Abstract
The enzyme arginase, purified from bovine liver, was covalently immobilized by the glutaraldehyde method to the inner surface of Cuprophan hollow fibers of a conventional hemodialyzer with a surface 1.3 m3. The yield of the process was 0.3 μg/cm2 of active enzyme at physiological pH. The immobilization method did not adversely affect the physical and mechanical properties of hollow fibers neither their hemocompatibility. After sterilization with ethylene oxide, the bioreactor was able to metabolize five liters of 50 μM arginine solution at pH 7.4, in six hours.
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