Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270 | ||||
| Arab Journal of Nuclear Sciences and Applications | ||||
| Article 13, Volume 52, Issue 2, April 2019, Page 94-102 PDF (776.42 K) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/ajnsa.2019.3804.1090 | ||||
 View on SCiNiTO | ||||
| Author | ||||
ola ahmad haggar 
| ||||
| microbiology, Faculity of science El-azher university | ||||
| Abstract | ||||
| Purification of laccase enzyme by anion exchange chromatography using DEAE sepharose and sephacryl HR are successful in purifying laccase. The molecular weight of laccase was 75 KDa determined by SDS- PAGE. The optimum pH for activity was 5 and for stability was (6.5-7.5), the optimum temperature for activity was 35oC and stability of the enzyme was stable up to 55oC, the enzyme retained 100% of its activity after 20 minutes incubation, 85% of its activity after 1h incubation at the same temperature. The energy of activation (Eact) of the purified laccase between 20oC and 45oC at its optimum pH was 16.3 k Jmol-1. The apparent Km value of the enzyme for ABTS was estimated to be 1.4 mM under standard assay conditions, kcat value of ABTS was calculated to be 3450 min-1, Vmax is the maximum initial rate in the Michaelis- Menten equation (1.2 µmol L-1 min -1).Microencapsulation of laccase was exhibited that free laccase (35U/ml) has higher activity than encapsulated laccase (24.3 U/ml). | ||||
| Keywords | ||||
| : Laccase; Pleurotus ostreatus; Purification; properties; Microencapsulation | ||||
|
Statistics Article View: 356 PDF Download: 425 |
||||
