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A general method for immobilization of glycoproteins on regenerable immobilized metal‐ion carriers: application to glucose oxidase from Penicillium chrysogenum and horseradish peroxidase
Author(s) -
Chaga G.
Publication year - 1994
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1994.tb00306.x
Subject(s) - glucose oxidase , chemistry , potassium periodate , horseradish peroxidase , penicillium chrysogenum , immobilized enzyme , peroxidase , agarose , chromatography , metal ions in aqueous solution , covalent bond , biochemistry , thermostability , sodium periodate , enzyme , metal , organic chemistry , catalysis
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.