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Denaturation is a process in which proteins or nucleic acids lose the quaternary
structure, tertiary structure and secondary structure which is present in their native state, by
application of some external stress or compound such as a strong acid or base, a concentrated
inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat. Protein is
large molecules made up of small amino acids. Protein folding is keys to whether a globular
protein or a membrane protein can do its job correctly. It must be folded into the right shape
to function. But hydrogen bonds, which play a big part in folding, are rather weak, and it does
not take much heat, acidity, or other stress to break some and form others, denaturing the
protein. The shape of a protein is associated with food processing properties, such as
solubility, gel formation, and enzyme activity.
In the egg whites the albumin will change from clear to white. We will explore how
the following denature egg albumin by heat that done by cooking, acids and bases (can form
ions side groups of amino acids), by organic compound and also by heavy metal (react with
disulphide bonds).

To study the different effect of denaturation of protein found in the white albumin.

Materials / Apparatus:
Raw eggs
10% Sodium chloride (NaCl)
10% sodium bicarbonate (NaHCO3)
1% Silver nitrate (AgNO3)
Test tube
Hot plate or Bunsen burner
Stirring rod or Glass rod.

1. A 300 ml of water was place in a beaker 400ml and heat to boiling.
2. The test tube was label from 1 until 5.
3. The raw egg was separated and placed the egg white in a test tube until half filled.

The egg yolk was discards.

The test tube number 1 in the boiling water and allow cooking till egg turns white.
The 5 ml of 10% of sodium chloride was put to test tube number 2 and stir.
The 5 ml of 10% of sodium bicarbonate was put to test tube number 3 and stir.
The 5 ml of vinegar was put to the test tube number 4 and stir.
The 5 ml of 1% AgNO3 was put to the test tube number 5 and stir.
The observation was recorded in the table below.

Table 5.1: Denaturation of Egg White Protein.
Test tube




White solid formed.

NaCl - ionic compound

Clear colour and have very little white precipitate.

NaHCO3 - base

Little white precipitate.

Vinegar - acid

A lot of white precipitate

AgNO3 heavy metal

White precipitate layer on the top.

In this experiment, we need to study the different effect of denaturation protein that found in
white egg albumin. The function principle tells that changing the structure of a protein will

affect its function. Often that means that function is lost. Denaturation of a protein means loss
of the protein function due to the structural change in the protein caused by some chemical
physical factor such as high temperature that may cause the folded protein to unfold, to
When the albumin was heat until it become white solid it will disrupt hydrogen bonds and
non-polar hydrophobic interactions. As results, after heat the albumin change colour from
colourless to white solid formed. This occurs because heat increases the kinetic energy and
violently that the bonds are disrupted. The protein in eggs denatured and coagulated during
cooking. Other foods are cooked to denature the proteins to make it easier for enzymes to
digest them. Medical supplies and instruments are sterilized by heating to denature proteins in
bacteria and thus destroy the bacteria.
The denaturation of egg white protein is due to the addition strong acids or bases affect the
groups that compose the protein, changing the net charge. These changes or the absence of
one or more charge can affect the protein folding by repulsion of charges and the
hydrophobic interactions, causing denaturation. In most experiments, strong acids and bases
that are used are usually sodium chloride respectively. Hydrophobic bonds in globular protein
backbones can also be broken by organic solvent. Salt such as NaCl allow the protein to salt
out which causes precipitation by the binding of the salt ions to the charged side chains.
Heavy metal act to denature protein in much the same manner as acids and bases. Heavy
metal salt usually contain Ag+, Cd+, Pb+ and other metals with high atomic weights. Since,
salts are ionic they disrupt salt brides in proteins. The reaction of a heavy metal salt with a
protein usually leads to an insoluble metal protein salt. This reaction is used for its
disinfectant properties in external applications. For example, AgNO3 is used to prevent
gonorrhoea infections in the eyes of new born infants. Heavy metals may also disrupt
disulphide bonds because of their high affinity and attraction for sulphur and will also lead to
the denaturation of protein.

There are a lot of factor that can affect the denaturation of egg white albumin. For example
heat, addition of strong acids and bases, exposure to organic solvents and also addition of

heavy metal. Protection of proteins against denaturation is one result of the buffering of
biological solutions such as blood and the aqueous interior of living cells. If blood would Ph
changed much from its normal value, proteins in the blood would begin to pucker, buckle,
twist into different shapes, and unravel, with potential loss of function.

1) Which method appeared to have the most dramatic denaturing effect on egg albumin? Why
do you think this method had a greater affect?
The heat is the most dramatic denaturing effect on egg albumin because it denatures
the protein and changes the conformational shape of the protein and the bonds that maintain it
2) Of the methods you tested, which would be more likely be used in food industry?
In the food industry they most likely to use the method of heat as well, in fact, boiling an egg
is already a favourite of many when it comes to different cooking method because the
application of heat is safe for the food industry.


1. Adler, Nissen J, 1975. Enzymic hydrolysis of protein for increased solubility. Journal
of Agricultural and Food chemistry. 24(6).1090-1093.
3. Dyer, J.M, Plowman, Clerens,S,. 2010. Proteomic evaluation and location of UVBinduced photo of egg albumin. 2011. 27(6).1090-1090.