Electrochemical regulation of immobilized alkaline phosphatase activity

The activity of alkaline phosphatase (E.C. 3.1.3.1) immobilized on graphite electrodes varies with the electrode potential change ( U < 0 V). This is accounted for by the pH change at the surface of the working electrode caused by the electrochemical reduction of dissolved oxygen. The effects of...

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Bibliographic Details
Published in:Bioelectrochemistry and Bioenergetics 1986, Vol.16 (2), p.205-212
Main Authors: Kulys, J.J., Jasaitis, J.J., Razumas, V.J.
Format: Article
Language:English
Subjects:
alkaline phosphatase
immobilized enzymes
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Summary:The activity of alkaline phosphatase (E.C. 3.1.3.1) immobilized on graphite electrodes varies with the electrode potential change ( U < 0 V). This is accounted for by the pH change at the surface of the working electrode caused by the electrochemical reduction of dissolved oxygen. The effects of oxygen concentration, buffer concentration and the solution ionic strength on the electrochemical modulation of enzyme activity have been studied. A kinetic model of a conjugated electrochemical and enzymatic process which interpretes the observed processes is suggested.
ISSN:0302-4598
DOI:10.1016/0302-4598(86)85003-6