Amperometric fructose sensor based on direct bioelectrocatalysis

Ikeda, Tokuji; Matsushita, Fumio; Senda, Mitsugi

doi:10.1016/0956-5663(91)85015-o

Cited by 130 publications

(51 citation statements)

References 10 publications

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“…Another pioneer in bioelectrochemistry, T. Ikeda, had found that several multi-cofactor-containing redox enzymes could communicate directly with carbon electrodes. The ones that Ikeda and coworkers had been studying at the time all have a catalytic domain containing either a flavin or pyrroloquinoline quinone (PQQ) and additionally another domain containing at least one haem group, which was looked upon as a "built-in mediator", [58] with examples such as d-gluconate dehydrogenase, [59] fructose dehydrogenase [60] and alcohol PQQ dehydrogenase.…”

Section: Reaction With Cytochrome Cmentioning

confidence: 99%

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

et al. 2010

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Cellobiose dehydrogenase catalyses the oxidation of aldoses--a simple reaction, a boring enzyme? No, neither for the envisaged bioelectrochemical applications nor mechanistically. The catalytic cycle of this flavocytochrome is complex and modulated by its flexible cytochrome domain, which acts as a built-in redox mediator. This intramolecular electron transfer is modulated by the pH, an adaptation to the environmental conditions encountered or created by the enzyme-producing fungi. The cytochrome domain forms the base from which electrons can jump to large terminal electron acceptors, such as redox proteins, and also enables by that path direct electron transfer from the catalytically active flavodehydrogenase domain to electrode surfaces. The application of electrochemical techniques to the elucidation of the molecular and catalytic properties of cellobiose dehydrogenase is discussed and compared to biochemical methods. The results lead to valuable insights into the function of this cellulose-bound enzyme, but also form the basis of exciting applications in biosensors, biofuel cells and bioelectrocatalysis.

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Section: Reaction With Cytochrome Cmentioning

confidence: 99%

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

et al. 2010

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“…FDH is a membrane bound enzyme containing PQQ as the bound cofactor and has additionally a heme group attached. It is reported to function only on the surface of carbon pastes and only with the addition of a surfactant such as Triton-X 100 to the contacting buffer [17,56,65,751. One attempt to mix the enzyme into carbon paste totally failed arid no activity for fructose could be obtained [75].…”

Section: Sensors For Saccharidesmentioning

confidence: 99%

“…Recently, Ikeda and co-workers [17] have focused on sensors based on adsorbing flavo-and PQQ-enzymes also having a heme-group within the structure on carbon paste electrodes. They showed that a direct electron transfer is possible and give examples of sensors for NAD(P)H based on diaphorase [73], fructose based on fructose dehydrogenase [65], and D-gluconate based on D-gluconate dehydrogenase [ 501.…”

Section: Mediatorless Electron Transfer Reaction Between Redox Enzymementioning

confidence: 99%

Carbon paste electrodes modified with enzymes, tissues, and cells

1995

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A review is presented dealing with the use of carbon paste amperometric electrodes for electroanalytical purposes, with either the surface or the bulk being modified with biologically derived material such as enzymes, tissues, and cells. It covers virtually all the publications which have appeared from the very first enzyme-modified carbon paste electrode up to early 1994 and includes 220 references.

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“…Several different examples of this sensor have been reported, [25][26][27][28][29][30][31] but in almost all cases the lifetime of the immobilised FDH enzyme was short, ranging from hours up to 1-2 weeks. Only one paper has reported an enzyme lifetime of more than 1 month.…”

Section: Fructose Biosensormentioning

confidence: 99%

Rapid determination of lactulose in milk by microdialysis and biosensors

Moscone¹,

Bernardo²,

Marconi³

et al. 1999

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A simple and rapid flow system for the determination of lactulose in milk samples was developed. It is based on the hydrolysis of lactulose to galactose and fructose by the enzyme b-galactosidase immobilised in a reactor. The amount of fructose produced was measured with an electrochemical biosensor based on the fructose dehydrogenase enzyme, K 3 [Fe(CN) 6 ] as mediator and a platinum based electrochemical transducer. Parameters such as the enzyme immobilisation in the reactor and under the electrode surface, the lifetime of the b-galactosidase reactor and of the dehydrogenase biosensor and the flow parameters were studied and optimised. Fructose was determined in the range 1 3 10 26 -5 3 10 23 mol l 21 with an RSD of about 2% and a detection limit of 5 3 10 27 mol l 21 . The use of a microdialysis probe as the sampling system permitted the direct measurement of lactulose in milk samples without pre-treatment in the range 1 3 10 25 -5 3 10 23 mol l 21 . The sensitivity of the procedure allowed pasteurised, UHT and in-container sterilised milk to be distinguished.

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Amperometric fructose sensor based on direct bioelectrocatalysis

Cited by 130 publications

References 10 publications

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

Carbon paste electrodes modified with enzymes, tissues, and cells

Rapid determination of lactulose in milk by microdialysis and biosensors

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