Purification and characterization of extracellular amylolytic enzyme from Aspergillus species

Abstract

In the present study, the amylase enzyme producing potential of four different Aspergillus species was analyzed. The extracted amylase enzyme was purified by diethyl amino ethyl (DEAE) cellulose and Sephadex G-50 column chromatography and the enzyme activity was measured by using synthetic substrate starch. The partially purified enzyme exhibits maximum activity at the optimum pH (7.0), temperature (60 to 70°C) and substrate concentration (1.5 to 2.0%) under standard assay conditions. Among the four different Aspergillus species examined, Aspergillus flavipes showed maximum production of amylase. The characteristics of the partially purified enzyme such as optimum pH and temperature were also favourable for industrial applications.

Keywords: Aspergillus species, Sephadex G-50, column chromatography, diethyl amino ethyl (DEAE) cellulose