[Updated on Apr. 18] Integration of CiNii Articles into CiNii Research

Thermostabilization of Ovalbumin in a Developing Egg by an Alkalinity-regulated, Two-step Process.

  • HATTA Hajime
    Department of Food and Nutrition, Kyoto Women’s University
  • NOMURA Masayo
    Department of Food and Nutrition, Kyoto Women’s University
  • TAKAHASHI Nobuyuki
    Research Institute for Food Science, Kyoto University Present address: Division of Applied Life Sciences, The Graduate School of Agriculture, Kyoto University
  • HIROSE Masaaki
    Research Institute for Food Science, Kyoto University Present address: Division of Applied Life Sciences, The Graduate School of Agriculture, Kyoto University

Search this article

Abstract

Native ovalbumin has been known to convert into a heat-stable form, S-ovalbumin, either in an avian shell egg or in an isolated ovalbumin solution. Recently, similar conversion of ovalbumin in fertile eggs was also reported. We found that the conversion into S-ovalbumin was slower in fertile eggs than in unfertile eggs under the same incubation conditions on the basis of calorimetric analyses for the samples isolated from those eggs. During the incubation, there were differential pH changes of white in the fertile and unfertile eggs. When the pH of purified ovalbumin was manually adjusted so as to simulate the pH changes of egg white during the incubation, the course of the conversion into S-ovalbumin was very similar to that either in fertile or unfertile eggs. Therefore, we conclude that thermostabilization of ovalbumin in fertile eggs proceeds by a certain mechanism which depends on the alkalinity of egg white.

Journal

Citations (7)*help

See more

References(22)*help

See more

Related Articles

See more

Related Data

See more

Related Books

See more

Related Dissertations

See more

Related Projects

See more

Related Products

See more

Details

Report a problem

Back to top