO nanorods can be effectively grown and modified with Fe2O3 nanoparticles to enhance stability, surface roughness, and performance. The cholesterol oxidase (ChOx) enzyme is immobilized over Fe2O3 nanoparticles decorated ZnO nanorods for cholesterol detection. With cholesterol addition in buffer solution, the electro-oxidation of cholesterol on enzyme immobilized surface led to increased the biosensor’s current response. The cholesterol EGT biosensor detected cholesterol in wide-linear range (i.e., 0.1 to 60.0 mM) with high sensitivity (37.34 μA mM−1cm−2) compared to conventional electrochemical sensors. Furthermore, we obtained excellent selectivity, fabrication reproducibility, long-term storage stability, and practical applicability in real serum samples. The demonstrated EGT biosensor can be extended with changing enzymes or nanomaterials or hybrid nanomaterials for specific analyte detection.
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Liu, Guodong, Yuehe Lin, Veronika Ostatná, and Joseph Wang. "Enzyme nanoparticles-based electronic biosensor." Chemical Communications, no. 27 (2005): 3481. http://dx.doi.org/10.1039/b504943a.

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Polan, Vojtěch, Jan Soukup, and Karel Vytřas. "Screen-Printed Carbon Electrodes Modified by Rhodium Dioxide and Glucose Dehydrogenase." Enzyme Research 2010 (March 3, 2010): 1–7. http://dx.doi.org/10.4061/2010/324184.

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The described glucose biosensor is based on a screen-printed carbon electrode (SPCE) modified by rhodium dioxide, which functions as a mediator. The electrode is further modified by the enzyme glucose dehydrogenase, which is immobilized on the electrode's surface through electropolymerization with m-phenylenediamine. The enzyme biosensor was optimized and tested in model glucose samples. The biosensor showed a linear range of 500–5000 mg L−1 of glucose with a detection limit of 210 mg L−1 (established as 3σ) and response time of 39 s. When compared with similar glucose biosensors based on glucose oxidase, the main advantage is that neither ascorbic and uric acids nor paracetamol interfere measurements with this biosensor at selected potentials.
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Rafat, Neda, Paul Satoh, and Robert Mark Worden. "Electrochemical Biosensor for Markers of Neurological Esterase Inhibition." Biosensors 11, no. 11 (November 16, 2021): 459. http://dx.doi.org/10.3390/bios11110459.

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A novel, integrated experimental and modeling framework was applied to an inhibition-based bi-enzyme (IBE) electrochemical biosensor to detect acetylcholinesterase (AChE) inhibitors that may trigger neurological diseases. The biosensor was fabricated by co-immobilizing AChE and tyrosinase (Tyr) on the gold working electrode of a screen-printed electrode (SPE) array. The reaction chemistry included a redox-recycle amplification mechanism to improve the biosensor’s current output and sensitivity. A mechanistic mathematical model of the biosensor was used to simulate key diffusion and reaction steps, including diffusion of AChE’s reactant (phenylacetate) and inhibitor, the reaction kinetics of the two enzymes, and electrochemical reaction kinetics at the SPE’s working electrode. The model was validated by showing that it could reproduce a steady-state biosensor current as a function of the inhibitor (PMSF) concentration and unsteady-state dynamics of the biosensor current following the addition of a reactant (phenylacetate) and inhibitor phenylmethylsulfonylfluoride). The model’s utility for characterizing and optimizing biosensor performance was then demonstrated. It was used to calculate the sensitivity of the biosensor’s current output and the redox-recycle amplification factor as a function of experimental variables. It was used to calculate dimensionless Damkohler numbers and current-control coefficients that indicated the degree to which individual diffusion and reaction steps limited the biosensor’s output current. Finally, the model’s utility in designing IBE biosensors and operating conditions that achieve specific performance criteria was discussed.
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Al-Furjan, M. S. H., Kui Cheng, and Wenjian Weng. "Influences of Mg Doping on the Electrochemical Performance of TiO2Nanodots Based Biosensor Electrodes." Advances in Materials Science and Engineering 2014 (2014): 1–8. http://dx.doi.org/10.1155/2014/965821.

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Electrochemical biosensors are essential for health monitors to help in diagnosis and detection of diseases. Enzyme adsorptions on biosensor electrodes and direct electron transfer between them have been recognized as key factors to affect biosensor performance. TiO2has a good protein adsorption ability and facilitates having more enzyme adsorption and better electron transfer. In this work, Mg ions are introduced into TiO2nanodots in order to further improve electrode performance because Mg ions are considered to have good affinity with proteins or enzymes. Mg doped TiO2nanodots on Ti substrates were prepared by spin-coating and calcining. The effects of Mg doping on the nanodots morphology and performance of the electrodes were investigated. The density and size of TiO2nanodots were obviously changed with Mg doping. The sensitivity of 2% Mg doped TiO2nanodots based biosensor electrode increased to 1377.64 from 897.8 µA mM−1 cm−2and itsKMappdecreases to 0.83 from 1.27 mM, implying that the enzyme achieves higher catalytic efficiency due to better affinity of the enzyme with the Mg doped TiO2. The present work could provide an alternative to improve biosensor performances.
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Zhao, Dong Jiao, Yan Hong Chen, Chen Di Tu, Yao Fang Xuan, and Feng Na Xi. "Construction of Reagentless Biosensor Based on Self-Assembly and Electrodeposition for Determination of Hydrogen Peroxide." Advanced Materials Research 441 (January 2012): 442–46. http://dx.doi.org/10.4028/www.scientific.net/amr.441.442.

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A general methodology to prepare reagentless biosensor was developed based on self-assembly and electrodeposition. Redox active inorganic multilayers consisting of copper hexacyanoferrate (CuHCF) multilayers were formed by successive self-assembly. A simple and controllable electrodeposition approach was established for one-step fabrication of chitosan-enzyme layer on CuHCF modified electrode. Horseradish peroxidase was selected as the model enzyme. With CuHCF as the electroactive mediator, the developed reagentless biosensor exhibited a fast amperometric response for the determination of hydrogen peroxide (H2O2). The linear response ranged from 1.4 × 10-5 to 2.0 × 10-4 M with a detection limit of 1.2 × 10-6 M. The biosensor exhibited high reproducibility and long-time storage stability. The proposed methodology could serve as a versatile platform for fabrication of electrochemical biosensors.
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Dissertations / Theses on the topic "Enzyme-based biosensor"

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Dewa, Andrew Steven. "A silicon-based enzyme biosensor utilizing Langmuir-Blodgett film immobilization." Case Western Reserve University School of Graduate Studies / OhioLINK, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=case1057002686.

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Veisi, Zeinab. "Detection of COX-2 enzyme using highly sensitive electrospun polyaniline nanofiber-based biosensor." Thesis, Wichita State University, 2013. http://hdl.handle.net/10057/6846.

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This research attempted to determine the practicality of the integration of electrospun polyaniline nanofiber as the main sensing component into interdigitated gold microelectrodes to develop a biosensor platform for sensitive, selective, and label-free detection the of Cyclooxygenase-2 (COX-2) biomarker from pure and human serum samples. COX-2 is an important enzyme in pain biomarkers, inflammation and cancer cell proliferation, so it is necessary to develop a reliable biosensor that can sensitively and objectively quantify COX-2 enzyme expression for clinical diagnosis. Polyaniline nanofibers were prepared at four different diameters using electrospinning performed at four different flow rates. The performance of the electrospun polyaniline nanofiber based biosensor was evaluated in comparison with a plain control biosensor using electrochemical impedance spectroscopy. Significant improvement was observed in the sensitivity of the electrospun polyaniline nanofiber based biosensor revealing the remarkable capability of electrospun polyaniline nanofiber in robust and rapid detection of the COX-2 biomarker. This improvement was attributed to the large specific surface area of electrospun polyaniline nanofiber as well as its highly porous structure which enhances size-matched confinement, transduction and signal strength, thus increasing the sensitivity of the biosensor significantly. The fabricated nanofiber based biosensor was able to detect the target antigen with concentrations as low as 0.01pg/ml and 10fg/ml in pure and human serum samples, respectively, as well as remarkable selectivity towards Human Serum Albumin suggesting the significant contribution of this nanofiber based platform to the enhanced strength and sensitivity in COX-2 analyte detection.
Thesis (M.S.)--Wichita State University, College of Engineering, Dept. of Mechanical Engineering
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Sumner, Claire. "Development of a biosensor based on enzyme-catalysed degradation of thin polymer films." Thesis, University of Sheffield, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.341818.

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Sok, Vibol. "Amperometric enzyme-based detection of agriculturalpesticides on novel carbon nano-onion composites." Doctoral thesis, Universitat Rovira i Virgili, 2018. http://hdl.handle.net/10803/665119.

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Actualment hi ha una gran preocupació sobre l'ús de pesticides en l'agricultura i els seus possibles efectes secundaris. Això fa que el desenvolupament de sistemes de detecció sensibles i robustos sigui un pas important en aquesta direcció. D'altra banda, les nano-cebes de carboni (CNOs) són materials molt atractius i prometedors amb estructures definides i propietats electroquímiques notables que amb prou feines s'han estudiat en biosensors. L'objectiu general d'aquesta tesi és estudiar la interacció de diferents plaguicides amb peroxidasa i tirosinasa amb l'objectiu de desenvolupar biosensors per a la seva detecció basats en elèctrodes modificats amb CNOs. Per aconseguir aquest objectiu general, s'ha estudiat: 1) la inhibició de les activitats de peroxidasa i tirosinasa per tres dels plaguicides més utilitzats (2,4-D, 2,4,5-T i glifosat), 2) l'ús d'CNOs oxidades com a suports per a la immobilització d'enzims i un estudi de l'activitat i estabilitat dels enzims immobilitzades, 3) el desenvolupament de biosensors electroquímics per a detecció dels plaguicides abans esmentats basats en els elèctrodes modificats amb composites contenint enzims i CNOs. Aquesta tesi és, per tant, una contribució a un camp de ràpid creixement relacionat amb el desenvolupament de noves classes de nanomaterials de carboni que té com a objectiu ampliar les seves aplicacions actuals en la construcció de sistemes de detecció nous amb millors prestacions.
Actualmente existe una gran preocupación sobre el uso de pesticidas en la agricultura y sus posibles efectos secundarios. Esto hace que el desarrollo de sistemas de detección sensibles y robustos sea un paso importante en esta dirección. Por otro lado, las nano-cebollas de carbono (CNOs) son materiales muy atractivos y prometedores con estructuras definidas y propiedades electroquímicas notables que apenas se han estudiado en biosensores. El objetivo general de esta tesis es estudiar la interacción de diferentes plaguicidas con peroxidasa y tirosinasa con el objetivo de desarrollar biosensores para su detección basados ​​en electrodos modificados con CNOs. Para lograr este objetivo general, se ha estudiado: 1) la inhibición de las actividades de peroxidasa y tirosinasa por tres de los plaguicidas más utilizados (2,4-D, 2,4,5-T y glifosato), 2) el uso de CNOs oxidadas como soportes para la inmovilización de enzimas y un estudio de la actividad y estabilidad de las enzimas inmovilizadas, 3) el desarrollo de biosensores electroquímicos para detección de los plaguicidas antes citados basados ​​en los electrodos modificados con composites conteniendo enzimas y CNOs. Esta tesis es, por lo tanto, una contribución a un campo de rápido crecimiento relacionado con el desarrollo de nuevas clases de nanomateriales de carbono que tiene como objetivo ampliar sus aplicaciones actuales en la construcción de sistemas de detección novedosos con mejores prestaciones.
There is currently a strong concern on the use of pesticides in agriculture and their possible side effects. This makes the development of sensitive and robust detection systems an important step in this direction. On the other hand, carbon nano-onions are very attractive and promising materials with defined structures and remarkable electrochemical properties that have been scarcely studied in biosensing. The overall objective of this thesis is to study the interaction of different pesticides with peroxidase and tyrosinase with the aim to develop biosensors for pesticide detection based on CNO-modified electrodes. To achieve this general objective, the following aspects have been focused on: 1) the inhibition of peroxidase and tyrosinase activities by three of the most used pesticides (2,4-D, 2,4,5-T and glyphosate), 2) the use of oxidized CNOs as supports for the immobilization of enzymes and a study of the activity and stability of the immobilized enzymes, 3) the development of electrochemical biosensors for pesticide detection based on the prepared CNO-enzyme modified electrodes. This thesis is thus a contribution to a rapidly growing field related with the development of new classes of carbon nano-onion based nanomaterials that aims at expanding their current applications in the construction of novel detection systems with improved performances.
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Campbell, Alan S. "Enzymatic Biosensor and Biofuel Cell Development Using Carbon Nanomaterials and Polymer-Based Protein Engineering." Research Showcase @ CMU, 2017. http://repository.cmu.edu/dissertations/859.

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The development of enzymatic biosensors and enzymatic biofuel cells (EBFCs) has been a significant area of research for decades. Enzymatic catalysis can provide for specific, reliable sensing of target analytes as well as the continuous generation of power from physiologically present fuels. However, the broad implementation of enzyme-based devices is still limited by low operational/storage stabilities and insufficient power densities. Approaches to improving upon these limitations have focused on the optimization of enzyme activity and electron transfer kinetics at enzyme-functionalized electrodes. Currently, such optimization can be performed through enzyme structural engineering, improvement of enzyme immobilization methodologies, and fabrication of advantageous electrode materials to enhance retained enzyme activity density at the electrode surface and electron transfer rates between enzymes and an electrode. In this work, varying electrode materials were studied to produce an increased understanding on the impacts of material properties on resulting biochemical, and electrochemical performances upon enzyme immobilization and an additional method of electroactive enzyme-based optimization was developed through the use of polymer-based protein engineering (PBPE). First, graphene/single-wall carbon nanotube cogels were studied as supports for membrane- and mediator-free EBFCs. The high available specific surface area and porosity of these materials allowed the rechargeable generation of a power density within one order of magnitude of the highest performing glucose-based EBFCs to date. Second, two additional carbon nanomaterial-based electrode materials were fabricated and examined as EBFC electrodes. Graphene-coated single-wall carbon nanotube gels and gold nanoparticle/multi-wall carbon nanotube-coated polyacrylonitrile fiber paddles were utilized as electroactive enzyme supports. The performance comparison of these three materials provided an increased understanding of the impact of material properties such as pore size, specific surface area and material surface curvature on enzyme biochemical and electrochemical characteristics upon immobilization. Third, PBPE techniques were applied to develop enzyme-redox polymer conjugates as a new platform for enzymatic biosensor and EBFC optimization. Poly(N-(3-dimethyl(ferrocenyl) methylammonium bromide)propyl acrylamide) (pFcAc) was grown directly from the surface of glucose oxidase (GOX) through atom-transfer radical polymerization. Utilization of the synthesized GOX-pFcAc conjugates led to a 24-fold increase in current generation efficiency and a 4-fold increase in EBFC power density compared to native GOX. GOX-pFcAc conjugates were further examined as working catalysts in carbon paper-based enzymatic biosensors, which provided reliable and selective glucose sensitivities and allowed a systematic analysis of sources of instability in enzyme-polymer conjugate-based biosensors and EBFCs. The knowledge gained through these studies and the in-depth characterization of an additional layer of optimization capacity using PBPE could potentially enhance the progress of enzymatic biosensor and EBFC development.
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Sanghera, G. S. "Electrochemical biosensors for food based systems (enzyme electrodes)." Thesis, Cardiff University, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.376828.

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Berners, Manfred Otto Maria. "Development of enzyme based sensors for use in neurochemistry." Thesis, University of Oxford, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.307034.

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Martin, Stacey Peter. "Enzyme-based quartz crystal biosensors for analytes of biomedical significance." Thesis, University of Surrey, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.402575.

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Paliwal, Sheetal Simonian Aleksandr L. "Development of enzyme-based biosensors for the detection of organophosphate neurotoxins." Auburn, Ala, 2008. http://repo.lib.auburn.edu/EtdRoot/2008/FALL/Materials_Engineering/Dissertation/Paliwal_Sheetal_0.pdf.

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Öh, Clara. "Biosensor based on immobilized amine transaminase for detection of amphetamine." Thesis, KTH, Skolan för kemi, bioteknologi och hälsa (CBH), 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-278584.

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Amine transaminases (ATA) catalyse the transfer of an amino group from one molecule and replaces a ketone or aldehyde with the amino group, the amino group on the amino-donor is replaced with a ketone or aldehyde. This enzyme, ATA from Chromobacterium violaceum, has previously been used to catalyse the reaction involving amphetamine, therefore, it might be possible to use this enzyme to convert amphetamine and the product absorbs in the UV spectrum and can therefore be measured spectrophotometrically. The aim of the project was to explore the possibility of using ATA in a portable biosensor for the detection of amphetamine. A literature study of commercially available portable biosensors was performed, activity of the free enzyme was tested against two substrates, methylbenzylamine (MBA) and amphetamine. Research on immobilization techniques, materials, and surface functionalization was done to chose suitable methods for immobilizing ATA. Two immobilization methods were suggested and one of the methods, ionic immobilization through His-tag towards Ni2+ on the surface, was tested for enzyme activity toward MBA. The enzyme activity of the free enzyme in solution towards MBA was comparable to previously reported enzyme activity, however, no enzyme activity towards amphetamine was observed. No activity was observed for the immobilized enzyme, but it might be due to the experimental design, more experiments need to be performed to draw conclusions.
Amintransaminaser (ATA) katalyserar överförandet av en amingrupp från en molekyl och ersätter en keton eller aldehyd med den amingruppen, amingruppen på amin-donatorn ersätts med en keton eller aldehyd. Det här enzymet, ATA från Chromobacterium violaceum (CvATA), har tidigare använts för att katalysera en reaktion som involverar amfetamin, därför skulle detta enzym kunna användas på amfetamin. Produkten av reaktionen absorberar i UV spektrumet och kan mätas med en spektrofotometer. Målet med projektet var att utforska möjligheten av att använda CvATA i en biosensor för att detektera amfetamin. En litteraturstudie på kommersiellt tillgängliga bärbara biosensorer genomfördes, aktiviteten av det fria enzymet testades mot två substrat, metylbenzylamin (MBA) och amfetamin. Information samlades om immobiliseringstekniker, material, och ytfunktionalisering gjordes för att välja ut lämpliga metoder för immobilisering av CvATA. Två immobiliseringsmetoder föreslogs och en av metoderna, immobilisering via enzymets His6-tagg och Ni2+ joner på ytan, testades för enzymaktivitet mot MBA. Enzymaktiviteten av det fria enzymet i lösning mot MBA var i samma storleksordning som tidigare rapporterad enzymaktivitet, men ingen enzymaktivitet mot amfetamin kunde observeras. Ingen aktivitet kunde observeras för det immobiliserade enzymet, men det kan vara på grund av designen på experimentet, fler experiment behöver göras för att kunna dra några fler slutsatser.
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Books on the topic "Enzyme-based biosensor"

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Zhou, Dao Min. An investigation of some electrochemical characteristics of enzyme based disposable biosensors and other relevant electrodes. [S.l: The Author], 1994.

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Oh, Jonghak. Biosensors: Microorganism Sensor,Biomimetic Sensor,Electrochemical Biosensor,Immune Sensor,Glucose Sensor,Optical Biosensors,DNA/Nucleic Acid Sensor,Cell-Based Biosensor,Enzyme Sensor. Independently Published, 2021.

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Patra, Sanjukta, Debasree Kundu, and Manashjit Gogoi. Enzyme-Based Biosensors: Recent Advances and Applications in Healthcare. Springer Singapore Pte. Limited, 2022.

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Qhobosheane, Monde T. Two-dimensional enzyme-based biosensors for spatially resolved imaging and monitoring of neurochemicals. 2003.

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Book chapters on the topic "Enzyme-based biosensor"

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Cao, Shunsheng, Juanrong Chen, Xin Jin, Weiwei Wu, and Zhiyuan Zhao. "Enzyme-Based Biosensors: Synthesis and Applications." In Biosensor Nanomaterials, 95–115. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527635160.ch5.

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Gau, Jen-Jr, Esther H. Lan, Bruce Dunn, and Chih-Ming Ho. "Enzyme-Based Electrochemical Biosensor with DNA Array Chip." In Micro Total Analysis Systems 2000, 509–12. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-017-2264-3_119.

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Koch, Claudia, Arshak Poghossian, Christina Wege, and Michael J. Schöning. "TMV-Based Adapter Templates for Enhanced Enzyme Loading in Biosensor Applications." In Methods in Molecular Biology, 553–68. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7808-3_35.

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Simonian, A. L., E. I. Rainina, P. F. Fitzpatrick, and J. Wild. "Enhancement of the Specificity of an Enzyme-Based Biosensor for L-Tryptophan." In Advances in Experimental Medicine and Biology, 833–40. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4709-9_106.

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Arduini, Fabiana, and Aziz Amine. "Biosensors Based on Enzyme Inhibition." In Advances in Biochemical Engineering/Biotechnology, 299–326. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/10_2013_224.

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Gazel, Nilay, and Huseyin B. Yildiz. "Enzyme-Based Biosensors in Food Industry via Surface Modifications." In Surface Treatments for Biological, Chemical, and Physical Applications, 227–52. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2016. http://dx.doi.org/10.1002/9783527698813.ch7.

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Kauffmann, J. M. "Lipid Based Enzyme Electrodes for Environmental Pollution Control." In Biosensors for Direct Monitoring of Environmental Pollutants in Field, 107–14. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-015-8973-4_10.

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Compagnone, D., M. Bugli, P. Imperiali, G. Varallo, and G. Palleschi. "Determination of Heavy Metals Using Electrochemical Biosensors Based on Enzyme Inhibition." In Biosensors for Direct Monitoring of Environmental Pollutants in Field, 220–26. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-015-8973-4_21.

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Brett, Christopher, and Ana Maria Oliveira-Brett. "DNA and Enzyme-Based Electrochemical Biosensors: Electrochemistry and AFM Surface Characterization." In Nanobioelectrochemistry, 105–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-29250-7_6.

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Csöoregi, Elisabeth, Szilveszter Gáspñr, Mihaela Niculescu, Bo Mattiasson, and Wolfgang Schuhmann. "Amperometric Enzyme-Based Biosensors for Application in Food and Beverage Industry." In Physics and Chemistry Basis of Biotechnology, 105–29. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/0-306-46891-3_4.

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Conference papers on the topic "Enzyme-based biosensor"

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Yi-Hua Zheng, Tse-Chao Hua, and Fei Xu. "A Thermal Biosensor Based on Enzyme Reaction." In 2005 IEEE Engineering in Medicine and Biology 27th Annual Conference. IEEE, 2005. http://dx.doi.org/10.1109/iembs.2005.1616824.

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Sun, Xia, and Xiangyou Wang. "Organophosphorous pesticides detection system based on amperometric enzyme biosensor." In 2010 2nd International Conference on Information Science and Engineering (ICISE). IEEE, 2010. http://dx.doi.org/10.1109/icise.2010.5690230.

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Kanakamedala, Senaka K., Haidar T. Alshakhouri, Mangilal Agarwal, Ji Fang, and Mark A. DeCoster. "A simple enzyme based biosensor on flexible plastic substrate." In SPIE NanoScience + Engineering, edited by Hooman Mohseni and Manijeh Razeghi. SPIE, 2010. http://dx.doi.org/10.1117/12.860587.

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Smiechowski, M. F., and A. R. Ward. "5.1.4 Impedance-Based Immobilized Enzyme Biosensor for Detection of Organophosphates." In 14th International Meeting on Chemical Sensors - IMCS 2012. AMA Service GmbH, Von-Münchhausen-Str. 49, 31515 Wunstorf, Germany, 2012. http://dx.doi.org/10.5162/imcs2012/5.1.4.

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Zahn, Jeffrey D., Ajay A. Deshmukh, Alexandros P. Papavasiliou, Albert P. Pisano, and Dorian Liepmann. "An Integrated Microfluidic Device for the Continuous Sampling and Analysis of Biological Fluids." In ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/mems-23912.

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Abstract Enzyme based biosensors suffer from loss of activity and sensitivity. One major reason is due to large molecular weight proteins adsorbing on the surface of the sensor. These proteins affect sensor signal stability and disrupt enzyme function. Thus, one fruitful way to minimize the loss of sensor activity is to filter out large molecular weight compounds before they come in contact with the enzyme based biosensor. Further, the removal of free protein from biological solution helps to increase sensor accuracy and lifetime. Therefore, a microdialysis microneedle is introduced that is capable of excluding large MW compounds based on size. These microneedles have been integrated into a planar microfluidic system capable of sampling and analyzing biological solutions. The integrated microfluidic system includes the assembly of microneedles with on-chip flow channels and electronics together with previously designed positive displacement micropumps, microvalves and a planar electro-chemical sensor for biological detection. Multichannel fluidic control for biological sampling, sensor cleansing and recalibration is demonstrated with integrated sensor operation.
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Wang, Zhuqing, Mitsuteru Kimura, Naoki Inomata, and Takahito Ono. "A freestanding microfluidic-based thermocouple biosensor for enzyme-catalyzed reaction analysis." In 2016 IEEE 11th Annual International Conference on Nano/Micro Engineered and Molecular Systems (NEMS). IEEE, 2016. http://dx.doi.org/10.1109/nems.2016.7758200.

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Huang, Yue, and Andrew J. Mason. "A redox-enzyme-based electrochemical biosensor with a CMOS integrated bipotentiostat." In 2009 IEEE Biomedical Circuits and Systems Conference (BioCAS). IEEE, 2009. http://dx.doi.org/10.1109/biocas.2009.5372093.

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Chunyan Li, Zhizhen Wu, J. A. Hartings, N. Rajan, N. Chahine, C. Cheyuo, Ping Wang, et al. "Brain-friendly amperometric enzyme biosensor based on encapsulated oxygen generating biomaterial." In 2012 34th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2012. http://dx.doi.org/10.1109/embc.2012.6347362.

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Ravariu, Cristian, and Vijay Arora. "Modeling of Enzyme-FET Biosensor Based on Experimental Glucose-Oxidase Receptor." In 2021 43rd Annual International Conference of the IEEE Engineering in Medicine & Biology Society (EMBC). IEEE, 2021. http://dx.doi.org/10.1109/embc46164.2021.9630120.

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Hsu, Che-Wei, Fang-Ci Su, Po-Yu Peng, Hong-Tsu Young, Mike Yang, and Gou-Jen Wang. "A Novel Non-Enzymatic Electrochemical Glucose Biosensor Based on a Simple Lithographic Process." In ASME 2015 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/detc2015-46954.

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Diabetes is a severe public health problem globally. There are about 387 million people worldwide suffer from this medical condition. Regular detection of a diabetes patient’s blood glucose is essential to maintain the blood sugar level. In this study, a novel non-enzyme glucose biosensor based on a simple lithographic process is proposed. Photoresist AZ-1518 is spinning-coated on a silicon wafer. Exposure and development using a mask with hexagonal close-packed circle array is than conducted to generate a hexagonal close-packed column array of the AZ-1518. The diameter of each circle is set as 4 μm. A thermal melting process is than employed to convert each photoresist column into a photoresist hemisphere. Finally, a gold thin film is then sputtered onto the hemisphere array of AZ-1518 to form the sensing electrode. The sensing area is measured to be enhanced by 8.8 folds. Actual glucose detections demonstrated that the proposed simple non-enzyme glucose biosensor can operate in a linear range of 2.8 mM–27.8 mM and a sensitivity of 18.7 μA mM−1cm−2. A detection limit of 9 μM (S/N = 3) was measured. The proposed novel glucose biosensor possesses advantages of enzyme free, simple fabrication process, low cost, and easy to long-term preservation. It is feasible for future clinical applications.
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Reports on the topic "Enzyme-based biosensor"

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Delwiche, Michael, Boaz Zion, Robert BonDurant, Judith Rishpon, Ephraim Maltz, and Miriam Rosenberg. Biosensors for On-Line Measurement of Reproductive Hormones and Milk Proteins to Improve Dairy Herd Management. United States Department of Agriculture, February 2001. http://dx.doi.org/10.32747/2001.7573998.bard.

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The original objectives of this research project were to: (1) develop immunoassays, photometric sensors, and electrochemical sensors for real-time measurement of progesterone and estradiol in milk, (2) develop biosensors for measurement of caseins in milk, and (3) integrate and adapt these sensor technologies to create an automated electronic sensing system for operation in dairy parlors during milking. The overall direction of research was not changed, although the work was expanded to include other milk components such as urea and lactose. A second generation biosensor for on-line measurement of bovine progesterone was designed and tested. Anti-progesterone antibody was coated on small disks of nitrocellulose membrane, which were inserted in the reaction chamber prior to testing, and a real-time assay was developed. The biosensor was designed using micropumps and valves under computer control, and assayed fluid volumes on the order of 1 ml. An automated sampler was designed to draw a test volume of milk from the long milk tube using a 4-way pinch valve. The system could execute a measurement cycle in about 10 min. Progesterone could be measured at concentrations low enough to distinguish luteal-phase from follicular-phase cows. The potential of the sensor to detect actual ovulatory events was compared with standard methods of estrus detection, including human observation and an activity monitor. The biosensor correctly identified all ovulatory events during its testperiod, but the variability at low progesterone concentrations triggered some false positives. Direct on-line measurement and intelligent interpretation of reproductive hormone profiles offers the potential for substantial improvement in reproductive management. A simple potentiometric method for measurement of milk protein was developed and tested. The method was based on the fact that proteins bind iodine. When proteins are added to a solution of the redox couple iodine/iodide (I-I2), the concentration of free iodine is changed and, as a consequence, the potential between two electrodes immersed in the solution is changed. The method worked well with analytical casein solutions and accurately measured concentrations of analytical caseins added to fresh milk. When tested with actual milk samples, the correlation between the sensor readings and the reference lab results (of both total proteins and casein content) was inferior to that of analytical casein. A number of different technologies were explored for the analysis of milk urea, and a manometric technique was selected for the final design. In the new sensor, urea in the sample was hydrolyzed to ammonium and carbonate by the enzyme urease, and subsequent shaking of the sample with citric acid in a sealed cell allowed urea to be estimated as a change in partial pressure of carbon dioxide. The pressure change in the cell was measured with a miniature piezoresistive pressure sensor, and effects of background dissolved gases and vapor pressures were corrected for by repeating the measurement of pressure developed in the sample without the addition of urease. Results were accurate in the physiological range of milk, the assay was faster than the typical milking period, and no toxic reagents were required. A sampling device was designed and built to passively draw milk from the long milk tube in the parlor. An electrochemical sensor for lactose was developed starting with a three-cascaded-enzyme sensor, evolving into two enzymes and CO2[Fe (CN)6] as a mediator, and then into a microflow injection system using poly-osmium modified screen-printed electrodes. The sensor was designed to serve multiple milking positions, using a manifold valve, a sampling valve, and two pumps. Disposable screen-printed electrodes with enzymatic membranes were used. The sensor was optimized for electrode coating components, flow rate, pH, and sample size, and the results correlated well (r2= 0.967) with known lactose concentrations.
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