Glucose oxidase was immobilized by electropolymerization into films of polyaniline, polyindole, polypyrrole, poly(o-phenylediamine), and polyaniline crosslinked with pphenylenediamine. The kinetics and the behavior of the entrapped enzyme toward elevated temperature, organic solvent denaturation, an
Reversible denaturation behavior of immobilized glucose oxidase
β Scribed by M. D. Gouda; M. S. Thakur; N. G. Karanth
- Book ID
- 111634210
- Publisher
- Springer-Verlag
- Year
- 2002
- Tongue
- English
- Weight
- 93 KB
- Volume
- 102-103
- Category
- Article
- ISSN
- 0273-2289
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## Abstract Studies have been performed in a tubular flow reactor to characterize the deactivation of immobilized glucose oxidase. The effects of oxygen concentration in the range of 0.09 to 0.467m__M__ and hydrogen peroxide concentrations in the range of 0.1 to 10m__M__ were studied. A simple math
Glucose oxidase has been immobilized onto a thin platinum strip, by co-crosslinking with bovine serum albumin and glutaraldehyde. The retention of redox characteristics of glucose oxidase has been verified by cyclic voltammetry. The activity of the immobilized enzyme reduces to a quarter of its valu