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Abstract Different topics are clarified in this chapter as follows: I. Proteolytic Enzymes I’ Proteolytic enzymes are considered as group of hydrolyzing enzymes that deal with hydrolysis of peptide bonds of protein and a small or large peptide. Some enzymes do not require an adjacent terminal carboxyl or amino group and may even be prevented from acting by such groups while others require such a free terminal group. The former termed endopeptidases which act in the middle of the peptide chain breaking protein molecules up into smaller fragments. The latter exopeptidases cannot hydrolyse link in the middle of the chain but some act fromthe carboxyl and other from the amino end of the chain.U? Endopeptidase and exopeptidase enzymes co-operate very effectively in protein digestion in which the main function of the former is to produce a large number of free ends at which the latter can act. On the other hand, the endopeptidases are divided into sub-sub group on the basis of the catalytic mechanism and enzyme active site as follows: 1- Serine - proteinases This group of enzymes are so named because they characterized by the possession of peculiarly reactive serine residue that is essential for their enzymatic activity. These enzymes differ greatly in the specificity of the reaction catalyzed but they all possess the common feature of being able to catalyze the hydrolysis of esters (2), All of this enzymes have an active and catalytically essential histidine as well as similar kinetic mechanism (2) , The catalytically essential histidine and serine are located at the substrate binding site together with invariant aspartic. |