Journal articles: '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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Edwards, Christopher, Surachet Duanghathaipornsuk, Mark Goltz, Sushil Kanel, and Dong-Shik Kim. "Peptide Nanotube Encapsulated Enzyme Biosensor for Vapor Phase Detection of Malathion, an Organophosphorus Compound." Sensors 19, no. 18 (September 6, 2019): 3856. http://dx.doi.org/10.3390/s19183856.

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This study explores the use of a butyrylcholinesterase (BChE)-based, reversible reaction biosensor using screen-printed electrodes (SPEs) having a smaller working surface area than the single-use electrodes previously studied. Previous research demonstrated the prospective application of a single-use biosensor fabricated with an acetylcholinesterase (AChE) enzyme encapsulated in peptide nanotubes (PNTs) and enhanced with horseradish peroxidase (HRP) to detect organophosphorus compounds (OPCs) in aqueous and gas phases. In the current study, potential improvements to the biosensor are investigated. BChE-based biosensors were fabricated using PNTs, HRP, and Nafion in combination to increase the reactive surface area, enhance sensitivity, and maintain enzyme stability. Cyclic voltammetry (CV) was used along with the new modified sensor to measure malathion concentration in the gas phase. The results show that a BChE-based biosensor could reliably measure gas phase malathion concentrations between 6–25 ppbv by CV with the extent of inhibition linearly proportional to the malathion concentration (R2 = 0.941). This research demonstrated that fabricated BChE-based biosensors could be stored without cold storage requirement for up to six weeks with minimal performance degradation. Moreover, the sensor electrodes were each reused several times, and were still useable at the conclusion of the research. This research demonstrates the potential of fabricating a reusable, inexpensive biosensor that is capable of OPC detection with high sensitivity and a low detection limit without a long-term cold storage requirement.

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Thompson, Richard B., and Eric R. Jones. "Enzyme-based fiber optic zinc biosensor." Analytical Chemistry 65, no. 6 (March 1993): 730–34. http://dx.doi.org/10.1021/ac00054a013.

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Papkovsky, Dmitry B., Janos Olah, and Ilya N. Kurochkin. "Fibre-optic lifetime-based enzyme biosensor." Sensors and Actuators B: Chemical 11, no. 1-3 (March 1993): 525–30. http://dx.doi.org/10.1016/0925-4005(93)85298-o.

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Yang, Zhengpeng, and Chunjing Zhang. "Single-enzyme nanoparticles based urea biosensor." Sensors and Actuators B: Chemical 188 (November 2013): 313–17. http://dx.doi.org/10.1016/j.snb.2013.07.004.

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Sikarwar, Bhavna, Pushpendra K. Sharma, Brajesh K. Tripathi, Mannan Boopathi, Beer Singh, and Yogesh K. Jaiswal. "Enzyme Based Electrochemical Biosensor for Ethanolamine." Electroanalysis 28, no. 4 (November 24, 2015): 881–89. http://dx.doi.org/10.1002/elan.201501046.

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Tomassetti, Mauro, Riccardo Pezzilli, Giuseppe Prestopino, Francesco Di Biagio, Corrado Di Natale, and Pier Gianni Medaglia. "A New Clark-Type Layered Double Hydroxides-Enzyme Biosensor for H2O2 Determination in Highly Diluted Real Matrices: Milk and Cosmetics." Processes 9, no. 11 (October 21, 2021): 1878. http://dx.doi.org/10.3390/pr9111878.

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A new catalase amperometric biosensor for hydroperoxides detection has been built as part of research aimed at the development of biosensors based on layered double hydroxides (LDH) used as support for enzyme immobilization. The fabricated device differs from those developed so far, usually based on an LDH enzyme nanocomposite adsorbed on a glassy carbon (GC) electrode and cross-linked by glutaraldehyde, since it is based on an amperometric gas diffusion electrode (Clark type) instead of a GC electrode. The new biosensor, which still uses LDH synthesized by us and catalase enzyme, is robust and compact, shows a lower LOD (limit of detection) value and a linearity range shifted at lower concentrations than direct amperometric GC biosensor, but above all, it is not affected by turbidity or emulsions, or by the presence of possible soluble species, which are reduced to the cathode at the same redox potential. This made it possible to carry out accurate and efficient determination of H2O2 even in complex or cloudy real matrices, also containing very low concentrations of hydrogen peroxide, such as milk and cosmetic products, i.e., matrices that would have been impossible to analyze otherwise, using conventional biosensors based on a GC–LDH enzyme. An inaccuracy ≤ 7.7% for cosmetic samples and ≤8.0% for milk samples and a precision between 0.7 and 1.5 (as RSD%), according to cosmetic or milk samples analyzed, were achieved.

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Fallatah, Ahmad, Nicolas Kuperus, Mohammed Almomtan, and Sonal Padalkar. "Sensitive Biosensor Based on Shape-Controlled ZnO Nanostructures Grown on Flexible Porous Substrate for Pesticide Detection." Sensors 22, no. 9 (May 5, 2022): 3522. http://dx.doi.org/10.3390/s22093522.

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Developing an inexpensive, sensitive, and point-of-use biosensor for pesticide detection is becoming an important area in sensing. Such sensors can be used in food packaging, agricultural fields, and environmental monitoring of pesticides. The present investigation has developed a zinc oxide (ZnO)-based biosensor on porous, flexible substrates such as carbon paper and carbon cloth to detect organophosphates such as paraoxon (OP). Here, the influence of morphology and underlying substrate on biosensor performance was studied. The biosensors were fabricated by immobilizing the acetylcholinesterase (AChE) enzyme on ZnO, which is directly grown on the flexible substrates. The ZnO biosensors fabricated on the carbon cloth demonstrated good performance with the detection limit of OP in the range of 0.5 nM–5 µM, higher sensitivity, and greater stability.

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Li, Yongjin. "Reed Membrane as a Novel Immobilization Matrix for the Development of an Optical Phenol Biosensor." Current Analytical Chemistry 16, no. 3 (May 15, 2020): 316–20. http://dx.doi.org/10.2174/1573411015666190617105551.

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Background: Biocompatible and easily available immobilization matrix is vital for the construction of enzyme-based biosensor. Methods: Reed membrane was selected as a novel immobilization matrix to construct an optical phenol biosensor. Tyrosinase from mushroom was immobilized in a reed membrane using glutaraldehyde as a cross-linker. The detection scheme was based on the measurement of the color intensity of the adduct resulting from the reaction of 3-methyl-2-benzothiazolinone hydrazone (MBTH) with the quinone produced from the oxidation of phenol by tyrosinase. The performance of such method including specificity, sensitivity, repeatability and practical use were validated. Results: The prepared biosensor demonstrated optimum performance at pH 6-7, temperature of 40°C and a linear response in the phenol concentration range of 5-100 μM. It also showed good operation stability for repeated measurements (over 200 times) and good storage stability after it had been kept at 4°C for 2 months. Conclusion: Reed membrane is a novel matrix for immobilization of enzyme. The prepared biosensor permits good sensitivity, reproducibility and stability. It is anticipated that reed membrane is a promising solid support for fabricating other enzyme-based biosensors.

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Bagal-Kestwal, Dipali R., and Been-Huang Chiang. "Exploration of Chitinous Scaffold-Based Interfaces for Glucose Sensing Assemblies." Polymers 11, no. 12 (November 28, 2019): 1958. http://dx.doi.org/10.3390/polym11121958.

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The nanomaterial-integrated chitinous polymers have promoted the technological advancements in personal health care apparatus, particularly for enzyme-based devices like the glucometer. Chitin and chitosan, being natural biopolymers, have attracted great attention in the field of biocatalysts engineering. Their remarkable tunable properties have been explored for enhancing enzyme performance and biosensor advancements. Currently, incorporation of nanomaterials in chitin and chitosan-based biosensors are also widely exploited for enzyme stability and interference-free detection. Therefore, in this review, we focus on various innovative multi-faceted strategies used for the fabrication of biological assemblies using chitinous biomaterial interface. We aim to summarize the current development on chitin/chitosan and their nano-architecture scaffolds for interdisciplinary biosensor research, especially for analytes like glucose. This review article will be useful for understanding the overall multifunctional aspects and progress of chitin and chitosan-based polysaccharides in the food, biomedical, pharmaceutical, environmental, and other diverse applications.

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Quintanilla-Villanueva, Gabriela Elizabeth, Donato Luna-Moreno, Edgar Allan Blanco-Gámez, José Manuel Rodríguez-Delgado, Juan Francisco Villarreal-Chiu, and Melissa Marlene Rodríguez-Delgado. "A Novel Enzyme-Based SPR Strategy for Detection of the Antimicrobial Agent Chlorophene." Biosensors 11, no. 2 (February 9, 2021): 43. http://dx.doi.org/10.3390/bios11020043.

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Chlorophene is an important antimicrobial agent present in disinfectant products which has been related to health and environmental effects, and its detection has been limited to chromatographic techniques. Thus, there is a lack of research that attempts to develop new analytical tools, such as biosensors, that address the detection of this emerging pollutant. Therefore, a new biosensor for the direct detection of chlorophene in real water is presented, based on surface plasmon resonance (SPR) and using a laccase enzyme as a recognition element. The biosensor chip was obtained by covalent immobilization of the laccase on a gold-coated surface through carbodiimide esters. The analytical parameters accomplished resulted in a limit of detection and quantification of 0.33 mg/L and 1.10 mg/L, respectively, fulfilling the concentrations that have already been detected in environmental samples. During the natural river’s measurements, no significant matrix effects were observed, obtaining a recovery percentage of 109.21% ± 7.08, which suggested that the method was suitable for the fast and straightforward analysis of this contaminant. Finally, the SPR measurements were validated with an HPLC method, which demonstrated no significant difference in terms of precision and accuracy, leading to the conclusion that the biosensor reflects its potential as an alternative analytical tool for the monitoring of chlorophene in aquatic environments.

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Singh, Nandini, Anurag Verma, Ishman Kaur, and Soham Chattopadhyay. "A Comprehensive Review on the Potential Use of Immobilized Lipase as Biosensor –Present Scenario and Prospects." Research Journal of Biotechnology 17, no. 4 (March 25, 2022): 145–50. http://dx.doi.org/10.25303/1704rjbt145150.

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Lipases that catalyze the hydrolysis of triglycerides play an outstanding role in developing biosensors used in various industries. With the latest developments and progress in biotechnology, nanobiotechnology and electronics, the demand for enzyme-based biosensors increases day by day. This review introduces different techniques and methods adopted to develop biosensors from lipase and discusses their properties and characteristics to demonstrate present scope, opportunities and challenges in biosensor technology. A focus of industries has shifted towards eco-friendly, high yield products with high profitability index. The use of enzymes seems to be the golden choice. With this review, we focus on the usage of an immobilized enzyme (lipase) in biosensors. We discuss various deficits in the immobilization and assay techniques, in brief, to bring about attention to the need for advancements in them to increase the overall accuracy of the biosensor in the present scenario.

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Stasyuk, Nataliya Ye, Oleh V. Smutok, Andriy E. Zakalskiy, Oksana M. Zakalska, and Mykhailo V. Gonchar. "Methylamine-Sensitive Amperometric Biosensor Based on (His)6-TaggedHansenula polymorphaMethylamine Oxidase Immobilized on the Gold Nanoparticles." BioMed Research International 2014 (2014): 1–8. http://dx.doi.org/10.1155/2014/480498.

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A novel methylamine-selective amperometric bienzyme biosensor based on recombinant primary amine oxidase isolated from the recombinant yeast strainSaccharomyces cerevisiaeand commercial horseradish peroxidase is described. Two amine oxidase preparations were used: free enzyme (AMO) and covalently immobilized on the surface of gold nanoparticles (AMO-nAu). Some bioanalytical parameters (sensitivity, selectivity, and storage stability) of the developed biosensors were investigated. The sensitivity for both sensors is high:1450 ± 113and700 ± 30 A−1·M−1·m−2for AMO-nAu biosensor, respectively. The biosensors exhibit the linear range from 15 μM to 150 μM (AMO-nAu) and from 15 μM to 60 μM (AMO). The developed biosensor demonstrated a good selectivity toward methylamine (MA) (signal for dimethylamine and trimethylamine is less than 5% and for ethylamine 15% compared to MA output) and reveals a satisfactory storage stability. The constructed amperometric biosensor was used for MA assay in real samples of fish products in comparison with chemical method. The values obtained with both approaches different methods demonstrated a high correlation.

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Yan, Caiyun, Kaifeng Jin, Xiangyi Luo, Jinhua Piao, and Fang Wang. "Electrochemical Biosensor Based on Chitosan- and Thioctic-Acid-Modified Nanoporous Gold Co-Immobilization Enzyme for Glycerol Determination." Chemosensors 10, no. 7 (July 2, 2022): 258. http://dx.doi.org/10.3390/chemosensors10070258.

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An electrochemical biosensor based on chitosan- and thioctic-acid-modified nanoporous gold (NPG) co-immobilization glycerol kinase (GK) and glycerol-3-phosphate oxidase (GPO) was constructed for glycerol determination in wine. The NPG, with the properties of porous microstructure, large specific surface area, and high conductivity, was beneficial for protecting the enzyme from inactivation and denaturation and enhancing electron transfer in the modified electrode. The co-immobilization of the enzyme by chitosan-embedding and thioctic-acid-modified NPG covalent bonding was beneficial for improving the catalytic performance and stability of the enzyme-modified electrode. Ferrocene methanol (Fm) was used as a redox mediator to accelerate the electron transfer rate of the enzyme-modified electrode. The fabricated biosensor exhibited a wide determination range of 0.1–5 mM, low determination limit of 77.08 μM, and high sensitivity of 9.17 μA mM−1. Furthermore, it possessed good selectivity, repeatability, and stability, and could be used for the determination of glycerol in real wine samples. This work provides a simple and novel method for the construction of biosensors, which may be helpful to the application of enzymatic biosensors in different determination scenarios.

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Valencia, Germán Ayala, Luci Cristina de Oliveira Vercik, and Andrés Vercik. "A new conductometric biosensor based on horseradish peroxidase immobilized on chitosan and chitosan/gold nanoparticle films." Journal of Polymer Engineering 34, no. 7 (September 1, 2014): 633–38. http://dx.doi.org/10.1515/polyeng-2014-0072.

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Abstract A new conductometric biosensor was developed and characterized; the biosensor was based on horseradish peroxidase that was deposited in chitosan and chitosan/AuNPs films. The biosensors were characterized by scanning electron microscopy and current-voltage curves. Current-voltage curves in biosensors showed that the electrical conductivity and bistability in biosensors can be modulated by horseradish peroxidase. Horseradish peroxidase catalyzed the reduction of H2 O2 to H2 O with the oxidation of the prosthetic group (Fe3+) in the enzyme to Fe4+=O. Conductometric signal in the biosensors increased with the gradual increase of H2 O2 concentration, and it was due to the H2 O2 reduction. Linear hydrogen peroxide detection was observed for a concentration between 0 and 15 mm. The results proved that these biosensors could have promising industrial applications, due to its rapid and sensitive H2 O2 detection.

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Mashuni, Mashuni, Halimahtussaddiyah Ritonga, M. Jahiding, Bonni Rubak, and Fitri Handayani Hamid. "Highly Sensitive Detection of Carbaryl Pesticides Using Potentiometric Biosensor with Nanocomposite Ag/r-Graphene Oxide/Chitosan Immobilized Acetylcholinesterase Enzyme." Chemosensors 10, no. 4 (April 7, 2022): 138. http://dx.doi.org/10.3390/chemosensors10040138.

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Novel, sensitive, selective, efficient and portable electrochemical biosensors are needed to detect residual contaminants of the pesticide 1-naphthyl methylcarbamate (carbaryl) in the environment, food, and essential biological fluids. In this work, a study of nanocomposite-based Ag reduced graphene oxide (rGO) and chitosan (CS) that optimise surface conditions for immobilisation of acetylcholinesterase (AChE) enzyme to improve the performance of catalytic biosensors is examined. The Ag/rGO/CS nanocomposite membrane was used to determine carbaryl pesticide using a potentiometer transducer. The AChE enzyme-based biosensor exhibits a good affinity for acetylthiocholine chloride (ATCl). It can catalyse the hydrolysis of ATCl with a potential value of 197.06 mV, which is then oxidised to produce a detectable and rapid response. Under optimal conditions, the biosensor detected carbaryl pesticide at concentrations in the linear range of 1.0 × 10−8 to 1.0 μg mL−1 with a limit of detection (LoD) of 1.0 × 10−9 μg mL−1. The developed biosensor exhibits a wide working concentration range, detection at low concentrations, high sensitivity, acceptable stability, reproducibility and simple fabrication, thus providing a promising tool for pesticide residue analysis.

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Ahlawat, Jyoti, Vishakha Aggarwal, Ranjana Jaiwal, and C. S. Pundir. "An Improved Amperometric Lactose Biosensor Based on Enzyme Nanoparticles." International Journal of Applied Sciences and Biotechnology 10, no. 1 (March 29, 2022): 21–30. http://dx.doi.org/10.3126/ijasbt.v10i1.44155.

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A desolvation method was used for the synthesis of β-galactosidase (β-GAL) and glucose oxidase (GOD) nanoparticles (NPs) using ethanol. The enzyme nanoparticles (ENPs) were characterized by transmission electron microscopy (TEM) and Fourier transform Infra-red spectroscopy (FTIR) and were co-immobilized covalently onto surface of polycrystalline Au electrode. An improved amperometric lactose biosensor was constructed using ENPs (β-GALNPs/GODNPs) modified Au electrode as working electrode, Ag/AgCl as reference electrode and Pt wire as auxiliary electrode connected through potentiostat. Cyclic voltammetry (CV) and scanning electron microscope (SEM) were used for the study of working electrode before and after immobilization of ENPs. The biosensor showed maximum current at 0.25V within 5s, at pH 6.5 and 25oC. The limit of detection (LOD) was i.e. 1mg/ml and working range was 1-10 mg/mL. The analytical recovery of added lactose (5 and 10 mg/mL) was 94.73±0.5% and 96.4±0.9%, respectively. Coefficient of variation (CV) within and between batch were <3.0 and <4.0 respectively. The biosensor exhibited a good correlation (R2=0.91) between lactose level in milk as measured by standard (enzymatic colorimetric) method and present biosensor. The biosensor was employed for quantification of lactose in milk from human, cow, buffalo and goat. The working electrode lost 50% of its initial activity within 3 months, after its 120 uses, while being stored dry at 4ºC. Int. J. Appl. Sci. Biotechnol. Vol 10(1): 21-30.

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Vokhmyanina, Darya V., Ksenia D. Andreeva, Maria A. Komkova, Elena E. Karyakina, and Arkady A. Karyakin. "‘Artificial peroxidase’ nanozyme – enzyme based lactate biosensor." Talanta 208 (February 2020): 120393. http://dx.doi.org/10.1016/j.talanta.2019.120393.

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Thompson, Richard B., and Eric R. Jones. "Correction. Enzyme-Based Fiber Optic Zinc Biosensor." Analytical Chemistry 65, no. 17 (September 1993): 2407. http://dx.doi.org/10.1021/ac00065a602.

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Gerard, Manju, and B. D. Malhotra. "Application of polyaniline as enzyme based biosensor." Current Applied Physics 5, no. 2 (February 2005): 174–77. http://dx.doi.org/10.1016/j.cap.2004.06.016.

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Bóka, Beáta, Nóra Adányi, Diána Virág, Ivo Frebort, and Attila Kiss. "Enzyme Based Amperometric Biosensor for Adenine Determination." Electroanalysis 25, no. 1 (November 13, 2012): 237–42. http://dx.doi.org/10.1002/elan.201200387.

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Zusfahair, Zusfahair, Dian Riana Ningsih, Elok Dwi Putri Lestari, and Amin Fatoni. "Development of Urea Biosensor Based on Immobilized Urease in Chitosan Cryogel." Molekul 14, no. 1 (June 4, 2019): 64. http://dx.doi.org/10.20884/1.jm.2019.14.1.523.

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The development of biosensors using biological components has an important role in detecting the disease early because it has good selectivity and accuracy. In this study, a biosensor which made is a urea biosensor, based on immobilization urease in chitosan using adsorption techniques, to measure urea levels by colorimetric analysis with bromothymol blue (BTB) as an indicator. The purpose of this study was to find out how to measure urea levels using biosensors based on urease immobilization in chitosan and find out the biosensor performance including optimum enzymatic reaction time, linearity, the limit of detection, repetition, and determination of disrupting compounds. The study began with the making of an immobilization supporting matrix using chitosan which was made in the form of cryogel through an ionic gelation process which adsorbs the urease enzyme. Cryogel urease catalyzes the hydrolysis of urea into NH4+ and CO2-. The reaction product was added with the BTB indicator, and the color change formed was measured using a spectrophotometer. The results showed that the performance of urea biosensors was good enough for urea level detection systems by producing enzymatic reaction times at 15 minutes, linearity at 0.9951, detection limit at 0.018 mM, not affected by the addition of 0.05 mM ascorbic acid and 0.4 mM uric acid. This urea biosensor can be used up to 5 repetitions.

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CHEN, L. Y., B. X. GU, G. P. ZHU, Y. F. WU, S. Q. LIU, and C. X. XU. "TYROSINASE BIOSENSOR BASED ON ZINC OXIDE NANORODS." Nano 02, no. 05 (October 2007): 281–84. http://dx.doi.org/10.1142/s1793292007000647.

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A phenol biosensor based on the skillful immobilization of tyrosinase on zinc oxide ( ZnO ) nanorods was proposed. The ZnO nanorods fabricated by a simple vapor-phase transport method possess a high aspect ratio, good electron communication, chemical purity, smooth and positive charged surface and are ready for immobilization of biochemicals with low isoelectric point (IEP). Electrochemical measurement and Scanning Electron Microscopic (SEM) analysis showed that the enzyme of tyrosinase with IEP 4.5 can be adsorbed on the surface of ZnO nanorods and kept its bioactivity of the oxidation of phenol to a large extent. This led us to develop phenol biosensor with good stability and reproducibility. The proposed method creates a new way to develop biosensors using nanostructured materials with high IEP.

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Umar, Ahmad, Mazharul Haque, Shafeeque G. Ansari, Hyung-Kee Seo, Ahmed A. Ibrahim, Mohsen A. M. Alhamami, Hassan Algadi, and Zubaida A. Ansari. "Label-Free Myoglobin Biosensor Based on Pure and Copper-Doped Titanium Dioxide Nanomaterials." Biosensors 12, no. 12 (December 8, 2022): 1151. http://dx.doi.org/10.3390/bios12121151.

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In this study, using pure and copper-doped titanium dioxide (Cu-TiO2) nanostructures as the base matrix, enzyme-less label free myoglobin detection to identify acute myocardial infarction was performed and presented. The Cu-TiO2 nanomaterials were prepared using facile sol–gel method. In order to comprehend the morphologies, compositions, structural, optical, and electrochemical characteristics, the pure and Cu-TiO2 nanomaterials were investigated by several techniques which clearly revealed good crystallinity and high purity. To fabricate the enzyme-less label free biosensor, thick films of synthesized nanomaterials were applied to the surface of a pre-fabricated gold screen-printed electrode (Au-SPE), which serves as a working electrode to construct the myoglobin (Mb) biosensors. The interference study of the fabricated biosensor was also carried out with human serum albumin (HSA) and cytochrome c (cyt-c). Interestingly, the Cu-doped TiO2 nanomaterial-based Mb biosensor displayed a higher sensitivity of 61.51 µAcm−2/nM and a lower detection limit of 14 pM with a response time of less than 10 ms.

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Lee, Seo-Eun, Se-Eun Jeong, Jae-Sang Hong, Hyungsoon Im, Sei-Young Hwang, Jun Kyun Oh, and Seong-Eun Kim. "Gold-Nanoparticle-Coated Magnetic Beads for ALP-Enzyme-Based Electrochemical Immunosensing in Human Plasma." Materials 15, no. 19 (October 3, 2022): 6875. http://dx.doi.org/10.3390/ma15196875.

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A simple and sensitive AuNP-coated magnetic beads (AMB)-based electrochemical biosensor platform was fabricated for bioassay. In this study, AuNP-conjugated magnetic particles were successfully prepared using biotin–streptavidin conjugation. The morphology and structure of the nanocomplex were characterized by scanning electron microscopy (SEM) with energy-dispersive X-ray analysis (EDX) and UV–visible spectroscopy. Moreover, cyclic voltammetry (CV) was used to investigate the effect of AuNP-MB on alkaline phosphatase (ALP) for electrochemical signal enhancement. An ALP-based electrochemical (EC) immunoassay was performed on the developed AuNP-MB complex with indium tin oxide (ITO) electrodes. Subsequently, the concentration of capture antibodies was well-optimized on the AMB complex via biotin–avidin conjugation. Lastly, the developed AuNP-MB immunoassay platform was verified with extracellular vesicle (EV) detection via immune response by showing the existence of EGFR proteins on glioblastoma multiforme (GBM)-derived EVs (108 particle/mL) spiked in human plasma. Therefore, the signal-enhanced ALP-based EC biosensor on AuNP-MB was favorably utilized as an immunoassay platform, revealing the potential application of biosensors in immunoassays in biological environments.

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Soldatkin, O. O., O. V. Soldatkina, V. M. Arkhypova, I. I. Piliponskiy, L. S. Rieznichenko, T. G. Gruzina, S. M. Dybkova, S. V. Dzyadevych, and A. P. Soldatkin. "APLLICATION OF GOLD NANOPARTICLES FOR IMPROVEMENT OF ANALYTICAL CHARACTERISTICS OF CONDUCTOMETRIC ENZYME BIOSENSORS." Sensor Electronics and Microsystem Technologies 18, no. 1 (March 31, 2021): 20–34. http://dx.doi.org/10.18524/1815-7459.2021.1.227408.

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In this work, the possibility of application of gold nanoparticles for modification of bioselective elements of conductometric biosensors to improve their analytical characteristics has been tested. A bioselective elements of biosensors based on acetylcholinesterase, butyrylcholinesterase and glucose oxidase have been studied as a model of such system. Immobilization of enzymes on the surface of conductometric transducers was carried out by covalent crosslinking of enzymes by using a crosslinking agent (glutaraldehyde). The conditions for immobilization of acetylcholinesterase with gold nanoparticles in BSA membranes were optimized. The optimal concentration of glutaraldehyde, time of immobilization process, ratio of an amount of enzyme and gold nanoparticles, and the concentration and size of gold nanoparticles were selected. The improved characteristics of the developed biosensors based on enzymes and gold nanoparticles were investigated and compared with the characteristics of biosensors based only on enzymes without nanoparticles addition. It was shown, how the addition of gold nanoparticles to the bioselective element of the biosensor affects the stability of biosensors. In particular, the reproducibility of signals during continuous operation of biosensors, the reproducibility of the manufacture of biosensors and their stability during storage were investigated. Thus, it was shown, that the application of gold nanoparticles in the composition of bioselective elements can improve some characteristics of biosensors, which may be promising for further biosensor application

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Pratama, Ahmad Irvan, Aisyah Sahara, and Sintia Intan Agsari. "Analysis of Blood Hemoglobin Levels Using Biosensors Based on Heme Oxygenase from Serratia marcescens." Current Biochemistry 7, no. 1 (June 1, 2020): 37–46. http://dx.doi.org/10.29244/cb.7.1.5.

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Hemoglobin levels are influenced by nutrition, iron conditions, and body metabolism. One of the medical disorders related to human blood, especially erythrocyte levels is anemia. This condition causes the need for effective and efficient methods of measuring blood hemoglobin levels, including in terms of cost. One alternative measurement of hemoglobin levels that can be used is the heme oxygenase-based sensor from Serratia marcescens. This study aims to develop techniques to measure blood hemoglobin levels by utilizing biological sensor based on heme oxygenase fromSerratia marcescens. The stages of the experiments include: rejuvenation and production of Serratia marcescens isolates, isolation of heme oxygenase, purification of enzymes with ammonium sulphate 45-65% and 65-85% saturation, measurement of protein content and enzyme activity, enzyme immobilization to the surface of carbon electrodes, and assay of biosensor heme oxygenase kinetics. Test of protein content and enzyme activity produces enzyme specific activity at 45-65% fraction of 0.0158 U/mg and at 65-85% fraction of 0.0069 U/mg, so the fraction to be used in biosensors is 45-65% fraction. The biosensor kinetics test results in a hemoglobin level of 12.0, 13.8, and 14.3 g/dL in blood samples A, B, and, C, while the hemoglobin level measured in a standard laboratory test is 12.0, 13.8, and 14.3 g/dL. It was concluded that the biosensors developed in this study can measure hemoglobin levels in blood samples with a precision of 0.8 and an accuracy of 96.04%.

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Insawang, Mekhala, Kongphope Chaarmart, and Tosawat Seetawan. "Development of Biosensors for Ethanol Gas Detection." Instrumentation Mesure Métrologie 21, no. 2 (April 30, 2022): 49–57. http://dx.doi.org/10.18280/i2m.210203.

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This work developed a biosensor for the measurement of ethanol gas in the air. The biosensors were synthesized by mixing signal layer materials containing SiO2 and polyimide (PI) substrates using the enzyme Alcohol Dehydrogenase (ADH) and coenzyme Nicotinamide Adenine Dinucleotide (NAD+) as a biosensor. The electrodes were coated on biosensors by DC magnetron sputtering method for test the response performance of the developed biosensors. The ADH/NAD+ was immobilized on the Ag electrode by Glutaric dialaehyde 25 wt. % cross-linking procedure. It was found that, alcohol biosensors can be exhibited sensing ethanol gas at even low concentrations from 300 ppb to very high concentrations up to 1900 ppm, response time 3 s, recovery times 1-2 minutes and good sensitivity. The SiO2 substrate has excellent, which provides significant advantages for wearable electronic device that compact, easy to use and reduce direct contact with alcoholics. The alcohol biosensors can adoption in next generation to other electronic devices, because easy to integrate, such as a module alcohol biosensor with wireless or the fabrication of the RCL circuit. Furthermore, the alcohol biosensors based on SiO2/Ag/ADH, PI/Ag/ADH is artificial intelligence strategy for stable practical wearable electronic devices.

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Fois, Marco, Paola Arrigo, Andrea Bacciu, Patrizia Monti, Salvatore Marceddu, Gaia Rocchitta, and Pier Andrea Serra. "The Presence of Polysaccharides, Glycerol, and Polyethyleneimine in Hydrogel Enhances the Performance of the Glucose Biosensor." Biosensors 9, no. 3 (July 30, 2019): 95. http://dx.doi.org/10.3390/bios9030095.

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The use of amperometric biosensors has attracted particular attention in recent years, both from researchers and from companies, as they have proven to be low-cost, reliable, and very sensitive devices, with a wide range of uses in different matrices. The continuous development of amperometric biosensors, since their use involves an enzyme, is specifically aimed at keeping and increasing the catalytic properties of the loaded protein, so as to be able to use the same device over time. The present study aimed to investigate the impact of glycerol and polysaccharides, in the presence of polycationic substances to constitute a hydrogel, in enhancing the enzymatic and analytic performance of a glucose biosensor. Initially, it was possible to verify how the deposition of the starch-based hydrogel, in addition to allowing the electropolymerization of the poly(p-phenylenediamine) polymer and the maintenance of its ability to shield the ascorbic acid, did not substantially limit the permeability towards hydrogen peroxide. Moreover, different biosensor designs, loading a mixture containing all the components (alone or in combination) and the enzyme, were tested in order to evaluate the changes of the apparent enzyme kinetic parameters, such as VMAX and KM, and analytical response in terms of Linear Region Slope, highlighting how the presence of all components (starch, glycerol, and polyethyleneimine) were able to substantially enhance the performance of the biosensors. The surface analysis of the biosensors was performed by scanning electron microscope (SEM). More, it was shown that the same performances were kept unchanged for seven days, proving the suitability of this biosensor design for short- and mid-term use.

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Smith, Dustin D., Joshua P. King, D. Wade Abbott, and Hans-Joachim Wieden. "Development of a Real-Time Pectic Oligosaccharide-Detecting Biosensor Using the Rapid and Flexible Computational Identification of Non-Disruptive Conjugation Sites (CINC) Biosensor Design Platform." Sensors 22, no. 3 (January 26, 2022): 948. http://dx.doi.org/10.3390/s22030948.

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Fluorescently labeled, solute-binding proteins that change their fluorescent output in response to ligand binding are frequently used as biosensors for a wide range of applications. We have previously developed a “Computational Identification of Non-disruptive Conjugation sites” (CINC) approach, an in silico pipeline utilizing molecular dynamics simulations for the rapid design and construction of novel protein–fluorophore conjugate-type biosensors. Here, we report an improved in silico scoring algorithm for use in CINC and its use in the construction of an oligogalacturonide-detecting biosensor set. Using both 4,5-unsaturated and saturated oligogalacturonides, we demonstrate that signal transmission from the ligand-binding pocket of the starting protein scaffold to the CINC-selected reporter positions is effective for multiple different ligands. The utility of an oligogalacturonide-detecting biosensor is shown in Carbohydrate Active Enzyme (CAZyme) activity assays, where the biosensor is used to follow product release upon polygalacturonic acid (PGA) depolymerization in real time. The oligogalacturonide-detecting biosensor set represents a novel enabling tool integral to our rapidly expanding platform for biosensor-based carbohydrate detection, and moving forward, the CINC pipeline will continue to enable the rational design of biomolecular tools to detect additional chemically distinct oligosaccharides and other solutes.

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Kratasyuk, Valentina A., Elizaveta M. Kolosova, Oleg S. Sutormin, Viktoriya I. Lonshakova-Mukina, Matvey M. Baygin, Nadezhda V. Rimatskaya, Irina E. Sukovataya, and Alexander A. Shpedt. "Software for Matching Standard Activity Enzyme Biosensors for Soil Pollution Analysis." Sensors 21, no. 3 (February 2, 2021): 1017. http://dx.doi.org/10.3390/s21031017.

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This work is dedicated to developing enzyme biosensor software to solve problems regarding soil pollution analysis. An algorithm and specialised software have been developed which stores, analyses and visualises data using JavaScript programming language. The developed software is based on matching data of 51 non-commercial standard soil samples and their inhibitory effects on three enzyme systems of varying complexity. This approach is able to identify the influence of chemical properties soil samples, without toxic agents, on enzyme biosensors. Such software may find wide use in environmental monitoring.

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Guan, Hua Nan, De Fu Chi, and Jia Yu. "Photoelectrochemical Acetylcholinesterase Biosensor Incorporating Zinc Oxide Nanoparticles." Advanced Materials Research 183-185 (January 2011): 1701–6. http://dx.doi.org/10.4028/www.scientific.net/amr.183-185.1701.

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A novel photoelectrochemical biosensor incorporating nanosized ZnO semiconductor crystals with enzyme to enhance photochemical reaction has been investigated. In this work, the ZnO nanoparticles and acetylcholinesterase (AChE) were immobilized on Pt electrode by chitosan (CHI) via layer-by-layer technique (LbL) to fabricate a biological-inorganic hybrid system. Micrographs of (ZnO/CHI/AChE) films were obtained by scanning electron microscope, and photoelectrochemical properties of the resulting biosensors were measured by a three electrodes system and an ultraviolet lamp. Under ultraviolet light, the photo-effect of the ZnO nanoparticles showed enhancement of the biosensor to detect pesticide. Based on the inhibition of organophosphate pesticides on the AChE activity, using malathion as a model compound, the inhibition of dimethoate was proportional to its concentration ranging from 0.25 to 1.50 and from 1.75 to 10.00 μM, with a detection limit of 10 nM estimated at a signal-to-noise ratio of 3. The developed biosensor exhibited good reproducibility and acceptable stability, thus providing a new promising tool for analysis of enzyme inhibitors.

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Rajarathinam, Thenmozhi, Dinakaran Thirumalai, Sivaguru Jayaraman, Seonghye Kim, Minho Kwon, Hyun-jong Paik, Suhkmann Kim, Mijeong Kang, and Seung-Cheol Chang. "Enzyme Nanosheet-Based Electrochemical Aspartate Biosensor for Fish Point-of-Care Applications." Micromachines 13, no. 9 (August 29, 2022): 1428. http://dx.doi.org/10.3390/mi13091428.

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Bacterial infections in marine fishes are linked to mass mortality issues; hence, rapid detection of an infection can contribute to achieving a faster diagnosis using point-of-care testing. There has been substantial interest in identifying diagnostic biomarkers that can be detected in major organs to predict bacterial infections. Aspartate was identified as an important biomarker for bacterial infection diagnosis in olive flounder (Paralichthys olivaceus) fish. To determine aspartate levels, an amperometric biosensor was designed based on bi-enzymes, namely, glutamate oxidase (GluOx) and aspartate transaminase (AST), which were physisorbed on copolymer reduced graphene oxide (P-rGO), referred to as enzyme nanosheets (GluOx-ASTENs). The GluOx-ASTENs were drop casted onto a Prussian blue electrodeposited screen-printed carbon electrode (PB/SPCE). The proposed biosensor was optimized by operating variables including the enzyme loading amount, coreactant (α-ketoglutarate) concentration, and pH. Under optimal conditions, the biosensor displayed the maximum current responses within 10 s at the low applied potential of −0.10 V vs. the internal Ag/AgCl reference. The biosensor exhibited a linear response from 1.0 to 2.0 mM of aspartate concentrations with a sensitivity of 0.8 µA mM−1 cm−2 and a lower detection limit of approximately 500 µM. Moreover, the biosensor possessed high reproducibility, good selectivity, and efficient storage stability.

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Kaur, Rasleen, and S. Keshavkant. "Enzyme Based Biosensor for Onsite Detection of Chromium." NewBioWorld 3, no. 2 (December 31, 2021): 1–7. http://dx.doi.org/10.52228/nbw-jaab.2021-3-2-1.

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Environment has own permissible limit of heavy metals (HMs) in its every component (soil, water and air). Excess use of HMs overcomes this limit hence, leading to toxicity affecting the life on Earth. Due to the oxidizing property of the chromium (Cr), one of the HMs, it is widely used for a number of purposes such as manufacturing of stainless steel, in tannery industry, as cleaning agent for glassware, etc. Chromium has two main stable oxidation states; hexavalent (VI) and trivalent (III), out of which earlier is comparatively more toxic than the later form. Solubility of Cr (VI) in ground water had led to the need of designing a sensitive device which can be quite efficient in monitoring of its presence in the environment. In this review, an attempt has been made to collate information, so far available, on the use of microbial system for intake and detoxification of Cr following use of chromate reductase (CR) enzyme.

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Trivedi, U. B., D. Lakshminarayana, I. L. Kothari, P. B. Patel, and C. J. Panchal. "Amperometric fructose biosensor based on fructose dehydrogenase enzyme." Sensors and Actuators B: Chemical 136, no. 1 (February 2009): 45–51. http://dx.doi.org/10.1016/j.snb.2008.10.020.

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Ren, Xiangling, Liuqing Yang, Fangqiong Tang, Chuanmiao Yan, and Jun Ren. "Enzyme biosensor based on NAD-sensitive quantum dots." Biosensors and Bioelectronics 26, no. 1 (September 15, 2010): 271–74. http://dx.doi.org/10.1016/j.bios.2010.05.014.

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Sadeghi, Susan, Ebrahim Fooladi, and Mohammad Malekaneh. "A nanocomposite/crude extract enzyme-based xanthine biosensor." Analytical Biochemistry 464 (November 2014): 51–59. http://dx.doi.org/10.1016/j.ab.2014.07.013.

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Ilangovan, R., D. Daniel, A. Krastanov, C. Zachariah, and R. Elizabeth. "Enzyme based Biosensor for Heavy Metal Ions Determination." Biotechnology & Biotechnological Equipment 20, no. 1 (January 2006): 184–89. http://dx.doi.org/10.1080/13102818.2006.10817330.

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Kondoh, Jun, Teruo Imayama, Yoshikazu Matsui, and Showko Shiokawa. "Enzyme biosensor based on surface acoustic wave device." Electronics and Communications in Japan (Part II: Electronics) 79, no. 7 (1996): 69–75. http://dx.doi.org/10.1002/ecjb.4420790708.

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Zhang, Maogen, Conor Mullens, and Waldemar Gorski. "Amperometric glutamate biosensor based on chitosan enzyme film." Electrochimica Acta 51, no. 21 (June 2006): 4528–32. http://dx.doi.org/10.1016/j.electacta.2006.01.010.

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Lei, Yongjiu, Ruize Sun, Xiangcheng Zhang, Xinjian Feng, and Lei Jiang. "Oxygen-Rich Enzyme Biosensor Based on Superhydrophobic Electrode." Advanced Materials 28, no. 7 (December 12, 2015): 1477–81. http://dx.doi.org/10.1002/adma.201503520.

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Journal articles on the topic 'Enzyme-based biosensor'

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