Purification and Biochemical Characterization of pH Tolerant and Acid Stable α-amylase from Aspergillus oryzae JGI 21 Isolated from Soil.

This paper describes the purification and characterization of a novel acid stable and pH tolerant α-amylase from a Aspergillusoryzae JGI 21 isolated from Mangalore. The enzyme displayed a molecular weight of 22 kDa and it was stable over a broad range of acidic and alkaline pH with maximum activity and stability at 6.5. The optimum temperature of enzyme stability was found to be around 24+/-2°C. The purification of α-amylase by ammonium sulphate precipitation and ion-exchange chromatography resulted in 23.56 fold increase in its activity (100.38 U/mg protein). Considering its promising properties, this enzyme can find potential applications in the food industry as well as in laundry detergents. [ABSTRACT FROM AUTHOR]