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In the present study, amylase was produced using submerged fermentation technology from Bacillus ARF. The enzyme was purified to 5.9 folds as compared to crude enzyme extract by using 40% ammonium sulfate. The temperature and pH at which amylase showed maximum activity were found to be 50 ˚C and 7.0, respectively. The time course for enzyme substrate reaction was 20 minutes. The kinetic studies of amylase revealed the Km and Vmax values as 5.73 mg/mL and 2437 U/mL/min respectively. Different metal ions were tested for their stimulatory or inhibitory effects on amylase activity, among which, K+ was found to be the activator of enzyme at 1mM concentration, whereas the enzyme was inhibited in the presence of Hg2+, Mg2+, Cd2+, Ba2+ and Na+ . Enzyme activity was found almost unchanged in the presence of Ca2+ .
Riaz Aliya, Ahmad Sana, Gilani Rida, Siddiqui Ayesha. (2020) PARTIAL PURIFICATION AND CHARACTERIZATION OF AMYLASE: AN IMPERATIVE CARBOHYDRASE FOR STARCH-BASED INDUSTRIES, , Volume 17, Issue 1.
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