Abstract.
The structures of the blend membrane of regenerated silk fibroin and glucose oxidase were investigated by means of FT-IR spectra, electronic absorption spectra and SEM. The structures of the membranes were partly transferred from silk I to silk II after the membrane had been treated with ethanol. It was found that the glucose oxidase in the membrane existed in molecular aggregates and the blend membrane had an islands sea structure. p-Benzoquinone in solution was employed to speed up the electron transfer between glucose oxidase in a regenerated silk fibroin membrane and a glassy carbon electrode. The effects of pH, temperature, concentration of p-benzoquinone and applied potential on the sensor were examined. The major advantage of water dispersed regenerated silk fibroin is its ability to immobilize the enzyme without any significant loss of enzymatic activity.
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Received: 26 January 1995 / Revised: 15 March 1995 / Accepted: 22 March 1995
Acknowledgements. This work is supported by the National Science Foundation of China and the Electroanalytical Chemistry Open Laboratory of Changchun Institute of Applied Chemistry, Chinese Academy of Sciences.
Correspondence to: J. Deng
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Qian, J., Liu, Y., Liu, H. et al. Characteristics of regenerated silk fibroin membrane in its application to the immobilization of glucose oxidase and preparation of a p-benzoquinone mediating sensor for glucose. Fresenius J Anal Chem 354, 173–178 (1996). https://doi.org/10.1007/PL00012725
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DOI: https://doi.org/10.1007/PL00012725