PROTEINS

Proteins are complex organic compounds that contain the elements carbon, hydrogen, oxygen
and nitrogen. Nitrogen is the characteristic element for all amino acids and therefore all
proteins. Frequently amino acids contain sulphur and phosphorus and less frequently they
contain iron, copper, iodine and zinc.

CHEMICAL COMPOSITION OF PROTEINS

Proteins do contain the amino group, Carboxyl group, Hydrogen and the variable as illustrated
below.

R= variable.
C = Carbon atom
COOH = Carboxyl group/ weak acid.
H = Hydrogen atom.
NH2 = Amino group / weak alkali

FORMATION OF THE PROTEIN

Proteins are made up of Amino acids which are joined together by the peptide bond, the Amino
acids can be combined together to form proteins by the process called condensation which
involves elimination of water.
The bond which joins two amino acids is called a dipeptide bond and the bond which joins
many amino acids is called a polypeptide bond.

1
 AMINO ACIDS
These are the building blocks of proteins.
OR
Amino acids are the sub units from which proteins are made.
CLASSIFICATION OF AMINO ACIDS.
These can be classified according to;
Manufacture, that is say;
Amino acids are classified into essential amino acids and non-essential amino acids.
Essential amino acids are the amino acids which cannot be synthesized by the body but rather
obtained through our diet and examples include; Isoleucine, leucine, Tryptophane, Methionine,
Histidine, Phenylalanine, Threonine, valine, lysine. Non-essential amino acids are the amino
acids which can be synthesized by the body and examples include; Norleucine, Alanine,
Asparagine, Aspartic acid, Cysteine, Glutamic acid, Glutamine, Glycine, Proline, serine,
Tryosine.
NB.
Of the above Amino acids, Arginine and histidine are very essential in children.
Normally the body synthesizes all the non-essential amino acids it needs as long as it is
provided with the adequate supply to use for manufacture of the amino acids. [Proper diet]

IMPORTANT PROTEINS WITH WHERE THEY ARE FOUND.

Each protein has its own chemical name and below are some of them;

Animal protein location vegetable protein location

Myosin……………………meat. Gluten …………….…..wheat

Caseinogens………………cheese. Glysine………………..soyabeans

Lactoalbumin………..……milk. Excelsin............……….nut.

Albumin……………………eggs Zein……………………maize

Haemoglobin……………...blood. Legumine………………pulses.

Collagen/elastine.……….connective tissues

PROTEIN REQUIREMENTS.

The recommended intake of protein each day is 1g for each kg body weight for example if the
body weighs 70kg he will require 70g of protein each day but more is required in children,
teenagers adolescents ,pregnant and lactating mothers.

AVERAGE REQUIREMENTS OF PROTEINS.

Children………30-50g

2
Average adult…….60-70g.

Pregnant female…….90g
ENERGY VALUE OF PROTEINS
1g once oxidized produces 4kilocalories/17kilo joules of energy.
CLASSIFICATION OF PROTEINS
Proteins are classified according to;
The chemical structure, Biological value, Sources and functions.
Classification according to structure;
These are classified into two that is to say simple proteins and conjugated proteins.
Simple proteins include globular, waxes and fibrous proteins.
FIBROUS PROTEINS.
These have less internal bonding and there polypeptides are Stretched so that the molecules
have a relatively linear shape.
They have a characteristic spring like structures which give them an elastic structure for
example elastin found in arteries and tendons, gluten found in flour.
The non-elastic protein is produced from zigzag structure such as collagen in animal tissues,
keratin in hair and nails.

GLOBULAR PROTEINS
These have substantial amount of internal bonding with the polypeptide chains being very
much folded to form a spherical molecule.
Examples of globular proteins include albumin, plasma proteins (blood).
Globular proteins are relatively soluble in water and body fluids. They are easily denatured,
destroyed since their internal structure is easily disorganized.
They form plasma proteins like enzymes, haemoglobin and hormones.

CONJUGATED PROTEINS
These are classified into lipoproteins, haemoglobin, glucoproteins, nucleoproteins and
flavoproteins .
They contain prosthetic component.
The term prosthetic refers to a non protein and in this case a protein group is attached to simple
globular protein.
Derive proteins these come from prosthetic meaning non protein .these are proteins which
undergo a change in their structure in the way they exist in nature. The non-protein attaches to
simple globular forming conjugated protein.
LIPOPROTEINS.
These are lipids with a protein coat around it.
They are transported through the blood in form of lipoproteins.
This enables lipids to become more soluble since the proteins are more soluble.
CLASSIFICATIONS OF LIPOPROTEINS.
Chylomicrons.
Very low density lipoproteins. (VLDL)

3
Low density lipoproteins. (LDL)
High density lipoproteins. (HDL)

CHYLOMICRONS
They have the highest amount of lipids than proteins hence they are the list dense.
They consist the highest amount of triglycerides.
They are synthesized from intestinal mucosa cells after a meal and they are transported to the
liver.
VERY LOW DENSITY LIPOPROTEINS
Found in the liver in the fasting intervals.
Replace chylomicrons as the major transport of lipids.
They saturate in blood for a few hours.
They are then converted to lipids.
LOW DENSITY LIPOPROTEINS.
They transport mainly cholesterol from the liver to the peripheral tissues.
Combine with blood calcium to form plaques in blood arteries.
Transport cholesterol and plaques.
They are very dense due to high amount of proteins they contained.
They are formed during cell metabolism.
They also transport phospholipids.
Takes cholesterol away and they are destroyed.
NB: Cholesterol is transported from the blood by lipoproteins especially low density
lipoproteins .plaques forms at the places where the arteries branch, they form and narrow the
blood vessels.

CLASSIFICATION OF PROTEIN ACCORDING TO BIOLOGICAL VALUE.

Biological value is a measure of how nourishing a protein is,
amount of amino acids∈the body
Biological value can be calculated as; x 100 .
amount of amino acids∈the diet
This can be classified as; high biological value proteins, low biological value proteins and no
biological value proteins.
High Biological value proteins are proteins which contain most of the essential amino acids in
the proportion required by the body. Most of their nitrogen is available for growth and repair of
cells. They are mostly obtained from foods of animal origin with the exception of soya beans.
Low biological value proteins are proteins which are insufficient in one or more of the essential
amino acids in the proportion required by the body and are mainly of plant origin with the
exception of gelatin.
No biological value proteins are proteins that does not contain biological value for
example gelatin

BIOLOGICAL VALUE OF SOME FOODS

Food Percentage biological value

4
 Eggs 100
Milk 95
Meat/fish 80-90
Soya beans 74
Rice 67
Maize 40
Gelatin 00

CLASSIFICATION OF PROTEINS ACCORDING TO SOURCES

These include plant sources and animal sources.
Plant sources; Example include nuts e.g. pea nuts, ground nuts, cashew nuts. Beans both fresh,
processed and dried. Peas e.g. pigeon peas, cow peas and whole cereals and bread. Potatoes and
other vegetables contain very small amounts.
Animal sources examples include; meat including poultry and processed meat, fish including
shell frozen and canned fish, eggs including preserved egg; milk including skimmed, dried and
condensed milk; cheese especially hard cheese; soya beans.
LIMITING AMINO ACIDS
This is an essential amino acids lacking in the protein to make it complete .For example maize
lacking lysine, legumes are lacking tryptophan, soya beans lacking methionine.
SUPPLEMENTARY VALUE OF PROTEIN

This refers to the ability of one protein food to make good the deficiency of another protein
food. For example bread which is deficient in lysine but rich in tryptophan when combined
with gelatine which is rich in lysine and also deficient in tryptophan, they will complement
each other. All the essential amino acids will be obtained.

CHARACTERISTICS/PROPERTIES OF PROTEINS.
 Most proteins are insoluble in water and form colloidal suspensions.
 They have a large molecular weight and protein solutions are colloids.
 They do not pass through semi permeable membranes due to their large size.
 Proteins are amphoteric in nature that is to say, are to react with acids and bases due to the
presence of the basic amino group and acidic carboxylic group in the amino acid molecule.
 Proteins can be denatured once subjected to chemicals or heat.
 Proteins undergo coagulation when heated, mixed with acids and alkalis.
 They undergo hydrolysis to form polypeptides and eventually amino acids. This happens in
the presence of enzymes for example during digestion.

5
 Proteins undergo mallard reaction. Which is the browning reaction in which the amino group
reacts with the aldehyde group of sugar to produce a brown colour on application of dry heat
eg in cakes, biscuits, and bread are browned in this way.
 Proteins form salts with both anions and cations based on their net charge ie ion bonding
capacity.
 They have an isoelectric point. Which is the point at which protein molecule do move in an
electric field.
FUNCTIONS OF PROTEINS
 Helps in growth, maintenance and repair of cells.
 Help in the manufacture of essential body compounds like enzymes which aid food digestion.
 Formation of hormones like luteinizing hormone and follicle stimulating hormone which
helps to regulate the menstrual cycle.
 Proteins help in the body fluid balance. Due to their colloidal nature they have a large
molecular weight. As such protein molecules cannot easily move across the semi permeable
membrane hence creating a colloidal osmotic pressure that allows water and other fluids to
move freely in and out of the cell maintaining balance of fluids in and out of the cell.
 They help to maintain the acid-base balance in the blood (buffer-action) they pick up
hydrogen ions when blood is too acidic and give up the hydrogen ion in case it is too alkaline
preventing acidosis and alkalosis which are dangerous. This is due to the carboxyl and amino
groups in amino acids.
 Proteins help in defense and immunity of the body. Antibodies are protein in nature and
provide protection against infectious microorganisms and produce substances that inactivate
poisons produced by bacteria.
 Proteins are used as a source of energy in the body. This is during the period of starvation in
the process of deamination where the carboxyl group is oxidized to release energy and amino
group converted to urea with the help of the liver.
 Proteins help in electrolyte balance. Sodium ions are concentrated on the outside of the cell
while potassium ions are concentrated inside. However these ions tend to diffuse in and out
the cell respectively, so protein carriers help to transport them into their positions by
potassium-sodium pumps.
 They are also involved in blood clotting through thrombin, Fibrinogen and other protein
factors.
 Actin, Myosin acts as contractile proteins important for muscle contraction.
DIGESTTION OF PROTEINS.
MOUTH
The food is masticated into small particles which are then mixed with saliva secreted from the
salivary gland. The smell, sight, thought of food and presence of food in the mouth stimulate
salivary gland to produce plenty of saliva.
The saliva moistens the food which eases mixing and with the help of the tongue it’s rolled into
a bolus and pushed down the pharynx with the upward movement of the tongue through the
esophagus to the stomach.
STOMACH
In the stomach, food is mixed with gastric juice which contains; hydrochloric acid and enzymes.
The hydrochloric acids in the stomach neutralize the alkali, kill microorganisms and also activate

6
pepsinogen to pepsin. Pepsin begins protein hydrolysis by reacting with proteins breaking them
to peptones. Rennin clots the milk into casein.
DUODENUM
In the duodenum bile secreted from the liver to neutralize the acid. The enzyme trypsin from
the pancreatic juice pours into the duodenum from pancreas converting peptones into peptides
and amino acids.
ILLEUM
Here amino peptidase releases amino acids from nitrogen containing substance. Dipeptidase
breaks down any remaining dipeptide into free amino acids. Pepsin converts any remaining
protein into amino acids.
Free amino acids are then absorbed into the blood stream through the villi and pass via hepatic
portal vein into the liver.
Many amino acids are immediately released into the blood stream and passed into the body
tissues where they are built up again in order to form new cells to repair and manufacture
proteins and substances for example hormones and enzymes.
The nitrogen from excess proteins is converted into urea in the liver and the remaining carboxyl
groups are utilized for energy production.
EFFECTS OF HEAT ON PROTEINS.
 It coagulates and usually shrinks when heated.
 It may harden e.g. in the egg white and form skin for example in the milk.
 Over cooking will denature proteins and on over cooking most them can get tough and
therefore indigestible.
 Some proteins such as meat change colour for example red to brown.
 In meat connective tissues change gelatin and extractives are released making it more
digestible especially when converted to moist heat.
 Some amino acids are destroyed in the protein foods.
 Egg whites are set at 60 degrees just before the egg yolk.
 The meat protein myosin and actin coagulate and shrink when heated.
 The gluten in wheat flour after stretching by the raising agents sets to give structure to
baked products ie in cakes and bread.

EFFECTS OF PROTEIN DEFICIENCY

Retarded growth especially in children.
Accumulation of fats in the liver which may lead to its failure to function.
Failure of damaged liver to synthesize proteins.
Digestion and absorption are impaired leading to diarrhea, water and electrolyte loss.
Muscle wasting due to usage of all the remaining fat deposits and proteins from the muscles.
Oedema which involves accumulation of fluids in the tissues arises.
Poor skeletal development.
Mental retardation.
Malfunction of various organs due to hormone and enzyme deficiency.
Over indulgence in high calorie foods leading to obesity.
It also results to some nutrition\al diseases such as kwashiorkor, marasmas, and protein calorie
malnutrition.

7
KWASHIOKOR
This is a deficiency disease caused by lack of proteins in the diet,. It affects children aged 1-
3years who are weaned off the breast early and are not provided with sufficient proteins in the
diet.
This can be caused by cases of poverty, ignorance, culture, wars, natural calamities like famine,
parasites like worms in the body and food unavailability
SYMPTOMS OF KWASHIORKOR
Retarded growth most especially in children, here the child usually has body weight and height
which are below normal for the age.
Muscles wasting as the child become too thin for their height and it can easily be noticed from
the thin upper arms.
Oedema, this is the swelling of the body due to retention of fluid in the body tissues, it usually
stars with a slight swelling of the feet and it can be spread to legs.
Mental changes, here the child is always not interested and always miserable. He/ she is always
irritated, and in severe cases brain development may be impaired, low intelligent quotient(I.Q)
the child has scarce silky hair compared to the dark coarse thick textured hair of an African
child.
Enlargement of the liver leading to a pot belly development.
Anaemia due to the protein need for synthesis of red blood cells which is not available.
Poor appetite.
Sores on the mouth and lips.
Diarrhoea where the stools are very loose and contain undigested food particles.
MARASMAS
This usually occurs in infants between 6-18months of age, when the mothers breast milk
provides insufficient proteins and calories due to malnourishment of the mother marasmas
results causes the marasmas the child is neither getting adequate supply of breast milk or any
alternative food for them, this may be due to death of mother, failure of lactation and bottle
feeding other than breast feeding
Early cessation of breast feeding does not necessarily lead to marasmas but rather poverty that
leads to unavailability of milk to feed the baby.
SYMPTOMS OF MARASMAS
Retarded growth.
Extreme muscle wasting, here there is little or no subcutaneous fats left under the skin.
The skin wrinkles especially around the thighs and buttocks.
The child is always alert and interested in what is taking place.
The child is grossly overweight.
The child is less miserable and less irritable.
The child has enough appetite and can easily suck their hands and eat their clothes.
The child has sunken cheeks and bulging eyes with a wrinkled look of an old person giving
another wide awake appearance.
The hair and skin do not have any change.
Their stools may be loose.

8
Protein calorie malnutrition in adults.
Patient is remarkable underweight for his/her size unless he/she is grossly eodematous.
The muscles are wasted and there is a reduced subcutaneous fat left.
Mental changes are common and patient is usually disinterested and has an appearance of being
in dreamy world.
It is difficult to attract the patient’s attention.
Diarrhea is frequent and it has an offensive smell.
The hair chose a difference in texture and colour for example, thin and brown, much softer and
silky and curly and it has lost its natural shine.
The protein is lost and the patient becomes very weak.
Blood stained stools.
Severe diarrhoea.
Malaria.
DENATURATION
This is the un twisting of the protein molecules leading to loss of structure and function and this
is always irreversible.
CAUSES OF DENATURATION
 Application of heat as disrupts the hydrogen bonds and to a lower extent salt links.
 When heat is applied the peptide chains are moved apart and structure is interfered with. The
protein looses its binding power and is considerable shrinkage.
 The protein coagulates as the molecule are packed tightly together. This causes a skin to form
on milk, eggs to coagulate.
 Vigorous agitation such as whipping can result into physical separation of hydrogen bonds
and some salt links in Eggs.
 Addition of chemicals such as,
 Alkaloid agents as they disrupt salt links and form bonds between themselves and protein
molecules for example tannic acid.
 Salts of heavy metals which provide one which disrupt the links producing their own salt
links for example mercury, lead and silver.
 Acids and alkalis provide charged ions which alter the charges of the protein molecules thus
interfering with the salt links for example lemon juice causes milk to curdle.
 Organic solvents like ethanol disrupts hydrogen bonding between protein molecules since
they capable of hydrogen bonding themselves to expose polar groups.
 Alcohol and vinegar have a preservative effect on food since they denature the enzyme that
could cause food spoilage.
DEAMINATION OF PROTEINS
This is the process that involves the removal of the amino group from the acid molecule with the
help of the liver through the kidneys in the form of urea.
NB.
When proteins are broken by digestive enzymes into amino acids most of it is used for rebuilding
into body proteins. Excess proteins are not stored hence undergo deamination.

9
The nitrogen containing amino group is removed from the amino acid molecule and converted
into ammonia which in turn is converted into less toxic urea that could be released into the blood
stream and eventually excreted from the body by the kidney as urine, skin sweat.
The rest of the molecule is oxidized by gluconeogenesis or ketogenesis to pyruvate and acetyl
CoA to produce heat and energy.
The energy is not stored as glycogen. The amino acid surplus can also be metabolized into fat by
combustion of the acid pyruvate and acetyl CoA which are which are then synthesized to fatty
acids.
CONDITIONS FOR DEAMINATION
During starvation when the amino acids have to be broken to supply energy.
Excess supply of amino acids which cannot be stored in the body.
NITROGEN BALANCE
This is the ratio of Nitrogen intake and Nitrogen loss from the body.
There are three forms of nitrogen balance that is to say, positive, negative, and net nitrogen
balance.
POSITIVE NITROGEN BALANCE; is when the amount nitrogen absorbed in the body is
equal to amount of nitrogen supplied in form of amino acids. This occurs after a rich protein
meal and can be recognized when there is a continuous growth of the body, hair, nails, fast
healing of wounds.
NEGATIVE NITROGEN BALANCE; Is when the amount of nitrogen out of the body is more
than nitrogen nitrogen taken in. It occurs after surgery, illness and bleeding.
NET NITROGEN BALANCE; Is when the Nitrogen intake is equal to nitrogen loss.
NB. Nitrogen can be lost through the skin as sweat, when hair and nails are cut, when a person
loses a lot of blood, occurrence of malabsorption disorder like diarrhea ,obligatory urine loss i.e
lost in urine, profuse sweating.

10