Partial Purification of Amylase from the Culture Filtrates of Aspergillus flavus Grown on Cassava Peels

Abstract

Amylase from a Cassava peel culture of Aspergillus flavus was partially purified by Ammonium Sulphate precipitation as well as dialysis. The dialysed 60% (NH4)2 SO4 precipitated enzyme had an activity of 1.087 mg T.R.S released/ min/mg protein which was two folds of the activity of the crude culture filtrate. Hydrogen ion concentration as well as temperature had profound influence on enzyme activity of the partially purified enzyme while Amylase activity increased progressively as pH was increased from 3 to 7 reaching a maximum of 1.68 mg T.R.S released/min/mg/protein at PH 7.0. A rapid decrease in amylase activity was observed as pH was increased from 7 to 9 while the amylase activity increased with increase in temperature from 300C to 450C and reached a maximum of 1.15 mg T.R.S. released/min/mg/protein at 450C. Subsequent increase in temperature resulted into decrease in activity of the amylase enzyme.