Abstract:
P - Amylase (EC 3.2.1.2, a-I,4-D- glucanmaltohydrolase) obtained by acid treatment was
purified by Gel filteration and ion exchange chromatography. The homogeneity ofthe enzyme
was established by polyacrylamide gel electrophoresis. The pure enzyme yielded 26% while
the purification fold was 21. The optimum temperature was 60°C. The molecular weight was
estimated to be 46,000. The Michaelis-Menten constant, Km, was 3.3mg/ml while its
maximum velocity, Vmax was 2.00/1 mol/min/m\. The enzyme stability was examined with
MgS04, CaCh, and NaCI. Tryptic digest ind icated the presence of both cationic and anionic
peptides. The pH dependence of stability of the enzyme to temperature was studied at 50°C,
60°C and 70°e.
