The objective of the research was to study the purification and partial characterization of thermostable α-amylase from the newly isolated Acremonium sporosulcatum. The enzyme was purified in a biphasic system and involving ammonium sulfate precipitation and sephadexG-100 gel through ion exchange chromatography. The enzyme was shown to 58kDa by sodium dedecyl sulfate poly acrylamide gel electrophoresis and was purified 2.1 fold with a yield of 50.74%, it was stable between pH 6.8 and 8.4. This enzyme was almost 100% stable at 50°C even after the activity was decreased gradually. Influence of metal ions such as Fe2+, Zn2+, Cu2+ and Ca2+ are involved in the maximum production. Increasing the concentration of CaCl2 and H3Bo4 inhibited the α-amylase. The substrate specificity of the enzyme on soluble starch, glycogen and dextrin were could stabilize the enzyme.
α-amylase, Acremonium sporosulcatum, and enzyme purification stapes, Metal ions
