Dr.

Muna Abdullahi
Nutritionist & Dietitian
Macro - nutrient

Proteins
Proteins
• Proteins are complex organic compound that made up of hundreds or thousands
of smaller units called amino acids, which are attached to one another in long
chains.

• Proteins do most of the work in cells and are required for the structure, function,
and regulation of the body's tissues and organs.
Cont..

• Protein provides the body with building blocks (amino acids) for muscle and
other important structures such as the brain, nervous system, immune system,
blood, skin, and hair.
Chemical composition of protein
• Protein differ from carbohydrates and fats in that they contain nitrogen in
addition of carbon, hydrogen and oxygen and few contain sulfur, most of
proteins contain phosphorus and some specialized proteins contain iron,
iodine, copper and other organic elements.

• In the absence of glucose or carbohydrate, the body can reverse-process protein

(a conversion called gluconeogenesis) to use as energy.
Chemical formula

• Protein have general chemical formula : RCH(NH2)COOH, where C is carbon,

H is hydrogen, N is nitrogen, O is oxygen, and R is a variable group, varying
in composition and structure, called a side chain.
Protein have many functions that include:

• Building & repairing tissues and muscle

• Regulatory functions-hemoglobin, for carries oxygen to the tissue

• Formation of enzymes, hormones and other secretions

• Energy producer and body temperature

• Immune function
Structure of protein
• Peptide bonds

• Each protein in your cells consists of one or more polypeptide chains.

• Each of these polypeptide chains is made up of amino acids, linked together in a

specific order.
Four types of protein structure
1. Primary Structure

2. Secondary Structure

3. Tertiary Structure

4. Quaternary Structure
Properties of protein

• Proteins are colloids; they act both as weak acids and bases.

• Proteins are soluble in sodium hydroxide and when the alkaline solutions of
proteins are acidified, the proteins are precipitated.

• properties dictated by side chain (R)Polar (hydrophilic(water loving): contain O

and N

• Nonpolar (hydrophobic(water hating)

• Acidic: negative charge, Basic: positive charge

• When proteins are heated, a decrease in their solubility is observed, this is known
Classification of protein
• Proteins can be classified as:

( a) Simple proteins: On hydrolysis they yield only the amino

acids.

Examples are: albumins, globulins, glutelins, albuminoids,

histones and protamines.
Cont..
b. Conjugated proteins: These are simple proteins combined with
some non-protein material in the body.

Examples are: nucleoproteins, glycoproteins, phosphoproteins,

haemoglobins and lecithoproteins.

(c) Derived proteins: These are proteins derived from simple or

conjugated proteins by physical or chemical means.

Examples are: denatured proteins and peptides.

Types of protein in human body
1. Structural proteins : is forms of proteins for a skeleton or
contributes to the mechanical/powered properties of a living
organism, cell,

-Function: Support

Example: Collagen and elastin provide a fibrous framework in animal,

human connective tissues such as tendons and ligaments

- Keratin is the protein of hair,, nails, hoof, feathers

2. Storage Proteins: serve as biological reserves/ storage of
metal ions and amino acids, used by organisms.
Function: Storage of amino acids and metal ion

Example: Ovalbumin is the protein of egg whites

Casein is the protein is mammal milk

Ferritin is an example of a storage protein that stores iron.

3. Transport Proteins: is a protein that serves the
function of moving other materials within an organism.
Function: transport other substances

Example: hemoglobin transports oxygen from the lungs

to the other parts of the body.
4. Hormonal Proteins: are biological molecules used in
multicellular organisms to direct and coordinate
development, growth, and reproduction.
Function: coordination of bodily activities.

Example: Insulin helps control the concentration of sugar

in blood.
5. Receptor Proteins: located within the cell surface
membrane, which binds to a specific molecule.
Function: response of cell to chemical stimuli/motivation

Example: neuron receptors respond to chemicals

released by other nerve cells
6. Contractile proteins: are proteins responsible for contraction skeletal muscle.

• Function: Movement
Example: Actin and myosin are the proteins responsible for muscle movement

7. Defensive Proteins: are know as antibodies and are found in the immune
system.
Function: Protection against disease

• Example: Antibodies combat bacteria and viruses

8. Enzymatic Proteins: act as catalysts in biochemical reactions,
meaning that they speed the reactions up.
Function: Speed up chemical reactions

Example: trypsin, pepsin, amylase

Amino acids
• Amino acids are organic compounds that combine to form proteins.

• Amino acids and proteins are the building blocks of life.

• When proteins from food are digested or broken down, amino acids are left.

• The human body uses amino acids to make proteins to help the body.
 How Amino acids link together

• There are 20 different amino acids which make up proteins.

• Each amino acid consists of a central carbon.

• The central carbon is bonded to an amine group (NH2), a carboxyl group

(COOH), a hydrogen atom and an R group.

• Amino acids can be linked together when the amine group of one amino acid is
bonded to the carboxyl group of a different amino acid.
Cont…

• The COOH donates an OH group and the NH2 donates a H.

• The OH and H come together to form a water molecule,(H2O) so this

process is called dehydration synthesis - water is removed to form
something new.

• The bond which holds the amino acids together is called a polypeptide.
Function of Amino acid
• Amino acids build muscles,

• Cause chemical reactions in the body,

• Transport nutrients,

• Prevent illness, and carry out other functions.

Cont…
• Amino acid deficiency can result in

• Decreased immunity,

• Digestive problems,

• Depression,

• Fertility issues,

• Lower mental alertness,

• Slowed growth in children, and many other health issues.

Amino acids are classified into three groups:
1. Essential amino acids

2. Nonessential amino acids

3. Conditional amino acids

ESSENTIAL AMINO ACIDS
• Essential amino acids cannot be made by the body. As a result, they must come
from food.

• The 9 essential amino acids are:

1. histidine,

2. isoleucine,

3. leucine,

4. lysine,

5. methionine,
CONT..

6. phenylalanine,

7. threonine,

8. tryptophan, and

9. Valine.
NONESSENTIAL AMINO ACIDS
• Nonessential means that our bodies produce an amino acid, even if we do not
get it from the food we eat.

• 11 Nonessential amino acids include:

1. alanine,

2. arginine,

3. asparagine,

4. aspartic acid,

5. cysteine,
CONT…
6. glutamic acid,

7. glutamine,

8. glycine,

9. proline,

10. serine, and

11. tyrosine.
CONDITIONAL AMINO ACIDS

• Although 11 of the amino acids are nonessential, humans may require some of
them if they are under stress or have an illness.

• During these times, the body may not be able to make enough of these amino
acids to keep up with the increased demand. These amino acids are
“conditional,” which means that a person may require them in certain
situations.
Conditional amino acids include:
1. arginine,

2. cysteine,

3. glutamine,

4. tyrosine,

5. glycine,

6. ornithine, (is a non-proteinogenic amino acid that plays a role in the urea cycle.)

7. proline, and

8. serine.
Nutritional classification protein quality:
• based on the ability of a protein to support growth and maintenance

1. high quality (complete) protein: contain all essential amino acid in sufficient

ratios and quantities to support growth and maintenance (Animal protein).

2. medium quality (partially complete) protein: Contain all essential amino acids

but deficient in one or more essential amino acids hence support maintenance but

not growth (plant protein) e.g: cereals (lys),legumes(met)).

3. Low quality (totally incomplete) protein:

• Lack one or more essential amino acids hence does not support both
growth and maintenance (gelatin and zein (trp))-protein in the maize.

• Gelatin is a mixture of peptides and proteins produced by partial

hydrolysis of collagen extracted from the skin, bones, of animal body
parts.
CONT..
• Improvement of medium quality proteins:

• The quality of plant based proteins can be improved by their ability to

supplement the deficiency of one another dietary protein

supplementation (?) cereals (lys)+legumes (meth) e.g: bread + foul or

Rice + beans
Protein digestion
• Protein digestion occurs in the stomach and duodenum in which 3 main
enzymes,

• pepsin secreted by the stomach and trypsin and chymotrypsin secreted by the
pancreas, break down food proteins into polypeptides that are then broken down
by various exopeptides and dipeptides into amino acids.
CONT..
• The digestive enzymes however are mostly secreted as their inactive
precursors, the zymogens. For example, trypsin is secreted by pancreas in the
form of trypsinogen, which is activated in the duodenum by enterokinase to form
trypsin.

• Trypsin then cleaves proteins to smaller polypeptides.

Protein absorption
• In the lower parts of the small intestine, the amino acids are transported from
the intestinal lumen through the intestinal cells to the blood.

• This movement of individual amino acids requires special transport proteins

and the cellular energy molecule, adenosine triphosphate (ATP).

• Once the amino acids are in the blood, they are transported to the liver.

• As with other macronutrients, the liver is the checkpoint for amino acid
distribution, where they are then resynthesized into new tissue proteins or are
catabolized for energy.
Protein Metabolism

• Protein turnover – the degradation and synthesis of endogenous protein.

• When proteins break down, they free amino acids to join the general
circulation…what happens next?
• Recycled to make new proteins
• OR
• Nitrogen is removed and remaining part of amino acid is used for energy
(Deamination: NH2 is removed to make urea)
Half Life of Body Proteins
• Red Blood Cell – 120 days

• Intestinal Mucosal Cell - <1 day

• Liver Cells – very long half life

• Collagen – several 100 days

• Muscle protein – 100 days

Foods that supply protein
• Foods in abundance are :

• Milk,

• Yogurt, and Cheese Group and

• the Meat, Poultry, Fish,

• Beans, Eggs, and Nuts e.tc

Cont..
• Servings of foods from the Vegetable Group and the Bread, Cereal, Rice and
Pasta Group can also contribute a moderate amount of protein to the diet.

• Fruits and Fats/Oils do not supply a significant amount of protein to the diet.
Protein Requirements:

• RDA = 0.8 grams per kg body wt. or

• 10-20% of kcalorie intake

Protein–energy malnutrition (PEM),

• Protein–energy malnutrition (PEM), is a form of malnutrition that is

defined as a range of pathological conditions arising from coincident
(parallel) lack of dietary protein and/or energy (calories) in varying
proportions.

• The condition has mild, moderate, and severe degrees.

• Types include:

1. Kwashiorkor (protein malnutrition predominant)

2. Marasmus (deficiency in calorie intake)

3. Marasmic kwashiorkor (marked protein deficiency and marked calorie

insufficiency signs present, sometimes referred to as the most severe form of
malnutrition)
Protein Energy Malnutrition
• Protein-energy malnutrition or PEM is the condition of lack of energy due to the
deficiency of all the macronutrients and many micronutrients.

• It can occur suddenly or gradually. It can be graded as mild, moderate or severe.

In developing countries, it affects children who are not provided with calories and
proteins. In developed countries, it affects the older generation.
Classification Of Protein Energy Malnutrition
• PEM can be classified into two types:

• Primary PEM

• Secondary PEM
Cont..
• Primary PEM

• This type of protein-energy malnutrition is found in children. It is rarely found

in the elders, the main cause being depression. It can also be caused due to
child or elder abuse. In children,

• PEM is primarily of two types:

• Kwashiorkor

• Marasmus
Kwashiorkor
• This occurs due to the abandonment(reject) of breastfeeding before the actual age
due to the birth of a younger sibling.

• Kwashiorkor may also be the outcome of acute illness such as gastroenteritis.

• It is confined only to a few parts of the world such as rural regions of Africa,
Pacific Islands, Caribbean. In these places, the food is low in protein and high in
carbohydrates.

• It causes leakage of the cell membrane, releasing the intravascular fluid and
proteins. This results in oedema.
Marasmus
• Weight Loss

• Fat and muscle depletion

• Most common in developing countries.

• More common than Kwashiorkor

• Prevalent in children younger than those affected by Kwashiorkor

• Cell-mediated immunity is impaired, making the children more susceptible to

infections.
Secondary PEM
• It is caused due to disorders in the gastrointestinal tract.

• It can be caused due to infections, hyperthyroidism, trauma, burns, and other

critical illnesses.

• It decreases appetite and impairs nutrient metabolism.

Treatment of Protein Energy Malnutrition
• Protein Energy Malnutrition can be treated in the following ways:

• Oral feeding

• Avoiding lactose

• Supportive care

• Reduction in poverty

• Improving nutritional education and public health measures

• Starvation can be treated by providing a balanced diet

• Multivitamin supplements

• Treat infections and fluid and electrolyte abnormalities, in severe cases

CONT..
• PEM can be treated by providing a balanced diet. The micronutrients should be
taken twice, the daily recommended allowance until recovery.
Protein Excess
• The excess protein comes when the consumption is much more than the
requirement then May contribute to weight gain since many high protein foods
are also high in fat (may also increase risk for heart disease)

• Increased risk of kidney disease

• Amino acid supplementation is not needed for body building if there is enough
AAS in the body.