MOLECULAR CHARACTERIZATION OF CRUDE ENZYMATIC EXTRACT FROM ALGERIAN CAMEL ABOMASUM (CAMELUS DROMEDARIUS)

Authors

  • Souad ISSELNANE Laboratoire de recherche de Biochimie Analytique et Biotechnologies (LABAB), Université Mouloud Mammeri de Tizi Ouzou, 15 000, Algérie
  • Saliha BOUDJENAH-HAROUN Université Ouargla, Faculté des Sciences de la Nature et de la Vie, Laboratoire de Recherche sur la Phoeniciculture,Ouargla 30000,Algérie
  • Abdelwahab NOUANI Laboratoire de Technologie Alimentaire, Université M’Hamed Bouguera, Boumerdes, 35 000, Algérie
  • Saliha SI AHMED-ZENNIA Laboratoire de recherche de Biochimie Analytique et Biotechnologies (LABAB), Université Mouloud Mammeri de Tizi Ouzou, 15 000, Algérie
  • Belaid BOUAZZA Laboratoire de recherche de Biochimie Analytique et Biotechnologies (LABAB), Université Mouloud Mammeri de Tizi Ouzou, 15 000, Algérie
  • Benalia YABRIR Laboratoire d’exploration et valorisation des Ecosystèmes steppiques, Université de Djelfa, Algérie
  • Abderrahmane MATI Laboratoire de recherche de Biochimie Analytique et Biotechnologies (LABAB), Université Mouloud Mammeri de Tizi Ouzou, 15 000, Algérie

DOI:

https://doi.org/10.9755/ejfa.2015-07-490

Keywords:

abomasum, chromatography, dromedary, electrophoresis, milk clotting enzyme

Abstract

Camel milk cannot be coagulated with bovine chymosin, most likely due to major variations between the primary k casein structures of the two species. Recently we have shown that the crude gastric extracts (CGE) from adults’ dromedaries provide satisfactory milk clotting activity and limited proteolytic activity towards the camel milk. In the present study, we have isolated and characterized the CGE from dromedary abomasum. The CGE was separated and purified by DEAE-Cellulose column chromatography and Sephacryl S200 gel filtration. From various collected fractions, we characterized two fractions (F3 and F5) presenting a milk clotting activity and were eluted at 0.1 M and 0.45 M NaCl respectively. Interestingly, the F5 fraction had the highest milk clotting activity. The purified enzyme was resolved as a single protein band on SDS-PAGE with a molecular weight estimated about 38 kDa which was not affected by the addition of β-mercaptoethanol. In native PAGE, the enzyme migrated as a single band having a high intensity with similar electophoretic mobility to that of porcine pepsin. Using two dimensional electrophoresis, we found that the band obtained from the native-PAGE was concentrated on a single spot, quite intense.

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Published

2017-11-04

How to Cite

ISSELNANE, S., S. BOUDJENAH-HAROUN, A. NOUANI, S. S. AHMED-ZENNIA, B. BOUAZZA, B. YABRIR, and A. MATI. “MOLECULAR CHARACTERIZATION OF CRUDE ENZYMATIC EXTRACT FROM ALGERIAN CAMEL ABOMASUM (CAMELUS DROMEDARIUS)”. Emirates Journal of Food and Agriculture, vol. 28, no. 3, Nov. 2017, pp. 217-23, doi:10.9755/ejfa.2015-07-490.

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