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).
haggar, O. (2019). Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270. Arab Journal of Nuclear Sciences and Applications, 52(2), 94-102. doi: 10.21608/ajnsa.2019.3804.1090
MLA
ola ahmad haggar. "Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270", Arab Journal of Nuclear Sciences and Applications, 52, 2, 2019, 94-102. doi: 10.21608/ajnsa.2019.3804.1090
HARVARD
haggar, O. (2019). 'Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270', Arab Journal of Nuclear Sciences and Applications, 52(2), pp. 94-102. doi: 10.21608/ajnsa.2019.3804.1090
VANCOUVER
haggar, O. Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270. Arab Journal of Nuclear Sciences and Applications, 2019; 52(2): 94-102. doi: 10.21608/ajnsa.2019.3804.1090
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