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Modifications glucose oxidase

Seymom-, S.L. and Klinman, J.P. (2002). Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase the relationship of modification of the protein envelope to C-H activation and turmeUng. Biochemistry 41, 8747-8758... [Pg.76]

Figure 12.7 (a) Modification of glucose oxidase with a polymerizable thioaniline functionality,... [Pg.345]

L. Q. Chen, X.E. Zhang, W.H. Xie, Y.F. Zhou, Z.P. Zhang and A.E.G. Cass, Genetic modification of glucose oxidase for improving performance of an amperometric glucose biosensor, Biosens. Bioelectron., 17 (2002) 851-857. [Pg.545]

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. [Pg.73]

Retama JR, Lopez-Ruiz B, Lopez-Cabarcos E (2003) Microstructural modifications induced by the entrapped glucose oxidase in cross-linked polyacrylamide microgels used as glucose sensors. Biomaterials 24 2965-2973... [Pg.162]

Enzyme Assay Procedure. The catalytic potency of the immobilized g-galactosidase was determined in a plug flow reactor ( 9). Glucose liberated by the catalytic activity of 3-galactosi-dase on lactose was determined by the glucose oxidase-chromogen method (21 ) with some modifications. [Pg.211]

Fig. 1.12. Schematb drawing of the glucose oxidase molecule, showing the electron-transfer distances involved in the various steps of moving an electron from its two flavin adenine dinucleotide/reduced flavin adenine dinucleotide (FAD/FADHg) centers to a metal electrode. Left The enzyme before modification. Right The modified enzyme, after chemical attachment of an array of electron transfer relays ( R ). (Reprinted from Y. Degani and A. Heller, J. Phys. Chem. 91 1286, 1987.)... Fig. 1.12. Schematb drawing of the glucose oxidase molecule, showing the electron-transfer distances involved in the various steps of moving an electron from its two flavin adenine dinucleotide/reduced flavin adenine dinucleotide (FAD/FADHg) centers to a metal electrode. Left The enzyme before modification. Right The modified enzyme, after chemical attachment of an array of electron transfer relays ( R ). (Reprinted from Y. Degani and A. Heller, J. Phys. Chem. 91 1286, 1987.)...

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