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  • Title: Covalent immobilization of invertase and horseradish peroxidase on concanavalin A-Seralose via carbohydrate moieties.
    Author: Husain S, Jafri F.
    Journal: Biochem Mol Biol Int; 1995 Jul; 36(3):669-77. PubMed ID: 7549967.
    Abstract:
    Invertase from Baker's yeast (Saccharomyces cerevisiae) and Horseradish peroxidase (HRP) were covalently immobilized on Concanavalin A precoupled to Seralose via carbohydrate moieties. Covalent coupling of glycoenzymes was achieved by periodate induced aldehydic groups of glycosyls with amino groups of Concanavalin A, at different pH values. A bifunctional reagent such as glutaraldehyde crosslinks the glycoenzymes with lectin both intra and intermolecularly. Therefore, attempts were made to introduce covalent linkages between glycoenzymes and Concanavalin A-Seralose without intramolecular crosslinking in either. The immobilized preparations of glycoenzymes exhibited high yield of immobilization and eta value. About 90 and 85% covalent coupling could be observed in invertase and HRP at pH 7.0 respectively, as determined by treatment with 0.5 M methyl alpha-D-mannopyranoside. All immobilized glycoenzyme preparations exhibited marked stabilization towards thermal inactivation.
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