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