Extraction and purification of α-amylase from gastrointestinal tract of Cyprinus carpio

This study included the extraction and purification of α-amylase from the gastrointestinal tract of fish using several stages involved, raw extract (crude), sedimentation with ammonium sulphate with different saturation rates, dewatering and gel filtration by the Sephadex G100 gel. These processes were conducted under various conditions to find optimum pH and temperature of activity and enzymatic stability as well as determination of kinetic constants. The study also included estimation the molecular weight of the extracted enzyme according to the standard curve of the known molecular weight proteins. Results showed that the specific efficiency, enzymatic yield and the molecular weight of the enzyme were 1166.6 enzymatic units mg⁻¹ of extracted solution, 12.3% and 52.8 kg Dalton respectively. The ideal temperature was 70 C° and the optimum pH ranged from 6.5 to 7.5. The maximum activity of the enzymatic interaction was 75.78 micromole min⁻¹ respectively. The study aimed to purify and identify the alpha-amylase from the residual fish's intestines, as an available source to use it for preparing food and medical substances to improve human health.