Development of the Purification Method of Ovotransferrin in Egg White

난백 내 Ovotransferrin의 분리방법에 관한 연구

  • Jang, A. (Korea Food Research Institute) ;
  • Jo, Y.J. (Department of Animal Science and Biotechnology, Seoul National University) ;
  • Lee, M. (Department of Animal Science and Biotechnology, Seoul National University) ;
  • Kim, J.C. (Department of Food and Life Sciences, Inje University)
  • 장애라 (한국식품연구원) ;
  • 조윤제 (서울대학교 동물생명공학전공) ;
  • 이무하 (서울대학교 동물생명공학전공) ;
  • 김재철 (인제대학교 식품생명과학부)
  • Published : 2005.12.31


This study was carried out to separate ovotransferrin in chicken egg white by gel chromatography and heparin affinity chromatography. In gel filtration which was performed with 50mM Phosphate buffer (pH 7.2, 0.15M salt) at a flow rate of 2.0 ml/min, ovotransferrin and ovalbumin were eluted together in fraction number 11-16. In order to separate pure ovotransferrin, fraction No. 12-14 of them which have high concentration of ovotransferrin were concentrated and rechromatographed. However, the ovotransferrin did not separated clearly. In heparin affinity chromatography, the separation was performed with 50mM ethylaminetetraacetic acid (EDTA, pH7.2) and 50mM Phosphate buffer (pH 7.2, 0.15M salt contained) on ferrous and ferric ion saturated column at as same flow rate as gel filtration system's. Ovotransferrin and albumin were eluted together at 10-15min (fraction No.3) and 15-20min (fraction No.4), respectively. However, purified ovotransferrin was eluted at 156-165min and 165-175min (tube No.32-33) with 50 mM phosphate buffer (pH 7.2, 0.15M salt free), respectively. Heparin affinity chromatography with ferric ion saturated column was resulted in the best separation of ovotransferrin rather than separation by gel chromatography and ferrous ion saturated heparin affinity chromatography.


Ovotransferrin;Gel chromatography;Heparin affinity chromatography;SDS-PAGE


  1. Bartfeld, N. S. and Law, H. J. 1990. Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta. J. Biol. Chem. 265:21684-21691
  2. Burley, R. W. and Vadehra, D. V. 1989. The Avian Egg: Chemistry and Biology. John Wiley & Sons, Inc. New York
  3. Cunningham, F. E. and Lineqeaver, H. 1965. Stabilization of egg white proteins to pasteurizing temperatures above 60$^{circ}C$. Food Technology. 19: 1442-1446
  4. Garibaldi, J. A. 1960. Factors in egg white which control growth of bacteria. Food Res. 25(3):337-344
  5. Itoh, T., Sugawara, H. and Adachi, S. 1979. Comparative chemical studies on the quail (COTURNIX COTURNIX JAPONICA) egg ovotransferrin. Comp. Biochem. Physiol. 62B:41-44
  6. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 15; 227(5259):680-685
  7. Nichol, H. and Locke, M. 1989. The characterization of ferritin in an insect. Insect Biochem. 19: 587-602
  8. Parviz, A. and Baugh, R. F. 1966. A simple and rapid procedure for preparation of large quantities of pure ovotransferrin, Archives of Biochemistry and Biophysics, 118: 138-144
  9. Shibusawa, Y. and Ito, Y. 1991. Protein separation with aqueous-aqueous polymer systems by two types of counter-current chromatographs. J Chromatogr. Jul 26; 550(1-2):695-704
  10. Vachier, M. C., Piot, M. and Awade, A. C. 1995. Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrix. J. Chromatography B, 664. 201-210
  11. Woodworth, R. C. and Schade, A. L. 1959. Conalbumin: A rapid, High-Yield Preparation from Egg White, Archives of Biochemistry and Biophysics. 82:78-82
  12. Williams, J. 1962. A comparison of conalbumin and transferrin in the domestic fowl. Biochem. J. 83:355-364

Cited by

  1. Inhibitory Effect on Angiotensin-converting Enzyme (ACE) and Optimization for Production of Ovotransferrin Hydrolysates vol.30, pp.2, 2010,
  2. Identification of Proteins in Egg White Using Ion Exchange Cartridge and RP-HPLC vol.50, pp.4, 2012,