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3 answers

As to your "WHY":

THE EGG WHITE CONTAINS A LOT OF PROTEINS (approx. 10% protein in 85% water).
In normal conditions (pH, T, solvent, ...) protein molecules have a special 3-dimensional shape. When heat is applied, in the temperature range of 50-70 deg. (approx.) this shape breaks down
BECAUSE OF THE INCREASED INTRAMOLECULAR THERMAL MOTION.

The thermal denaturation leads to a loss of solubility since denatured protein molecules show a high tendency to aggregate and (further) to coagulate, gelate..., and so the EGG WHITE become suitable for eating in spite of drinking.

As to your "Thermodynamics":

Obviously, all these processes are going by lowering of function "G" (the Gibb's Free Energy). Particularly, the denaturation is an endothermic process since energy is needed in order to break intramolecular interactions. It is accompanied by a large increase in S (the entropy) compared to the native structure.
The exact thermodynamics of all these processes is far from simple and brief explanation.

So,
Google it (more than 200K hits),
and cook it by yourself.

2006-09-11 02:02:16 · answer #1 · answered by kaned 2 · 0 0

Dude, all of your "correlate w/ thermodynamics" suggest that you're doing homework. Maybe you should try reading your textbook, instead of typing these questions.

2006-09-07 07:09:51 · answer #2 · answered by Iridium190 5 · 0 1

Dude! how should i know?

2006-09-07 05:21:30 · answer #3 · answered by Avatari 2 · 0 1

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