Denaturation of Macromolecules


  • The development of disorganization of native macromolecule structure is thought as denaturation.
  • Denaturation leads to the loss of secondary, tertiary and quaternary structure of proteins.
  • This involves a modification in physical, chemical and biological properties of macromolecule molecules.

Denaturation of Macromolecules


  1. Carbohydrates
  2. Nucleic acids
  3. Proteins


Physical agents Heat, violent shaking X-rays, ultraviolet light radiation. Chemical agents: Acids, alkalies, organic solvents (ether, alcohol), salts of significant metals (Pb, Hg), urea, salicylate.


  1. The native volute structure of macromolecule is lost.
  2. The first structure of a macromolecule with amide linkages remains intact i.e., amide bonds aren’t hydrolysed.
  3. The macromolecule loses its biological activity.
  4. Denaturised macromolecule becomes insoluble within the solvent during which it absolutely was originally soluble.
  5. The body of denaturised macromolecule (solution) will increase whereas its physical phenomenon decreases.
  6. Denaturation is related to increase in ionizable and sulfhydryl teams of macromolecule- this is often because of loss of H and disulfide bonds.
  7. Denaturised macromolecule is a lot of simply digestible. this is often because of hyperbolic exposure of amide bonds to enzymes- preparation causes macromolecule denaturation and, therefore, burned food (protein) is a lot of simply digestible.
  8. Denaturation is typically irreversible. as an example, dish are often ready from AN egg (protein-albumin) however the reversal isn’t attainable.
  9. Careful denaturation is usually reversible (known as renaturation)- haemoprotein undergoes denaturation within the presence of salt. By removal of salt, haemoprotein is renatured.
  10. Denatured macromolecule can’t be crystallized.   Coagulation: The term ‘coagulum’ refers to a semi-solid viscous precipitate of macromolecule.
  • Irreversible denaturation leads to curdling. curdling is optimum and needs llowes temperature at isoelectric hydrogen ion concentration.
  • Albumins and globulins (to a lesser extent) ar thick proteins.
  • Heat curdling take a look at is usually wont to find the presence of albumen in piss.
  •  Flocculation: it’s the method of macromolecule precipitation at isoelectric hydrogen ion concentration. The precipitate is said as flocculum.
  • Casein (milk protein) are often simply precipitated once adjusted to isoelectric hydrogen ion concentration (4.6) by dilute ethanoic acid. action is reversible.