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Rotating disc electrode characterization of immobilized glucose oxidase

✍ Scribed by Susan R. Mikkelsen; R.Bruce Lennox

Publisher
Elsevier Science
Year
1991
Tongue
English
Weight
669 KB
Volume
195
Category
Article
ISSN
0003-2697

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✦ Synopsis

The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose Km for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design.

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