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Preparation and Properties of Asparaginase Entrapped in the Lattice of Polyacrylamide Gel

Department of Biochemistry, Research Laboratory of Applied Biochemistry, Tanabe Seiyaku Co., Ltd., Kashima-cho, Higashiyodogawa-ku, Osaka, Japan

Immobilization of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) was investigated by lattice entrapment using hydrophilic polyacrylamide gel. As a result, about a 30% yield of immobilized asparaginase was obtained.

The optimum pH of the immobilized asparaginase shifted by 1 pH unit to the acid side in comparison with that of native enzyme. The apparent Michaelis constant of immobilized enzyme was about 200 times higher than that of the native enzyme. The immobilized asparaginase was found to be stable during continuous operation and to be resistant to attack by proteolytic enzymes. L-Asparagine in blood was completely decomposed by the immobilized asparaginase column.

Received 1/25/74. Accepted 6/26/74.