Glucose Oxidase Directly Immobilized onto Highly Porous Gold Electrodes for Sensing and Fuel Cell applications

Toit, Hendrik du; Lorenzo, Mirella Di

doi:10.1016/j.electacta.2014.06.074

Cited by 76 publications

(61 citation statements)

References 41 publications

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“…The K m value of GOx/MCPE was lower than GOx/MCPE from previous study (0.61 mM) [9] and much lower than one reported for the highly porous gold (hPG) electrodes with GOx (A. niger) immobilized by absorption (GOx/hPGE) (6.3±0.7 mM) [4], GOx/chitosan/ferrocene electrodes (1.5 mM) [17] and the native GOx from A. niger in solution (27 mM) [18]. This indicates that the immobilized GOx onto MCP electrodes has high enzymatic activity and higher affinity for glucose than GOx onto hPG electrodes and the soluble enzyme with a low diffusion barrier.…”

Section: Kinetic Parameters Of Gox/mcpecontrasting

confidence: 66%

“…The enzymatic affinity towards glucose was estimated in terms of the Michaelis-Menten constant (K m ) and was calculated by using electrochemical version of the Lineweaver-Burk equation of the enzyme kinetics (as shown in Fig. 7) [4]. The reciprocal of the current was plotted versus the reciprocal of the glucose concentration in the range of 12-480 µM.…”

Section: Kinetic Parameters Of Gox/mcpementioning

confidence: 99%

“…The applications of GOx onto electrode surfaces for sensors and biofuel cells need the development of a functional immobilization system. For these features, the efficient electron transfer achievement between the enzyme active centre and the electrode is crucial that usually requires a mediated electron transfer (MET) mechanism [4]. The function of these mediators to transfer an electron more rapidly (in solution) to the electrode surface [5].…”

Section: Introductionmentioning

confidence: 99%

“…The function of these mediators to transfer an electron more rapidly (in solution) to the electrode surface [5]. The small redox active particles and polymers are often used as electron transfer carriers (mediators), such as organic dyes, ferrocene and its derivatives, modified vitamin complexes and conducting salts [4].…”

Section: Introductionmentioning

confidence: 99%

“…Glucose Oxidase (GOx) from Aspergillus niger (SIGMA), aniline, (NH) 4 6 ], teflon tubes, Pt, Cu, and Ag/AgCl electrodes.…”

Section: Experimental Section Materialsmentioning

confidence: 99%

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Immobilization of Glucose Oxidase on Modified-Carbon-Paste-Electrodes for Microfuel Cell

et al. 2018

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Section: Kinetic Parameters Of Gox/mcpecontrasting

confidence: 66%

Section: Kinetic Parameters Of Gox/mcpementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Glucose Oxidase (GOx) from Aspergillus niger (SIGMA), aniline, (NH) 4 6 ], teflon tubes, Pt, Cu, and Ag/AgCl electrodes.…”

Section: Experimental Section Materialsmentioning

confidence: 99%

See 3 more Smart Citations

Immobilization of Glucose Oxidase on Modified-Carbon-Paste-Electrodes for Microfuel Cell

et al. 2018

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Enzymatic Fuel Cells and Biosensors

ul Haque,

Yasir,

Ciocan

et al. 2023

Microbial Electrochemical Technologies

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How to engineer glucose oxidase for mediated electron transfer

Gutierrez

Wallraf

Balaceanu

et al. 2018

Biotech & Bioengineering

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Glucose oxidase (GOx) is of high industrial interest for glucose sensing because of its high β-d-glucose specificity. The efficient and specific electrochemical communication between the redox center and electrodes is crucial to ensure accurate glucose determination. The efficiency of the electron transfer rates (ETR) with GOx, together with quinone diamine based mediators, is low and differs even among mediator derivatives. To design optimized enzyme-mediator couples and to describe a mediator binding model, a joint experimental and computational study was performed based on an oxygen-independent GOx variant V7 and two quinone diimine based electron mediators (QDM-1 and QDM-2), which differ in polarity and size, and ferrocenemethanol (FM). A site saturation library at position 414 was screened with all three mediators and yielded four beneficial substitutions Tyr, Met, Leu, and Val. The variants showed increased mediator activity for the more polar QDM-2 with a simultaneously decreased activity for the less polar and smaller QDM-1 and for FM. The variant GOx V7-I414Y exhibited the biggest change for the quinone diimine derivatives compared with V7 (QDM-1: 55.9 U/mg V7, 33.2 U/mg V7-I414Y; QDM-2: 2.7 U/mg V7, 12.9 U/mg V7-I414Y). Theoretical ETR calculated based on the Marcus theory were in good agreement with the experimental results. Molecular docking studies revealed a preferable binding of the two QD mediators directly in the active site, 3.5 Å away from the N5 atom of the flavin adenine dinucleotide (FAD) and in direct vicinity to position 414. In summary, position 414 in the active site was identified to modulate the electron shuttling from the FAD of the GOx to small water-soluble mediators dependent on the polarity and size of residue 414 and on the polarity and size of the mediator. The presented mediator binding model offers a promising possibility for the design of optimized enzyme-mediator couples.

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Glucose Oxidase Directly Immobilized onto Highly Porous Gold Electrodes for Sensing and Fuel Cell applications

Cited by 76 publications

References 41 publications

Immobilization of Glucose Oxidase on Modified-Carbon-Paste-Electrodes for Microfuel Cell

Immobilization of Glucose Oxidase on Modified-Carbon-Paste-Electrodes for Microfuel Cell

Enzymatic Fuel Cells and Biosensors

How to engineer glucose oxidase for mediated electron transfer

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