EXTRACTION, PURIFICATION AND CHARACTERIZATION OF CAMELS PEPSIN (Camelus dromedarius
Abstract
ABSTRACTThe results of the current study revealed that chymosen and pepsin are themajor enzymes constituents of the camel aqueous abomasal homogenates.Enzymes were precipitated with ammonium sulphate at 35-80% saturation, andfurther purification involved chromatography on DEAE cellulose-32 and gelfiltration on Sephadex G-100. Three activity peaks (P1, P2 and P3) were elutedat 0.24, 0.43 and 0.54 M NaCl, and P2 and P3 completely inactivatedribonuclease confirming that they are pepsin (A and B), whereas P1 showedvery little activity indicating that it is chymosin. In addition to that, the milkclotting activity was distributed in order of 11.62, 52.98 and 35.40% forchymosin, pepsin A and B, respectively. Pepsin A and B had molecular weightapproximate 35000 and 36500 Dalton respectively. Also, pepsins are notglycoproteins, but contained 0.7 and 1.1 mol of organic phosphate per 1 mol ofprotein, for pepsin, A and B respectively. The results also showed that bothisoenzymes neither serin or thiol nor metallo proteases, and tyrosine may notparticipating at the active site of the pepsins.Key words: Camel pepsin, Purification, Camelus Dromedarius.
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