Denaturation of Proteins
Denaturing forces the protein to assume
new conformation with lowest possible free energy
Causes of denaturing, changes in the surrounding environment such as
pH, ionic strength, temperature, solvent composition
Denaturing is when the protein undergoes major changes in the
secondary, tertiary and quaternary structure
pH, at extreme pH values the electrostatic static repulsion between protein molecules is significantly high causing
them to unfold and rearrange
The native state of protein molecules id
thermodynamically the most stable and has the lowest amount of free energy
It is important to note that the primary structure of proteins
do not change
loss of activity of enzymes, reduction in allergens, texture development, emulsification and improved digestibility are all examples of the
effect of denaturation in foods
Temperature, at a higher temperature
hydrophobic interactions are stronger than polar interactions forcing the polymer to rearrange itself
salt, some salts can alter the hydrogen bonding within water and make it more non-polar causing protein to
unfold as hydrophobic molecules can now be exposed to water