581
Views
15
CrossRef citations to date
0
Altmetric
Original Articles

Thermostabilization of Ovotransferrin by Anions for Pasteurization of Liquid Egg White

, , , &
Pages 1839-1845 | Received 05 Jan 2006, Accepted 24 Mar 2006, Published online: 22 May 2014

  • 1) Mine, Y., Recent advances in the understanding of egg-white protein functionality. Trends Food Sci. Tech., 6, 225–232 (1995).
  • 2) Kobayashi, M., Gutierrez, M. A., and Hatta, H., Microbiology of eggs. In “Hen Eggs: Their Basic and Applied Science,” eds. Yamamoto, T., Juneja, R. J., Hatta, H., and Kim, M., CRC Press, Boca Raton, pp. 179–191 (1997).
  • 3) Matsuda, T., Watanabe, K., and Sato, Y., Heat-induced aggregation of egg-white proteins as studied by vertical flat-sheet polyacrylamide-gel electrophoresis. J. Food Sci., 46, 1829–1834 (1981).
  • 4) Nakamura, R., and Matsuda, T., A new protein band appearing in the electrophoretic pattern of egg-white heated at below 60 °C. J. Food Sci., 48, 87–91 (1983).
  • 5) Watanabe, K., Matsuda, T., and Nakamura, R., Heat-induced aggregation and denaturation of egg-white proteins in acid media. J. Food Sci., 50, 507–510 (1985).
  • 6) Yamashita, H., Ishibashi, J., Hong, Y. H., and Hirose, M., Involvement of ovotransferrin in the thermally induced gelation of egg white at around 65 °C. Biosci. Biotechnol. Biochem., 62, 593–595 (1998).
  • 7) Hirose, M., The structural mechanism for iron uptake and release by transferrins. Biosci. Biotechnol. Biochem., 64, 1328–1336 (2000).
  • 8) Kurokawa, H., Mikami, B., and Hirose, M., Crystal structure of diferric hen ovotransferrin at 2.4 Å resolution. J. Mol. Biol., 254, 196–207 (1995).
  • 9) Lin, L. N., Mason, A. B., Woodworth, R. C., and Brandts, J. F., Calorimetric studies of serum transferrin and ovotransferrin. Estimates of domain interactions, and study of the kinetic complexities of ferric ion binding. Biochemistry, 33, 1881–1888 (1994).
  • 10) Mizutani, K., Mikami, B., Aibara, S., and Hirose, M., Structure of aluminium-bound ovotransferrin at 2.15 Å resolution. Acta Crystallogr., D61, 1636–1642 (2005).
  • 11) Lineweaver, H., and Cunningham, F. E., U. S. Patent 3251697 (May, 1966).
  • 12) Watanabe, K., Xu, J. Q., and Shimoyamada, M., Inhibiting effects of egg white dry-heated at 120 °C on heat aggregation and coagulation of egg white and characteristics of dry-heated egg white. J. Agric. Food Chem., 47, 4083–4088 (1999).
  • 13) Watanabe, K., Nakamura, Y., Xu, J. Q., and Shimoyamada, M., Inhibition against heat coagulation of ovotransferrin by ovalbumin dry-heated at 120 °C. J. Agric. Food Chem., 48, 3965–3972 (2000).
  • 14) Matsudomi, N., Oka, H., and Sonoda, M., Inhibition against heat coagulation of ovotransferrin by ovalbumin in relation to its molecular structure. Food Res. Int., 35, 821–827 (2002).
  • 15) Matsudomi, N., Kanda, Y., Yoshika, Y., and Moriwaki, H., Ability of alpha s-casein to suppress the heat aggregation of ovotransferrin. J. Agric. Food Chem., 52, 4882–4886 (2004).
  • 16) Hirose, M., Oe, H., and Doi, E., Thiol-dependent gelation of egg-white. Agric. Biol. Chem., 50, 59–64 (1986).
  • 17) Fukada, H., Sturtevant, J. M., and Quiocho, F. A., Thermodynamics of the binding of L-arabinose and of D-galactose to the L-arabinose-binding protein of Escherichia coli. J. Biol. Chem., 258, 13193–13198 (1983).
  • 18) Okamoto, I., Mizutani, K., and Hirose, M., Iron-binding process in the amino- and carboxyl-terminal lobes of ovotransferrin: quantitative studies utilizing single Fe3+-binding mutants. Biochemistry, 43, 11118–11125 (2004).
  • 19) Nakamura, R., and Omori, I., Protective effect of some anions on the heat-denaturation of ovotransferrin. Agric. Biol. Chem., 43, 2393–2394 (1979).
  • 20) Nakamura, R., Umemura, O., and Takemoto, H., Effect of heating on the functional properties of ovotransferrin. Agric. Biol. Chem., 43, 325–330 (1979).
  • 21) Mizutani, K., Muralidhara, B. K., Yamashita, H., Tabata, S., Mikami, B., and Hirose, M., Anion-mediated Fe3+ release mechanism in ovotransferrin C-lobe: a structurally identified SO4 2− binding site and its implications for the kinetic pathway. J. Biol. Chem., 276, 35940–35946 (2001).
  • 22) Mizutani, K., Yamashita, H., Mikami, B., and Hirose, M., Crystal structure at 1.9 Å resolution of the apoovotransferrin N-lobe bound by sulfate anions: implications for the domain opening and iron release mechanism. Biochemistry, 39, 3258–3265 (2000).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.