Immobilization of catalase on crosslinked polymeric hydrogels—effect of anion on the activity of immobilized enzyme
✍ Scribed by Bo Jiang; Yong Zhang
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 345 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0014-3057
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✦ Synopsis
Bovine liver catalase was entrapped in polyacrylamide (GI), 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 GI 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 GI at low pH. On the other hand, there is no marked improvement in the thermal stability of the immobilized catalase.
📜 SIMILAR VOLUMES
Papain was immobilized on polymer supports with spacer arms of varying nature and length. As the length of the spacer arm increased, there was a marked increase in the extent of enzyme immobilization and activity of immobilized enzymes. When a long, flexible and hydrophilic polyethylene glycol space