Preparation and Characteristics of a Enzyme Electrode Based on Immobilization of Tyrosinase in Electropolymerized Polypyrrole Film

Authors

Liu-shui YAN, Dept. of Chem., Shandong University, Jinan 250100, China;
Qia WEI, Dept. of Environmental and Chem. Eng., Nanchang Institute of Aeronautical Technology, Nanchang 330034, China;
Cheng-Yi WANG, Dept. of Environmental and Chem. Eng., Nanchang Institute of Aeronautical Technology, Nanchang 330034, China;
Rong-rong SHI, Dept. of Environmental and Chem. Eng., Nanchang Institute of Aeronautical Technology, Nanchang 330034, China;
Xiao-tong MA, Dept. of Environmental and Chem. Eng., Nanchang Institute of Aeronautical Technology, Nanchang 330034, China;

Corresponding Author

Liu_shui YAN

Abstract

A sensitive and stable amperometric enzyme electrode was constructed, based on the immobilization of tyrosinase in potentiostatically electropolymerized polypyrrole film at a platinum electrode. The influence of pH and potential on immbilization was discussed. SEM micrographs and CV curves of films obtained before and after incorparation of tyrosinase molecular were analyzed and compared each other. The enzyme electrode responds linearly to p-cresol over a concentration range of 5×10 -8 ～1×10 -6 mol/L with an optimum pH of 6.6, It exhibited kinetic characteristics of the typical enzyme-catalyzed reaction with an apparent Michaelis constant of 2.2 ×10 -5 mol/L.

Keywords

Tyrosinase, Polypyrrole, Electrochemical imobilization, Enzyme electrode Bioelectrochemical activity

DOI Link

https://doi.org/10.61558/2993-074X.1384

Publication Date

2000-05-28

Online Available Date

2000-05-28

Revised Date

2000-05-28

Received Date

2000-05-28

Recommended Citation

Liu-shui YAN, Qia WEI, Cheng-Yi WANG, Rong-rong SHI, Xiao-tong MA. Preparation and Characteristics of a Enzyme Electrode Based on Immobilization of Tyrosinase in Electropolymerized Polypyrrole Film[J]. Journal of Electrochemistry, 2000 , 6(2): 222-226.
DOI: 10.61558/2993-074X.1384
Available at: https://jelectrochem.xmu.edu.cn/journal/vol6/iss2/11

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