The latex of Carica papaya is a rich source of the cysteine endopeptidases, including papain, glycyl endopeptidase, chymopapain and caricain , which as well as several parasitic proteases among of the papaya endopeptidases. The widely used term protease is synonymous with peptidase. Peptidases comprise two groups of enzymes: the endopeptidases and the exopeptidases, which cleave peptide bonds at points within the protein and remove amino acids sequentially from either N or C-terminus respectively. Purification of papain from papaya latex has traditionally been achieved by precipitation methods, the solubility of protein depends on, among other things, the salt concentration in the solution. At low concentrations, the presence of salt stabilizes the various charged groups on a protein molecule, thus attracting protein into the solution and enhancing the solubility of protein. However, the purified enzyme still remains contaminated with other proteases. An alternative purification strategy has involved the use of various chromatographic techniques including ion exchange, covalent, or affinity chromatography, but here the initial processing of the latex is essential before samples can be applied on a chromatography column.