Abstract
Abstract The study included purification of pepsin enzyme EC: 3.4.23.1 that produced by using a mixed inoculum consisting of Staphylococcus sciuri and Pythium sp. and using the whey as a local carbon source obtained from a previous study. Pepsin was purified first by using salts of ammonium sulphate with saturation rates ranging between (30–80)%, and then the process of dialysis with distilled water, the process was performed with distilled water and the process of purification of the enzyme was completed using the DEAE-Cellulose ion exchange column and then the gel filtration using the Sephadex G-300 column. The enzymatic activity was 1.998 U/ml at 3.714 times, with 39.1%. The optimal pH for the partially purified pepsin was 3.0 and the optimal temperature for t pepsin activity was 35 Co and 5% of casein.
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