| Abstract: | Extracellular α-amylase (EC 3.2.1.1) from Bacillus coagulans B 49 was purified to homogeneity by ion-exchange chromatography and gel filtration. The optimum pH and temperature for dextrinizing activity were 6–7 and 70°C and for saccharolytic activity were 7 and 60°C, respectively. Calcium inhibited α-amylase activity even at low concentrations (10 m
), and most of its activity could be restored by dialysis against EDTA. Other cations such as Mg2+, Fe2+, and Hg2+ also inhibited amylase activity, while Mn2+ exhibited a slight stimulatory effect. The activity of the enzyme was not affected by ethylenediaminetetraacetic acid (EDTA). |
