Glucose oxidase chemically modified

R.M. Ianniello, T.J. Lindsay, and A.M. Yacynych, Differential pulse voltammetric study of direct electron transfer in glucose oxidase chemically modified graphite electrodes. Anal. Chem. 54, 1098-1101 (1982). 

Figure 17.17 Schematic representation of a single-compartment glucose/02 enzyme fuel cell built from carbon fiber electrodes modified with Os -containing polymers that incorporate glucose oxidase at the anode and bilirubin oxidase at the cathode. The inset shows power density versus cell potential curves for this fuel cell operating in a quiescent solution in air at pH 7.2, 0.14 M NaCl, 20 mM phosphate, and 15 mM glucose. Parts of this figure are reprinted with permission from Mano et al. [2003]. Copyright (2003) American Chemical Society.

Y. Degani and A. Heller, Direct electrical communication between chemically modified enzymes and metal electrodes. I. Electron transfer from glucose oxidase to metal electrodes via electron relays, bound covalently to the enzyme. J. Phys. Chem. 91, 1285-1289 (1987). 

J. Pei and X. Li, Amperometric glucose enzyme sensor prepared by immobilizing glucose oxidase on CuPtC16 chemically modified electrode. Electroanalysis 11, 1266-1272 (1999). 

Wilner I, Heleg-Shabtai V, Blonder R, Katz E, Tao G. Electrical wiring of glucose oxidase by reconstitution of FAD-modified monolayers assembled onto Au-electrodes. Journal of the American Chemical Society 1996, 118, 10321-10322. 

Roth J. P Wincek R. Nodet G. Edmondson D. E. Mclntire W. S. Klinman J. P. Oxygen isotope effects on electron transfer to 02 probed using chemically modified flavins bound to glucose oxidase. J. Am. Chem. Soc. 2004, 126, 15120-15131. 

Figure 8.12 Schematic illustration of the layer-by-layer deposition on an Au electrode initially with positively charged poly(diallydimethylammonium) chloride (PDDA) and negatively charged poly(sodium 4-styrenesulfonate). Subsequent depositions entailed (I) PDDA-modified Prussian blue nanoparticles (P-PB), followed by (II) negatively charged glucose oxidase (GOx).55 (Reprinted with permission from W. Zhao et al., Langmuir 2005, 21, 9630-9634. Copyright 2005 American Chemical Society.) (See color insert.)...

Alternative Polymers for Immobilizing Bizymes. Vinyl acetate (after hydrolysis with bicarbonate) and polycarbonate have also been chemically modified to accommodate glucose oxidase (Donlan,A.M. Mcxx3y,G.J. Thomas,J.D.R., Uiiversity of Wales (Allege of Cardiff, unpublished data). 

All electrodes react with their environment via the surfaces in ways which will determine their electrochemical performance. Properly selected surface modification can effectively enhance the electrode heterogeneous catalysis property, especially selectivity and activity. The bulk materials can be chosen to provide mechanical, chemical, electrical, and structural integrity. In this part, several surface modification methods will be introduced in terms of metal film deposition, metal ion implantation, electrochemical activation, organic surface coating, nanoparticle deposition, glucose oxidase (GOx) enzyme-modified electrode, and DNA-modified electrode. 

Carbonaceous substrates (graphite and glassy carbon) are generally preferred because of their mechanical, chemical, and electrochemical properties. Excellent results are also obtained by chemically modified platinum (154,156,179) and tin(IV) oxide electrodes (155). For example, glucose oxidase has been successfully immobilized by cross-linking the enzyme with BSA and GA onto an electrochemically oxidized platinum surface, with silanization using 3-amino-propyltriethoxysilane ... 

Figure 3-5. (A) Assembly of reconstituted glucose oxidase on a PQQ-FAD monolayer linked to an Au-electrode. (H i Faradaic impedance spectra of the modified electrode at time intervals of reconstitution, (a) 0.1 h, (b) 0.25 h. (c) 0.5 h. (d) 1 h. (e) 2 h, (f) 4 h. Inset Interfacial electron transfer resistance of the modified electrode at time-intervals of reconstitution. (C) Cyclic voltammograms corresponding to the bioelectrocatalyzed oxidation of glucose, 80 mM, by the enzyme-functionalized electrode at time-intervals of reconstitution (a) 0 h, (b) 0.1 h, (c) 0.25 h, (d) 0.5 h, (e) 1 h, (f) 2 h, (g) 4 h. Inset Electrocatalytic currents transduced by the enzyme-modified electrode at time-intervals of reconstitution. Reproduced with permission from ref. 32. Copyright 2002 American Chemical Society.

ADP AFP ab as ALAT AP ASAT ATP BQ BSA CEH CK CME COD con A CV d D E E EC ECME EDTA EIA /e FAD FET FIA G GOD G6P-DH HBg HCG adenosine diphosphate a-fetoprotein antibody antigen alanine aminotranferase alkaline phosphatase aspartate aminotransferase adenosine triphosphate benzoquinone bovine serum albumin cholesterol ester hydrolase creatine kinase chemically modified electrode cholesterol oxidase concanavalin A coefficient of variation (relative standard deviation) layer thickness diffusion coefficient enzyme potential Enzyme Classification enzyme-chemically modified electrode ethylene diamine tetraacetic acid enzyme immunoassay enzyme loading factor flavin adenine dinucleotide field effect transistor flow injection analysis amplification factor glucose oxidase glucose-6-phosphate dehydrogenase hepatitis B surface antigen human chorionic gonadotropin... 

The mediators are bound to amino acids near the prosthetic group. For fixation of the relays the protein has to be unfolded and renatured after the chemical modification procedure. The small distance between the bound mediator molecules (maximum 1 nm) provides a very fast tunneling process. Enzyme electrodes employing glucose oxidase or lactate oxidase modified in this way operate like mediator-modified electrodes, without reagent addition. Owing to their favorable structure, such sensors respond to the analyte in less than... 

Degani, Y., Heller, A., Direct Electrical Conununication between Chemically Modified Enzymes and Metal Electrodes. 1. Electron Ttansfer from Glucose Oxidase to Metal Electrodes via Electron Relays, Bound Covalently to the Enzyme , J. Phys. Chem. 91 (1987) 1285-1289. 

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