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In this structure, the side group R is different for different amino acids. Although over 80 amino
acids are known, only 26 occur naturally in living systems. Twenty of these naturally occurring
amino acids are frequently combined in proteins. The following are two examples (Glycine
and alanine).
Peptide Formation
When two amino acids are linked by a condensation reaction, a dipeptide is formed.
The different superscripts on R1 and R2 indicate different R groups and therefore different
amino acids. The carbon nitrogen single bond is the newly formed amide or peptide bond. Note
that the dipeptide still has functional groups at both ends, so that further condensation reactions
with other amino acids are possible, resulting in an increase in the length of the peptide chain.
A polypeptide is formed when a large number of amino acids are linked. The term polypeptide
comes from the many –CONH- groups that occur at intervals along the polymer chain. The
figure below shows polypeptide formation.
When 50 or more amino acids have been condensed together, the polypeptide formed is called
a protein. Protein structures are very complicated. Insulin for example, has a molecular formula
of C254H377N65O75S6. Each protein is made from an arrangement of amino acids that is different
from every other proteins. Proteins have a very high relative molecular mass ranging from 6000
to 100000. In living systems the process of condensing amino acids is known as protein
synthesis and this is guided by the DNA in the cells.
Hydrolysis of proteins
Hydrolysis of proteins is the splitting of the peptide bonds in a protein by the action of water
to form smaller peptides or individual amino acids. If all peptide bonds are broken the
hydrolysis is complete. If some bonds are broken, the hydrolysis is partial.
Our digestive system breaks down the proteins we eat into amino acids. For example, enzymes
in the stomach, such as pepsin and rennin catalyse the splitting of the peptide bonds in proteins
to release the amino acids. The hydrochloric acid in the stomach provides the correct acidic
medium for the reaction. Digestion of protein is a hydrolysis reaction.
Hydrolysis of proteins can be accomplished in the laboratory in the presence of acid or alkali.
The acid or alkali acts as the hydrolysing agent.
Acid hydrolysis of proteins
Treat the protein with concentrated hydrochloric acid at 𝟔𝟎𝑶 𝑪 for 24 hours or longer, in the
absence of oxygen
Alkaline hydrolysis of proteins
Treat the protein with concentrated sodium hydroxide for 6-8 hours. In the laboratory the
hydrolysis is complete and a mixture of amino acids is left. These amino acids can be separated
by chromatography.
In the body, the amino acids obtained from hydrolysis of proteins can then be used to synthesize
the many specialised proteins that are essential to health. While our bodies can convert some
amino acids into others which we need, it is not capable of making eight of the naturally
occurring amino acids. These eight essential amino acids are known as the essential amino
acids. We must eat food which can supply our requirements of these essential amnio acids.
Foods such as meat, milk, cereals and vegetables are important constituents of our diets,
because they supply these essential amino acids.
Tests for proteins and amino acids
You are aware that polymers and their monomers have very different properties. This
difference can be used to follow the hydrolysis of proteins. Before the hydrolysis, any tests for
the presence of free amino acids should be negative. At the end of the hydrolysis, tests for the
proteins should be negative.
Testing for amino acids
Reagent: ninhydrin solution
Procedure: add 1cm3 of ninhydrin to food or solution of amino acid. Boil for 1-2
minutes, then allow to cool.
Results: a blue color indicates that amino acids (or proteins which contain a free amino
acid group) are present.
Testing for proteins
Reagent: NaOH(aq) and copper sulphate(aq) (known as the biuret reagent).
Procedure: add biuret reagent to food material in water and heat
Results: a violet colour indicates the presence of proteins
Another test for Protein
Intimately mix the food sample with soda lime (a mixture of sodium hydroxide and
calcium oxide)
Place the mixture in a hard glass test-tube.
Heat the mixture, placing a moist strip of red litmus at the mouth of the test-tube.
If the food contains proteins, ammonia gas will be given off, turning the red litmus paper blue.
Polysaccharides
Polysaccharides are polymers that belong to a group of naturally occurring compounds
containing carbon, hydrogen and oxygen based on the formula Cx(H2O)y. The simplest
carbohydrates are the monosaccharides, which have a general formula of C nH2nOn. Some
examples of these simple sugars are glucose, fructose and galactose. These all contain six
carbon atoms and have the same molecular formula, C6H12O6 but they have different structures
and are therefore isomers. The figure below shows one way that the structure of glucose can
be shown:
Glucose molecules are the building blocks for the carbohydrate polymers. The condensation of
glucose molecules can occur in a stepwise manner forming disaccharides, trisaccharides, and
eventually more complex carbohydrates, the polysaccharides. Examples are shown below.
Polysaccharide formation
Disaccharides and polysaccharides contain an ether linkage that is the C-O-C linkage. This
linkage is commonly called the ‘glycosidic’ linkage. Disaccharides have two reactive (end) –
OH groups. These reactive groups may undergo further condensation reactions to yield a
trisaccharides and eventually, the polysaccharides.
Hydrolysis of carbohydrates
The polymerisation of glucose molecules to form a polysaccharide such as starch is a
condensation reaction. Hydrolysis is the reverse of the condensation process. Starch molecules,
for example, are broken down partially to maltose or completely to glucose.
Testing for carbohydrates
Testing for starch
Reagent: iodine solution
Procedure: to a sample of starch (or food) and water, add a few drops of iodine solution.
Results: a blue-black colour develops if starch is present
Testing for a reducing sugar
Reagent: Benedict reagent or Fehling’s solution.
Procedure: to glucose or food or water, add Benedict reagent and heat.
Results: A series of colour changes are seen. Eventually an orange-red precipitate is obtained,
indicating the presence of reducing sugars.
Triglycerides
A triglyceride is a triester formed by the condensation reactions between a trihydroxyl alcohol
known as glycerol and three long-chain organic acids known as fatty acids. As mentioned
before, fats and oils are not polymers even though they are formed by the same type of chemical
reaction, condensation. Fats and oils are triglycerides.