Body Building Foods - Protein

10 Essential Amino Acids for Children

Protein - it orginitated from a Greek Word 8 Essential Amino Acids for Adult
proteios meaning “to hold first place” or “is of
Classification of amino acids
prime importance”. based on Essentiality

Mulder - a dutch chemist, proposed the name in Essential Nonessential

1840 and until now, the word is used due to its Amino Acids Amino Acids
unique function of building and repairing cells and
Histidine Alanine
other specialized roles in metabolism that cannot Isoleucine Asparagine
be accomplished or performed by other nutrients. Leucine Aspartic acid
Lysine Cystine
Amino Acids - are the building blocks of protein. Methionine Glutamic acid
Phenylalanine Glutamine
Elements of Protein Threonine Glycine
Tryptophan Proline
C - Carbon
Valine Serine
H - Hydrogen Arginine Tyrosine
O - Oxygen
N - Nitrogen - elements of protein that
According to Metabolic Pathway
distinguishes it from other nutrients.
- Glucogenic amino acids are those that
form pyruvate or intermediates of the
CLASSIFICATION OF AMINO ACIDS
Krebs cycle which can be converted to
According to Dietary Requirement or Essentiality
glucose or glycogen.
● Essential (indispensable) amino
- Ketogenic amino acids are those that can
acids(EAAs) - are those that the human
give rise to acety1CoA or acetoacetate
body cannot make at all or cannot be
resulting in the formation of fat or ketone
synthesized at a rate sufficient to meet
bodies.
growth and maintenance requirements.
They must therefore be provided pre
formed in the diet, either as free amino Glucogenic Glucogenic Ketogenic
acids or as constituents of dietary Amino Acids and Amino Acids
proteins. Ketogenic
Amino Acids
● Semi-essential(conditionally
indispensable) amino acids - are those Alanine Isoleucine Leucine
that are normally not essential but become Arginine Phenylalani Lysine
essential under certain clinical conditions. Asparagine ne
They must be supplied by the diet when Aspartic Threonine
the need for these amino acids exceeds acid Tryptophan
Cysteine tyrosine
the body’s ability to produce them. Amino
Glutamine
acids that power the requirements for an Glutamic
EAA but cannot repeat it entirely. acid
● Nonessential (dispensable) amino Glycine
acids (NEAAs) - are those that can be Histidine
synthesized in the body from EAAs or Methionine
from an available source of nitrogen to Proline
Serine
form the amino group and a carbon
valine
skeleton composed of fragments from
carbohydrate or fat to form the rest of the
structure. Dietary proteins usually provide
these amino acids but it is not essential CLASSIFICATIONS OF PROTEINS
that they do so. According to Chemical Structure
● Simple Proteins - yield only amino acids
upon complete hydrolysis. Ex. albumins,
 globulins, gliadin, keratin, collagen,
elastin, zein, myosin, and many others.
● Compound or conjugated proteins -
simple proteins combined with a non-
protein or prosthetic group, thus facilitating
functions that neither constituent could
properly perform by itself. Ex.
mucoproteins, glycoproteins,
nucleoproteins, lipoproteins,
phosphoproteins, chromoproteins,
flavoproteins, and metalloproteins.
● Derived proteins - substances resulting
from the decomposition of simple and
compound proteins by the action of heat
and other physical forces or by hydrolytic
agents. Ex. peptones, proteoses, and
peptides which are formed in the various
stages of protein digestion.
According to Amino Acid content
● Complete protein - Contains all the EAAs
in proportions capable of maintaining life
and supporting a normal rate of growth
when they are the sole source of protein in
the diet. Considered as a high biological
value protein. All animal proteins except
gelatin are complete proteins but not
necessarily identical in biological value.
● Partially complete protein - contains all
the EAAs but a relatively small amount of
one or some of the amino acids necessary
for growth. Can maintain life but cannot
support a normal rate of growth when
used as the sole source of protein in the
diet. Ex. gliadin and hordein.
● Totally incomplete protein - lacks one or
more of the EAAs and is therefore
incapable of replacing or rebuilding new
tissues, hence cannot support life or
growth when used as the sole source of
protein in the diet. Considered as a low
biological value protein. E.x zein and
gelatin
ROLES OF PROTEINS
As building materials for growth and repair
● Proteins are structural components of all
body tissues, enzymes, hormones, and
various body fluids and secretions.
● Proteins furnish the amino acids required
to build and repair body tissues.
● Nucleoproteins contain the blueprint for
the synthesis of all body proteins.
As regulators of body processes
● As enzymes and hormones, they aid in
digestion and regulate a variety of actions
in the body.
● As antibodies, they maintain the body’s
resistance to disease and infection.
● As lipoproteins, they transport
triglycerides, cholesterol, phospholipids,
and fat-soluble vitamins.
● Albumin is of vital importance in the
regulation of osmotic pressure and in the
maintenance of fluid balance.
● Because of their amphoteric property, they
maintain acid-base balance of blood and
tissues.
● Actin and myosin regulate muscle
contraction.
● Specific protein carriers transport nutrients
to the tissues.
As source of energy and glucose
● Proteins provide 4kcal/gram. However,
protein foods are expensive and are not a
recommended source of energy.
FACTORS THAT AFFECT PROTEIN
REQUIREMENT
1. Body size
2. Effect of growth
3. Effect of pregnancy and lactation
4. Effect of aging
5. State of health
6. Effect of physical activity
7. Quality of proteins
8. Adequacy of calories
FACTORS AFFECTING PROTEIN UTILIZATION
1. Amino-acid balance (egg)
2. Immobility
3. Emotional stress
4. Calorie
5. Intake
6. Inborn error of metabolism
7. Food processing
DIGESTION
● In the mouth
○ chewing and crushing moisten
protein-rich foods and mixing them
with saliva before swallowing.
 ● In the stomach
○ HCI uncoils (denatures) the
tangled strands of protein and
activates proteolytic enzymes
which attack the peptide bonds.
○ HCI converts pepsinogen (inactive
enzyme) to pepsin (active
enzyme).
○ Pepsin inhibits the synthesis of
pepsinogen.
○ Pepsin cleaves the large
polypeptides of protein into smaller
polypeptides and some amino
acids.
pepsin
Protein smaller polypeptides
HC
● In the Small intestine
○ pancreatic and intestinal proteases
hydrolyze polypeptides into short
peptide chains.
○ Enteropeptidase (also
enterokinase) converts trypsinogen
(inactive enzyme) to trypsin (active
enzyme).
○ Trypsin converts
chymotrypsinogen (inactive
enzyme) to chymotrypsin active
enzyme.
○ Peptidase enzymes on the
membrane surfaces of intestinal
cells split most of the tripeptides
and dipeptides into single amino
acids.
GENERAL PRINCIPLES OF PROTEIN
METABOLISM
1. The amino acids are in a dynamic state.
There is constantly an exchange, mixing,
intermingling among them.
2. The all or none law applies in formation of
cells and tissues, the amino acids needed
to synthesize a particular protein should
be all present at the same time as the
right amount and in the site where the
protein is formed.
3. There is a limited number of amino acids
that are labile, ex they are reserved for
immediate use to maintain nitrogen
balance.
4. Synthesis of a particular protein is
controlled by a genetic material, the DNA
(deoxyribonucleic acid). The RNA
(ribonucleic acid) has the code or formula
for a particular protein to be formed.
5. Protein metabolism is closely related with
fat and carbohydrate metabolism.
NITROGEN BALANCE (NB)
- Is the quantitative difference between
nitrogen input (nitrogen intake) and
nitrogen output(excretion in the urine,
feces, adn sweat)
- Positive NB exists when intake is greater
than output.
- Negative NB exists when intake is less
than output.
PROTEIN SYNTHESIS
Protein synthesis is controlled by two
types of nucleic acids, located primarily in the
cytoplasm of the cell.
● DNA
- Genetic material in the nucleus
which initiates and directs protein
synthesis. It contains and stores
the genetic blueprint (genetic
information) necessary to control
the sequence of amino acids
during protein synthesis.
- Forms part of the chromosome
structure the amount of DNA per
set of chromosomes is constante
for a given species.
- Consists of subunits called
nucleotides; a combination of 3
nucleotides forms a coding unit or
codon. The sequins of nucleotides
in DNA is the code of pattern for
the synthesis of the new protein.
- Functions as a template to make
strands of m-RNA to initiate
protein synthesis.
● RNA - carries out the actual synthesis of
protein.
Two types of RNA are involved in protein
synthesis: messenger RNA(m-RNA) and transfer
RNA(t-RNA).
RECOMMENDED PROTEIN INTAKE
Dietary protein usually constitutes 10-15% of
the energy value of well balanced diets and
seldom exceeds 20%. Whereas the fat in the
body can be derived from dietary carbohydrates
and the carbohydrates from protein, the proteins
of the body are solely dependent on the proteins
in the food for their formation and maintenance.
Food protein is the only source of the essential
amino acids and it is the only practical source of
nitrogen with which to build the non-essential
amino acids and other nitrogen-containing
compounds the body needs.
FOOD SOURCES
All foods of animal origin(meat, fish, poultry, eggs,
seafoods, milk, and dairy products) are excellent
sources of protein, and except for the gelatin in
collagenous tissues, contain all the essential
amino acids.
Of the plant foods, legumes, nuts, seeds, cereal
grains, and processed vegetable proteins are
good sources of protein, but the proteins they
contain lack or contain insufficient amounts of
certain essential amino acids.
Proteinoid - synthetic source of protein.
PROTEIN NUTRITURE
Protein-Energy Malnutrition (PEM) - refers to a
class of clinical disorders resulting from varying
combinations and degrees of protein and energy
deficiency usually accompanied by additional
physiologic and environmental stresses.
Often aggravated by infection and accompanied
by other nutritional deficiencies such as severe
vitamin A deficiency.
The forms of PEM are:
a. Marasmus - named from the Greek word
meaning “dying away”. Marasmic children
look like “little old people” with just skin
and bones.
b. Kwashiorkor - acute PEM basically due
to inadequate protein intake. Appears in
infants and young children in the late
breastfeeding and post-weaning phases
when the diet is high in carbohydrate and
low in quality and quantity of protein.
Characterized by hypoalbuminemia and
enlarged fatty liver (pot belly).
Sybcytabeiys fat is usually preserved but
muscle wasting is often masked by
edema.
c. Marasmic Kwashiorkor - deficiency of
both protein and energy. Characterized by
the edema of kwashiorkor with the wasting
of marasmus. Child suffers the effects of
both malnutrition and infection.
Researchers believe that kwashiorkor and
marasmus are two stages of the same
disease. A child with marasmus can later
develop kwashiorkor. Some research
indicates that marasmus represents the
body’s adaptation to starvation and that
kwashiorkor develops when adaptation
fails.
PROTEINS AND HEALTH
1. Heart Disease
 Food rich in animal protein tends to be
rich in saturated fats. There is a
correlation between animal protein intake
and heart disease although no
independent effect has been
demonstrated. On the other hand,
substituting soy protein for animal protein
lowers blood cholesterol, especially in
those with hypercholesterolemia.
 The amino acid arginine may protect
against heart disease because it slows the
progression of atherosclerosis. The exact
amount needed to defend against heart
disease has not yet been determined.
 Research suggests that elevated levels of
the amino acid homocysteine may be an
independent risk factor for heart disease.
It is not yet fully understood what factors
raise homocysteine in the blood or
whether elevated levels are a cause or an
effect of heart disease.
2. Kidney Disease
- A high protein intake increases the
work of the kidneys, but does not
appear to cause kidney disease.
Taking protein in moderation may
slow down the progression of
kidney disease and limit the
formation of kidney stones in
people who have these conditions
3. Weight Management
- Protein-rich foods are often fat-rich
foods that contribute to weight gain
with its accompanying health risks.
A high-protein diet may result in
weight loss, but only because it is
 low in calories. A diet that provides
adequate protein, moderate fat,
and sufficient energy from
carbohydrates can better support
weight loss and good health.
4. Cancer
- Population studies suggest a
correlation between high intakes of
animal proteins and some types of
cancer, notably cancer of the
colon, breast, kidneys, pancreas,
and prostate. However, further
studies are needed to establish the
role of protein in etiology cancer.
5. Protein and Amino Acid Supplements
- People take protein supplements
to build muscle or spare body
protein while losing weight. Amino
acid supplements are expensive
and less completely digested than
protein-rich foods. Simple amino
acids do not occur naturally in
foods and offer no benefit to the
body. The body was not designed
to handle the high concentrations
and unusual combinations of
amino acids in supplements.
- An excess of one amino acid can
create such a demand for a carrier
that it limits the absorption of
another amino acid, presenting the
possibility of a deficiency or
toxicity.
- Single amino acid supplements
like tryptophan have been used to
relieve pain, depression and
insomnia. The use of tryptophan
for these purposes is still
experimental. The FDA issued a
recall of all products containing
manufactured tryptophan after
more than 1,500 people who took
tryptophan supplements developed
a rare blood disorder known as
eosinophilia-myalgia syndrome
(EMS). It is characterized by
severe muscle and joint pains,
high fever, and in over three dozen
cases, death.