Catalase was entrapped in thermally reversible poly(isopropylacrylamide-co-hydroxyethylmethacrylate) (pNIPAM/HEMA) copolymer hydrogels. The thermoresponsive hydrogels, in cylindrical geometry, were prepared in an aqueous buffer by redox polymerization. It was observed that upon entrapment, the activ
Immobilization of α-chymotrypsin in thermally reversible isopropylacrylamide-hydroxyethylmethacrylate copolymer gel
✍ Scribed by H. Çiçek; A. Tuncel
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 297 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0887-624X
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✦ Synopsis
In this study, a-chymotrypsin was immobilized via physical entrapment within thermally reversible poly(isopropylacrylamide-co-hydroxyethylmethacrylate), poly(NIPAM-co-HEMA) copolymer gels. The thermoresponsive gel matrices in cylindrical geometry were prepared in an aqueous buffer medium by a redox polymerization method. The kinetic behavior of enzyme-gel cylinders was investigated in a batch reactor. The results indicated that the overall reaction rate was controlled by the substrate diffusion through the gel matrix. Due to the thermoresponsive character of the carrier gel, the maximum activity was achieved at 30ЊC with the enzyme-gel system while the free enzyme exhibited maximum activity at 40ЊC.
📜 SIMILAR VOLUMES
In this study, a-chymotrypsin was immobilized via physical entrapment within large, uniformly spherical, and thermally reversible poly(N-isopropylacrylamide) [poly(NIPAM)] beads. The gel beads were prepared in an aqueous dispersion medium by using Ca-alginate gel as the polymerization mold. In this
A temperature-responsive N-isopropylacrylamide (NIPAAm) oligomer with an ester functional end group and a molecular weight of 3300 was prepared by chain-transfer polymerization using b-mercaptopropionic acid and subsequently activated by N-hydroxysuccinimide (NHS). This oligomer was coupled to a-chy