Improved operational stability of mediated glucose enzyme electrodes for operation in human physiological solutions

Bennett, Richard; Leech, Dónal

doi:10.1016/j.bioelechem.2020.107460

Cited by 24 publications

(13 citation statements)

References 54 publications

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“…The peak current varies linearly with the square root of scan rate at higher scan rates when semi‐infinite diffusion within the film limits the current response [34] . The surface coverage (Γ os ) of the redox polymer, estimated by integrating the area under the peak for CVs recorded at slow scan rate in the absence of glucose, is 144±3 nmol cm −2 , which confirms multi‐layer formation, similar to results obtained by others for the co‐immobilization of enzymes and osmium‐based redox polymers [35–38] . On addition of glucose to the electrochemical cell, sigmoidal shaped responses characteristic of an electrocatalytic (EC’) process are observed.…”

Section: Resultssupporting

confidence: 85%

An Oxygen Insensitive Amperometric Glucose Biosensor Based on An Engineered Cellobiose Dehydrogenase: Direct versus Mediated Electron Transfer Responses

et al. 2022

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Cellobiose dehydrogenase (CDH) is capable of oxidizing cellobiose and related carbohydrates and generating electrical current at carbon-based electrodes through direct electron transfer (DET) or mediated electron transfer (MET) mechanisms. As a result, CDHs have been utilized as biocatalysts in biosensors and biofuel cell anodes. A novel engineered ascomycetous Class II CDH with enhanced glucose activity was tested as a bioelectrocatalyst for application to DET or METbased glucose biosensors with the electrode component amount selection optimized for maximum current in 5 mM glucose solutions. The optimised DET biosensor showed a similar sensitivity and 3-fold lower K M,app when compared to non-optimised DET sensor based on the same engineered CDH. The optimized MET biosensor had a similar K M,app to nonoptimized MET biosensor. However, it showed 15-fold improvement in j max and 17-fold improvement in sensitivity over the DET biosensor. The sensor signals are not affected by the presence of oxygen, although operation in artificial serum results in 43 % and 28 % lower sensitivity for the DET and MET sensors, respectively. While no individually tested potential interferent breaches a mean absolute relative difference of 20 % of the current, the cumulative co-operative effect in complex media, such as artificial serum, decreases the glucose oxidation current signal.

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Section: Resultssupporting

confidence: 85%

An Oxygen Insensitive Amperometric Glucose Biosensor Based on An Engineered Cellobiose Dehydrogenase: Direct versus Mediated Electron Transfer Responses

et al. 2022

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“…The current generation curve was fitted to a simple exponential decay to obtain the half-life ( t 1/2 ) of the cell of 24 h ( R 2 = 0.99). GOx wired with osmium polymers to graphite electrodes has previously showed a 20% reduction in its activity after 12 h in phosphate-buffered saline (PBS) . BOD may also desorb over time from the surface of the biocathode due to the physisorption-based immobilization of the enzyme, as previously reported. , Likewise, the formation of hydrogen peroxide during the oxidation of glucose at the bioanode may further compromise the stability of the EFC and affect the catalytic activity of the biocathode over time …”

Section: Resultsmentioning

confidence: 80%

Self-Powered Detection of Glucose by Enzymatic Glucose/Oxygen Fuel Cells on Printed Circuit Boards

Gonzalez-Solino

Bernalte

Royo

et al. 2021

ACS Appl. Mater. Interfaces

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Monitoring glucose levels in physiological fluids can help prevent severe complications associated with hypo- and hyper-glycemic events. Current glucose-monitoring systems require a three-electrode setup and a power source to function, which can hamper the system miniaturization to the patient discomfort. Enzymatic fuel cells (EFCs) offer the opportunity to develop self-powered and minimally invasive glucose sensors by eliminating the need for an external power source. Nevertheless, practical applications demand for cost-effective and mass-manufacturable EFCs compatible with integration strategies. In this study, we explore for the first time the use of gold electrodes on a printed circuit board (PCB) for the development of an EFC and demonstrate its application in saliva. To increase the specific surface area, the PCB gold-plated electrodes were modified with porous gold films. At the anode, glucose oxidase is immobilized with an osmium redox polymer that serves as an electron-transfer mediator. At the cathode, bilirubin oxidase is adsorbed onto the porous gold surface with a blocking agent that prevents parasitic reactions while maintaining the enzyme catalytic activity. The resulting EFC showed a linear response to glucose in phosphate buffer within the range 50 μM to 1 mM, with a sensitivity of 14.13 μA cm –2 mM –1 . The sensor was further characterized in saliva, showing the linear range of detection of 0.75 to 2 mM, which is within the physiological range, and sensitivity of 21.5 μA cm –2 mM –1 . Overall, this work demonstrates that PCBs are suitable platforms for EFCs, paving the way for the development of fully integrated systems in a seamless and miniaturized device.

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“…These biosensing devices operate in the interstitial fluid (ISF) layer; therefore, we tested our designed configuration under a fluid that simulates the human ISF ( Figure S10 ). 31 As expected, lower bioelectrocatalytic currents were observed due to interactions with bovine serum albumin (BSA) proteins and high salts; nevertheless, the sensor was active and enabled glucose sensing without any additional coating step. Besides biosensing applications, the developed bioanode can be utilized in EBFC applications.…”

Section: Resultsmentioning

confidence: 63%

Utilization of FAD-Glucose Dehydrogenase from T. emersonii for Amperometric Biosensing and Biofuel Cell Devices

et al. 2021

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Flavin-dependent glucose dehydrogenases (FAD-GDH) are oxygen-independent enzymes with high potential to be used as biocatalysts in glucose biosensing applications. Here, we present the construction of an amperometric biosensor and a biofuel cell device, which are based on a thermophilic variant of the enzyme originated from Talaromyces emersonii . The enzyme overexpression in Escherichia coli and its isolation and performance in terms of maximal bioelectrocatalytic currents were evaluated. We examined the biosensor’s bioelectrocatalytic activity in 2,6-dichlorophenolindophenol-, thionine-, and dichloro-naphthoquinone-mediated electron transfer configurations or in a direct electron transfer one. We showed a negligible interference effect and good stability for at least 20 h for the dichloro-naphthoquinone configuration. The constructed biosensor was also tested in interstitial fluid-like solutions to show high bioelectrocatalytic current responses. The bioanode was coupled with a bilirubin oxidase-based biocathode to generate 270 μW/cm 2 in a biofuel cell device.

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Improved operational stability of mediated glucose enzyme electrodes for operation in human physiological solutions

Cited by 24 publications

References 54 publications

An Oxygen Insensitive Amperometric Glucose Biosensor Based on An Engineered Cellobiose Dehydrogenase: Direct versus Mediated Electron Transfer Responses

An Oxygen Insensitive Amperometric Glucose Biosensor Based on An Engineered Cellobiose Dehydrogenase: Direct versus Mediated Electron Transfer Responses

Self-Powered Detection of Glucose by Enzymatic Glucose/Oxygen Fuel Cells on Printed Circuit Boards

Utilization of FAD-Glucose Dehydrogenase from T. emersonii for Amperometric Biosensing and Biofuel Cell Devices

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