D-fructose dehydrogenase

Figure 17.12 Direct electrocatal3ftic oxidation of D-fnictose at a glassy carbon electrode painted with a paste of Ketjen black particles modified with D-fructose dehydrogenase from a Gluconobacter species. The enzyme incorporates an additional heme center allowing direct electron transfer from the electrode to the flavin active site. Cyclic voltammograms were recorded at a scan rate of 20 mV s and at 25 + 2 °C and pH 5.0. Reproduced by permission of the PCCP Owner Societies, from Kamitaka et al., 2007.

P.A. Paredes, J. Parellada, V.M. Fernandez, I. Katakis and E. Dominguez, Amperometric mediated carbon paste biosensor based on D-fructose dehydrogenase for the determination of fructose in food analysis, Biosens. Bioelectron., 12(12) (1998) 1233-1243. 

D-Fructose dehydrogenase (EC 1.1.99.11) from Gluconobacter industrius is a 140 kDa membrane-bound quinohemoprotein with a PQQ and a heme c-containing subunit. 

Redox proteins that include quinone cofactor units play important roles in biological ET processes. Some of the quinoproteins include the quinone cofactor in a non-covalently linked configuration, such as the pyrroloquinoline quinone, PQQ, dependent enzymes, whereas other quinoproteins include the quinone cofactor covalently-linked to the protein, for example topaquinone (2,4,6-trihydroxyphenylalanine quinone, TPQ) dependent enzymes. A number of quinoproteins include in addition to the quinone cofactor an ET cofactor unit in another protein subunit. These cofactors may be metal ions or a cytochrome-type heme cofactor such as D-fructose dehydrogenase that is a heme containing PQQ-dependent enzyme. ... 

T. Ikeda, F. Matushita and M. Senda, D-Fructose dehydrogenase-modified carbon paste electrode containing p-benzoquinone as a mediated amperometric fructose sensor, Agric. Biol. Chem. 54(11), 2919-24 (1990). (fructose in fruits). 

D-Fructose dehydrogenase. D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor. 

Tkac, J. Vostiar, I. Sturdik, E. Gemeiner, P. Mastihuba, V. Annus, J. Fructose biosensor based on d-fructose dehydrogenase immobilised on a ferrocene-embedded cellulose acetate membrane. Anal. Chim. Acta 2001, 439, 39—46. 

A fructose biosensor based on D-fructose dehydrogenase (FDH) was developed by using tris(l,10-phenathroline)cobalt (II) complex (Co(phen)3) as a redox mediator [52(b)], A self-assembled monolayer (SAM) of cystamine was formed on a gold electrode and then FDH was covalently bound on the SAM using glutaraldehyde which cross-links the amino acid groups of cystamine with the FDH. With the use of the Co(phen)3 mediator, the catalytic current was increased by the addition of D-fructose. 

Subsequently, DMFc is regenerated at the ITIES producing a feedback current response at the tip. A similar mechanism was also suggested for the oxidation of DMFc by cytochrome c at the ITIES.Alternatively, DMFc" " may transfer to the aqueous side of the interface to participate in the enzymatic reaction homogeneously and catalytically. This mechanism was supported by Osakai and co-workers, who carried out quantitative voltammetric studies to propose a reaction-layer mechanism for glucose oxidase, " D-fructose dehydrogenase,and cytochrome c (Fig. 22). ... 

Ameyama M, Shinagawa E, Matsushita K, Adachi O (1981a) D-Fructose dehydrogenase of Gluconohacter industrius purification, characterization, and application to enzymatic microdetermination of D-fractose. J Bacteriol 145(2) 814-823... 

Ameyama M. 1982. Enzymatic microdetemtination of D-glucose, D-fructose, D-gluconate, 2-keto-D-gluconate, aldehyde, and alcohol with memhrane-hound dehydrogenases. Meth Enzymol 89 20-29. 

This enzyme [EC 1.1.1.14], also known as L-iditol 2-dehydrogenase and polyol dehydrogenase, catalyzes the reaction of L-iditol with NAD+ to produce L-sorbose and NADH. The enzyme will also convert D-glucitol to D-fructose. 

SORBITOL DEHYDROGENASE FRUCTOSE-1,6-BISPHOSPHATASE FRUCTOSE-2,6-BISPHOSPHATASE D-Fructose 2,6-bisphosphate, 6-PHOSPHOFRUCTO-2-KINASE Fructose-1,6-bisphosphate aldolase, ALDOLASE... 

Schematic of the polyol pathway showing the NADPH-dependent reduction of open chain D-glucose to sorbitol, which is catalyzed by ALR2. This step is followed by the NAD+-dependent oxidation of sorbitol by sorbitol dehydrogenase to yield D-fructose.

Paredes et al. [15] Fructose Honey Fruit juices Soft drinks D-PQQ-fructose dehydrogenase/physically included in the electrode matrix, also containing mediator and polyethyleneimine (PEI) Carbon paste electrode/ 0.1 V vs. Ag/AgCl Os(bpy)2Cl2 (included in the electrode matrix)... 

C.A.B. Garcia, G. de Oliveira Neto and L.T. Kubota, New fructose biosensors utilizing a polypyrrole film and D-fructose 5-dehydrogenase immobilized by different processes, Anal. Chim. Acta., 374(2-3) (1998) 201-208. 

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