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CHAPTER THREE
PROTEINS
TENSAY BAYESSA (BSC, MPH,
MBA)
PROTEIN
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Proteins are organic compounds made up of
many smaller amino acid molecules linked
together by peptide bonds.
Amino acids are organic compounds composed of
carbon, hydrogen, oxygen, and nitrogen.
Sulphur, phosphoros , iron and cobalt may also
be found in some group of amino acids.
AMINO ACIDS
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There are 20 different amino acids from
which all the living bodies are composed of.
Amino acids are grouped in to two based
on essentiality.
Essential Amino Acids
Non Essential Amino Acids
1. Essential Amino acids
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Are amino acids that
cannot be
manufactured by the
human body and they
must be taken in food.
Includes nine of the
twenty amino acids:
2. Non essential Amino acids:
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Are amino acids that can
be manufactured by the
human body.
The liver synthesize them
as long as structural
components especially
nitrogen are available.
The eleven non essential
amino acids are:
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CLASSIFICATION OF PROTEINS
I. Based on amino acids contained
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A. Complete proteins:
Contain all the nine essential amino acids in
qualities that can best support growth..
Food sources:
Animal proteins ( meat, poultry, fish, eggs,
diary products)
Plant proteins ( soya bean)
High quality proteins: are foods containing the
best balance and assortment of essential and
non essential amino acids for protein synthesis.
Exa: Eggs and Breast milk
B. Incomplete Proteins
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Are proteins lacking one or more of the
essential amino acids.
Food Sources:
Grains (oats, barley, wheat, corn)
Legumes (peas, beans, lentiles)
Incomplete protein…
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The amino acids that are missing
in incomplete proteins are called
Limiting Amino acids because
their absence affect the
synthesis of many kinds of
proteins in the body.
Complementary combination
protein: refers to the mixture of
two or more sources of incomplete
proteins that provides all the
essential amino acids.
Example:
Peanut butter on whole grain
Cheese and pasta
Black beans +
Cheese pizza
rice
II. Based on chemical composition
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A. Simple Proteins:
Completely hydrolyze in to amino acids.
Example: egg albumin
B. Compound/Conjugated Proteins:
Composed of protein and non protein
components.
Example:
Hemoglobin= Protein + hem
Lipoprotein = Protein + Lipid
Mucin = Protein + Carbohydrate
Casein = Protein + Phosphoric acid
III. Based on Conformation
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Globular protein:
Are tightly folded poly-peptide chains
Mostly soluble in water.
E.g. Enzymes, hormones, Hemoglobin
Fibrous Protein:
Are poly peptide chains arranged in parallel manner
along an axis.
They are tough and insoluble in water.
Example:
Collagen of tendon and bone matrix.
Keratin of hair, skin, nails
Elastin of blood vessels
IV. Based on Chemical Structure
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Primary Structure: Linear and determined by number and
sequence of amino acids in the chain.
Secondary Structure:
Straight, folded or coiled.
Alpha helical and Beta pleated sheet.
Hydrogen bonds stabilize folds of helical spirals.
E.g. Keratin
Tertiary Structure:
3D globular and fibrous protein formed due to strong intra-
molecular bonding, hydrogen bonding and sulphide bond.
E.g. Myoglobin.
Quaternary Structure:
Are proteins containing more than one poly peptide chains
joined together by electrostatic bonding. E.g. Hemoglobin
IV. Based on Chemical Structure
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Primary Structure: Linear and determined by number and
sequence of amino acids in the chain.
Secondary Structure:
Straight, folded or coiled.
Alpha helical and Beta pleated sheet.
Hydrogen bonds stabilize folds of helical spirals.
E.g. Keratin
Tertiary Structure:
3D globular and fibrous protein formed due to strong intra-
molecular bonding, hydrogen bonding and sulphide bond.
E.g. Myoglobin.
Quaternary Structure:
Are proteins containing more than one poly peptide chains
joined together by electrostatic bonding. E.g. Hemoglobin
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DIGESTION, ABSORPTION
AND
METABOLISM OF PROTEIN
Digestion
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Because of complex structure of proteins, a
number of protein digesting enzymes/proteases.
These enzymes are produced by the Stomach,
Pancreas and Intestinal glands.
In the mouth: mechanical break down/mastication/.
In the stomach: stomach mucosa secretes inactive
pepsinogen that can be activated to pepsin by HCl.
Pepsinogen Hcl Pepsin
(inactive) (active)
Protein Pepsin Small polypeptides
Digestion
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In the small intestine:
i. The pancreas secret trypsin, chymotrypsin
and carboxypeptidase.
Polypeptides Trypsin, chymotrypsin
Dipeptides
Polypeptides Carboxypeptidase Amino
acids
ii. Intestinal glands secret intestinal
proteases (aminopeptidase and dipeptidase)
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N.B.
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Cooking increases digestibility.
Over heating can destroy some amino
acids.
Cooking with water makes proteins more
palatable.
ABSORPTION
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Occur through the intestinal walls by means of
‘active transport’ coupled with Na+ using
carrier molecules.
There are two main sources of ‘amino acid pool’
Digestion and absorption of dietary protein
Breakdown of tissue protein.
PROTEIN METABOLISM
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Dietary NH3
Protein Digestion Urea
Absorptio
n
Catabolism Keto acid
Amino Acid Deaminatio Energy
Pool n source
(Essential + in the liver
Non essential
Tissue aa’s) Anabolis Tissue
Catabolis m protein
Protein
m synthesis for
Breakdow growth and
n maintenance
Plasma
Protein
PROTEIN CATABOLISM
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The first step in amino acid catabolism is the
removal of nitrogen (amino groups).
Amino groups all collected in the form of
glutamate and goes to urea cycle.
The carbon skeleton will be involved in the
intermediately metabolic path way to release
energy
Total calories provided by one gram of protein
is 4killocalorie
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FUNCTIONS OF PROTEIN
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Growth and Maintenance (Building Blocks)
Proteins make muscles, bones, other cells/tissues.
Collagen protein forms connective tissue and
synthesis of scar tissues.
Keratin proteins make hair, nails, and skin
Production of bio-communicators and bio-
catalyst.
Most hormones and all enzymes.
Immune system response
Globular proteins are the major constituents of anti
bodies.
Fluid and electrolyte regulation
FUNCTIONS OF PROTEIN
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Acid-Base Balance or Buffering Effect: protein
regulate the balance between the acidic and
the basic property of our body fluid due to –
COOH acid and –NH2 basic group.
Transportation: carrier proteins and pumps
serves as a transporters. Example:
Hemoglobin transport oxygen in the blood.
Source of energy: when the energy intake
from CHOs and lipids is inadequate, protein is
metabolized for energy.
NITROGEN BALANCE
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It is the condition where nitrogen intake from food is
equal to nitrogen excreted through urine, feces, sweat,
etc.
It occurs in a healthy, non growing adult person taking
adequate amount of energy from CHOs.
Factors affecting nitrogen balance:
Pregnancy
Lactation
Growth
Recovery from illness
Starvation
Devastating illness
HEALTH IMPORTANCE OF PROTEIN
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Excessive consumption of protein will be followed by
an increased rate of deamination by the liver, that may
bring:
High level of keto-acid----ketosis
Increased urea production by the liver and excreted by
kidney cause stress to the liver and kidney.
Deficiency of protein: PEM (protein energy malnutrition)
Affect children below 5 years.
Manifested by mild to severe wasting, stunting and
mental retardation.
Includes: Marasmus, Kwashiorkor and Marasmic-
Kwashiorkor
Methods of Assessing Protein Quality
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Protein quality: refers to the ability of a
protein to provide the function of
maintenance and support growth in a growing
animal.
Includes:
Protein Efficiency Ratio (PER)
Net protein untilization (NPU)
Amino Acid Score (AAS)
Biological Value (BV)
Methods .....
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Protein Efficiency Ratio (PER):
determined by weight gained by growing
animal per gram protein ingested.
PER = Weight gained (G)
Protein intake (G)
Any protein with PER value above 2.7 is an
excellent protein quality.
Methods .....
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Net Protein Utilization (NPU):
It is a ratio or percentage of protein utilized
in body building from total protein ingested.
NPU = Ingested protein – (Fecal N2 +
Urinary N2)
Ingested protein
Methods .....
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Amino Acid Score:
It is the concentration of limiting amino acids in gram of
proteins of reference food.
Limiting amino acid is the one in the smallest quantity in that
food.
Example
Lysine in cereals
Methonine in legumes
Tryptophan in corn
The reference protein is usually egg and milk.
AA score = mg of Laa in a gram of test protein *100
mg of Laa in a gram of reference protein
Methods .....
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Biological value:
Refers to the amount of protein retained in
the human body for maintenance and
growth.
Measures protein quality and its efficiency
for growth.
High BV proteins are better for nitrogen
retention.
High BV are more anti catabolic than LBV.
Methods .....
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Protein biological value of some selected foods:
Egg = 93.7
Milk = 84.5
Fish = 76
Beef = 74
Soya bean = 72.8
Rice polished = 64
Wheat whole = 64
Corn = 60
Beans dry = 58
RDA of Protein
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Age Gram ofProtein Gram/
(Year) 1000Kcal
Infants 0 – 0.5 2.2 /kg --------
0.5 - 1 2/kg ---------
Childre 1-3 23 17.7
n 4-6 30 16.7
7 - 10 36 15.0
Males 11 - 14 44 15.7
15 - 18 54 18.0
19 - 22 54 18.0
23 - 50 56 20.7
RDA of Protein...
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Age Gram Gram/
(Year) ofProtein 1000Kcal
Female 11 -14 44 18.3
s 15 - 18 48 22.9
19 - 22 46 21.9
23 - 50 46 23.0
51+ 46 25.6
• Pregnant = +30
• Lactating = +20
• N.B. For adults in general intake of 0.8 g of protein /Kg
body weight is adequate.
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Thanks !!
