[X-ray microanalysis of the activity of immobilized glucose oxidase on enzyme electrode].
The localization of activity of glucose oxidase (GOD) on the pussian blue modified electrode by SiO2 sol-gel was studied by X-ray microanalysis. Glucose and Ce(NO3)3 served as substrate and capture respectively. Substrate was catalysed by immobilized GOD toproduce H2O2, and the H2O2 was captured by Ce(NO3)3 to form precipitate. The precipitation deposited the active site of immobilized GOD on the enzyme electrode. The X-ray microanalysis showed that the distribution of active enzyme on the surface of the enzyme electrode was uniform, and the GOD immobilized maintained high activity. The X-ray analysis exhibited that the properties of the enzyme electrode depended on the distribution of enzyme activity on its surface from the view of microstructure, and the developed GOD electrode was of high sensitivity and excellent stability. The results agreed with the results of the electrochemical study.
Li
Tong
T
College of Chemistry and Environmental Science, Hebei University, Baoding 071002, China.
Yao
Zi-hua
ZH
Qui
Man-de
MD
AN
Wei
W
Shi
Da-gang
DG
D015374:Biosensing Techniques / Q000379:methods*; D002563:Cerium / Q000378:metabolism; D055664:Electrochemical Techniques; D004577:Electron Probe Microanalysis / Q000379:methods*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D012822:Silicon Dioxide / Q000737:chemistry; D013379:Substrate Specificity
D004800:Enzymes, Immobilized; C032786:cerium nitrate; D002563:Cerium; D012822:Silicon Dioxide; D006861:Hydrogen Peroxide; D005949:Glucose Oxidase; D005947:Glucose