Biochemical characterization of phytase purified from Aspergillus niger S2.

Background: Phytic acid is the large reservoir of phosphorous of plant origin feed of monogastric animals. These animals are incapable of metabolizing phytic acid due to lack of phytase enzyme production. Phytases are a group of enzymes which are involved in hydrolyzing phytic acid and releasing inorganic phosphate Microorganisms are the main sources of phytases especially purified from filamentous fungi Aspergillus nigerS2. Materials and Methods: In the present study, a three step purification study of phytase from Aspergillus niger S2 was done by using Sephadex G-50. The active fractions pooled after chromatography step was used for molecular mass determination through sodium dodecyl sulphatepoly acrylamide gel electrophoresis (SDSPAGE). Phytase activity was determined at different pH between 3.0 and 8.0. The effect of temperature on enzyme activity was studied of temperature range of 30-60 °C. The action of the enzyme on several phosphorylated substrates was tested at concentrations of 3mM. The phytase enzyme function was tested on digestion of plant material. Results: The molecular mass of A. niger phytase S2was also found to be 50kDa. The enzyme showed optimal pH at 5.0. The enzyme showed maximum activity at 400C. The enzyme showed high substrate affinity towards sodium phytate. The purified enzyme activity on digestion of grass and hay showed positive results with increased protein content, reducing sugar and phosphate. Conclusion: The purified enzyme of the present study with these specifications can able to play a vital role in feed industry as a feed supplement in order to metabolize phytic acid and hence reduce soil pollution and eutrophication. [ABSTRACT FROM AUTHOR]