4.

Proteins
Proteins are chemical compounds that contain the same atoms as
carbohydrates and lipids including carbon, hydrogen and oxygen but with an
importance difference, proteins also contain nitrogen atoms. These atoms
bond with each other to form amino acids. Proteins also contain sulphur and
phosphorus. Proteins are build from basic units called amino acids. The amino
acids combine to form proteins by means of peptide bonds which join the
carboxylic carbon of one amino acid with the nitrogen of the amino group of
another. The resulting peptide has a free carboxyl at one end and a free amino
group at the other end permitting addition of other amino acids at either ends.
Proteins are amphoteric i.e. it has one end that is basic and the other that is
acidic. Most proteins also contain phosphorus, and some specialised proteins
contain very small amounts of iron, copper, and other inorganic elements. The
presence of nitrogen distinguishes protein from carbohydrate and fat.
All amino acids have the same basic structure - a carbon atom core with four
bonding sites: one site holds a hydrogen atom (H), one an amino group (NH2)
and one an acid group (COOH). Attached to the fourth bonding site is a side
group (R group), which contains the atoms that give each amino acid its own
distinctive identity, Figure 4.1.

NH2 (amino group)

I
(Hydrogen H – C – COOH (acid group)
atom) I
R
Side group (varies)

Figure 1: The basic structure of an amino acid

Types of Amino Acids
 Amino acids are classified into two groups: essential and
non-essential amino acids.
a. Essential Amino Acids (Indispensable)
These are the indispensable amino acids that the body cannot synthesize and
must be provided through the diet that we eat. There are nine essential amino
acids. The adult human body requires 8 of them for repair and body
maintenance while the growing child requires 9 of them. They include:
▪ Threonine
▪ Lysine
▪ Isoleucine
▪ Leucine
▪ Methionine
▪ Phenylalanine
▪ Tryptophan
▪ Valine
▪ Histidine (for children)
b. Non-essential Amino Acids (Dispensable)
These are dispensable amino acids that the body enzymes can synthesize in
sufficient amounts to meet its needs, provided there is sufficient amount of
protein to furnish the nitrogen needed.
Since the body is capable of synthesizing sufficient amounts to meet its needs,
they are regarded as non-essential in the diet, though they are as essential in
protein synthesis as the essential amino acids. If adequate amounts are not
present when protein is being synthesized, the non-essential amino acids can
be formed from unused essential amino acids. The non-essential amino acids
are:
▪ Alanine
▪ Arginine
▪ Asparaginine
▪ Aspartic acid
▪ Cysteine
▪ Glutamic acid
▪ Glutamine
▪ Glycine
▪ Hydroxyproline
▪ Proline
▪ Serine
▪ Taurine
▪ Tyrosine
Note:
o Arginine is classified as semi-essential since growth is retarded if it is not
available
o The presence of cystine and tyrosine in the diet will reduce the requirement
for methionine and phenylalanine respectively, hence they are also classed
as semi-essential.
4.1Classification of Proteins
Proteins may be classified on the basis of either their physical and chemical
properties or their nutritional qualities.
a. Physical-Chemical Properties
Each of the three groups within this classification may be subdivided into a
number of classes according to solubility.
-Simple proteins upon hydrolysis by acids, alkalies, or enzymes yield only
amino acids or their derivatives. Examples of this group are: albumins and
globulins found within all body cells and in the blood serum.
-Conjugated proteins are composed of simple proteins combined with a
non-protein substance. This group includes lipoproteins, the vehicles for
the transport of fats in the blood; nucleoproteins, the proteins of the cell
nuclei; phosphoproteins, such as casein found in milk and ovovitellin.
-Derived proteins are substances resulting from the decomposition of
simple and conjugated proteins. These include rearrangements within the
molecule without breaking the peptide bond, such as that occurring with
coagulation, and also substances formed by hydrolysis of the protein to
smaller fragments referred to as proteoses, peptones, and peptides.
b. Nutritional Quality of Proteins
Individual proteins have been found to differ in their ability to maintain life and
support growth. This ability depends on the biological value of the proteins,
which in turn is determined by the amino acid make-up, and how well it is
digested and absorbed.
Depending on their ability to maintain life and promote growth, proteins have
long been classified as complete, partially complete and totally incomplete.
Complete Proteins
Proteins that contain all the amino acids in the proportions needed by the body
are considered to have a high biological value and are referred to as complete
proteins. A complete dietary protein contains all the essential amino acids in
relatively the same proportions as the human body requires to maintain body
tissues and to promote a normal growth rate. It may or may not contain all the
non-essential amino acids. Generally, proteins derived from animal sources fall
in this category because of their similarity to the human protein tissue. The
only exception is gelatine (the protein in animal connective tissues) as it lacks
in tryptophan. Egg, milk, and meat (including some fish) proteins are all
complete but not necessarily identical in quality. Wheat germ and dried yeast
have a biologic value approaching that of animal sources.
Partially Complete Proteins
These proteins supply only some of the amino acids in limited amounts. They
will maintain life, but will not support growth as they lack sufficient amounts
of some of the amino acids necessary for growth. Gliadin, one of a number of
proteins found in wheat, is a notable example of proteins of this group. Adults
under no physiologic stress can maintain satisfactory nutrition for indefinite
periods when consuming sufficient amounts of protein from certain cereals or
legumes.
Totally incomplete proteins
These proteins are incapable of replacing or building new tissue, and hence
cannot support life, nor promote growth. Zein, one of the proteins found in
corn and gelatine are classic examples of such proteins that are incapable of
even permitting life to continue.
4.2 Functions of Proteins
1. Tissue maintenance and growth:
Protein is essential for the growth and maintenance of body tissue. They
constitute the chief solid matter of muscles, organs, and endocrine glands.
They are major constituents of the matrix of bones and teeth; skin, nails, and
hair; and blood cells and serum. As old skin cells fall off, new cells made
largely of protein grow from underneath to compensate.
Normal tissue growth in infancy, childhood and during pregnancy and
lactation necessitates additional amino acids over and above those needed for
tissue maintenance.
2. Formation of essential body regulating compounds (Hormones,
haemoglobin, anti - toxins and enzymes)
Hormones, enzymes and most other regulatory materials in the body are
protein substances. Hormones such as insulin, thyroxin and adrenaline have
vital regulatory functions in the body. The body's many hormones are also
messenger molecules. Various glands in the body release hormones in response
to changes in the internal environment. The blood carries the hormones to the
target tissues where they elicit the appropriate responses to restore normal
conditions. For example, when blood glucose rises, the pancreas releases the
hormone insulin, which stimulates the cell’s transport proteins to pump
glucose into the cells faster than it can leak out. Then, as blood glucose falls,
the pancreas reduces its insulin output.
Every cell contains many different enzymes each of which is responsible for
directing specific chemical reactions necessary to the cells life processes.
Enzymes are catalysts for metabolic processes and they are proteins in nature.

3. Regulation of fluid balance

Proteins assist in regulating the fluid balance of the cells. The body's fluids are
contained inside the blood vessels (intravascular), within the cells
(intracellular), and between the cells (intercellular). Fluids can move freely
between the compartments, but proteins are large and cannot pass freely
across cell membranes, so they remain in the blood cells where they attract
water. Their presence in the blood vessels creates pressure needed to draw
fluid back into the cell so that it does not accumulate outside the cell tissues. If
there is a deficiency of proteins, too much fluid collects outside the cells in the
intercellular spaces, causing oedema.
4. Maintenance of blood neutrality
Proteins also help to maintain the balance between acids and bases within the
body fluids. Normal body processes continually produce acids and bases,
which the blood carries to the kidneys and lungs for excretion. For normal
function, it is essential that the blood be maintained at nearly neutral, slightly
alkaline or basic state. A change in PH (acidity or alkalinity) for example can
alter enzymes so that they no longer function. The presence of protein in the
blood prevents too much acid or base from accumulating as it attracts either
acid or base depending on the body needs.
N.B.
A failure to regulate the blood’s acid – base balance will lead to either acidosis
or alkalosis. Extremes of either condition will lead to coma and eventually
death.
5. Regulation of electrolyte balance:
Proteins help to regulate the composition of body fluids by moving molecules of
the electrolytes into and out of cells. They act as “pumps’’ along cell
membranes where they pick compounds (such as sodium or potassium) from
one side of the membrane and deposit on the other side, thus enabling cells to
pick and release substances as needed. In this way, the concentration of
sodium and potassium in the fluids inside and outside of the cells is regulated.
An imbalance of the two electrolytes in the body is critical to neural
transmissions and muscle contractions, and could lead to irregular heartbeats,
muscular weakness, kidney failure, and even death.
6. Provision of Transport Mechanisms:
Proteins participate in the transport of nutrients and other substances in the
body, especially those that are not water soluble like the lipids (through
formation of lipoproteins) and fat-soluble vitamins. Many vitamins and
minerals depend on protein for transport.
Albumin, the chief protein in the blood serum, carries free fatty acids and acts
as a carrier for many drugs. The protein haemoglobin carries oxygen from the
lungs to the cells.

[Link] formation
Antibodies are ‘’giant’’ protein molecules that assist the body in fighting
infection and other toxic conditions. When the body detects invaders, (harmful
microorganisms), antibodies are formed specifically to fight the invaders. The
antibodies work so swiftly and efficiently that in a normal, healthy individual,
most diseases do not get started. Without sufficient protein, the body cannot
maintain its resistance to disease.
7. Provision of energy
Proteins are used as a source of energy if sufficient carbohydrates and fats are
not provided to meet the energy demands of the body. One gram of protein
yields 4 kcals.
However, using protein for energy purposes is unnecessarily expensive and
they also become unavailable for body building and repair.
Other Roles:
Proteins form integral parts of most body structures such as skin, muscles,
and bones. They also participate in some of the body's most important
activities such as blood clotting and vision. For example, when a tissue is
injured, a rapid chain of events leads to the production of fibrin (a stringy,
insoluble mass of protein fibres that forms a clot from liquid blood). Later and
more slowly, the protein collagen forms a scar to replace the clot and
permanently heal the cut.
The light-sensitive pigments in the cells of the retina are molecules of the
protein opsin. Opsin responds to light by changing its shape, thus initiating
the nerve impulses that convey the sense of sight to higher brain centres.
4.3 Sources of Proteins
Protein occurs almost in all foods since it is part of the cell structure, but the
content in different foods varies. The two basic sources include:
Animal Sources: These include; fish eggs, milk and milk products, poultry
and meat from all kinds of animals and insects.
Plant Sources: These in includes all types of legumes, nuts, seeds, bread,
cereals and cereal products and some dark green vegetables (available in small
amounts).
Note: Cereals are the primary source of protein for majority of the world
population.
Table 2: Average protein content of some foods
Food Average Serving Protein(G) Protein Quality
Whole Milk 1 Cup 8 Complete
Meat, fish, poultry 100g cooked 15-25 Complete
Eggs 1 whole 6g Complete
Dried beans or peas ½ cup 7-8g Incomplete
Bread, wheat 1 slice 2-3g Incomplete
Maize ½ cup 2 Incomplete
Macaroni/spaghetti ½ cup cooked 2 Incomplete
Vegetables ½ cup cooked 1-3 Incomplete
Fruits ½ cup 1-2 Incomplete
Orange 1 (one) 1 Incomplete
Peanut Butter 1 Table Spoon 5 Incomplete
Carrots ½ cup 1 Incomplete
Brocolli ½ cup 3 Incomplete

4.4 Dietary Protein Allowances

The recommended daily allowance (RDA) for protein is an average of 0.8g/kg
body weight per day. It is recommended that about 12% of the total calories
should be provided by proteins. However, during periods of increased growth,
proteins should provide about 14% of the calories.
It is desirable that at least one of the daily protein intake be derived from
animal sources. It is also important this protein is even throughout the day for
efficient use.
Age and body size affects a person protein need. Young individuals who are still
growing need more protein for growth compared to the amount of living tissue
to be maintained and repaired. Also the larger a person is greater the amount
of living tissue to be maintained and repaired.
RDA for various groups
The following are average RDAs for various groups of individuals.
Infants 0-6 months 2.2/kg body weight
7-12 months 2.0/kg body weight
a. Children 1-3 years 23g
4-6 years 30g
7-10 Years 36g
b. Male 11-12 Years 44g
15-22 Years 54g
23-50 Years 56g
51 Years + 56g
c. Female 11-14 Years 44g
15-18 Years 48g
19-22 Years 46g
23-50 Years 46g
51 Years + 46g
d. Pregnant Mothers +30g
e. Lactating Mothers +20g

Note: protein intake should be increased above the normal daily allowance
during periods of illness and convalescence.
Complementary Proteins
These are two or more proteins whose amino acid assortments complement
each other in such a way that, the essential amino acids missing in one are
supplied by the other and together they make a complete protein.
Generally, plant proteins are of lower quality, hence lower biological value than
animal proteins, and also offer less protein per unit of food (either weight or
measure). However, they do not all lack the same amino acids. When a variety
of foods are eaten together in a meal, one protein food may supply the amino
acid which is lacking in another food.
A food that supplies the amino acid that is absent or in short supply in another
is said to complement the other food. For example, legumes are high in lysine
and low in methionine, while grains are low in lysine and high in methionine.
When these foods are eaten together they complement one another and provide
high quality protein.
4.5 Digestion and Absorption of Proteins
Mouth
Protein are crushed and moistened in the mouth.
Stomach
In the stomach, hydrochloric acid denatures proteins so that digestive enzymes
can act on the peptide bonds, and also converts the inactive form of enzyme
pepsinogen to active form pepsin. Pepsin breaks down large polypeptides into
smaller polypeptides and some amino acids.
Small intestine
In small intestine, pancreatic and intestinal proteases hydrolyzes polypeptides
further into short peptide chains oligopeptides, tripeptides, dipeptides and
amino acids.
Trypsin - among other proteases which digest protein in the small intestine,
breaks large proteins to peptides.
Absorption
The cells of the small intestine absorb amino acids and have peptidase
enzymes on their surfaces that split most of the dipeptides and tripeptides into
single amino acids. The membranes of intestinal cells transport the amino
acids into the cells, where they are released into the bloodstream.
Metabolism of Proteins
Proteins are not stored in the body. When energy intake is adequate, the amino
acids derived from dietary protein are used first to make body proteins.
The end products of protein metabolism are the same as those that result from
metabolism of carbohydrates and fats. These are carbon-dioxide, water and
energy. However, the body must get rid of leftover nitrogen as urea. This strains
the body in the case of excessive protein intake in the diet.

Deficiency of Proteins
Deficiency of proteins and energy foods leads to kwashiorkor. This is Ghanaian
name that means a displaced person/child.
Symptoms:
● Round swollen cheeks
● Oedema in the legs and hands. Too fat as swollen with water. When press a
finger, it leaves a hole/dent.
● Big stomach
● Weak lose muscle
● Pale thin hair that is easily pulled out.
● Pale skin that peels off easily.
● Sad looking and inactive
● May stop walking and growing
Kwashiorkor is got quite easily. Children may die early or get well quickly if
attended to.
Marasmic kwashiorkor
This is a state where a child is very thin like marasmic child but
also has oedema like a kwashiorkor child. The child is inactive and
has no appetite.
Note: Most under nutrition is not seen. It is therefore important to
take a child for growth monitoring so that loss of weight can be
identified early and corrective feeding done.
Excess of Protein Intake
Excess of protein intake leads to deamination and elimination of
proteins through the urine. Excess intake also heavily stresses the
kidneys and the liver as these organs struggle to eliminate the
excess nitrogen from the amino acids. Since excess proteins can be
converted into fat, excess intake also leads to obesity.
Recommended Dietary Allowances
0.8-1 g/kg of body weight per day.