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Separate or simultaneous immobilization of glucose oxidase and peroxidase on latex particles and their function
Author(s) -
Kawaguchi Haruma,
Koiwai Naoko,
Ohtsuka Yasujii
Publication year - 1988
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1988.070350315
Subject(s) - glucose oxidase , peroxidase , chemistry , enzyme , immobilized enzyme , sodium borohydride , chromatography , biochemistry , catalysis
Glucose oxidase and peroxidase were immobilized individually or simultaneously on aminated latex particles by using sodium meta ‐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 enzymes.