Immobilized d-Amino Acid Oxidase Preparation,Some Enzymatic Properties,and Potential Uses

Immobilization of d-amino acid oxidase was investigated by covalently binding the enzyme to cyanogen bromide activated polysaccharides. Among polysaccharides tested, Sepharose 6B was found to be the best carrier.

Some enzymatic properties of the immobilized enzyme were investigated and compared with those of the native enzyme. The optimum pH of the immobilized enzyme was shifted by 0.5 pH units to the acid side in comparison with that of the native enzyme. With regard to substrate specificity, heat stability and effect of temperature, no significant differences were observed between the immobilized and native enzymes.

The immobilized enzyme was conveniently used for a determination of d-amino acids and an analysis of optical purity of l-amino acids.