What happens to a boiled egg albumin?

When you boil an egg, the albumin (the egg white) undergoes a series of changes:

1. Denaturation:

* The heat disrupts the weak bonds (hydrogen bonds) holding the protein molecules in their original, folded structure.

* This unfolding process is called denaturation.

* The denatured proteins become more compact and aggregated.

2. Coagulation:

* As the heat continues, the denatured protein molecules interact with each other and form cross-links.

* These cross-links create a network of proteins, trapping water and giving the albumin its solid, white texture.

* This process is called coagulation.

3. Color change:

* The albumin turns from clear to white due to the scattering of light by the coagulated protein molecules.

In summary, boiling an egg albumin leads to:

* Denaturation: Unfolding of protein molecules.

* Coagulation: Formation of a protein network, giving the albumin its solid texture.

* Color change: From clear to white.

Other effects:

* Increased viscosity: The albumin becomes thicker and stickier.

* Reduced water solubility: The coagulated protein is less soluble in water.

* Changes in taste and smell: The boiled egg albumin has a different taste and smell compared to raw egg albumin.

These changes are irreversible, which is why a boiled egg does not return to its original, liquid state when it cools down.