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Milk
Milk
Cooked egg protein has a higher digestibility rate of 90.9% compared to raw egg protein, which
has a digestibility rate of 51.3%.
Digestibility of proteins from eggs is significantly influenced by cooking. Cooking eggs not only
denatures the protein for easier digestion and allows our bodies to absorb more of the protein
efficiently
Sweet milk, which is fresh and unfermented, contains lactose in its original form and may be
more challenging for those with lactose intolerance to digest.
Milk after reaching the stomach, is acted upon by the proteolytic enzyme pepsin.
Pepsin hydrolyzes the milk protein, soluble casein into insoluble paracasein which precipitates
as calcium paracaseinate to form semi-solid curd.
Heat addition.
If a protein containing food mixture is heated, the proteins become more solid; that is, they
coagulate. This is because heat causes protein molecules to move faster through the water in
the food mixture, and the molecules collide and bond with each other in large, three-dimensional
networks
During protein coagulation, proteins may undergo denaturation as they come together and form
a new structure. Essentially, denaturation can be a precursor to coagulation, providing the
structural changes necessary for proteins to aggregate and form a cohesive structure.
Addition of Chemicals
the addition of specific chemicals alter the protein structure and induce coagulation. When an
acid is added to a protein-containing solution, it alters the pH of the environment. Proteins have
optimal pH ranges for stability and solubility, and deviation from this range can lead to
denaturation and coagulation.
For example, the addition of acids like vinegar can coagulate proteins in milk, leading to the
formation of curd in the process of cheese-making.
The process of baking breaks down complex starches present in the dough to simpler sugars,
which are easily digestible.