Abstract
Bovine liver catalase was entrapped in polyacrylamide (G1), poly(sodium acrylate) (G2) and poly(acrylamide-co-sodium acrylate) (G3) gels crosslinked with N, N′-methylenebisacrylamide. The percentage of entrapment was found to be about 85%. The enzyme immobilized in G1 has very low activity; enzyme in G3 exhibits the highest activity. The influences of the support matrix on the pH and thermal stability of the immobilized catalase were also examined. It was found that catalase immobilized in G2 and in G3 has a higher stability than free catalase and catalase in G1 at low pH. On the other hand, there is no marked improvement in the thermal stability of the immobilized catalase.
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