Entrapment of porous and stable concanavalin A–peroxidase complex into hybrid calcium alginate–pectin gel
✍ Scribed by Mahreen Matto; Qayyum Husain
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2006
- Tongue
- English
- Weight
- 140 KB
- Volume
- 81
- Category
- Article
- ISSN
- 0268-2575
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Ammonium sulfate‐fractionated proteins of turnip (Brassica rapa) were used for the simultaneous purification and immobilization of peroxidase by using crude jack bean extract. The concanavalin A–turnip peroxidase complex retained nearly 70% of the original activity. Calcium alginate–pectin‐entrapped soluble turnip peroxidase and the concanavalin A complex of peroxidase retained 63% and 52% of the original activity, respectively. The concanavalin A–peroxidase complex, the alginate–pectin‐entrapped soluble peroxidase and the alginate–pectin‐entrapped concanavalin A–peroxidase complex showed very high stability against denaturation mediated by heat, pH, urea, organic solvents and detergents. The exposure of soluble and immobilized turnip peroxidase to trypsin resulted in an enhancement of the peroxidase activity. The concanavalin A–peroxidase complex entrapped preparation was markedly more stable as compared with the directly entrapped soluble enzyme preparation. The results suggested that such preparations have great potential in the construction of bioreactors to be used for the remediation of aromatic compounds present in polluted wastewater/industrial effluents. Copyright © 2006 Society of Chemical Industry