AbstractGlucose oxidase and peroxidase were immobilized individually or simultaneously on aminated latex particles by using sodiummeta‐periodide and borohydride. The amount of immobilized enzymes and their activity depended on the surface potential of particles and the surface density of their own, respectively. In the simultaneous immobilization of two enzymes, the predominant immobilization of peroxidase is attributed to higher carbohydrate content in peroxidase compared with that in glucose oxidase. Simultaneously immobilized enzymes worked better in the determination of glucose than the mixture of separately immobilized ones because of the close proximity of the two enzyme
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