Isolation, Purification and Characterization of Asparaginase from Aspergillus Species

Abstract

The L-asparaginase enzyme was purified to homogeneity from Asparaginase has been purified from Aspergillus terreus and Aspergillus niger that were grown under submerged fermentation. Different purification steps (including Ammonium sulfate fractionation dialysis and column chromatography) were applied to the crude culture filtrate to obtain a pure enzyme preparation. In SDS PAGE, both enzymes migrated as polydisperse aggregates yielding broad and diffused bonds. These two fractions yielded one band corresponding to a molecular weight range from above 94 KDa (Asparaginase). The enzyme exhibited distinctly under different pH and temperature profiles.  The optimum pH and temperature for asparaginase were found to be 7 and 35°C respectively. Such as Asparaginase  is 503.3, 303.3 U/ml and 3.6%, 4.21% respectively.  Hence the purified enzyme will be used in industrials applications as well as clinical trails.