PROTEINS

• Whereas plant structure is primarily carbohydrates, the structure of humans

and animals are built on protein.
• Proteins are macromolecules consisting of long chains of amino acid subunits.
The Recommended Dietary Allowance (RDA) for protein is 0.8g/k body weight
for a healthy adult.
• Protein requirements increase during hyper metabolic stress and in disease.
Protein rich foods are obtained primarily from animal flesh or from animal
products such as eggs and milk.
• Most plant foods are relatively poor in protein, with the exception of legumes.
Dietary proteins are powerful compounds that build and repair body tissues,
from hair and fingernails to muscles.
• In addition to maintaining the body’s structure, proteins speed up chemical
reactions in the body, serve as chemical messengers, fight infection, and
transport oxygen from the lungs to the body’s tissues.
• Although protein provides 4 calories of energy per gram, the body uses
protein for energy only if carbohydrate and fat intake is insufficient. When
tapped as an energy source, protein is diverted from the many critical
functions it performs for our bodies.
• Proteins are made of smaller units called amino acids. Of the more than 20
amino acids our bodies require, eight (nine in some older adults and young
children) cannot be made by the body in sufficient quantities to maintain
health
• These amino acids are considered essential and must be obtained from
food.
• When we eat food high in proteins, the digestive tract breaks this dietary
protein into amino acids. Absorbed into the bloodstream and sent to the
cells that need them, amino acids then recombine into the functional
proteins our bodies need.
• Some people, especially developed countries, consume more protein than
the body needs. Because extra amino acids cannot be stored for later use,
the body destroys these amino acids and excretes their by-products.
• Alternatively, deficiencies in protein consumption may result in health
problems. Marasmus and kwashiorkor, both life-threatening conditions, are
the two most common forms of protein malnutrition.
1.Discuss the causes, signs and symptoms of Marasmus and kwashiorkor
2.What are the differences between the two conditions
• Some health conditions, such as illness, stress, and pregnancy and breast-
feeding in women, place an enormous demand on the body as it builds
tissue or fights infection, and these conditions require an increase in protein
consumption.

• To support their rapid development, infants and young children require

relatively more protein than adults. Once in adolescence, sex hormone
differences cause boys to develop more muscle and bone than girls; as a
result, the protein needs of adolescent boys are higher than those of girls.
• Proteins are built from amino acids. Amino acids are the subunits of
proteins in much the same way that monosaccharide sugars are the sub-
units of polysaccharides.
• About 20 naturally-occurring amino acids have been identified with
certainty and they all have an NH2 (amino) group and a COOH (carboxyl)
group

• They include alanine, arginine, asparagine, aspartic acid, cysteine,

glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, proline, serine, threonine, tryptophan,
tyrosine, and valine.
• All 20 are constructed according to a general formula shown below:
• As the formula shows, the amino and carboxyl groups are both
attached to a single carbon atom, which is called the alpha carbon
atom.
• Attached to the carbon atom is a variable group (R); it is in their R
groups that the molecules of the 20 standard amino acids differ from
one another. In the simplest of the acids, glycine, the R consists of a
single hydrogen atom.
• Other amino acids have more complex R groups that contain carbon
as well as hydrogen and may include oxygen, nitrogen, or sulphur, as
well.
• In alanine R is CH3, in valine it is C3H7.
• Amino acids unite to form proteins in much the same way that
monosaccharide sugars combine to form polysaccharides, and fatty
acids and glycerol to form fats.
• The first step in this process involves the combination of two amino
acids by a reaction between the amino and the carboxyl groups.
• The process involves the loss of a water molecule (condensation) and
the two amino acids become joined by a peptide link to form a
dipeptide.
• Continued condensation leads to the addition of further amino acids
resulting in the formation of a long chain called a polypeptide.
• A particular polypeptide may be composed of as many as a hundred amino
acids.
• A typical protein consists of one or more polypeptide chains which may be
folded, branched and cross-linked at intervals.
• The cross-linkages may be of several sorts: hydrogen, bonds, ionic bonds or
sulphur bridges. The sulphur bridges are the strongest and contribute to the
great toughness of certain proteins.
• Although there are about 20 naturally occurring amino acids, the number of
possible ways in which they can be combined is almost infinite.
• The individuality of a particular protein is determined by the sequence of
amino acids comprising its polypeptide chains, together with the pattern of
branching, folding and cross-linkages.
• Some proteins contain only a proportion of the known amino acids, others
contain all of them.
 Protein structure
• Proteins assume four structures:
• Primary structure: Is the chain of amino acids of which the polypeptides are
composed. Peptide bonds are formed between sequential amino acids
according to directions on mRNA. The completed protein is a linear chain of
amino acids.
• Secondary structure: This structure refers to the helical coiling of the chains.
Attractions between R groups of amino acids create helices and pleated
sheet structures.
• Tertiary structure: This refers to the way the helically coiled chains are
folded. Helices and pleated sheets are folded into compact domains.
• Quaternary structure: Refers to a structure were several polypeptide chains
are clumped together (i.e. When a protein is made up of more than one
polypeptide chain).
Protein structure is critical for protein function. If the linear protein sequence is
altered, as in certain genetic diseases, the protein is unable to form active sites
and its activity is limited or eliminated entirely.

One feature of proteins related to their structure is that they have both acidic
and basic properties. This is due to the presence of amino (basic) and carboxyl
(acidic) ions at the free ends of the polypeptide chains. This makes it possible
for the protein to combine with basic or acidic substances, enabling them to
function as buffers.
 Classification of proteins according
to structure
1) Fibrous proteins
•These are made up of peptide chains twisted into string like structures, the
molecules resemble a fiber either as a coil or simply extended.
•Fibrous proteins give protein molecules a distinct elastic property evident in
wool, hair and dough gluten.
• Examples of fibrous proteins are collagen, keratin, fibrinogen, and muscle
proteins.
 Collagen
• makes up bone, skin, tendons, and cartilage, is the most abundant protein
found in vertebrates.
• The molecule usually contains three very long polypeptide chains, each with
about 1000 amino acids that twist into a regularly repeating triple helix and
give tendons and skin their great tensile strength.
• When long collagen fibrils are denatured by boiling, their chains are shortened
to form gelatin.
Keratin
• Makes up the outermost layer of skin and the hair, scales, hooves, nails, and
feathers of animals, twists into a regularly repeating coil called an alpha helix.
• Serving to protect the body against the environment, keratin is completely
insoluble in water.
• Its many disulfide bonds make it an extremely stable protein, able to resist the
action of proteolytic (protein-hydrolyzing) enzymes.
 Fibrinogen
• is a blood plasma protein responsible for blood clotting. With the
catalytic action of thrombin, fibrinogen is converted into molecules of
the insoluble protein fibrin, which link together to form clots.

Muscle protein
• Myosin, the protein chiefly responsible for muscle contraction,
combines with actin, another muscle protein, forming actomyosin,
the different filaments of which shorten, causing the contracting
action.
 2) Globular proteins
• These are proteins which have their molecules in a tangled/globular chain
(coiled into a compact spherical molecule).
• Such proteins are relatively soluble and readily go into colloidal suspension.
• They play a dynamic role in body metabolism.
• Examples are albumin, globulin, casein, haemoglobin, all of the enzymes, and
protein hormones.
• The albumins and globulins are classes of soluble proteins abundant in animal
cells, blood serum, milk, and eggs.
• Haemoglobin is a respiratory protein that carries oxygen throughout the body
and is responsible for the bright red colour of red blood cells.
 Enzymes
• All of the enzymes are globular proteins that combine rapidly with other
substances, called substrate, to catalyze the numerous chemical reactions in the
body.
• Chiefly responsible for metabolism and its regulation, these molecules have
catalytic sites on which substrate fits in a lock-and-key manner to trigger and
control metabolism throughout the body.
Hormones
• Come from the endocrine glands. They stimulate target organs that in turn initiate
and control important activities—for example, the rate of metabolism and the
production of digestive enzymes and milk.
• Insulin, secreted by the islets of Langerhans, regulates carbohydrate metabolism
by controlling blood glucose levels.
• Thyroglobulin, from the thyroid gland, regulates overall metabolism
• Calcitonin, also from the thyroid, lowers blood calcium levels.
 Antibodies
• Also called immunoglobulins, antibodies make up the thousands of
different proteins that are generated in the blood serum in reaction
to antigens (body-invading substances or organisms).
• A single antigen may elicit the production of many antibodies, which
combine with different sites on the antigen molecule, neutralize it,
and cause it to precipitate from the blood.
 Conjugated proteins
• In general proteins fall into two groups discussed above, sometimes
however, proteins may, according to structure be called conjugated
proteins.
• Many structures found in organisms consist of protein combined with
another compound to form a conjugated protein. The non protein
component to which the protein is attached is called the prosthetic
group. Egg yolk, mucus and haemoglobin are all examples of conjugated
proteins.
• In egg yolk the prosthetic group is phosphoric acid, in mucus it is a
carbohydrate, in haemoglobin it is an iron-containing pigment called
haem.
• If the protein is conjugated with a carbohydrate the resulting compound
is called a glycoprotein.
 Classification of proteins according
to Biological Value

• Biological value of a protein is the measure of how nourishing a

protein is, i.e. how much of a protein will be made available to the
body for protein synthesis.
• Proteins with essential amino acids in the proportion required by the
human body are said to have high biological value-their nitrogen is
available for growth and repair. According to this classification, we
have complete and incomplete proteins
•.
• Complete proteins contain essential amino acids and are regarded as
proteins of high biological value.
• This is because they contain amino acids in all proportions which
promote growth when used as a sole source of protein in the diet.
• Animal proteins, found in such food as eggs, milk, meat, fish, and
poultry, are considered complete proteins because they contain all of
the essential amino acids our bodies need
• Incomplete proteins are poor quality proteins i.e. proteins of
low biological value. They have a limited value and if used as a
sole source of protein in a diet, they cannot support growth.
• Most vegetable proteins except soybean are incomplete
proteins. Plant proteins, found in vegetables, grains, and beans,
lack one or more of the essential amino acids.
• However, plant proteins can be combined in the diet to provide
all of the essential amino acids (also known as
supplementation).
• A good example is rice and beans. Each of these foods lacks
one or more essential amino acids, but the amino acids
missing in rice are found in the beans, and vice versa.
• So when eaten together, these foods provide a complete
source of protein. Thus, people who do not eat animal
products (e.g. Vegetarians) can meet their protein needs
with diets rich in grains, dried peas and beans, rice, nuts, and
tofu.
Biological value of protein = Protein used by the body X 100

Protein taken in as food

Biological values of some foods

Egg 100%

Milk 95%

Meat/ Fish 80/ 90%

Soybean 74%

Rice 67%

Cereals (wheat) 63%

Maize 40%
 Supplementary value of a
protein
• Supplementary value of a protein refers to the capacity of a
protein to make good of another’s deficiency. If one
consumes one type of protein that is lacking certain amino
acids in combination to another containing the missing
amino acid, then there will be supplementation between the
two products.
• An example is eating bread and gelatine; bread is deficient in
lysine whereas gelatine is relatively rich in lysine but
deficient in tryptophan. Others include fish and rice, legumes
and cereals.
 Proteins in the diet

• Proteins are important constituents of the diet, in the body’s

cells the various proteins are assembled from the necessary
amino acids and it is therefore imperative that all the amino
acids should be available in sufficient quantities.
• In humans, all but ten of the amino acids can be synthesised
by the body itself from compounds derived from the
metabolism of various food substances.
• This involves a process called transamination-the amino group is
removed from one of the dietary amino acids and transferred to a
carbohydrate derivative which is thereby converted into a new
amino acid.
• Since these particular amino acids are not required in the diet they
are known as non essential amino acids.
• The remaining ten amino acids cannot be synthesised by the body
itself, at any rate fast enough, and so they have to be supplied in
the diet.
• They are known as essential amino acids. Two of them are
required for growth only and are not required by the adult. The
other eight are required all the time, though they vary in their
degree of indispensability.
• Older views of the nutritional classification of amino acids
categorized them into two groups, essential (indispensable) and
non essential (dispensable).
• Although this classification has been maintained, the definition of
non essential amino acids has become blurred as more information
on the intermediary metabolism of these compounds becomes
available.
• Recent authors now divide non essential amino acids into two
classes; truly non essential and conditionally essential.
• Non-essential amino acids are now more rigidly defined as those
synthesized by either reductive amination of a keto acid by
ammonium or by transamination of a carbon chain synthesized in
the central pathway of the Kreb’s cycle.
• According to this definition, only glutamate, aspartate and alanine
should be regarded as truly non-essential.

• Conditionally essential amino acids are now defined as those that

derive from the metabolism of either other amino acids or other
complex nitrogenous metabolites.
• A key point is that the synthesis of these amino acids does not
involve the simple transamination.
• The term ‘conditionally essential’, recognizes that in principle
these amino acids may be needed in the diet unless abundant
amounts of their precursors are available for their synthesis at
nutritionally significant rates.

• Note: there may be physiological circumstances (e.g. in the new-

born) in which the enzymes involved in what are quite complex
synthetic pathways may be present in inadequate amounts, so
that there is then a dietary requirement for this amino acid.
 General functions of proteins
• Forming structures of the body: cell membranes, connective tissue,
muscle fibers, skeletal materials.
• Like fat and carbohydrates, proteins can be broken down to
release energy. Protein is only used as a source of energy in
conditions of starvation, even then it is always the less essential
tissues such as skeletal muscles and gut wall which are used first.
• Proteins also act as regulators in that they control the chemical
reactions and metabolic processes which occur in organisms
 Deficiency of proteins
The effects of protein deficiency include the following:
1. In pregnant women the baby may be stillborn or
premature
2. In infants and early childhood: Stunted growth, mental
retardation and kwashiorkor.
3. In adults, weakness, anaemia, thin muscles, diarrhoea,
recurrent infections, delay in wound healing, oedema, and
liver cirrhosis.
 Sources:

• Animal proteins (best for body-building): Milk, curds, cheese,

egg, fish and meat.
• Vegetable proteins: Groundnuts and soya beans are the best
sources of proteins. Others are
• Cereals, pulses, legumes (peas and beans) oil seeds.
 Protein processing and
Digestibility
Digestibility of protein sources is affected by multiple factors:
• Proteins are kept in proper configuration by hydrogen and ionic
interactions; these bonds are loosened in the presence of acid,
salt, and heat.
• By denaturing proteins these methods also soften connective
tissue in proteins and release muscle proteins from their
attachments, thereby making all proteins more available to
digestive enzymes.
• Plant protein is less well digested than animal protein, partly because it
is encased in carbohydrate cell walls and is less available. Some plants
also contain enzymes that interfere with protein digestion.
• These enzymes must be heat inactivated before consumption. For
example soy beans contain a trypsinase that inactivates trypsin, the
major protein digesting enzyme in the intestine.
Food processing can also damage amino acids and reduce their
digestibility in the following ways:
• Mild heat treatment in the presence of reducing sugars (glucose and
galactose), as in milk processing, causes loss of available lysine.
• Lactose reacts with lysine side chains and renders them unavailable.
This reaction can cause significant lysine loss at high temperature.
 Protein digestion and
absorption
• After ingestion, proteins are denatured by the acid in the stomach and
then pass into the small intestine where the peptide bonds are
hydrolysed by a variety of proteolytic enzymes.
• These bond-specific enzymes originate in the pancreas and include
trypsin, chymotrypsin, elastin and carboxypeptidase.
• The resultant mixture of free amino acids and small peptides is then
transported into the gut cells by a series of carrier systems, each specific
for a limited range of substrates.
• After hydrolysis of the peptides, the free amino acids are then secreted
into the bloodstream or are further metabolized within the gut itself.
• Absorbed amino acids pass into the portal vein and then in to the liver,
where a proportion of the amino acids is taken up and used: the
remainder pass into the systemic circulation and are then transported
into the tissues cells.
 Factors affecting protein
utilisation
Amino acid balance
•Each type of protein found in the body requires a specific
combination or specific ratio of amino acids. Unless the individual
consumes enough amino acids then the protein consumed will not
be utilised fully unless it is specific. The presence of all essential
acids is important for protein synthesis.
 Calorific value or intake
• Normally the major source of calories is carbohydrate and or fat. As
the calorific value of the diet drops below a certain critical point,
retention of nitrogen drops indicating that part of the protein was
deaminated and used for energy purposes. If the calorific value is
adequate, the level of protein utilization depends on protein need
and the quality of the protein.
Injury
• There is increased nitrogen excretion after injury. High protein
intakes immediately after injury neither prevents nor reverses the
nitrogen loss. These losses are recovered once healing starts.
 Properties of proteins
1) Denaturation
•This refers to the untwisting of protein molecules causing loss of
protein structure and function. This process is generally irreversible.
Soluble proteins are denatured either chemically or by the effect of heat
when their molecules unfold and lose most of their water solubility.
a)Denaturation by heat
This is the most frequent cause of denaturation. The application of
strong heat to most proteins especially albumen in eggs causes the
uniting bonds to break.
b) Denaturation by agitation
Heat coagulates proteins . The denatured protein fibers shorten
producing a shrunken appearance e.g In beating, shaking/whisking an
egg white causes (if excessive) solid sheets of denatured proteins
c) Denaturation by chemicals
Acids denature proteins, for example in milk forming a clot.
d) Denaturation by freezing
Freezing of foods containing proteins draws water out of the
protein molecules resulting into denaturation.