A general method for immobilization of glycoproteins on regenerable immobilized metal-ion carriers: application to glucose oxidase from Penicillium chrysogenum and horseradish peroxidase.
A general method for immobilization of glycoproteins on immobilized metal-ion carriers is described. The method includes oxidation of the carbohydrate moiety of the glycoprotein with potassium periodate, covalent modification with histidine and immobilization on bivalent metal ion-iminodiacetic acid-agarose. The method is exemplified with horseradish peroxidase and glucose oxidase from Penicillium chrysogenum. The modified and immobilized enzymes are stable for at least 2 months at 4 degrees C. The immobilized enzymes were used as enzyme electrodes for the determination of the glucose concentration.
Chaga
G
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Department of Biochemistry, Uppsala University, Sweden.
D015374:Biosensing Techniques; D004800:Enzymes, Immobilized; D005949:Glucose Oxidase / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D010408:Penicillium chrysogenum / Q000201:enzymology*
D004800:Enzymes, Immobilized; D006023:Glycoproteins; D008670:Metals; D005949:Glucose Oxidase; D006735:Horseradish Peroxidase