Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode

Monošík, Rastislav; Stredansky, Matuš; Lušpai, Karol; Magdolen, Peter; Šturdı́k, Ernest

doi:10.1016/j.enzmictec.2012.01.004

Cited by 51 publications

(22 citation statements)

References 24 publications

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“…Oxygen-insensitive flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) has been given much attention recently and there has been an increasing numbers of related reports on biosensors [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] and biofuel cells. 13,14,[16][17][18] Recently, the structure of FAD-GDH from Aspergillus flavus was unveiled and it was found that an FAD cofactor is buried deeply (∼1.4 nm) below the protein surface.…”

Section: Introductionmentioning

confidence: 99%

“…20 There are two approaches: mediated electron transfer (MET) and direct electron transfer (DET). MET is the utilization of electron transfer mediators such as potassium hexacyanoferrate (K3[Fe(CN)6]), 5 phenazine methosulfate, 3,7 osmium complexes, [8][9][10] phenothiazin, 13 and naphthoquiobne. 15 Small and mobile mediators ferry electrons from FAD, which originates from an enzyme-catalytic reaction, to the electron collector ( Fig.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of Direct and Mediated Electron Transfer in Electrodes with Novel Fungal Flavin Adenine Dinucleotide Glucose Dehydrogenase

et al. 2018

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Direct and mediated electron transfer (DET and MET) in enzyme electrodes with a novel flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from fungi are compared for the first time. DET is achieved by placing a single-walled carbon nanotube (CNT) between GDH and a flat gold electrode where the CNT is close to FAD within the distance for DET. MET is induced by using a free electron transfer mediator, potassium hexacyanoferrate, and shuttles electrons from FAD to the gold electrode. Cyclic voltammetry shows that the onset potential for glucose response current in DET is smaller than in MET, and that the distinct redox current peak pairs in MET are observed whereas no peaks are found in DET. The chronoamperometry with respect to a glucose biosensor shows that (i) the response in DET is more rapid than in MET; (ii) the current at more than +0.45V in DET is larger than the current at the current-peak potential in MET; (iii) a DET electrode covers the glucose concentration range for clinical requirements and is not susceptible to interfering agents at +0.45 V; and (iv) a DET electrode with the novel fungal FAD-GDH does not affect sensing accuracy in the presence of up to 5 mM xylose, while it often shows a similar response level to glucose with other conventionally used fungus-derived FAD-GDHs. It is concluded that our DET system overcomes the disadvantage of MET.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comparison of Direct and Mediated Electron Transfer in Electrodes with Novel Fungal Flavin Adenine Dinucleotide Glucose Dehydrogenase

et al. 2018

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“…FAD-GDH as a highly active [30] and selective [31,32] enzyme, pioneering in the field of glucose biosensors [33,34], is oxygen independent and a promising component for mediator-free charge transfer [35]. FAD-GDH as a highly active [30] and selective [31,32] enzyme, pioneering in the field of glucose biosensors [33,34], is oxygen independent and a promising component for mediator-free charge transfer [35].…”

mentioning

confidence: 99%

“…Inspired by all these aspects, we intended to design a novel formulation of materials that are based on physically immobilized FAD-dependent glucose dehydrogenase (FAD-GDH) in a PEDOT:PSS-PVA composite film. FAD-GDH as a highly active [30] and selective [31,32] enzyme, pioneering in the field of glucose biosensors [33,34], is oxygen independent and a promising component for mediator-free charge transfer [35]. In order to devote such a combination for the development of future biosensors, a thorough and fundamental evaluation of the applied materials was needed to generate a biocompatible and homogeneous matrix with good adhesion properties and a highly active enzyme in it.…”

mentioning

confidence: 99%

Activity determination of FAD‐dependent glucose dehydrogenase immobilized in PEDOT: PSS‐PVA composite films for biosensor applications

Riegel

Borzenkova

Haas

et al. 2016

Engineering in Life Sciences

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In this study, we propose an entirely new combination of materials as a novel formulation devoted for future generation of glucose biosensor. We combined poly(3,4‐ethylenedioxythiophene:polystyrene sulfonate) and poly(vinyl alcohol) as conducting matrix and immobilized the highly active and pioneering enzyme flavin adenine dinucleotide‐dependent glucose dehydrogenase (FAD‐GDH) into it. In this context, a good processability of the materials and the preservation of the enzymatic activity are critical steps to provide full device function later on. Thus, we thoroughly characterized the proposed pairing of materials: the influence of the composition on the film‐forming properties was investigated by scanning electron microscopy, optical microscopy, and photography; for the assessment of the enzymatic activity, we developed a spectrophotometric method. A great dependence is observed between activity and composition, ranging from inactive (1.6% retained activity) to highly active (91.5%). A high share of enzyme led to a higher enzymatic activity as long as the necessary condition of a pH higher than 6 was met. These first and fundamental findings can now be used as guidelines to tailor mediator‐free biosensors with enhanced selectivity and to enable the design of devices with improved performance.

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“…Owing to its high catalytic activity and substrate specificity, G6PD has been extensively used as reagent in varied enzymatic assays aiming determinations of ATP and hexose concentrations [5]. Besides, using G6PD in enzyme-based biosensor would be a good option due to advantages as specific measurement of target analyte in complex matrices (e.g., blood, food products, and environmental samples) [6,7]. However, the potential application of G6PD requires an efficient strategy to its recovery from remaining yeast cells of fermentation medium and, although particularly abundant in Saccharomyces cerevisiae, a baker or brewer yeast, C. guilliermondii could be a feasible option of this enzyme source.…”

Section: Introductionmentioning

confidence: 99%

Process Integration for the Disruption of Candida guilliermondii Cultivated in Rice Straw Hydrolysate and Recovery of Glucose-6-Phosphate Dehydrogenase by Aqueous Two-Phase Systems

Gurpilhares

Pessoa

Roberto

2015

Appl Biochem Biotechnol

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Remaining cells of Candida guilliermondii cultivated in hemicellulose-based fermentation medium were used as intracellular protein source. Recovery of glucose-6-phosphate dehydrogenase (G6PD) was attained in conventional aqueous two-phase systems (ATPS) was compared with integrated process involving mechanical disruption of cells followed by ATPS. Influences of polyethylene glycol molar mass (M PEG) and tie line lengths (TLL) on purification factor (PF), yields in top (Y T ) and bottom (Y B ) phases and partition coefficient (K) were evaluated. First scheme resulted in 65.9 % enzyme yield and PF of 2.16 in salt-enriched phase with clarified homogenate (M PEG 1500 g mol(-1), TLL 40 %); Y B of 75.2 % and PF B of 2.9 with unclarified homogenate (M PEG 1000 g mol(-1), TLL 35 %). The highest PF value of integrated process was 2.26 in bottom phase (M PEG 1500 g mol(-1), TLL 40 %). In order to optimize this response, a quadratic model was predicted for the response PFB for process integration. Maximum response achieved was PFB = 3.3 (M PEG 1500 g mol(-1), TLL 40 %). Enzyme characterization showed G6P Michaelis-Menten constant (K M ) equal 0.07-0.05, NADP(+) K M 0.02-1.98 and optimum temperature 70 °C, before and after recovery. Overall, our data confirmed feasibility of disruption/extraction integration for single-step purification of intracellular proteins from remaining yeast cells.

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Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode

Cited by 51 publications

References 24 publications

Comparison of Direct and Mediated Electron Transfer in Electrodes with Novel Fungal Flavin Adenine Dinucleotide Glucose Dehydrogenase

Comparison of Direct and Mediated Electron Transfer in Electrodes with Novel Fungal Flavin Adenine Dinucleotide Glucose Dehydrogenase

Activity determination of FAD‐dependent glucose dehydrogenase immobilized in PEDOT: PSS‐PVA composite films for biosensor applications

Process Integration for the Disruption of Candida guilliermondii Cultivated in Rice Straw Hydrolysate and Recovery of Glucose-6-Phosphate Dehydrogenase by Aqueous Two-Phase Systems

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