الفهرس 
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Abstract
The aims of the present work was to purify protease enzyme from the red seaweed Pterocladia capillacea. Protease was purified by 70 % ammonium sulfate and Sephadex G-200. The specific activity was 170units mg-1 protein and with 14.2 fold. The optimal casein concentration was 40% (w/v). The Km and Vmax values were 6.1 % (w/v) and 36.36 units mg-1protein.The final incubation time was 40 min. The optimal pH and optimal temperature were 7 and 40ºC. Ca+2 and Mg+2 were the best activator divalent cations. The other cations Hg2+, Cu2+, Al3+, Co2+ and Zn2+were inhibitors. Protease was activated by the amino acids cysteine and methionine. However, protease was activated by reduced glutathione, thiourea, thioglycolate, and acetyl cysteine. Method &Results: Protease was purified using ammonium sulfate and Sephadex G-200 the specific activity increased to 172 units mg-1 protein. The optimum time was 40 min. The enzyme activity increased with increasing the temperature up to 40ºC. Km value was calculated and it was 6.1 % (w/v) and Vmax was 36.36 mM/min. The optimal casein concentration was 40% (w/v). Protease was activated by the amino acids cysteine and methionine. Sarcosine and Sorbitol can protected the enzyme at 60ºC. Calcium alginate-immobilized protease and chitosan-immobilized protease expressed appreciable activities throughout 6 cycles. Compatibility of purified protease with the various detergents including Tide, Persil, and Ariel. Purified protease succeeded in hydrolysis of cow meet. Conclusion: from this study we recommended to use the enzyme in some biotechnological application such as:1- Compatibility of the immobilized protease with detergents for laundry purposes. 2-Digestion of cow meat by purified protease. 3- Milk- coagulation by purified algal protease. 4-Hydrolysis of blood clot by purified algal protease.