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Functionalized κ-carrageenan/hyperbranched poly(amidoamine)for protease immobilization: Thermodynamics and stability studies.
- Source :
-
International Journal of Biological Macromolecules . Apr2020, Vol. 148, p1140-1155. 16p. - Publication Year :
- 2020
-
Abstract
- Hyperbranched polyamidoamine (PAMAM) has a high density of surface amino groups. This feature was exploited in the surface modification of κ-carrageenan gel beads for successful protease immobilization. The optimum PAMAM pH was at 2.1 and 9.3. However, treatment of κ-carrageenan gel beads at the higher pH showed re-usability for more than seven successive times. As a result of central composite design optimization, the maximum immobilization yield was obtained by soaking 8 U for 24 h. The comparative thermodynamics studies showed an enhancement in the thermal stability at high temperature for the immobilized protease as well as increased half-life time from 24.06 min to 79.95 min. Also, the D-values increased from 165.03 min to 548.23 min for free and immobilized enzyme, respectively. Moreover, the enzyme stability enhancement for the immobilized protease catalyst was accompanied with a remarkable increase in the enthalpy and in the free energy. Immobilized protease onto Carr-PAMAM gel beads can retain 89% of its initial activity and lost only 11% after 8 weeks of storage at 4 °C. Furthermore, an effective removal of silver from used X-ray film by the immobilized protease was achieved for six repeated cycles. Unlabelled Image [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01418130
- Volume :
- 148
- Database :
- Academic Search Index
- Journal :
- International Journal of Biological Macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 142107472
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2020.01.122