Egg
Egg
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[5]
Protein structure
Protein structure
[1] Ovalbumin (Fig [5]) is an almost spherical glycophosphoprotein, the most common protein in egg white, being ~60 % of the whole. The peptide chain has 385 amino acids (MW = 42,700 Da). Hydroxyl groups from the side chains of serine-68 and serine-344 are esterified with phosphoric acid, and an oligosaccharide attaches to the side chain of asparagine-292.
Egg coagulation
Egg coagulation
coagulation:
[1] When an egg is heated (like on a pan), the abdumen (white yolk) solidifies. Coagulation (or gelation) is when the egg's proteins start to thicken. Egg whites coagulate at 60°C and yolks at 65°C, and full coagulation at 70°C. This process also happens as we cook meat, which shrinks when cooked.
An egg's coagulation is a chemical and physical process where heat, mechanical force, acids, or sugars cause egg proteins to denature then aggregate to form a solid/semi-solid network.
denature: unfold
aggregate: bond together
The 2 processes trap air and moisture, making a stable, 3D structure, as to why eggs thicken and set when cooked, providing volume and stability to dishes like cakes, custards, and soufflés.
Coagulation involves protein denaturation--when proteins lose their native water-soluble structure and become insoluble.
[3] Native unaltered proteins have a complex folded and coiled individual aminp acid chain protein primary structure, linear sequence of amino acids held together. As the linaer chains align together 3D structure, a protein secondary structure. An alpha helix coil is an example of a type of secondart structure.
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