Protein functionalities
Milk proteins

We can establish a global relationship between the structure of proteins and their functional properties: thus, we can link the primary structure of proteins (total hydrophobicity) to the ability to form a gel, emulsion or foam; the secondary structure (β-sheet richness) to the gelling capacity; the tertiary structure (surface hydrophobicity) to the formation and stabilization of emulsions or foams and finally the quaternary structure (size and shape of the protein assembly) to the ability to gel.

Changes in the environment are responsible for reversible or irreversible changes in protein structures, triggering the phenomena that reflect their functional properties.

The structure of proteins is not a fixed datum, but is dependent on the environment, so modifications to them would determine the formation and maintenance of a new system such...