Author： Vasudevan Palligarnai Como Karin
Publisher： Humana Press, Inc
ISSN： 0273-2289
Source： Applied Biochemistry and Biotechnology, Vol.128, Iss.2, 2006-02, pp. : 97-107
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Abstract
Catalase from bovine liver was covalently immobilized on hydrophilic polyurethane composite (CoFoam). The activity of the enzyme was assayed in the decomposition of H2O2 at pH 7.0 and 25°C. The effects of water-to-prepolymer ration the addition of a crosslinking agent, and the utilization of a spacer on enzyme, activity were examined. The results of immobilization of the enzyme in a large-scale unit are reported. The advantage of the CoFoam composite lies in the low drop in pressure in a packed-bed reactor at fairly large flow rates. For example, at flow rates of 10–12 L/min, the drop in pressure is typically 3 kPa. Enzymes immobilized on CoFoam represent a novel use as catalysts in packed-bed reactors owing to the low drop in pressure.
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