PURIFICATION AND SOME PHYSICOCHEMICAL CHARACTERISTICS OF AMYLASE FROM THE HEPATOPANCREAS OF GIANT AFRICAN SNAIL (Archachatina marginatat

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.