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

2.2.1 Types of Amino Acids
Amino acids are classified into two groups: essential and non-essential amino
acids.
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)
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:
Arginine is classified as semi-essential since growth is retarded if it is not
available
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.

2.2.2 Classification of Proteins

Proteins may be classified on the basis of either their physical and

chemical properties or their nutritional qualities.

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; keratin, collagen, and elastin in supportive tissues of the body,
hair and nails; globin in haemoglobin and myoglobin; and zein in corn,
gliadin and glutenin in wheat, legumin in peas, and lactalbumin and
lactoglobulin in milk.

Conjugated proteins are composed of simple proteins combined with a

nonprotein 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.
In eggs; metalloproteins, such as the enzymes that contain mineral
elements; mucoproteins, found in connective tissues, mucin, and
gonadotropic hormones; chromoproteins, such as haemoglobin and
visual purple; and flavoproteins, which are enzymes that contain the
vita- min riboflavin.
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.
 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.
2.2.3 Functions of Proteins
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.
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.
Cells can switch their protein machinery on or off in response to the body's
needs. Often hormones do the switching, with marvellous precision.
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.
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.
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.
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. A number of minerals also depend on proteins for
transport, e.g. the mineral iron. When iron enters an intestinal cell, it is
captured by a protein that will not let go unless the body needs it. Before
leaving the cell to enter the bloodstream, iron is attached to a carrier
protein, which may pass it on to a storage protein in the bone marrow or
other tissues, which will hold the iron until it is needed.
Antibodies 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.
Each antibody is designed to destroy a specific invader. Once the body has
manufactured antibodies against a particular antigen (such as the measles
virus), it develops a molecular memory known as immunity, such that it is
able to remember how to make them thereafter. Consequently, the next
time the body encounters the same invader, antibodies will be produced
even more quickly. When the body fails to get sufficient proteins from the
diet, production of antibodies is slowed and susceptibility to infections is
increased.
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.
2.2.4 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 Protein(G) Protein Quality
Serving
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

2.2.4 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 a bout 14% of the calories.
It is desirable that at lest one of the daily protein intake be derived from
animal sources. It is also important this protein evenly throughout te 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

Children 1-3 years 23g

4-6 years 30g

7-10 Years 36g

Male 11-12 Years 44g

15-22 Years 54g

23-50 Years 56g

51 Years + 56g

Female 11-14 Years 44g

15-18 Years 48g

19-22 Years 46g

23-50 Years 46g

51 Years + 46g

Pregnant Mothers +30g

Lactating Mothers +20g

Note: protein intake should be increased above the normal daily allowance
during periods of illness and convalescence.
2.2.5 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.
This measure of putting complementary proteins together in a meal is a
dietary strategy commonly used by many vegetarians and is usually referred
to as mutual supplementation. Combinations such as maize and beans, or
beans and rice, provide
high quality protein.
A number of researches have recently shown that different incomplete
proteins eaten any time during the same day can still be combined by the
body as complementary proteins to make complete proteins unlike the
previous believe that
the complementary proteins must be eaten at the same meal for the
balancing of the amino acids to occur.
Another way to improve the quality of vegetable proteins is to serve them
with small quantities of animal protein.

2.3 Lipids
The term a lipid is used scientifically to refer to a group of compounds, both
animal and plant that have a greasy, oily, or waxy consistency. They
comprise of triglycerides (fats and oils), phospholipids and sterols. These
are insoluble in water but are soluble in organic solvents such as ether,
alcohol, benzene, chloroform and acetone.
Triglycerides are the most obvious of the lipids, both in food and in the body,
as they represent 95% of the total food fats while the remaining 5% comes
from phospholipids (e.g. lecithin) and sterols (e.g. cholesterol.
In many occasions, the term fat is used to refer to all lipids.
Fats are essential nutrients in the human diet due to the energy value that
they contribute to the diet. They are especially useful components in the
diets that require high amounts of calories as they reduce bulk.
It is usually recommended that approximately 30% of the total calories in
our daily diet should come from fat.
2.3.1 Composition of Fats
Fats are composed of three elements namely; carbon, oxygen and hydrogen.
They are composed mainly of fatty acids. An acid is a substance made up of
a chain of carbon atomsto which hydrogen atoms and oxygen atoms are
attached. The characteristics of flavor, texture, melting point and nutritive
value depend on the kind of fatty acids as fat contains. A food fat, whether
solid or oil contains a mixture of fatty acids as fatty acids. All facts and oils
regardless of their acids contents have the same energy value, yielding nine
calories per gram, providing more energy than carbohydrate or proteins.
2.3.2 Characteristic of fats (physical) and chemical properties
The various characteristics of fats are;
Melting point
Each fat has its melting point and solidification point. Fats which contain a
high proportion of saturated fatty acids like stearic and palmitics are usually
solid at room temperature. Lard is mostly solid, but margarine can melt at a
temperature of 350
Emulsification
Fats are capable of forming emulsions with liquids. Fats and oils are lighter
than water. They are insoluble in water but form heterogeneous mixture
without water and when they are in the blood phospholipids and proteins
maintain emulsion.
Saponification
This refers to the formation of a soap of fatty acid and a cation. In the
alkaline medium of the intestine, for example free fatty acids may combine
with calcium to form an insoluble compound that is excreted in faeces. In
certain diseases characterized by poor fat absorption e.gsprue, the loss of
calcium can be significant. When fat are heated with sodium and potassium
hydroxide they readily undergo hydrolysis and become salts of fatty acids
such as sodium or potassium palmitate (soap). The hydrolysis of fats with
heat and alkaline into soap is known as saponification.
Hydrogenation
An unsaturated acid becomes saturated if it combines with hydrogen. The
process of hydrogenation takes place when unsaturated fats are exposed to
hydrogen in high temperature in the presence of a catalyst like nickel or
cobalt. The importance hydrogenation is that when oil becomes solid, can
easily be transported and exported.
Vegetable oils can be hydrogenated for example margarine, Kimbo and
vegetable ghee. Groundnuts, cotton seeds and coconut oils are usually used
for hydrogenation. Their melting point is between 35 and 37 degrees
centigrade. Apparently, the hydrogenation of fats has a disadvantage in that
the carotene that is usually present in the oils is lost during hydrogenation. It
is also reduces the linoleic acid content. This requires fortification of vitamins
especially A and D and color to be added.
Rancidity
The presence of air can induce oxidation of fats resulting in changes in flavor
and odour. This change is commonly known as rancidity. These changes are
accelerated upon exposure to light and in the presence of certain minerals.
This occurs readily in fats that have a high proportion of unsaturated fatty
acids.
Some fats are naturally protected from rapid oxidation by the presence of
anti-oxidants like Vitamin E.
2.3.3 Types of Lipids
Types of Lipids in body cells and tissues:
Triacyglycerols or Triglycerides (or TGs)
Glycerolphospholipids
Sphingolipids
Eicosanoids
Cholesterol
A class of lipids called triglycerides provides most of the energy dietary fat.
Triglycerides account for approximately 98% of the lipids in food and are the
major storage form of fat in the body. They are made up of two components:
glycerol and fatty acids.
2.3.4 Role of Lipids In The Body

Source of essential fatty acids

(The essential fatty acids are those that the body cannot synthesize and
must be supplied by food. These are polyunsaturated linoleic and linolenic
acids-captured in EFA section). Essential fatty acids are needed for the
normal functioning of all tissues, as they form a part of the structure of the
cell membrane especially the brain, helping to transport nutrients and
metabolites across the cell membrane. Linoleic is involved in the transport
and metabolism of cholesterol. Essential fatty acids are also involved in brain
development (Grey matter – 50% lipids and white matter – 70% lipids). EFA
are also required for the synthesis of prostaglandins, hormone like
compounds that act as regulators. Prostaglandins are synthesized mainly
from arachidonic acid.
Carrier of fat soluble vitamins
Fats serve as carriers of vitamins A, D, E and K. The conditions that interfere
with the absorption or use of fat reduce the amount of fat-soluble vitamins
available to the body.
Energy source
Fat is the body’s most concentrated energy source. Except for the cells of
the brain and central nervous system (CNS), all cells can use fatty acids
directly as an energy source.
Fat supplies more energy than carbohydrate and protein.
Reserve fuel supply source
Excess calories are stored in the adipose cells (group of specialized cells)
whether from protein, carbohydrate or fat. Fat that has been deposited in fat
tissue cannot be excreted; fat stores are only reduced when the calorie value
of the food eaten is less than the body’s energy needs, then fat is released to
provide energy. Serve as reserve fuel (bank balance) that can be drawn
when necessary, e.g. in time of illness or food intake is low or restricted.
Insulator and protector
Fat deposits beneath the skin help insulate the body, protecting from
excessive heat or cold. Fats round out the figure and pads the joints and
other body parts, such as the soles, palms, and buttocks, protecting them
from outside pressure. Fat also protects the vital organs, such as the heart
and kidneys, by holding them in position and protecting them from physical
trauma.
Provider of meal satisfaction
Fats add flavour, texture and taste to meals and help to make food
palatable. Fats remain in the stomach longer than either protein or
carbohydrate because they are digested and absorbed at lower rate. This
prolonged digestion contributes to a feeling of fullness and delays the onset
of hunger pangs. Fat has a high satiety effect.
Fat reduces the total volume of food taken, because of its high satiety value
and concentration of energy.
2.3.5 Digestion of Fats
Mouth
In the mouth fats are brought to a temperature which favours digestive
operations. There is no action of fats in the mouth.
Stomach
The gastric lipase is only capable of hydrolyzing alimentary fats which are
already emulsified e.g. egg yolk, ice cream and salad dressings, but the
action is not important. It is more important in infants. The presence of fats
in the foods delays emptying of the stomach. This mechanism of the delay
has been attributed to the inhibitory action of the stomach of a hormone
enterogastrone which is liberated when fat enters the duodenum.
Small intestine
As the chyme enters the duodenum the presence of fats stimulates the
intestinal wall to secrete cholecystokinin, a hormone that is carried to the
gall bladder by the bloodstream. The hormone stimulates the contraction of
gall bladder thereby forcing bile into the common duct and then into the
small intestine. Bile has several important functions in fat digestion and
absorption.