Thermostabilization of ovalbumin in a developing egg by an alkalinity-regulated, two-step process.
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.
Hatta
H
H
Department of Food and Nutrition, Kyoto Women's University, Japan.
Nomura
M
M
Takahashi
N
N
Hirose
M
M
D000818:Animals; D002152:Calorimetry, Differential Scanning; D004529:Egg White; D004530:Egg Yolk / Q000737:chemistry; D005260:Female; D006863:Hydrogen-Ion Concentration; D010047:Ovalbumin / Q000737:chemistry*; D010063:Ovum / Q000737:chemistry* / Q000254:growth & development; D011487:Protein Conformation; D011489:Protein Denaturation; D015053:Zygote / Q000737:chemistry*
D010047:Ovalbumin