Professional Documents
Culture Documents
Definition of Terms
• Nutrition - is a combination of processes by • Food - is any substance, organic or inorganic,
which a living organism receives and utilizes when ingested or eaten, nourishes the body by
materials or substances needed for the building and repairing tissues, supplying heat and
maintenance of its functions and for growth and energy and regulating bodily processes.
renewal of its components • Nutritional status (Nutriture) - is the condition of
• Nutrient - is a chemical component needed by the body resulting from the utilization of essential
the body for one or more of these three general nutrients.
functions: to provide energy, to build and repair • Optimum and Good Nutrition - means that the
tissues and to regulate life processes. body has an adequate supply of essential
• Enzymes - are organic catalysts that are protein nutrients that are efficiently utilized such that
in nature and are produced by living cells. A growth and good health are maintained at the
catalyst chemical reaction without itself highest possible level.
undergoing change. Biocatalysts like enzymes are • Malnutrition - is a condition of the body resulting
responsible for most chemical reactions in the from a lack of one or more essential nutrients
body. (nutritional deficiency) or it may be due to an
• Hormones - are organic substances produced by excessive nutrient supply to the point of creating
special cells of the body which are discharged toxic or harmful effects (E.g., overnutrition and
into the blood to be circulated and brought to hypervitaminosis)
specific organs or tissues that are remote from • Lavoisier - the father of Nutrition
the source or point of manufacture. They regulate • Francisco O. Santos - the father of Nutrition in the
vital processes which are highly specific. Philippines
• July - Nutrition Month
1. Cardiovascular (heart, blood vessels, ● Transports nutrients, gases, waste products; regulates body
blood) temperature, involved with the immune responses.
2. Digestive (mouth, esophagus, stomach, ● Digests and absorbs nutrients, eliminates waste products.
intestines, liver, pancreas)
3. Endocrine (endocrine glands, E.g. ● Helps regulate metabolism, reproduction water balance, etc (by
Thyroid, pituitary, adrenal glands) hormones secreted)
4. Immune (white blood cells, lymph, ● Provides defense against foreign substances.
spleen, thymus gland)
5. Integumentary (skin, hair, nails, sweat ● Protects the body, regulates temperature, aids in acid-base and water
glands) balance, production of Vitamin D.
6. Lymphatic (lymph vessels, nodes) ● Helps with fluid balance and fat absorption, removes foreign
substances from the blood
7. Muscular (skeletal, cardiac, and ● Maintains posture; directs body movement, produces body heat
smooth muscles)
8. Nervous (Brain, spinal cord, nerves, ● Controls intellectual functions, detects sensations and controls
sensory organs and receptors) movements.
9. Respiratory ● Regulates gas exchange and acid-base balance.
10. Reproductive ● Regulates sexual functions and reproduction
11. Skeletal(bones, joints, cartilages) ● Main frame body support, aids with body movements, stores
minerals, produces blood cells.
12. Urinary (kidneys, urinary tract) ● Removes waste products; regulates fluid, acid-base balance, aids with
homeostasis
Chapter II - Tools in Nutrition
1. Food Guides : The Food Pyramid Food Exchange Table
Food Guides translate quantitative nutritional
HHM EXCH C P F Kcal
requirements into simple, practical and non-
technical language using available and common Veg A As served As
B 1/2 cup desired 1 - 16
foods of the country.
3
Fruits varies 10 - - 40
Milk 4T 12 8 0 80
1 cup 10 170
Meat varies - 8 4 68
Fat 1tsp. - - 5 45
Sugar 1tsp. 5 - - 20
∓5 ∓5 ∓5 ∓25
5. Nutrient Density
Food pyramid teaches the principles of eating a
It is a relative measure of nutrients in a good in
variety of food everyday in proper amounts of
proportion to its caloric content.
servings.
6. Food and Nutrition Labeling
2. RENI (Recommended Energy and Nutrient Intake)
A system of describing processed foods or food
and RDA (Recommended Dietary Allowance)
properties of a food, thus facilitating the selection of
RENI is a nutrient-based dietary standard
a healthy diet.
recognized in the nutrition and health community
7. Nutritional Guidelines
as the source of information on recommended
These are primary recommendations to promote
intakes of energy and nutrients for the
good health habits through proper nutrition. They
maintenance of good health.
seek to foster an adequate and balanced diet as
RDA (Recommended Dietary Allowance) consists of
well as desirable food and nutrition practices and
the minimum requirements plus a safety factor
healthy habits suitable for the general population.
called “margin of safety” to allow for individual
The nutritional guidelines are intended to:
variations of body storage, state of health, nutrient
1. Provide the general public with
utilization and other day-to-day variations within a
recommendations about proper diet and
person.
wholesome practices to promote good
3. FCT (Food Composition Table)
health for themselves and their family.
Each food item has descriptions and the equivalent
2. Provide those concerned with nutrition
local names followed by its composition per
information and education with a handy
100gms edible portion
reference for their counseling and
4. FEL (Food Exchange Lists)
educational services.
The FEL is a grouping of common foods that have
practically the same amount of protein,
carbohydrate and fat. Within a group, one food
item can be exchanged with another provided the
specified serving portion is followed
● Proteins furnish the amino acids required to
build and repair body tissues. DIGESTION
● Nucleoproteins contain the blueprint for the ● In the mouth
synthesis of all body proteins. ○ chewing and crushing moisten protein-
As regulators of body processes rich foods and mixing them with saliva
● As enzymes and hormones, they aid in before swallowing.
digestion and regulate a variety of actions in ● In the stomach
the body. ○ HCI uncoils (denatures) the tangled
● As antibodies, they maintain the body’s strands of protein and activates
resistance to disease and infection. proteolytic enzymes which attack the
● As lipoproteins, they transport triglycerides, peptide bonds.
cholesterol, phospholipids, and fat-soluble ○ HCI converts pepsinogen (inactive
vitamins. enzyme) to pepsin (active enzyme).
● Albumin is of vital importance in the regulation ○ Pepsin inhibits the synthesis of
of osmotic pressure and in the maintenance of pepsinogen.
fluid balance. ○ Pepsin cleaves the large polypeptides
● Because of their amphoteric property, they of protein into smaller polypeptides
maintain acid-base balance of blood and and some amino acids.
tissues.
● Actin and myosin regulate muscle contraction. 𝑝𝑒𝑝𝑠𝑖𝑛
Protein smaller polypeptides
● Specific protein carriers transport nutrients to 𝐻𝐶
the tissues.
● In the Small intestine
○ pancreatic and intestinal proteases
As source of energy and glucose
hydrolyze polypeptides into short
● Proteins provide 4kcal/gram. However, protein
peptide chains.
foods are expensive and are not a
○ Enteropeptidase (also enterokinase)
recommended source of energy.
converts trypsinogen (inactive
enzyme) to trypsin (active enzyme).
FACTORS THAT AFFECT PROTEIN REQUIREMENT
○ Trypsin converts chymotrypsinogen
1. Body size
(inactive enzyme) to chymotrypsin
2. Effect of growth
active enzyme.
3. Effect of pregnancy and lactation
○ Peptidase enzymes on the membrane
4. Effect of aging
surfaces of intestinal cells split most of
5. State of health
the tripeptides and dipeptides into
6. Effect of physical activity
single amino acids.
7. Quality of proteins
8. Adequacy of calories
GENERAL PRINCIPLES OF PROTEIN METABOLISM
1. The amino acids are in a dynamic state. There
FACTORS AFFECTING PROTEIN UTILIZATION
is constantly an exchange, mixing,
1. Amino-acid balance (egg)
intermingling among them.
2. Immobility
2. The all or none law applies in formation of cells
3. Emotional stress
and tissues, the amino acids needed to
4. Calorie
synthesize a particular protein should be all
5. Intake
present at the same time as the right amount
6. Inborn error of metabolism
and in the site where the protein is formed.
7. Food processing
3. There is a limited number of amino acids that RECOMMENDED PROTEIN INTAKE
are labile, ex they are reserved for immediate • Dietary protein usually constitutes 10-15% of the
use to maintain nitrogen balance. energy value of well balanced diets and seldom
4. Synthesis of a particular protein is controlled by exceeds 20%. Whereas the fat in the body can be
a genetic material, the DNA (deoxyribonucleic derived from dietary carbohydrates and the
acid). The RNA (ribonucleic acid) has the code carbohydrates from protein, the proteins of the
or formula for a particular protein to be body are solely dependent on the proteins in the
formed. food for their formation and maintenance.
5. Protein metabolism is closely related with fat • Food protein is the only source of the essential
and carbohydrate metabolism. amino acids and it is the only practical source of
nitrogen with which to build the non-essential
NITROGEN BALANCE (NB) amino acids and other nitrogen-containing
- Is the quantitative difference between nitrogen compounds the body needs.
input (nitrogen intake) and nitrogen
output(excretion in the urine, feces, adn sweat) FOOD SOURCES
- Positive NB exists when intake is greater than • All foods of animal origin(meat, fish, poultry, eggs,
output. seafoods, milk, and dairy products) are excellent
- Negative NB exists when intake is less than sources of protein, and except for the gelatin in
output. collagenous tissues, contain all the essential amino
acids.
PROTEIN SYNTHESIS • Of the plant foods, legumes, nuts, seeds, cereal
Protein synthesis is controlled by two types of grains, and processed vegetable proteins are good
nucleic acids, located primarily in the cytoplasm of the sources of protein, but the proteins they contain
cell. lack or contain insufficient amounts of certain
● DNA essential amino acids.
o Genetic material in the nucleus which initiates • Proteinoid - synthetic source of protein.
and directs protein synthesis. It contains and
stores the genetic blueprint (genetic information) PROTEIN NUTRITURE
necessary to control the sequence of amino acids • Protein-Energy Malnutrition (PEM) - refers to a
during protein synthesis. class of clinical disorders resulting from varying
o Forms part of the chromosome structure the combinations and degrees of protein and energy
amount of DNA per set of chromosomes is deficiency usually accompanied by additional
constante for a given species. physiologic and environmental stresses.
o Consists of subunits called nucleotides; a • Often aggravated by infection and accompanied
combination of 3 nucleotides forms a coding unit by other nutritional deficiencies such as severe
or codon. The sequins of nucleotides in DNA is the vitamin A deficiency.
code of pattern for the synthesis of the new The forms of PEM are:
protein. a. Marasmus - named from the Greek word
o Functions as a template to make strands of m- meaning “dying away”. Marasmic children look
RNA to initiate protein synthesis. like “little old people” with just skin and bones.
b. Kwashiorkor - acute PEM basically due to
● RNA - carries out the actual synthesis of protein. inadequate protein intake. Appears in infants
and young children in the late breastfeeding
Two types of RNA are involved in protein synthesis: and post-weaning phases when the diet is high
messenger RNA(m-RNA) and transfer RNA(t-RNA). in carbohydrate and low in quality and quantity
of protein. Characterized by hypoalbuminemia
Meal Distribution
A
Veg B 5 3 2
Fruits 3 1 1 1
Milk 1 1
Sugar 5 5
Rice 8 2 1 2 1 2
Meat 5 2 2 1
Fat 6 2 2 2
Classification of amino acids based on Essentiality prosthetic group, thus facilitating functions that
neither constituent could properly perform by
Essential Amino Acids Nonessential Amino Acids itself. Ex. mucoproteins, glycoproteins,
nucleoproteins, lipoproteins, phosphoproteins,
Histidine Alanine
chromoproteins, flavoproteins, and
Isoleucine Asparagine
metalloproteins.
Leucine Aspartic acid
Lysine Cystine ● Derived proteins - substances resulting from
Methionine Glutamic acid the decomposition of simple and compound
Phenylalanine Glutamine proteins by the action of heat and other
Threonine Glycine physical forces or by hydrolytic agents. Ex.
Tryptophan Proline
peptones, proteoses, and peptides which are
Valine Serine
formed in the various stages of protein
Arginine Tyrosine
digestion.
According to Amino Acid content
According to Metabolic Pathway
● Complete protein - Contains all the EAAs in
- Glucogenic amino acids are those that form
proportions capable of maintaining life and
pyruvate or intermediates of the Krebs cycle
supporting a normal rate of growth when they
which can be converted to glucose or glycogen.
are the sole source of protein in the diet.
- Ketogenic amino acids are those that can give
Considered as a high biological value protein.
rise to acety1CoA or acetoacetate resulting in
All animal proteins except gelatin are complete
the formation of fat or ketone bodies.
proteins but not necessarily identical in
biological value.
Glucogenic Glucogenic and Ketogenic Amino ● Partially complete protein - contains all the
Amino Acids Ketogenic Amino Acids EAAs but a relatively small amount of one or
Acids some of the amino acids necessary for growth.
Alanine Isoleucine Leucine Can maintain life but cannot support a normal
Arginine Phenylalanine Lysine rate of growth when used as the sole source of
Asparagine Threonine protein in the diet. Ex. gliadin and hordein.
Aspartic acid Tryptophan ● Totally incomplete protein - lacks one or more
Cysteine tyrosine of the EAAs and is therefore incapable of
Glutamine
replacing or rebuilding new tissues, hence
Glutamic acid
cannot support life or growth when used as the
Glycine
Histidine sole source of protein in the diet. Considered as
Methionine a low biological value protein. Ex. zein and
Proline gelatin
Serine
valine ROLES OF PROTEINS
As building materials for growth and repair
CLASSIFICATIONS OF PROTEINS ● Proteins are structural components of all body
According to Chemical Structure tissues, enzymes, hormones, and various body
● Simple Proteins - yield only amino acids upon fluids and secretions.
complete hydrolysis. Ex. albumins, globulins,
● Proteins furnish the amino acids required to
build and repair body tissues. DIGESTION
● Nucleoproteins contain the blueprint for the ● In the mouth
synthesis of all body proteins. ○ chewing and crushing moisten protein-
As regulators of body processes rich foods and mixing them with saliva
● As enzymes and hormones, they aid in before swallowing.
digestion and regulate a variety of actions in ● In the stomach
the body. ○ HCI uncoils (denatures) the tangled
● As antibodies, they maintain the body’s strands of protein and activates
resistance to disease and infection. proteolytic enzymes which attack the
● As lipoproteins, they transport triglycerides, peptide bonds.
cholesterol, phospholipids, and fat-soluble ○ HCI converts pepsinogen (inactive
vitamins. enzyme) to pepsin (active enzyme).
● Albumin is of vital importance in the regulation ○ Pepsin inhibits the synthesis of
of osmotic pressure and in the maintenance of pepsinogen.
fluid balance. ○ Pepsin cleaves the large polypeptides
● Because of their amphoteric property, they of protein into smaller polypeptides
maintain acid-base balance of blood and and some amino acids.
tissues.
● Actin and myosin regulate muscle contraction. 𝑝𝑒𝑝𝑠𝑖𝑛
Protein smaller polypeptides
● Specific protein carriers transport nutrients to 𝐻𝐶
the tissues.
● In the Small intestine
○ pancreatic and intestinal proteases
As source of energy and glucose
hydrolyze polypeptides into short
● Proteins provide 4kcal/gram. However, protein
peptide chains.
foods are expensive and are not a
○ Enteropeptidase (also enterokinase)
recommended source of energy.
converts trypsinogen (inactive
enzyme) to trypsin (active enzyme).
FACTORS THAT AFFECT PROTEIN REQUIREMENT
○ Trypsin converts chymotrypsinogen
1. Body size
(inactive enzyme) to chymotrypsin
2. Effect of growth
active enzyme.
3. Effect of pregnancy and lactation
○ Peptidase enzymes on the membrane
4. Effect of aging
surfaces of intestinal cells split most of
5. State of health
the tripeptides and dipeptides into
6. Effect of physical activity
single amino acids.
7. Quality of proteins
8. Adequacy of calories
GENERAL PRINCIPLES OF PROTEIN METABOLISM
1. The amino acids are in a dynamic state. There
FACTORS AFFECTING PROTEIN UTILIZATION
is constantly an exchange, mixing,
1. Amino-acid balance (egg)
intermingling among them.
2. Immobility
2. The all or none law applies in formation of cells
3. Emotional stress
and tissues, the amino acids needed to
4. Calorie
synthesize a particular protein should be all
5. Intake
present at the same time as the right amount
6. Inborn error of metabolism
and in the site where the protein is formed.
7. Food processing
3. There is a limited number of amino acids that RECOMMENDED PROTEIN INTAKE
are labile, ex they are reserved for immediate • Dietary protein usually constitutes 10-15% of the
use to maintain nitrogen balance. energy value of well balanced diets and seldom
4. Synthesis of a particular protein is controlled by exceeds 20%. Whereas the fat in the body can be
a genetic material, the DNA (deoxyribonucleic derived from dietary carbohydrates and the
acid). The RNA (ribonucleic acid) has the code carbohydrates from protein, the proteins of the
or formula for a particular protein to be body are solely dependent on the proteins in the
formed. food for their formation and maintenance.
5. Protein metabolism is closely related with fat • Food protein is the only source of the essential
and carbohydrate metabolism. amino acids and it is the only practical source of
nitrogen with which to build the non-essential
NITROGEN BALANCE (NB) amino acids and other nitrogen-containing
- Is the quantitative difference between nitrogen compounds the body needs.
input (nitrogen intake) and nitrogen
output(excretion in the urine, feces, adn sweat) FOOD SOURCES
- Positive NB exists when intake is greater than • All foods of animal origin(meat, fish, poultry, eggs,
output. seafoods, milk, and dairy products) are excellent
- Negative NB exists when intake is less than sources of protein, and except for the gelatin in
output. collagenous tissues, contain all the essential amino
acids.
PROTEIN SYNTHESIS • Of the plant foods, legumes, nuts, seeds, cereal
Protein synthesis is controlled by two types of grains, and processed vegetable proteins are good
nucleic acids, located primarily in the cytoplasm of the sources of protein, but the proteins they contain
cell. lack or contain insufficient amounts of certain
● DNA essential amino acids.
o Genetic material in the nucleus which initiates • Proteinoid - synthetic source of protein.
and directs protein synthesis. It contains and
stores the genetic blueprint (genetic information) PROTEIN NUTRITURE
necessary to control the sequence of amino acids • Protein-Energy Malnutrition (PEM) - refers to a
during protein synthesis. class of clinical disorders resulting from varying
o Forms part of the chromosome structure the combinations and degrees of protein and energy
amount of DNA per set of chromosomes is deficiency usually accompanied by additional
constante for a given species. physiologic and environmental stresses.
o Consists of subunits called nucleotides; a • Often aggravated by infection and accompanied
combination of 3 nucleotides forms a coding unit by other nutritional deficiencies such as severe
or codon. The sequins of nucleotides in DNA is the vitamin A deficiency.
code of pattern for the synthesis of the new The forms of PEM are:
protein. a. Marasmus - named from the Greek word
o Functions as a template to make strands of m- meaning “dying away”. Marasmic children look
RNA to initiate protein synthesis. like “little old people” with just skin and bones.
b. Kwashiorkor - acute PEM basically due to
● RNA - carries out the actual synthesis of protein. inadequate protein intake. Appears in infants
and young children in the late breastfeeding
Two types of RNA are involved in protein synthesis: and post-weaning phases when the diet is high
messenger RNA(m-RNA) and transfer RNA(t-RNA). in carbohydrate and low in quality and quantity
of protein. Characterized by hypoalbuminemia
the absorption of vitamin A and its 2. Exogenous cholesterol - it is supplied in the diet,
precursor, carotene. mostly from the fatty portions of meat(brain,
● Source of essential fatty acids which are: glandular organs and egg yolk).
○ Components of cholesterol esters and
membrane phospholipids in retinal Very Low Density Lipoproteins
photoreceptors, cerebral gray matter, - The liver is the most active site of lipid synthesis.
testes and sperm; Lipids made in the liver and those collected from
○ Precursors of prostaglandins, chylomicron remnants are packaged with
thromboxanes, and prostacyclins which proteins as very-low-density lipoproteins(VLDL)
help regulate blood pressure, vascular and brought to other parts of the body as
dilation, blood clotting, lipolysis immune needed.
response, and the nervous system. - Body cells continue to remove triglycerides from
the VLDL as it travels through the body causing it
Classification of Lipids to shrink. As the VLDL loses triglycerides, it
1. Simple Lipids - or called neutral fats becomes more dense. The remaining lipoprotein
Triglycerides - is the chemical name for basic eventually becomes a low-density
fats or stored fats lipoprotein(LDL) which is loaded with cholesterol
2. Compound Lipids but only a few triglycerides.
3. Derived Lipids
a. Fatty acids - the key refined fuel forms of Low Density Lipoproteins
fat that the cell burns for energy. They are - The low-density lipoproteins circulate throughout
the basic structural units of fat the body making their contents available to the
b. Glycerol cells of all tissues. The cells take triglycerides,
c. Cholesterol - is a complex fat-like cholesterol, and phospholipids to build new
compound found practically in all body membranes, make hormones and other
tissues, especially the brain and nerve compounds, or store for later use. LDL receptors
tissues, bile, blood and liver where it is on the liver cells control blood cholesterol
mostly synthesized. It is an essential concentrations by removing LDL from circulation.
component of cell membranes and is - LDLs and VLDLs seem particularly effective in
required for cell growth, replication and depositing cholesterol in the arterial walls. High
maintenance. It is needed by the body for LDL cholesterol is associated with a high risk of
the following: heart disease and is thus referred to as “bad
i. It is the precursor of cholesterol”.
dehydrocholesterol, which has
vitamin D activity High Density Lipoproteins
ii. It is part of the bile acids, thus it helps - Only about one-fourth of the cholesterol in the
in the emulsification of dietary fat. blood is carried as HDL. This lipoprotein
iii. It is also utilized in the biosynthesis of appears to remove cholesterol from deposits
adrenocortical hormones, which are on arterial walls and transports it to the liver
important in the development of for disposal. HDL is called “good cholesterol”
secondary male and female due to this protective effect.
characteristics. - Elevated HDL represents cholesterol returning
Sources: from the rest of the body to the liver for
1. Endogenous cholesterol - it is synthesized breakdown and excretion.
mainly in the liver
Macrominerals Sources Deficiency Toxicity Functions
No. of No. of
Name carbon double Saturation Common Food Sources
atoms bonds