Isolation and purification of extracellular phytase from Sporobolomyces japonicas (L9)
Keywords:Sporobomyces japonicus, phytase, specific activity, Ca2 , Mn2 , Km
Phytase of the yeast Sporobolomyces japonicus (L9), isolated from Cat Tien National Forest, was cultivated in modified YPD medium with activity of 2.720 UI/ml and optimal temperature and pH of 400C and 4.0. A suitable precipitation agent is ethanol 96% with specific activity of 312.924 UI/mg protein. Ca2+ ion with 1mmol/ml reduced enzyme activity to 97% and Mn2+ with 5 mmol/mlreduced enzyme activity to 98%. Specific activity for peak 1 was 187.942 UI/mg protein and for peak 2-286.388 UI/mg protein. Total specific activity increased 1.8 times before chromatography work. Recovery efficiency of protein was 95.05% and recovery activity - 90.75%. The Michaelis-Menten constant (Km) was 0.0313 µM. The purified phytase had a molecular weight of 36.90 kDa.