Stabilisation of β-glucosidase entrapped in alginate and polyacrylamide gels towards thermal and proteolytic deactivation
✍ Scribed by Natividad Ortega; Maria D. Busto; Manuel Perez-Mateos
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1998
- Tongue
- English
- Weight
- 232 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0268-2575
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✦ Synopsis
b-D-Glucosidase was immobilised by entrapment in two di †erent matrices (calcium alginate and polyacrylamide gels), in order to compare how the immobilisation could stabilise the enzyme towards thermal and proteolytic deactivation. While the enzyme trapped in polyacrylamide gel showed an optimum temperature for activity at 10¡C lower than that of the free enzyme, the optimal temperature after immobilisation in alginate beads was not altered (60¡C). The immobilisation of enzyme in alginate beads caused a larger increase in the thermal stability than the entrapment in polyacrylamide gels. The stabilisation factors obtained as 55, 60 and 65¡C for b-glucosidase immobilised in alginate and polyacrylamide gels were 2É03, 3É06, 2É19 and 2É04, 0É35, 1É01, respectively. In contrast, the b-glucosidase immobilised in polyacrylamide gels was more resistant in proteolysis than that trapped in alginate beads.