期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 114, 期 9, 页码 3380-3386出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp912203d
关键词
-
资金
- National Natural Science Foundation of China (NSFC) [20975015, 20775009]
The lectin protein concanavalin A (Con A) and the glycoenzyme horseradish peroxidase (HRP) were assembled into {Con A/HRP}(n) layer-by-layer Films on electrodes mainly by biospecific affinity between them. The cyclic voltammetric (CV) response of ferricyanide (Fe(CN)(6)(3-)) at (Con A/HRP)(n) film electrodes was very sensitive to the environmental pH. The peak Currents of Fe(CN)(6)(3-) were quite large at pH 4.0 but greatly suppressed at pH 9.0, demonstrating reversible pH-sensitive on-off behavior. This property could be used to realize pH-controlled electrochemical reduction of H2O2 catalyzed by HRP immobilized in {Con A/HRP}(n) films and mediated by Fe(CN)(6)(3-) in solution. The modulation of the solution pH was also realized by in situ biochemical reactions with various enzymes in solution and was used to tune the pH-switchable bioelectrocatalysis. The possible mechanism of the pH-responsive on-off behavior of the films toward the probe was explored, and the electrostatic interaction between the films and the probe is believed to play a key role in deciding the pH-sensitive behavior of the films. This smart interface may be used to establish a foundation for fabricating novel pH-controllable electrochemical biosensors based on bioelectrocatalysis with immobilized enzymes.
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