Abstract
A procedure was studied to obtain a covalent attachment of glucose oxidase (GOD) to the surface of amorphous AlPO4 used as support. Immobilization of the enzyme is carried out through the e-amino group of lysine residues through an aromatic Schiff’s-base. The enzymatic activities of native and immobilized GOD systems were obtained in the oxidation of β-D(+)-glucose to D-gluconic acid. In different experiments the percentage of immobilized enzyme was in the range 50-90 % while the percentage of catalytically active immobilized enzyme was always near 90 %. Moreover, GOD immobilization increased its efficiency and operational stability when repeatedly used with respect to soluble enzymes.
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