Enzymatic and electrochemical reactions of xanthine oxidase immobilized on carbon materials.
An optimum way of immobilizing xanthine oxidase on graphite was found where a redox transformation of the enzyme was observed. The nature of the redox maxima was hypothesized on the basis of the dependence of the half-wave potential (Ep/2) on the pH of the solution. The enzymatic activity of xanthine oxidase adsorbed on two kinds of soot was studied by the oxidation of xanthine. The kinetic and activation parameters of the enzyme reaction were determined.
Horozova
E
E
Department of Physical and Theoretical Chemistry, University of Plovdiv, Bulgaria.
Dimcheva
N
N
Jordanova
Z
Z
D000327:Adsorption; D000818:Animals; D002244:Carbon; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D008892:Milk / Q000201:enzymology*; D010084:Oxidation-Reduction; D011199:Potentiometry / Q000379:methods; D013816:Thermodynamics; D014969:Xanthine Oxidase / Q000378:metabolism*
D004800:Enzymes, Immobilized; D002244:Carbon; D014969:Xanthine Oxidase