Direct electrochemistry of glucose oxidase immobilized on carbon nanotube for improving glucose sensing

Hyun, Kyuhwan; Han, Sang Won; Koh, Won Gun; Kwon, Yongchai

doi:10.1016/j.ijhydene.2014.12.019

Cited by 58 publications

(28 citation statements)

References 31 publications

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“…26 The electron transfer rate constant (k s ) of the catalytic structures was measured because k s was proportional to the reaction rate, followed by the EBC performance. For measuring the k s , Laviron's formula was used, 24,27,28 Based on the above data, the glucose oxidation reactivity of the catalytic structures (the reaction rate of the glucose oxidation reaction) was evaluated because the glucose oxidation reactivity is one of the major factors for determining catalytic activity and EBC performance. To achieve this, effects under two ambient conditions (air state and N 2 state) on the catalytic activity of the structures were initially investigated without glucose (Supplementary Figure S6), and then effects of the ambient conditions on the glucose oxidation reactivity of the catalytic structures were measured (Supplementary Figures S7 and S8).…”

Section: Resultsmentioning

confidence: 99%

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

2017

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A new enzyme catalyst consisting of pyrenecarboxaldehyde (PCA) and glucose oxidase (GOx) immobilized on polyethyleneimine (PEI) and a carbon nanotube supporter (CNT/PEI/[PCA/GOx]) is suggested, and the performance and stability of an enzymatic biofuel cell (EBC) using the new catalyst are evaluated. Using PCA, the amount of immobilized GOx increases (3.3 U mg − 1 ) and the electron transfer rate constant of the CNT/PEI/[PCA/GOx] is promoted (11.51 s − 1 ). Also, the catalyst induces excellent EBC performance (maximum power density (MPD) of 2.1 mW cm − 2 ), long-lasting stability (maintenance of 93% of the initial MPD after 4 weeks) and superior catalytic activity (flavin adenine dinucleotide redox reaction rate of 0.62 mA cm − 2 and Michaelis-Menten constant of 0.99 mM). These characteristics are ascribed to effects of (i) electron collection due to hydrophobic interactions, (ii) electron transfer pathways due to π-conjugated bonds and (iii) enzyme stabilization due to π-hydrogen bonds that are newly induced by the PCA/GOx composite. The existence of such positive interactions is properly verified using X-ray photoelectron spectroscopy and enzyme activity measurements. NPG Asia Materials (2017) 9, e386; doi:10.1038/am.2017.75; published online 2 June 2017 INTRODUCTIONThe demand for clean electrical energy is increasing as a result of weather changes caused by the greenhouse effect and depletion of fossil fuels. 1 To meet this demand, related research and development efforts are being eagerly pursued. As one of the efforts, enzymatic biofuel cells (EBCs) that convert bioenergy into electrical energy are being considered. 2,3 In particular, EBC systems employing glucose oxidase (GOx) as a biocatalyst have emerged because of their advantageous properties, such as biocompatibility, excellent selectivity toward specific substrates and strong activity near neutral pH and room temperature. 2 In addition, because EBC systems use human body-friendly fuels, such as glucose, glycerol, water and oxygen, for electricity generation, they can be embedded as power generators for the operation of artificial internal organs, such as artificial hearts and brains, insulin pumps or bone stimulators. [4][5][6][7][8] However, in spite of such promising facets of EBC systems, the commercialization of EBCs using GOx has been limited because of their low EBC performance and poor durability. 9 The disadvantages are attributed to the low immobilization ratio of GOx molecules, slow GOx-related reaction rate, low GOx activity and easy GOx denaturation. Of them, low GOx immobilization has been considered the main problem.

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Section: Resultsmentioning

confidence: 99%

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

2017

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“…These examples demonstrated that many researches had been concerted on the development of long-term detection systems, including crosslinking with glutaraldehyde, 23 mixing with BSA before including cross-linking with glutaraldehyde, 24 drop-casting, 14 layer assembly modify electrode. 14,[25][26][27][28][29][30] As we can see, linear detection cover physiological range could achieve, but longterm monitoring and store stability is denitely lower than that obtained with silk/D-sorbitol microneedle. Silk is a unique protein biopolymer, with six hydrophobic to one hydrophilic amino acid.…”

Section: Long-term Operational Stability and Storage Stability Of Thementioning

confidence: 99%

“…For optimizing temperature. Cyclic voltammetric was measured in microneedles with GOD at a potential of À0.1 V to 1.2 V (versus Ag/AgCl electrode), scan rate of 100 mV s À1 , 11.1 mM glucose, and pH 7.4 in electrolyte, at 25,30,35,40,45, 50 C.…”

Section: Electrochemical Performancementioning

confidence: 99%

Silk/polyols/GOD microneedle based electrochemical biosensor for continuous glucose monitoring

et al. 2020

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“…High thermal and solvent stability of immobilized enzymes was reported by Hermanová et al . Glucose oxidase was coated on carbon nanotubes (CNTs) via the physical adsorption method, and optimum immobilization conditions were investigated by Hyun et al . Long‐term thermal stability and activity of immobilized enzymes on CNTs were reported.…”

Section: Introductionmentioning

confidence: 99%

“…Lipase was immobilized on graphene by three different methods: physical adsorption, covalent attachment, and additional crosslinking. 18 High thermal and solvent stability of immobilized enzymes was reported by Hermanov a et al 18 Glucose oxidase was coated on carbon nanotubes (CNTs) via the physical adsorption method, and optimum immobilization conditions were investigated by Hyun et al 19 Long-term thermal stability and activity of immobilized enzymes on CNTs were reported. Glucose oxidase and horseradish peroxidase were coimmobilized on solid mesoporous silica nanoparticles, and the spatially controlled localization of different types of enzymes in a simple way was reported by Gustafsson et al 20 Laccase enzyme was immobilized on titania nanoparticles, and enzymatic decolorization was observed.…”

Section: Introductionmentioning

confidence: 99%

Cellulose monoacetate/polycaprolactone and cellulose monoacetate/polycaprolactam blended nanofibers for protease immobilization

Aykut

Sevgi

Demirkan

2017

J of Applied Polymer Sci

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Enzymes can be used multiple times when they are immobilized on a support. More enzymes can be immobilized on a surface when nanofibers are used as a supporting surface because the specific surface area increases tremendously. In this regard, polycaprolactam/cellulose monoacetate (PA6/CMA) and polycaprolactone/cellulose monoacetate (PCL/CMA) blended nanofibers (NFs) were prepared via an electrospinning process. Protease enzymes were immobilized on neat PA6, PCL, PA6/CMA, and PCL/CMA nanofibers and glutaraldehyde (GA) activated analogs through the physical adsorption method. The immobilized enzyme activity was measured by using a casein substrate, and the results were compared with free enzyme activity. Among all of the samples, the highest immobilization yield of about 82% was obtained with GA‐activated neat PCL NF samples. The best remaining activity of the immobilized enzymes on pure CMA NFs was found to be 59% after seven reuses. Even after nine reuses, enzyme activities are still observed on the CMA NF samples. It was expected that the addition of CMA in PCL and PA6 NFs would increase the reusability number to reach the reusability of CMA NFs, but it was not significantly enhanced. If CMA chains could be mostly collected on the sheath or close to the sheath of the NFs during the electrospinnig process, this target could be achieved. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45479.

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Direct electrochemistry of glucose oxidase immobilized on carbon nanotube for improving glucose sensing

Cited by 58 publications

References 31 publications

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

Silk/polyols/GOD microneedle based electrochemical biosensor for continuous glucose monitoring

Cellulose monoacetate/polycaprolactone and cellulose monoacetate/polycaprolactam blended nanofibers for protease immobilization

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