What happen to egg albumin when acid is added?

When acid is added to egg albumin, the protein undergoes a process called denaturation. Denaturation is the process by which the protein's structure is disrupted and its properties are changed. In the case of egg albumin, the addition of acid causes the protein to unfold and lose its solubility. This can be observed as the egg white turns from a clear liquid to a cloudy, opaque gel.

The addition of acid to egg albumin also causes the protein to precipitate. Precipitation is the process by which a substance comes out of solution and forms a solid. In the case of egg albumin, the protein precipitates out of solution as a white, flocculent solid.

The denaturation and precipitation of egg albumin by acid is a result of the disruption of the protein's hydrogen bonds and disulfide bonds. Hydrogen bonds are weak chemical bonds that form between a hydrogen atom and an electronegative atom, such as oxygen or nitrogen. Disulfide bonds are covalent bonds that form between two sulfur atoms. These bonds are responsible for holding the protein's structure together. When acid is added, the hydrogen bonds and disulfide bonds are broken, causing the protein to unfold and lose its solubility.

The denaturation and precipitation of egg albumin by acid is an important process in the food industry. It is used to make a variety of food products, such as mayonnaise, salad dressing, and meringue.