Production, Rapid Purification and Catalytic Characterization of Extracellular Phytase fromAspergillus Ficuum

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Abstract
A rapid purification scheme utilizing three chromatographic steps resulted in 6 fold purification of Aspergillus ficuum phytase (myo-inositol-hexakis-phosphate 3-phosphohydrolase, EC 3.1. 3.8). At pH 5.0 and 60°C the enzyme performed acceptably for 2.0 hr with only 30% diminished catalytic rate at the end. Substrate concentration exceeding 2nM was inhibitory. The inorganic orthophosphate, the product and a weak inhibitor, exhibited a Ki of 1.9 × 10−3M. The extracellular phytase has the potential for industrial use since it can be over produced, easily purified, remain catalytically active for a longer period and is not subjected to severe product inhibition.