Amperometric flow injection determination of fructose in honey with a carbon paste sensor based on fructose dehydrogenase

Parellada, Josefina; Domı́nguez, Elena; Fernández, Vı́ctor M.

doi:10.1016/0003-2670(96)87686-0

Cited by 51 publications

(21 citation statements)

References 23 publications

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“…The continuous application of oxidative potential might cause the denaturation of enzyme or modification of redox center of the enzyme. Parellada et al reported the similar results in operational stability in FIA system utilizing fructose dehydrogenase and also mentioned the denaturation of the enzyme by application of potential as a reason of short operational period of the FIA system (17) . The leakage of the electron mediator from the sensor assembly should also be a factor to be considered.…”

Section: Operational Stability Of the Enzyme Electrode In An Fia Systemsupporting

confidence: 60%

Amperometric Glucose Sensor Using Thermostable Co-Factor Binding Glucose Dehydrogenase

et al. 2003

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A thermostable mediator-type enzyme glucose sensor was constructed. The electrode was fabricated using chemically crosslinked thermostable co-factor binding glucose dehydrogenase (GDH) from thermophilic bacteria in carbon paste matrix. The electrode responded directly proportional to D-glucose concentration from 0.01 mM to 3 mM in stirred buffer containing 1 mM 1-methoxyphenazinemethosulfate as a mediator with the steady-state mode. The storage stability was examined by incubating the enzyme electrode at 50ºC during the measurement. The cross-linked GDH immobilized electrode showed good storage stability. Ninety percent of its initial response was retained after incubation in buffer solution for 9 days at 50ºC. The flow injection analysis (FIA) glucose sensing system was also constructed by immobilizing the cross-linked GDH and ferrocene as a mediator in the carbon paste matrix. The FIA system was able to measure 600 samples for 100 h.

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Section: Operational Stability Of the Enzyme Electrode In An Fia Systemsupporting

confidence: 60%

Amperometric Glucose Sensor Using Thermostable Co-Factor Binding Glucose Dehydrogenase

et al. 2003

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“…SM and DHSM are cationic polyhydroxyls (amyloglycosides), PEI is a cationic polymer and LA is an uncharged polyol. SM, DHSM and LA have shown beneficial effects on the activity of HRP [41], while PEI has shown activating effects on oxidases [12,14,16,17,47] and dehydrogenases [48,49] but no major influence on peroxidases [12,17]. The additives were used either separately in the paste, or in combination with LA.…”

Section: Additives Included In the Electrode Materialsmentioning

confidence: 99%

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

et al. 1998

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An amperometric biosensor for the detection of some monosaccharides was developed with co-immobilized pyranose oxidase (purified from the basidiomycete fungus Phanerochaete chrysosporium) and horseradish peroxidase in carbon paste. Due to rather low selectivity of pyranose oxidase, the biosensor could detect both predominating anomers of D-glucose as well as the substrates D-xylose, D-galactose, and d-gluconolactone. The best sensor performance was obtained from a carbon paste with covalently immobilized enzymes together with the additives lactitol and polyethylenimine, resulting in a sensitivity for glucose of 30.2 mA cm ¹2 mM ¹1 . The enzyme modified electrode was investigated in an automated flow injection system at the operating potential of ¹50 mV (vs. Ag/AgCl) with an injection frequency of 40 h ¹1 . The biosensor was also integrated as the detection unit in a liquid chromatographic system for the detection of monosaccharides to show its potential use in real applications.

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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 flow injection determination of fructose in honey with a carbon paste sensor based on fructose dehydrogenase

Cited by 51 publications

References 23 publications

Amperometric Glucose Sensor Using Thermostable Co-Factor Binding Glucose Dehydrogenase

Amperometric Glucose Sensor Using Thermostable Co-Factor Binding Glucose Dehydrogenase

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

Rapid determination of lactulose in milk by microdialysis and biosensors

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