Final published version
Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Enzymatic fuel cells with an oxygen resistant variant of pyranose-2-oxidase as anode biocatalyst
AU - Şahin, Samet
AU - Wongnate, Thanyaporn
AU - Chuaboon, Litavadee
AU - Chaiyen, Pimchai
AU - Yu, Eileen Hao
PY - 2018/6/1
Y1 - 2018/6/1
N2 - In enzymatic fuel cells (EnFCs), hydrogen peroxide formation is one of the main problems when enzymes, such as, glucose oxidase (GOx) is used due to the conversion of oxygen to hydrogen peroxide in the catalytic reaction. To address this problem, we here report the first demonstration of an EnFC using a variant of pyranose-2-oxidase (P2O-T169G) which has been shown to have low activity towards oxygen. A simple and biocompatible immobilisation approach incorporating multi-walled-carbon nanotubes within ferrocene (Fc)-Nafion film was implemented to construct EnFCs. Successful immobilisation of the enzymes was demonstrated showing 3.2 and 1.7-fold higher current than when P2O-T169G and GOx were used in solution, respectively. P2O-T169G showed 25% higher power output (maximum power density value of 8.45 ± 1.6 μW cm−2) and better stability than GOx in aerated glucose solutions. P2O-T169G maintained > 70% of its initial current whereas GOx lost activity > 90% during the first hour of 12 h operation at 0.15 V (vs Ag/Ag+). A different fuel cell configuration using gas-diffusion cathode and carbon paper electrodes were used to improve the power output of the fuel cell to 29.8 ± 6.1 µW cm−2. This study suggests that P2O-T169G with low oxygen activity could be a promising anode biocatalyst for EnFC applications.
AB - In enzymatic fuel cells (EnFCs), hydrogen peroxide formation is one of the main problems when enzymes, such as, glucose oxidase (GOx) is used due to the conversion of oxygen to hydrogen peroxide in the catalytic reaction. To address this problem, we here report the first demonstration of an EnFC using a variant of pyranose-2-oxidase (P2O-T169G) which has been shown to have low activity towards oxygen. A simple and biocompatible immobilisation approach incorporating multi-walled-carbon nanotubes within ferrocene (Fc)-Nafion film was implemented to construct EnFCs. Successful immobilisation of the enzymes was demonstrated showing 3.2 and 1.7-fold higher current than when P2O-T169G and GOx were used in solution, respectively. P2O-T169G showed 25% higher power output (maximum power density value of 8.45 ± 1.6 μW cm−2) and better stability than GOx in aerated glucose solutions. P2O-T169G maintained > 70% of its initial current whereas GOx lost activity > 90% during the first hour of 12 h operation at 0.15 V (vs Ag/Ag+). A different fuel cell configuration using gas-diffusion cathode and carbon paper electrodes were used to improve the power output of the fuel cell to 29.8 ± 6.1 µW cm−2. This study suggests that P2O-T169G with low oxygen activity could be a promising anode biocatalyst for EnFC applications.
KW - Biosensors
KW - Enzymatic fuel cells
KW - Ferrocene
KW - Glucose oxidase
KW - Nafion
KW - Pyranose-2-oxidase
U2 - 10.1016/j.bios.2018.01.065
DO - 10.1016/j.bios.2018.01.065
M3 - Journal article
C2 - 29427882
AN - SCOPUS:85041479039
VL - 107
SP - 17
EP - 25
JO - Biosensors and Bioelectronics
JF - Biosensors and Bioelectronics
SN - 0956-5663
ER -