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DEBRE MARKOS UNIVERSITY
COLLEGE OF MEDICINE AND HEALTH SCIENCE
DEPARTMENT OF ENVIRONMENTAL HEALTH
COMMUNITY NUTRITION
Prepared By: Group One
Acc. Year : - 2015/2023
SUBMITTED TO MATTHIAS K.
SUBMISION DATE 26/05/2015E.C
DEBRE MARKOS, ADDIS ABABA
Protein
 Objective
Define protein and list it’s composition.
you able to list and describe classification of protein.
You able to how the protein digest and absorbed in our body.
List and Describe food source.
List and describe requirement of protein and disease related to protein.
Proteins large biomolecules and macromolecules that comprise one or more
long chain of amino acid residues.
After water, protein is the most plentiful substance in the body.
Proteins grow, maintain, and replace the tissues in our bodies.
Therefore our muscles, organs, and immune systems are mostly made
Of protein Once protein is digested it is broken down into its amino acid.
You'll find protein in lots of yummy foods like eggs, nuts, beans, fish,
meat, and milk.
It is an organic compound contain C,H,O,N,Ss.
Protein is the 50% dry weight of cells (total cell weight 70%
of water + 30% of protein).
Protein is made up of amino acids
There are 20 amino acids in our body. Out of 20 amino acids 9 are essential
that need to take everyday from food and 11 are non essential that body can
make themselves.
CLASSIFICATION OF PROTEINS
•Classification Based on Functions
1. Catalytic proteins, e.g. enzymes
2. Structural proteins, e.g. collagen, elastic
3. Contractile proteins, e.g. myosin, actin.
4. Transport proteins, e.g. hemoglobin, myoglobin, albumin, transferrin
5. Regulatory proteins or hormones, e.g. ACTH, insulin, growth hormone
Classification based on Composition and Solubility
According to this classification, proteins are divided into
three main groups as simple, conjugated and derived proteins.
I- Simple proteins:
On hydrolysis gives only amino acids ,
Examples: 1- Albumin and globulins: present in egg, milk and
blood. They are proteins of high biological value
i.e. contain all essential amino acids and easily digested.
 Albumin is a protein made by the liver. It makes up about 60% of the t
otal protein in the blood and plays many roles.
 Albumin keeps fluid from leaking out of blood vessels and
transports hormones, vitamins, drugs, and substances like calcium throug
hout the body.
 Levels of albumin may decrease, to a greater or lesser degree, when co
nditions interfere with its production by the liver, increase protein brea
kdown, increase protein loss via the kidneys, and/or expand plasma vo
lume (diluting the blood).
 Albumin keeps fluid from leaking out of blood vessels and
transports hormones, vitamins, drugs, and substances like calcium throug
hout the body.
 Levels of albumin may decrease, to a greater or lesser degree, when c
onditions interfere with its production by the liver, increase protein bre
akdown, increase protein loss via the kidneys, and/or expand plasma v
olume (diluting the blood).
Two important causes of low blood albumin include:
 Severe liver disease since albumin is produced by the liver,
its level can decrease with loss of liver function; however, this
typically occurs only when the liver has been severely affected
Kidney disease one of the many functions of the kidneys is to
conserve plasma proteins such as albumin so that they are not
released along with waste products when urine is produced.
However, if a person's kidneys become damaged or diseased,
they begin to lose their ability to conserve albumin and other protein.
Globulins
 The globulins are a family of globular proteins that have higher
molecular weights than albumins and are insoluble in pure water
but dissolve in dilute salt solutions.
Types of globulins: e.g. antitrypsin e.g. Hepatoglobin: protein that
binds hemoglobin to prevent its excretion by the kidney -globulin:
e.g. transferrin:- protein that transport iron -globulins = Immunoglobulins
(antibodies) : responsible for immunity.
Conjugated protein
They are combinations of protein with a non-protein part, called prosthetic
group Conjugated proteins may be classified as follows
1. Glycoproteins: These are proteins combined with carbohydrates. Hydroxyl
groups of serine or threonine and amide groups of asparagine and glutamine f
orm linkages with carbohydrate residues. Blood group antigens and many ser
um proteins are glycoproteins.
2. Lipoproteins: These are proteins loosely combined with lipid components.
They occur in blood and on cell membranes.
3. Nucleoproteins: These are proteins attached to nucleic acids, e.g. Histones.
The DNA carries negative charges, which combines with positively charged p
rotein
4. Chromo proteins: These are proteins with colored prosthetic groups. Hemo
globin (Heme, red); Flavo proteins (Riboflavin, yellow) are some examples of
chromo proteins.
5. Phosphoproteins: These contain phosphorus. Casein of milk and vitelline of
egg yolk are examples. The phosphoric acid is esterified to the hydroxyl groups
of serine and threonine residues of proteins.
6. Metalloproteins: They contain metal ions. Examples are Hemoglobin
(Iron), Cytochrome (Iron), Tyrosinase (Copper) and Carbonic anhydrase (Zinc).
 Classification Depending on the Shape
Fibrous
1) polypeptides arranged in long strands or sheets
2) water insoluble(lot of hydrophobic AA's)
3) strong but flexible
4) Structural (keratin, collagen)
Globular
1) polypeptide chains folded into spherical or globular form
2) water soluble
3) contain several types of secondary structure
4) diverse functions (enzymes, regulatory proteins)
Classification Based on Nutritional Value Nutritionally Rich
Proteins
They are also called as complete proteins or first class proteins.
They contain all the essential amino acids in the required proportion.
On supplying these proteins in the diet, children will grow satisfacto
rily. A good example is casein of milk.
o Incomplete Proteins
• They lack one essential amino acid. They cannot promote body
growth I children; but may be able to sustain the body weight in
adults. Proteins from pulses are deficient in methionine, while p
proteins of cereals lack in lysine. If both of them are combined i
in the diet, adequate growth may be obtained.
 Poor Proteins
They lack in many essential amino acids and a diet based on these proteins
will not even sustain the original body weight. Zain from corn lacks trypto
phan and lysine.
Diseases caused by changes in protein structure
• Sickle Cell Anemia- single amino acid change in hemoglobin related to
disease.
• Osteoarthritis- single amino acid change in collagen protein causes joint
damage
Digestion and Absorption of protein
Introduction
 Proteins, the primary constituents of the body.
A regular & adequate supply of protein in the diet is essential for cell in
tegrity & function.
 Dietary proteins are the primary sources of the nitroger Adult man requi
res 70 to 100 gm protein/day.
 Díetary proteins serve three broad functions: Their constituent AAs are
used for synthesis of body proteins.
 The carbon skeletons of AAs can be oxidized to yield energy.
 Their "C"& "N" atoms may be used to synthesize other
nitrogenous and non-nitrogenous metabolites.
Amino acids are linked to each other by peptide linkage
Peptide bonds
AA1 AA2 AA3 AA4 AA5
 Digestion in Mouth
 No digestion of protein in mouth.
No proteolytic enzymes present in the saliva.
 Function of the saliva - lubricate the food, this helps in making food
soluble for the action of proteolytic enzymes.
After mastication and chewing, the bolus of /food enters stomach
where it is acted upon by gastric juice.
 Digestion in Stomach
Digestion of protein starts in stomach.
When proteins enters the stomach, it stimulates the secretion of the ho
rmone gastrin, from gastric mucosal cells.
This gastrin, in turn, stimulates the of gastric juice, which contains: -
• Hydrochloric acid.
• Pepsinogen (zymogen)
• Rennin in infants.
The pH of gastric juice is 1.5-2.5.
Protein Absorption
Protein absorption refers your body’s ability to break down the an
imal or plant protein sources you ingest in to individual building bl
ocks(amino acids), then use those building blocks to make the prot
ein your body needs for every day living, like maintaining and imp
roving muscle strength.
In adults essentially all protein is absorbed as tri peptides, di pepti
des or amino acids and this process occurs in in the duodenum or p
roximal jejunum of the small intestine.
The peptides and/or amino acids pass though the interstitial brush
border by facilitating diffusion or active transport.
Most protein absorption takes place in the duodenum and jejunum
Tripeptides, Dipeptides and AA are absorbed
There is minima absorption of peptides longer than three amino acids
Most AA are absorbed into the blood stream, but some remain in the
enterocytes and are used to support the cells 99% of protein enters the
bloodstream as amino acids.
Intracellular cytoplasmic peptidases digest everything into single
amino acids which are absorbed into the bloodstream or used by the
cell.
Protein Absorption- Peptides
Essentially no absorption of peptides longer than three amino acids.
 Di-and tri-peptides are more rapidly absorbed than free amino acids due
to PEPT1
Active transporter PEPT1 Coupled to sodium-hydrogen (NHE3).
Accommodates various sizes and charges.
Di- and tri-peptides are digested into amino acids by cytoplasmic peptid
ases PEPT1 exchanger.
 Some amino acids share the same transport system, so if a large
amount of one particular amino acid is consumed, the absorption
of other AA that share the same transporter may be inhibited.
 Clinical correlation Shortly after birth neonates can absorb intact
proteins. These neonates can absorb intact proteins.
• These proteins pass through the soluble(lumen) and membrane-
bound proteases remaining intact.
• Once mature the enterocytes do not have transporter's to transfer
intact protein across the plasm membrane.
• They can permeate tight junctions either.
 Function of protein
 Protein has many roles in your body. It helps repair and build your
body's tissues allow metabolic reaction to take place and coordinate
bodily function. Protein do most of the job in the cell and perform
various jobs.
1. Growth and maintenance
Your body needs protein for growth and maintenance of tissues.
2. Help's Your Body Repair Itself After Injury
Protein can help your body repair after it has been injured.
This makes perfect sense, as it forms the main building blocks of your
tissues and organs.
3. Causes Biochemical Reactions
Enzymes are proteins that aid the thousands of biochemical reactions
that take place within and outside of your cells.
4. Help with Immunity
Protein also plays an important role in the immune system. first step in
the immune response is to detect the foreign invader or antigen.
This is done by special proteins called pattern recognition receptors (PRR
s). After the immune system recognizes an antigen, it releases antibodies.
Antibodies are another type of protein that attacks antigens.
5. provide Structure
 Structural proteins are a type of protein responsible for cell shape and
providing support to major structures, such as hair, skin, and bones.
 Many structural proteins exist in the human body. Two of the most
common are collagen and keratin.
 Collagen is the structural protein that is present in bones, connectiv
e tissues, and skin. It is hard and fibrous and makes up approximately
one-third of the protein in the human body.
 keratin is also a structural protein that is found in hair, nails, and
skin as well as the linings of organs and glands. The amino acid compos
ition of keratin differs from collagen, giving them different functions.
6. Transport Materials
Another function of proteins in the human body is to transport other
materials around. Transport proteins move ions or molecules across
biological membranes. Haemoglobin is a protein that is present in red
blood cells.
7. Balance Fluids
One process that protein regulates is the fluid balance within the body.
Proteins called albumin and globulin are produced in the liver and
help maintain the fluid balance by attracting and retaining water in the
blood.
8. Provide Energy
when there is not an adequate supply of carbohydrates or fats, the human
body breaks down proteins to provide energy,
 Foods With Protein
 Getting enough protein on a daily basis is essential for your
overall health. many foods contain protein.
 The amount of protein foods you need depends on your age, sex,
height, weight, and physical activity. The amount can also depend on
whether or not you are pregnant or breast feeding. However, some
protein sources are better than other.
 You can get protein from both
plant and animal sources – here
are some of the best food sources
of protein.
 Plant protein sources
There are many sources of plant proteins, such as
• Legumes: lentils, beans, peas , edamame/soybeans , peanuts.
• Nuts and Seeds: almonds, pistachios, cashews, hazelnuts, pecans,
hemp seeds, squash and pumpkin seeds, sunflower seeds, flax seeds,
sesame seeds, chia seeds.
• Whole Grains: kamut, teff, wheat, quinoa, rice, wild rice, millet, oats,
buckwheat. While many vegetables and fruits contain some level of
protein, it’s generally in smaller amounts than the other plant-based foods
Some examples with higher protein quantities include corn, broccoli and
asparagus.
 Animal protein sources
Rich sources of animal proteins include
 eggs
 fish and seafood
 lean meat
 poultry
 dairy products such as milk, yogurt, and cheese
Generally, animal protein sources also supply other important nutrients.
 How much protein do you need?
 Anywhere from 10% to 35% of your calories should come from
protein. So if your needs are 2,000 calories, that’s 200–700 calories
from protein, or 50–175 grams. The recommended dietary allowance to
prevent deficiency for an average sedentary adult is 0.8 grams per
kilogram of body weight. For example, a person who weighs 75 kilogram,
should consume 60 grams of protein per day.
 Once you reach ages 40–50, sarcopenia, or losing muscle mass as you
age, begins to set in. To prevent this and to maintain independence and qu
ality of life, your protein needs increase to about 1–1.2 grams per kilogram
or 75–90 grams per day for a 75-kilogram person.
• People who exercise regularly also have higher needs, about 1.1–1.5
grams per kilogram. People who regularly lift weights, or are training for
a running or cycling event need 1.2–1.7 grams per kilogram.
Excessive protein intake would be more than 2 grams per kilogram of
body weight each day.
• If you are overweight, your weight is adjusted before calculating your
protein needs to avoid overestimating. You can see a dietitian to help
develop a personalized plan.
• Many factors can affect how much protein a person needs, including
their activity level, weight, height, and whether they are pregnant.
• The recommended 0.8 g/kg of daily protein requirement is largely
based on studies with young males, and this level of protein intake may
not be sufficient for many older people.
• It should be kept in mind that protein intake will decrease prominently
in patients whose oral intake decreases because protein sources in
comparison with carbohydrate and fat are generally tasteless and bitter
However, it is reported that protein intake via gastrointestinal hormones
can provide increased appetite.
• Daily protein requirement increases prominently in many diseases.
Even if protein restriction is suggested for chronic renal failure patients
before the renal replacement treatment, it is determined that renal failure
progresses faster in case of restrictions.
• The presence of gastric acid is important for the efficient absorption
of proteins from the gastrointestinal tract.
• During critical diseases, the daily protein requirement is significantl
y increased. Generally, it is suggested that to give protein at the level of
1.2–1.5 g/kg/day.
 Disease related to protein
Amyloidosis
• Amyloidosis is a group of diseases in which abnormal proteins, called
amyloid proteins, accumulate in organs or organ systems such as the heart,
kidneys, nervous system or gastrointestinal tract. There are different types
of amyloidosis, dependent on the type of protein being deposited in tissues
• The most common form of amyloidosis in the United States is called
primary amyloid. In primary amyloid, the protein being deposited is
a part of the antibody protein called the light chain.
 Health Consequences of Protein Deficiency
There are two main syndromes associated with protein deficiencies:
Kwashiorkor and Marasmus.
Kwashiorkor
• Kwashiorkor, also known as “edematous malnutrition” because
of its association with Edema (fluid retention).
• Kwashiorkor is caused by a lack of protein in the diet. Kwashiorkor
affects millions of children worldwide.
• The name Kwashiorkor comes from a language in Ghana and means
“rejected one”.
• Kwashiorkor is rare in developed countries. It’s mostly found in
developing countries with high rates of poverty and food scarcity.
• The main sign of kwashiorkor is too much fluid in the body's tissues,
which causes swelling under the skin (oedema). It usually begins in
the legs, but can involve the whole body, including the face.
Kwashiorkor is characterized by
• swelling (Edema) of the feet
and abdomen
• poor skin health
• growth retardation
• low muscle mass
• liver malfunction
• Most people who are affected by kwashiorkor recover fully if they
are treated early. kwashiorkor can be fatal if it's left untreated for too
long because children become very vulnerable to infections.
• Kwashiorkor can be corrected by eating more protein and more
calories overall, especially if treatment is started early.
 Marasmus
• Marasmus is a type of protein-energy malnutrition that can affect
anyone but is mainly seen in children. You can get marasmus if you
have a severe deficiency of nutrients like protein.
• It is more common in developing countries, like in some areas of
Asia and Africa. People in these nations are prone to having poor
access to food, making it difficult to get enough nutrients.
Symptoms of Marasmus
• Severe protein and calorie deficiency in children can result in
loss of fat and muscle mass. The most common symptom of
marasmus is being underweight due to malnourishment. The following
symptoms can occur due to deficiency, dehydration, electrolyte
imbalance, or infection.
Children With Marasmus
• Kwashiorkor and marasmus often coexist as a combined syndrome
termed marasmic kwashiorkor. Children with the combined syndrome
have variable amounts of edema and the characterizations and symptoms
of marasmus.
Reference
https://Www.sciencedirect.com
https://www.health.harvard.
https://pumbmed.ncbi.nlm.nih.gov
https://pressbooks-dev.oer.hawail.edu/humannutration
Group Member
Name ID
1. Habtamu Gezahegn…………………………… 1402733
2. Yinges Tsilfe……………………….................. 1307276
3. Tesfanesh Gizatu……………………………….. 1307184
4. Kalkidan Daneil…………………………………. 1305045
5. Mekdes Esubalew………………………………. 1308603
6. Mekdes Abineh…………………………………… 1304015
7. Absalat Abrham………………………………….. 1304852

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Protein.pptx

  • 1. DEBRE MARKOS UNIVERSITY COLLEGE OF MEDICINE AND HEALTH SCIENCE DEPARTMENT OF ENVIRONMENTAL HEALTH COMMUNITY NUTRITION Prepared By: Group One Acc. Year : - 2015/2023 SUBMITTED TO MATTHIAS K. SUBMISION DATE 26/05/2015E.C DEBRE MARKOS, ADDIS ABABA
  • 3.  Objective Define protein and list it’s composition. you able to list and describe classification of protein. You able to how the protein digest and absorbed in our body. List and Describe food source. List and describe requirement of protein and disease related to protein.
  • 4. Proteins large biomolecules and macromolecules that comprise one or more long chain of amino acid residues. After water, protein is the most plentiful substance in the body. Proteins grow, maintain, and replace the tissues in our bodies. Therefore our muscles, organs, and immune systems are mostly made Of protein Once protein is digested it is broken down into its amino acid. You'll find protein in lots of yummy foods like eggs, nuts, beans, fish, meat, and milk.
  • 5. It is an organic compound contain C,H,O,N,Ss. Protein is the 50% dry weight of cells (total cell weight 70% of water + 30% of protein). Protein is made up of amino acids There are 20 amino acids in our body. Out of 20 amino acids 9 are essential that need to take everyday from food and 11 are non essential that body can make themselves.
  • 6. CLASSIFICATION OF PROTEINS •Classification Based on Functions 1. Catalytic proteins, e.g. enzymes 2. Structural proteins, e.g. collagen, elastic 3. Contractile proteins, e.g. myosin, actin. 4. Transport proteins, e.g. hemoglobin, myoglobin, albumin, transferrin 5. Regulatory proteins or hormones, e.g. ACTH, insulin, growth hormone
  • 7. Classification based on Composition and Solubility According to this classification, proteins are divided into three main groups as simple, conjugated and derived proteins. I- Simple proteins: On hydrolysis gives only amino acids , Examples: 1- Albumin and globulins: present in egg, milk and blood. They are proteins of high biological value i.e. contain all essential amino acids and easily digested.
  • 8.  Albumin is a protein made by the liver. It makes up about 60% of the t otal protein in the blood and plays many roles.  Albumin keeps fluid from leaking out of blood vessels and transports hormones, vitamins, drugs, and substances like calcium throug hout the body.  Levels of albumin may decrease, to a greater or lesser degree, when co nditions interfere with its production by the liver, increase protein brea kdown, increase protein loss via the kidneys, and/or expand plasma vo lume (diluting the blood).  Albumin keeps fluid from leaking out of blood vessels and transports hormones, vitamins, drugs, and substances like calcium throug hout the body.  Levels of albumin may decrease, to a greater or lesser degree, when c onditions interfere with its production by the liver, increase protein bre akdown, increase protein loss via the kidneys, and/or expand plasma v olume (diluting the blood).
  • 9. Two important causes of low blood albumin include:  Severe liver disease since albumin is produced by the liver, its level can decrease with loss of liver function; however, this typically occurs only when the liver has been severely affected Kidney disease one of the many functions of the kidneys is to conserve plasma proteins such as albumin so that they are not released along with waste products when urine is produced. However, if a person's kidneys become damaged or diseased, they begin to lose their ability to conserve albumin and other protein.
  • 10. Globulins  The globulins are a family of globular proteins that have higher molecular weights than albumins and are insoluble in pure water but dissolve in dilute salt solutions. Types of globulins: e.g. antitrypsin e.g. Hepatoglobin: protein that binds hemoglobin to prevent its excretion by the kidney -globulin: e.g. transferrin:- protein that transport iron -globulins = Immunoglobulins (antibodies) : responsible for immunity.
  • 11. Conjugated protein They are combinations of protein with a non-protein part, called prosthetic group Conjugated proteins may be classified as follows 1. Glycoproteins: These are proteins combined with carbohydrates. Hydroxyl groups of serine or threonine and amide groups of asparagine and glutamine f orm linkages with carbohydrate residues. Blood group antigens and many ser um proteins are glycoproteins. 2. Lipoproteins: These are proteins loosely combined with lipid components. They occur in blood and on cell membranes. 3. Nucleoproteins: These are proteins attached to nucleic acids, e.g. Histones. The DNA carries negative charges, which combines with positively charged p rotein
  • 12. 4. Chromo proteins: These are proteins with colored prosthetic groups. Hemo globin (Heme, red); Flavo proteins (Riboflavin, yellow) are some examples of chromo proteins. 5. Phosphoproteins: These contain phosphorus. Casein of milk and vitelline of egg yolk are examples. The phosphoric acid is esterified to the hydroxyl groups of serine and threonine residues of proteins. 6. Metalloproteins: They contain metal ions. Examples are Hemoglobin (Iron), Cytochrome (Iron), Tyrosinase (Copper) and Carbonic anhydrase (Zinc).
  • 13.  Classification Depending on the Shape Fibrous 1) polypeptides arranged in long strands or sheets 2) water insoluble(lot of hydrophobic AA's) 3) strong but flexible 4) Structural (keratin, collagen) Globular 1) polypeptide chains folded into spherical or globular form 2) water soluble 3) contain several types of secondary structure 4) diverse functions (enzymes, regulatory proteins)
  • 14. Classification Based on Nutritional Value Nutritionally Rich Proteins They are also called as complete proteins or first class proteins. They contain all the essential amino acids in the required proportion. On supplying these proteins in the diet, children will grow satisfacto rily. A good example is casein of milk.
  • 15. o Incomplete Proteins • They lack one essential amino acid. They cannot promote body growth I children; but may be able to sustain the body weight in adults. Proteins from pulses are deficient in methionine, while p proteins of cereals lack in lysine. If both of them are combined i in the diet, adequate growth may be obtained.
  • 16.  Poor Proteins They lack in many essential amino acids and a diet based on these proteins will not even sustain the original body weight. Zain from corn lacks trypto phan and lysine. Diseases caused by changes in protein structure • Sickle Cell Anemia- single amino acid change in hemoglobin related to disease. • Osteoarthritis- single amino acid change in collagen protein causes joint damage
  • 17.
  • 18. Digestion and Absorption of protein Introduction  Proteins, the primary constituents of the body. A regular & adequate supply of protein in the diet is essential for cell in tegrity & function.  Dietary proteins are the primary sources of the nitroger Adult man requi res 70 to 100 gm protein/day.  Díetary proteins serve three broad functions: Their constituent AAs are used for synthesis of body proteins.  The carbon skeletons of AAs can be oxidized to yield energy.  Their "C"& "N" atoms may be used to synthesize other nitrogenous and non-nitrogenous metabolites.
  • 19. Amino acids are linked to each other by peptide linkage Peptide bonds AA1 AA2 AA3 AA4 AA5
  • 20.  Digestion in Mouth  No digestion of protein in mouth. No proteolytic enzymes present in the saliva.  Function of the saliva - lubricate the food, this helps in making food soluble for the action of proteolytic enzymes. After mastication and chewing, the bolus of /food enters stomach where it is acted upon by gastric juice.
  • 21.  Digestion in Stomach Digestion of protein starts in stomach. When proteins enters the stomach, it stimulates the secretion of the ho rmone gastrin, from gastric mucosal cells. This gastrin, in turn, stimulates the of gastric juice, which contains: - • Hydrochloric acid. • Pepsinogen (zymogen) • Rennin in infants. The pH of gastric juice is 1.5-2.5.
  • 22. Protein Absorption Protein absorption refers your body’s ability to break down the an imal or plant protein sources you ingest in to individual building bl ocks(amino acids), then use those building blocks to make the prot ein your body needs for every day living, like maintaining and imp roving muscle strength. In adults essentially all protein is absorbed as tri peptides, di pepti des or amino acids and this process occurs in in the duodenum or p roximal jejunum of the small intestine. The peptides and/or amino acids pass though the interstitial brush border by facilitating diffusion or active transport.
  • 23. Most protein absorption takes place in the duodenum and jejunum Tripeptides, Dipeptides and AA are absorbed There is minima absorption of peptides longer than three amino acids Most AA are absorbed into the blood stream, but some remain in the enterocytes and are used to support the cells 99% of protein enters the bloodstream as amino acids. Intracellular cytoplasmic peptidases digest everything into single amino acids which are absorbed into the bloodstream or used by the cell.
  • 24. Protein Absorption- Peptides Essentially no absorption of peptides longer than three amino acids.  Di-and tri-peptides are more rapidly absorbed than free amino acids due to PEPT1 Active transporter PEPT1 Coupled to sodium-hydrogen (NHE3). Accommodates various sizes and charges. Di- and tri-peptides are digested into amino acids by cytoplasmic peptid ases PEPT1 exchanger.
  • 25.  Some amino acids share the same transport system, so if a large amount of one particular amino acid is consumed, the absorption of other AA that share the same transporter may be inhibited.  Clinical correlation Shortly after birth neonates can absorb intact proteins. These neonates can absorb intact proteins. • These proteins pass through the soluble(lumen) and membrane- bound proteases remaining intact. • Once mature the enterocytes do not have transporter's to transfer intact protein across the plasm membrane. • They can permeate tight junctions either.
  • 26.  Function of protein  Protein has many roles in your body. It helps repair and build your body's tissues allow metabolic reaction to take place and coordinate bodily function. Protein do most of the job in the cell and perform various jobs. 1. Growth and maintenance Your body needs protein for growth and maintenance of tissues. 2. Help's Your Body Repair Itself After Injury Protein can help your body repair after it has been injured. This makes perfect sense, as it forms the main building blocks of your tissues and organs.
  • 27. 3. Causes Biochemical Reactions Enzymes are proteins that aid the thousands of biochemical reactions that take place within and outside of your cells. 4. Help with Immunity Protein also plays an important role in the immune system. first step in the immune response is to detect the foreign invader or antigen. This is done by special proteins called pattern recognition receptors (PRR s). After the immune system recognizes an antigen, it releases antibodies. Antibodies are another type of protein that attacks antigens.
  • 28. 5. provide Structure  Structural proteins are a type of protein responsible for cell shape and providing support to major structures, such as hair, skin, and bones.  Many structural proteins exist in the human body. Two of the most common are collagen and keratin.  Collagen is the structural protein that is present in bones, connectiv e tissues, and skin. It is hard and fibrous and makes up approximately one-third of the protein in the human body.  keratin is also a structural protein that is found in hair, nails, and skin as well as the linings of organs and glands. The amino acid compos ition of keratin differs from collagen, giving them different functions.
  • 29. 6. Transport Materials Another function of proteins in the human body is to transport other materials around. Transport proteins move ions or molecules across biological membranes. Haemoglobin is a protein that is present in red blood cells. 7. Balance Fluids One process that protein regulates is the fluid balance within the body. Proteins called albumin and globulin are produced in the liver and help maintain the fluid balance by attracting and retaining water in the blood. 8. Provide Energy when there is not an adequate supply of carbohydrates or fats, the human body breaks down proteins to provide energy,
  • 30.  Foods With Protein  Getting enough protein on a daily basis is essential for your overall health. many foods contain protein.  The amount of protein foods you need depends on your age, sex, height, weight, and physical activity. The amount can also depend on whether or not you are pregnant or breast feeding. However, some protein sources are better than other.  You can get protein from both plant and animal sources – here are some of the best food sources of protein.
  • 31.  Plant protein sources There are many sources of plant proteins, such as • Legumes: lentils, beans, peas , edamame/soybeans , peanuts. • Nuts and Seeds: almonds, pistachios, cashews, hazelnuts, pecans, hemp seeds, squash and pumpkin seeds, sunflower seeds, flax seeds, sesame seeds, chia seeds. • Whole Grains: kamut, teff, wheat, quinoa, rice, wild rice, millet, oats, buckwheat. While many vegetables and fruits contain some level of protein, it’s generally in smaller amounts than the other plant-based foods Some examples with higher protein quantities include corn, broccoli and asparagus.
  • 32.  Animal protein sources Rich sources of animal proteins include  eggs  fish and seafood  lean meat  poultry  dairy products such as milk, yogurt, and cheese Generally, animal protein sources also supply other important nutrients.
  • 33.  How much protein do you need?  Anywhere from 10% to 35% of your calories should come from protein. So if your needs are 2,000 calories, that’s 200–700 calories from protein, or 50–175 grams. The recommended dietary allowance to prevent deficiency for an average sedentary adult is 0.8 grams per kilogram of body weight. For example, a person who weighs 75 kilogram, should consume 60 grams of protein per day.  Once you reach ages 40–50, sarcopenia, or losing muscle mass as you age, begins to set in. To prevent this and to maintain independence and qu ality of life, your protein needs increase to about 1–1.2 grams per kilogram or 75–90 grams per day for a 75-kilogram person.
  • 34. • People who exercise regularly also have higher needs, about 1.1–1.5 grams per kilogram. People who regularly lift weights, or are training for a running or cycling event need 1.2–1.7 grams per kilogram. Excessive protein intake would be more than 2 grams per kilogram of body weight each day. • If you are overweight, your weight is adjusted before calculating your protein needs to avoid overestimating. You can see a dietitian to help develop a personalized plan.
  • 35. • Many factors can affect how much protein a person needs, including their activity level, weight, height, and whether they are pregnant. • The recommended 0.8 g/kg of daily protein requirement is largely based on studies with young males, and this level of protein intake may not be sufficient for many older people. • It should be kept in mind that protein intake will decrease prominently in patients whose oral intake decreases because protein sources in comparison with carbohydrate and fat are generally tasteless and bitter However, it is reported that protein intake via gastrointestinal hormones can provide increased appetite.
  • 36. • Daily protein requirement increases prominently in many diseases. Even if protein restriction is suggested for chronic renal failure patients before the renal replacement treatment, it is determined that renal failure progresses faster in case of restrictions. • The presence of gastric acid is important for the efficient absorption of proteins from the gastrointestinal tract. • During critical diseases, the daily protein requirement is significantl y increased. Generally, it is suggested that to give protein at the level of 1.2–1.5 g/kg/day.
  • 37.  Disease related to protein Amyloidosis • Amyloidosis is a group of diseases in which abnormal proteins, called amyloid proteins, accumulate in organs or organ systems such as the heart, kidneys, nervous system or gastrointestinal tract. There are different types of amyloidosis, dependent on the type of protein being deposited in tissues • The most common form of amyloidosis in the United States is called primary amyloid. In primary amyloid, the protein being deposited is a part of the antibody protein called the light chain.
  • 38.  Health Consequences of Protein Deficiency There are two main syndromes associated with protein deficiencies: Kwashiorkor and Marasmus. Kwashiorkor • Kwashiorkor, also known as “edematous malnutrition” because of its association with Edema (fluid retention). • Kwashiorkor is caused by a lack of protein in the diet. Kwashiorkor affects millions of children worldwide. • The name Kwashiorkor comes from a language in Ghana and means “rejected one”. • Kwashiorkor is rare in developed countries. It’s mostly found in developing countries with high rates of poverty and food scarcity.
  • 39. • The main sign of kwashiorkor is too much fluid in the body's tissues, which causes swelling under the skin (oedema). It usually begins in the legs, but can involve the whole body, including the face. Kwashiorkor is characterized by • swelling (Edema) of the feet and abdomen • poor skin health • growth retardation • low muscle mass • liver malfunction
  • 40. • Most people who are affected by kwashiorkor recover fully if they are treated early. kwashiorkor can be fatal if it's left untreated for too long because children become very vulnerable to infections. • Kwashiorkor can be corrected by eating more protein and more calories overall, especially if treatment is started early.  Marasmus • Marasmus is a type of protein-energy malnutrition that can affect anyone but is mainly seen in children. You can get marasmus if you have a severe deficiency of nutrients like protein.
  • 41. • It is more common in developing countries, like in some areas of Asia and Africa. People in these nations are prone to having poor access to food, making it difficult to get enough nutrients. Symptoms of Marasmus • Severe protein and calorie deficiency in children can result in loss of fat and muscle mass. The most common symptom of marasmus is being underweight due to malnourishment. The following symptoms can occur due to deficiency, dehydration, electrolyte imbalance, or infection.
  • 43. • Kwashiorkor and marasmus often coexist as a combined syndrome termed marasmic kwashiorkor. Children with the combined syndrome have variable amounts of edema and the characterizations and symptoms of marasmus.
  • 45. Group Member Name ID 1. Habtamu Gezahegn…………………………… 1402733 2. Yinges Tsilfe……………………….................. 1307276 3. Tesfanesh Gizatu……………………………….. 1307184 4. Kalkidan Daneil…………………………………. 1305045 5. Mekdes Esubalew………………………………. 1308603 6. Mekdes Abineh…………………………………… 1304015 7. Absalat Abrham………………………………….. 1304852