A glucose oxidase inmobilized electrode based on modified graphite.
Glucose oxidase (E. C. 1.1.3.4) was immobilized on electrochemically modified graphite to obtain an enzyme electrode. The working surface of the electrode was coated with gelatine to prevent desorption of the enzyme. In substrate (glucose) solutions the amperometric signal of the enzyme electrode was due to the electroreduction of H202 generated in the enzyme layer. The linearity of the electrode response was found up to a substrate concentration of 300 microM at a working potential of 0 mV (vs. Ag/AgCl). It was shown that the electrode did not respond to L-ascorbic and uric acid at that working potential. The response time was about 2 min. The enzyme electrode keeps about 50% of its initial activity after a one-week storage at 4 degrees C.
Dimcheva
Nina
N
Department of Physical Chemistry, University of Plovdiv, Bulgaria.
Horozova
Elena
E
Jordanova
Zinaida
Z
D001205:Ascorbic Acid / Q000378:metabolism; D001234:Aspergillus niger / Q000201:enzymology; D004566:Electrodes; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004867:Equipment Design; D005947:Glucose / Q000378:metabolism; D005949:Glucose Oxidase / Q000378:metabolism*; D006108:Graphite; D006861:Hydrogen Peroxide / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D011199:Potentiometry; D013379:Substrate Specificity; D014527:Uric Acid / Q000378:metabolism
D004800:Enzymes, Immobilized; D014527:Uric Acid; D006108:Graphite; D006861:Hydrogen Peroxide; D005949:Glucose Oxidase; D005947:Glucose; D001205:Ascorbic Acid