scholarly journals Electrosynthesis of Pyrenediones on Carbon Nanotube Electrodes for Efficient Electron Transfer with FAD‐dependent Glucose Dehydrogenase in Biofuel Cell Anodes

2019 ◽  
Vol 6 (20) ◽  
pp. 5242-5247 ◽  
Author(s):  
Pierre‐Yves Blanchard ◽  
Paulo Henrique M. Buzzetti ◽  
Bridget Davies ◽  
Yannig Nedellec ◽  
Emerson Marcelo Girotto ◽  
...  
2019 ◽  
Vol 19 (6) ◽  
pp. 3551-3557 ◽  
Author(s):  
Hiroaki Sakamoto ◽  
Ayako Koto ◽  
Ei-Ichiro Takamura ◽  
Hitoshi Asakawa ◽  
Takeshi Fukuma ◽  
...  

For increasing the output of biofuel cells, increasing the cooperation between enzyme reaction and electron transfer on the electrode surface is essential. Highly oriented immobilization of enzymes onto a carbon nanotube (CNT) with a large specific surface area and excellent conductivity would increase the potential for their application as biosensors and biofuel cells, by utilizing the electron transfer between the electrode-molecular layer. In this study, we prepared a CNT-enzyme complex with highly oriented immobilization of enzyme onto the CNT surface. The complex showed excellent electrical characteristics, and could be used to develop biodevices that enable efficient electron transfer. Multi-walled carbon nanotubes (MWCNT) were dispersed by pyrene butyric acid N-hydroxysuccinimide ester, and then N-(5-amino-1-carboxypentyl) iminodiacetic acid (AB-NTA) and NiCl2 were added to modify the NTA-Ni2+ complex on the CNT surface. Pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase (GDH) was immobilized on the CNT surface through a genetically introduced His-tag. Formation of the MWCNT-enzyme complex was confirmed by monitoring the catalytic current electrochemically to indicate the enzymatic activity. PQQ-GDH was also immobilized onto a highly ordered pyrolytic graphite surface using a similar process, and the enzyme monolayer was visualized by atomic force microscopy to confirm its structural properties. A biofuel cell was constructed using the prepared CNT-enzyme complex and output evaluation was carried out. As a result, an output of 32 μW/cm2 could be obtained without mediators.


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.


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