EXTRACTION, PURIFICATION AND CHARACTERIZATION OF CAMELS PEPSIN (Camelus dromedarius

	EXTRACTION, PURIFICATION AND CHARACTERIZATION OF CAMELS PEPSIN (Camelus dromedarius
Iraqi Journal of Biotechnology
Article 1, Volume 6, Issue 2, 2007, Pages 64-76
Abstract
ABSTRACT The results of the current study revealed that chymosen and pepsin are the major enzymes constituents of the camel aqueous abomasal homogenates. Enzymes were precipitated with ammonium sulphate at 35-80% saturation, and further purification involved chromatography on DEAE cellulose-32 and gel filtration on Sephadex G-100. Three activity peaks (P1, P2 and P3) were eluted at 0.24, 0.43 and 0.54 M NaCl, and P2 and P3 completely inactivated ribonuclease confirming that they are pepsin (A and B), whereas P1 showed very little activity indicating that it is chymosin. In addition to that, the milk clotting activity was distributed in order of 11.62, 52.98 and 35.40% for chymosin, pepsin A and B, respectively. Pepsin A and B had molecular weight approximate 35000 and 36500 Dalton respectively. Also, pepsins are not glycoproteins, but contained 0.7 and 1.1 mol of organic phosphate per 1 mol of protein, for pepsin, A and B respectively. The results also showed that both isoenzymes neither serin or thiol nor metallo proteases, and tyrosine may not participating at the active site of the pepsins. Key words: Camel pepsin, Purification, Camelus Dromedarius.
Keywords
Camel pepsin; Purification; Camelus Dromedarius

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