A pyrroloquinolinequinone-dependent glucose dehydrogenase (PQQ-GDH)-electrode with direct electron transfer based on polyaniline modified carbon nanotubes for biofuel cell application

2012 ◽  
Vol 82 ◽  
pp. 224-232 ◽  
Author(s):  
Ivo W. Schubart ◽  
Gero Göbel ◽  
Fred Lisdat
2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Erica Pinchon ◽  
Mary Arugula ◽  
Kapil Pant ◽  
Sameer Singhal

Recent studies have focused on tailoring the catalytic currents of multicopper oxidase (MCO) enzymes-based biocathodes to enhance oxygen reduction. Biocathodes modified with natural substrates specific for MCO enzymes demonstrated drastic improvement for oxygen reduction. Performance of 1-pyrenebutanoic acid, succinimidyl ester (PBSE), and 2,5-dimethyl-1-phenyl-1H-pyrrole-3-carbaldehyde (Di-Carb) oriented bilirubin oxidase (BOx) modified gas diffusion biocathode has been highly improved by incorporating hematin, a porphyrin precursor as electron transfer enhancement moiety. Hematin modified electrodes demonstrated direct electron transfer reaction of BOx exhibiting larger O2 reduction in current density in phosphate buffer solution (pH 7.0) without the need of a mediator. A remarkable improvement in the catalytic currents with 2.5-fold increase compared to non-hematin modified oriented BOx electrodes was achieved. Moreover, a mediatorless and compartmentless glucose/O2 biofuel cell based on DET-type bioelectrocatalysis via the BOx cathode and the glucose dehydrogenase (GDH) anode demonstrated peak power densities of 1 mW/cm2 at pH 7.0 with 100 mM glucose/10 mM NAD fuel. The maximum current density of 1.6 mA/cm2 and the maximum power density of 0.4 mW/cm2 were achieved at 300 mV with nonmodified BOx cathode, while 3.5 mA/cm2 and 1.1 mW/cm2 of current and power density were achieved with hematin modified cathode. The performance improved 2.4 times which attributes to the hematin acting as a natural precursor and activator for BOx activity enhancement.


Fuel Cells ◽  
2009 ◽  
pp. NA-NA ◽  
Author(s):  
V. Coman ◽  
R. Ludwig ◽  
W. Harreither ◽  
D. Haltrich ◽  
L. Gorton ◽  
...  

2019 ◽  
Vol 123 ◽  
pp. 114-123 ◽  
Author(s):  
Kohei Ito ◽  
Junko Okuda-Shimazaki ◽  
Kazushige Mori ◽  
Katsuhiro Kojima ◽  
Wakako Tsugawa ◽  
...  

2022 ◽  
pp. 193229682110706
Author(s):  
Yutaro Inoue ◽  
Yasuhide Kusaka ◽  
Kotaro Shinozaki ◽  
Inyoung Lee ◽  
Koji Sode

Background: The bacterial derived flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase (FADGDH) is the most promising enzyme for the third-generation principle-based enzyme sensor for continuous glucose monitoring (CGM). Due to the ability of the enzyme to transfer electrons directly to the electrode, recognized as direct electron transfer (DET)-type FADGDH, although no investigation has been reported about DET-type FADGDH employed on a miniaturized integrated electrode. Methods: The miniaturized integrated electrode was formed by sputtering gold (Au) onto a flexible film with 0.1 mm in thickness and divided into 3 parts. After an insulation layer was laminated, 3 openings for a working electrode, a counter electrode and a reference electrode were formed by dry etching. A reagent mix containing 1.2 × 10−4 Unit of DET-type FADGDH and carbon particles was deposited. The long-term stability of sensor was evaluated by continuous operation, and its performance was also evaluated in the presence of acetaminophen and the change in oxygen partial pressure (pO2) level. Results: The amperometric response of the sensor showed a linear response to glucose concentration up to 500 mg/dL without significant change of the response over an 11-day continuous measurement. Moreover, the effect of acetaminophen and pO2 on the response were negligible. Conclusions: These results indicate the superb potential of the DET-type FADGDH-based sensor with the combination of a miniaturized integrated electrode. Thus, the described miniaturized DET-type glucose sensor for CGM will be a promising tool for effective glycemic control. This will be further investigated using an in vivo study.


Author(s):  
Yuchen Hui ◽  
Xiaoyan Ma ◽  
Rong Cai ◽  
Shelley D. Minteer

Abstract A stable three-dimensional glucose/oxygen enzymatic biofuel cell is fabricated based on the method of polymer encapsulation-based immobilization. And three-dimensional carbon felt is used as the substrate of the bio-electrode for increasing enzymatic loading density. Gold nanoparticles and multi-wall carbon nanotubes are employed to promote direct electron transfer and enhance conductivity and electron conduction rate of bio-electrodes. Glucose dehydrogenase and bilirubin oxidase are immobilized with tetrabutylammonium bromide (TBAB) modified Nafion, which enhances the stability of the bio-electrodes by the immobilization method. A membrane-free glucose/oxygen biofuel cell is assembled with a high open-circuit voltage of 0.85 V and a maximum power density of 21.9 ± 0.1 μW/cm2 in 0.1 M pH 7.0 phosphate buffer solution with 100 mM glucose and air saturation. And the biofuel cell shows high stability to the condition. After 60 days of periodic storage experiments, the performance of the enzymatic biofuel cell still maintained 90.3% of its electrochemical performance.


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