PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR PHYTASE FROM ASPERGILLUS SPECIESM. PUGALENTHI AND V. VADIVEL
In the present study, the phytase enzyme producing potential of five different Aspergillus species was analyzed. The extracted phytase enzyme was purified by DEAE cellulose column chromatography and the enzyme activity was measured by using the synthetic substrate p- nitro phenyl phosphate (PNPP). The partially purified enzyme exhibits maximum activity at the optimum pH (5- 6), temperature (50- 90°C) and substrate concentration (1.0- 2.5 mg/ml) under standard assay conditions. Among the five different Aspergillus species examined, A. niger registers the highest production of phytase enzyme with maximum enzyme activity. The characteristics of the partially purified enzyme such as optimum pH and temperature are also favourable for the industrial applications. Supplementation of such microbial enzymes in the diets of monogastrics will enhance the bioavailability of phosphorous to the growing animals.
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