PROTEINS These EAAs must be eaten in food,

digested, absorbed and then brought to

Learning Objectives cells by circulating blood.

1. Explore the nature of proteins and amino The liver can create nonessential amino
acids. acids as long as structural components,
including nitrogen from other amino acids
2.Differentiate essential from non-essential
are available.
amino acids.
Essential Amino Acids
3. Enumerate the functions of protein.
- AA that the body cannot synthesize
4. Explain the functions of protein in
in amounts sufficiently to meet
absorption and digestion.
physiological needs
5. Discuss conditions that leads to protein
- Also called indispensable AA
deficiencies.
9 Essential amino acids
PROTEINS
Histidine
- are organic compounds formed by
the linking of many smaller Isoleucine
molecules of amino acids
Leucine
- Amino acids are organic compounds
made of carbon, hydrogen oxygen Lysine
and nitrogen.
Methionine
- nitrogen distinguishes protein from
Phenylalanine
other nutrients
Threonine
Amino Acids
Tryptophan
- building blocks of CHON
Valine
- each has an amino group and an acid
group attached to a central carbon REMEMBER: HillMPTTV

There are 20 amino acids from which all the
proteins that are required by plants and
animals are made.
There are 9 amino acids which can not be
made by the cells of the body. These are
the essential amino acids.
Nonessential Amino Acids
Are amino acids that the body can make
from itself.
Also called dispensable amino acids
Nonessential Amino Acids

Alanine
Arginine still have different functions because of the
sequencing or order of the amino acids.
Asparagine
2. The Secondary Structure level of protein-
Aspartic acid affects the shape of the chain of amino
Cysteine acids; these maybe straight, folded or
coiled.
Cystine
3. The tertiary structure level of protein-
Glutamic acid/ glutamine results when the polypeptide chain is so
coiled that the loops of the coil touch,
4As, 2Cs, 2Gs, PST
forming strong bonds within the chain itself.

4. The quarternary structural level of

Protein Chains protein – refers to proteins containing more
than one polypeptide chain.
Dipeptide
Denaturation
Tripeptide
A protein may not be able to perform its
Polypeptide original function if its structure or shape
changes. The shape maybe changed by
heat (cooking), ultraviolet light (exposure to
Peptide- is sunlight), acids (vinegar), alcohol and
mechanical action.
composed of two
Denaturation
or more amino
When proteins denature, they tend to bond
acids together, or coagulate, and form solid
clumps. An example of this is a cooked egg
Protein Composition
white, which changes from a transparent
4 Structural Levels of Protein fluid to an opaque solid.

1. Primary Structure of Protein- is Protein as a Nutrient in the Body

determined by the number,
The proteins we consume in our foods are
assortment, and sequence of amino
not the same proteins used by our bodies.
acids in polypeptide chains.
The only nutrient role protein in foods serve
Amino acids are linked together by
is to provide amino acids, the building
peptide bonds to form a practically
blocks of all protein.
unlimited number of proteins.

Two proteins may contain the same

assortment and number of amino acids yet
Digestion and Absorption
Proteases- protein enzymes produced by
stomach and pancreas required to hydrolyze
proteins into smaller and smaller peptides
until individual amino acids are ready for
absorption.
STOMACH
Pepsinogen– an inactive form of gastric
protease pepsin, which is secreted by
stomach mucosa.
Pepsin- becomes activated when it mixes
with hydrochloric acid. It breaks the bonds
Linking the amino acids of the protein
peptide bonds.
Rennin- is produced only during infancy . It
functions with calcium to thicken or
coagulate the milk protein casein which
slows the movement of milk nutrients from
the stomach , allowing additional digestion
time.
Small Intestine
Pancreatic and intestinal proteases continue
the hydrolysis of polypeptides. As the
smaller polypeptides touch the intestinal
walls, peptidases are released that
completes the hydrolysis of CHON into
absorbable units of amino acids and
dipeptides.
Pancreatic enzymes
Trypsinogen (pancreatic enzyme)- inactive
form of trypsin
Chymotrypsin and carboxypeptidase-
hydrolyzes polypeptides into dipeptides
Metabolism
Most CHON functions are a result of CHON
metabolism in cells.
Anabolism- enhanced by the effect of
growth hormone and testosterone
Catabolism- affected by glucocorticoids that
are enhanced by adrenocorticotropic
hormone secreted from the adrenal cortex.
Two Intestinal Peptidases
1. Aminopeptidase- releases free amino
acids from the amino end of short chain
peptides.
2. Dipeptidase- completes the hydrolysis of
CHON to amino acids.
Vitamin B6 (Pyridoxine)- helps in the
absorption of amino acids through the
intestinal wall by means of competitive
active transport.
Deamination- results in an amino acid group
breaking off from an amino acid molecule ,
resulting in one molecule each of ammonia
and a keto acid.
Nitrogen Balance
Nitrogen balance studies- are used to
determine the CHON requirements of the
body throughout the life cycle and to assign
value to the protein quality of foods to
determine their biologic value.
Positive nitrogen balance = when the body
adds protein
Negative nitrogen balance = when the body
loses protein
Fasting or starving people
Trauma such as burns
Functions of CHON
1. Growth and Maintenance- all growth
depends on a sufficient supply of amino
acids. These are needed to make the
proteins required to support muscle, tissue,
bone formation and the cells themselves.
Protein collagen also forms connective
tissues such as ligaments and tendons and
acts as a tendon to keep the walls of the
arteries intact.
2. Creation of communicators and catalysts
Some hormones are proteins.
Hormones act as communicators to alert
different parts of the body to changes or
regulate functions of organs.
Blood clotting factors depend
on protein substances as well.
3. Immune system response- the defense
system of our bodies depends on proteins
produced in response to foreign viruses and
bacteria that invade our bodies.
4. Fluid and electrolyte regulation- proteins
and minerals attract water, creating osmotic
pressure. As proteins circulate in our bodies,
they maintain body fluid and electrolyte
balance by keeping water appropriately
divided among the three components-
intravascular, intracellular and interstitial.
5. Acid-Base balance- blood proteins can
buffer the effects of fluids to maintain a
safe acidic level in body fluids.
The ability of protein to regulate the
balance between the acidic and base
characteristics of fluids is called buffering
effect.
6. Transportation- many nutrients including
lipids, minerals, vitamins and electrolytes
are carried in the blood by proteins such as
lipoproteins.
Hemoglobin, a special carrier composed of
protein, transports oxygen in the blood.
Oxygen is stored in our muscles in another
protein carrier, myoglobin.
Quality of Protein Foods
Complete Protein- contains all 9 EAAs in
sufficient quantities that best support
growth and maintenance of our bodies.
Sources are animal-derived foods including
meat, poultry, fish, eggs, and most dairy
products.
Soybeans- the only plant source that
provide all 9 EAAs
High Quality Protein Foods- foods that
contribute the best balance of EAAs and the
best assortment of NEEAs for protein
synthesis which are easily digestible.
The two highest quality protein foods are
eggs and human milk.
Incomplete Proteins- lacks one or more of
the 9 EAAs. These will not provide a
sufficient supply of amino acids and will not
support life. Sources are grains and
legumes.
Limiting Amino Acids- the EAAs that the
incomplete proteins lack.
Combining two or more foods with
incomplete proteins, to form complementary
proteins, can provide adequate amounts of
all the essential amino acids
 Ex: legumes + meat
Protein RDA
25g protein/day, 71g/day for pregnant
women
0.8g/kg (or 2.2lbs)
Vegetarianism (Veganism)
An ovo-vegetarian diet includes eggs but
not dairy products, a lacto-vegetarian diet
includes dairy products but not eggs, and
an ovo-lacto vegetarian diet includes both
eggs and dairy products.
The problem for vegan dietary pattern is the
lack of Vitamins D and B12, Ca and
omega=3 fatty acids
Flexitarianism- primarily consume
vegetarian foods with occasional meat,
chicken or fish consumption.
Protein-Energy Malnutrition (PEM)
- deficiency of protein and food
energy
2 Forms:
a. Marasmus
b. Kwashiorkor
A. Marasmus – results from severe
deprivation, or impaired absorption
of protein, energy, vitamins and
minerals
Marasmus
Nutrient deficiency is the main cause of
marasmus. It occurs in children that don't
ingest enough protein, calories,
carbohydrates, and other important
nutrients. This is usually due to poverty and
a scarcity of food.
Marasmus
Occurs frequently in children from 6 – 18
months.
Children with marasmus look little old, just
skin and bones.
Impairs brain development and learning
ability (mental retardation)
Body temperature drops below normal
Digestive enzymes are in short supply,
absorption fails.
Vulnerable to infection (dysentery)
Kwashiorkor
- results from severe acute
malnutrition
- originally a Ghanaian word meaning
a “sickness spirit that infects the first
child when the second child is born”
Kwashiorkor, also known as “edematous
malnutrition” because of its association with
edema (fluid retention), is a nutritional
disorder most often seen in regions
experiencing famine.
Kwashiorkor
Child’s limbs and belly become swollen with
edema, a distinguishing feature
Fatty liver develops due to lack of protein
carriers that transport fat out of the liver.
Hair loses its color, the skin becomes patchy
and scaly, with ulcers and sores that fail to
heal
Features of Marasmus and Kwashiorkor in
Children
 Marasmus Kwashiorkor
- infancy (less than 2 - older infants and
y/o) young children (1-3
- severe deprivation y/o)
or impaired - inadequate protein
absorption of intake or, more
protein, energy, commonly, infections
vitamins and - rapid onset; acute
minerals PEM
- develop slowly; - some wt. loss
chronic PEM - some muscle
- severe wt. loss wasting, with
- severe muscle retention of some
wasting with fat loss body fat

- growth: ≤60% - growth: 60-80%

weight-for-age weight-for-age
- no detectable - edema
edema - enlarged, fatty liver
- no fatty liver - apathy, misery,
- anxiety, apathy irritability, sadness
- appetite may be - loss of appetite
normal or impaired - hair is dry and
- hair is sparse, thin, brittle; easily pulled
and dry; easily out; changes color;
pulled out becomes straight
- skin develops
- skin is dry, thin, lesions, rashes
and wrinkled

Protein Supplements

Whey protein = a by-product of cheese

production; falsely promoted as increasing
muscle mass. Whey is the watery part of
milk that separates from the curds.

end