Proteins and Amino Acids

Ampong, Trisha

Garcia, Mekyla

Hilaga, Kaishe

Longos, Charlotte

Naag, Kate

Resomadero, Erjean

Villaver, Raul

( GROUP - 7)

BS Nutrition and Dietetics 1

BS ND 1A

A Written report submitted to Ms. Karyne June D. Simon, RND

In partial fulfillment of the course

HE 54- Basic Nutrition

JUNE 28, 2023

 Table of Contents

Introduction 1

Objectives 1

Nature of Proteins 2

Functions of Proteins 6

Determination Of Protein Quality 9

Protein Malnutrition 12

Protein Metabolism 13

Food Sources 15

Protein Requirement/Allowance and RENI 18

Conclusion 22

References

ii
 INTRODUCTION
The building blocks of proteins are amino acids. Proteins are what gives function in cells
that are performed by complex molecules. They are crucial to the body's structure, operation,
and regulation. Protein originated in the Greek word proteios meaning “ to hold first place” or “ is
of prime importance”. Gerardus Johannes Mulder, a Dutch chemist proposed the name in 1840.
Proteins are found throughout the body—in muscle, bone, skin, hair, and virtually every other
body part or tissue.
There are 20 common amino acids present in biological chemistry, and they are what
make up proteins, which are biopolymeric structures. Building blocks, hormones, enzymes,
structural support, biochemical catalysts, cellular death initiators, and structural support are all
functions of proteins. The four structural levels of proteins—primary, secondary, tertiary, and
quaternary—can also be used to further categorize them (LaPelusa, 2022).

The first level is known as the primary structure. It is made up of amino acid residues in a linear
arrangement. Peptide linkages hold each residue to the others in place. These links have
designated alpha, beta, and gamma carbon atom locations, which correspond to certain
positions in relation to the peptide linkage. The protein backbone is another name for this
structure .

Objectives:
1. Determine what is a Protein.
2. To be able to know the functions and classification of proteins;
3. Importance of protein and how much we should consume.

1
NATURE OF PROTEINS

- A protein is a naturally-occurring, unbranched polymer in which the monomer units are

amino acids
- Proteins are most abundant molecules in the cells after water – account for about 15% of
a cell’s overall mass

Amino acids are composed of a hydrogen atom, an amino (-NH2), a carboxyl (-COOH) group,
and a side chain (-R) attached to the same carbon atom.

Figure 1. Basic structure of Amino Acid.

Classification of Amino Acids

A. According to Essentiality

An essential amino acid (or indispensable amino acid) is one that cannot be synthesized by
the body from materials readily available, at a speed to keep up with normal growth rate.

A semi-essential (or semi-indispensable) amino acid reduces the need for a particular essential
amino acid or partially spares it. However, it can completely replace the essential amino acid.
"an amino acid that can maintain life processes for an adult but not enough for normal growth in
children." An example is arginine.

A non-essential amino acid is also called "dispensable amino acid cannot

because it is not a dietary essential. It can be synthesized by the body as long as the materials
for synthesis are adequate.

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 Figure 1.1 Essential, Semi-Essential And Non-Essential NAmino acids

B. According to the Chemical Composition of Their Side Chains

1. Basic Amino Acids - those with additional amino acid groups.

2. Acidic Amino Acids - contain additional carboxyl groups.
3. Neutral Amino Acids - those that contain additional acidic or basic groups classified into
aliphatic and aromatic or cyclic amino acids.
The aliphatic AAs have straight side chains, whereas aromatic or cyclic amino acids contain a
ring structure

Branched-chain amino acids (BCAA) are AAs having aliphatic side-chains with a branch (a
carbon atom bound to more than two other carbon atoms). There are three branched-chain
amino acids: leucine, isoleucine and valine

C. According to Hydrolytic Products and Sources

Other terms associated with groups of amino acids relate to their chemical reactions as:
glucogenic (they follow carbohydrate pathways in metabolism); ketogenic (they are converted
to ketone bodies like acetate); acidic, basic or neutral (depending on pH reactions).

See Table 4-2 for the three main groups of proteins according to products they yield upon
hydrolysis

D. According to Structure and Spatial Arrangement of Amino Acids

Fibrous Proteins: Alpha-Keratin & Collagen

-The polypeptide chains are arranged in long strands or sheets
3
-Have long, rod-shaped or string-like molecules that can intertwine with one another and form
strong fibers; water-insoluble
-Structural functions
Keratin - chief protein in hair
Collagen- connective tissue, in tendons and bone matrices

Globular proteins: Myoglobin & Hemoglobin are proteins wherein its structure is coiled and
tightly wounded and is relatively soluble in water. Examples are: casein in milk, cheese, albumin
in egg whites and milk, and globulin in red blood cells.

Figure 1.2 Structural Formulas of Amino Acids

Figure 1.3 Insulin Molecule showing amino acid sequence

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Insulin is a small protein consisting of 51 amino acids in two short polypeptide chains. S-S
represents the cross-links between cysteine molecules, known as disulfide bridges.

TABLE 1. The abbreviations of individual amino acids are as follows:

Amino Acid Three Letter Amino Acid Three Letter

Abbreviation Abbreviation

alanine ala arginine arg

asparagine asn isoleucine ile

leucine leu cysteine cys

glutamine gln glutamate glu

lysine lys phenylalanine phe

proline pro serine ser

glycine gly histidine his

threonine thr tyrosine tyr

valine val

Amino Acid Content of Proteins

Complete Proteins are proteins containing all the essential amino acids in amounts sufficient
for growth and maintenance of life.
Partially Complete Proteins are proteins that can maintain life but do not support growth; e.g.,
gliadin in wheat, legumin in legumes.
Incomplete Proteins are proteins that cannot support life and growth

Classification of protein
Several arbitrary classifications are used for dividing protein on their shape. Most commonly,
proteins are classified into three groups,
● Simple
● Conjugated
● Derived protein
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Each group is subdivided into a number of classes designated by their general names. Each
class contains a number of subclasses which have different physical and chemical properties
Learning Chemistry. (2022).

Simple protein
They give only amino acids or their derivatives on hydrolysis. Simple proteins are classified into
several classes such as albumin, globulin, prolamin, glutelin, and scleroprotein.

● Albumins
Albumins are simple proteins that are soluble in water and coagulated by heat. It is precipitated
by the solutions of ammonium sulfate. Some common examples of albumins are egg albumin,
serum albumin, and lactalbumin.

● Globulins
Globulins are proteins that are insoluble in water but soluble in dilute salts solution and
inorganic acids and alkalis. It is coagulated by heat and half saturated by ammonium sulfate
solutions. Globulins usually contain glycine. Some typical examples of globulins are serum
globulin, tissue globulin, and vegetable globulin.
● Prolamins
Prolamins are a group of plant storage proteins that are insoluble in water or salt solution but
soluble in dilute acids or alkalis. It contains large amounts of proline. Prolamins are found mainly
in plant seeds such as wheat, barley, rye, corn, sorghum, oats, etc.
● Glutelins
Glutelins are a class of propane prolamin proteins insoluble in water and dilute salt solution but
soluble in dilute acid or alkalis. They are found in the endosperm of certain seeds. Arginine,
proline, and glutamic acid are the main components of glutelins. It is found mainly in wheat
(glutenin) or rice (oyrzenin).
● Histones
Histones are a highly basic class of proteins soluble in water but insoluble in dilute ammonia
solution. They are not coagulated by heat and contain large amounts of histidine and arginine.
They are hydrolyzed by pepsin and trypsin. Histones are found in eukaryotic cell nuclei.
Histones are the proteins of DNA and hemoglobin. They play an important role in gene
regulation and DNA replication.
● Protamines
Prolamins are more basic than histones with a simple structure. They are collectively known as
sperm-specific nuclear basic proteins. Prolamins are soluble in water, dilute acids and dilute
ammonia. They are coagulated by heat and precipitated by ethanol solution. The arginine-rich
proteins prolamins are found in various nucleic acids. They are hydrolyzed by various enzymes
like trypsin and papain.
● Globins
Globins are heme-containing globular proteins that bind or transport oxygen to the cells.
Myoglobin and hemoglobin are the two important members of globins.
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Conjugated protein
Conjugated proteins contain a non-protein group or compound containing amino acid residues
attached to a protein part. The non-protein group is called the prosthetic group. Conjugated
protein can be separated from the protein parts by careful hydrolysis. According to the
prosthetic group, conjugated proteins are the following types,
● Nucleoproteins - These are the conjugated proteins that contain nucleic acid as a
prosthetic group.
● Chromoproteins - These are characterized by their color prosthetic group. Chlorophyll
and hemoglobin are the most common examples of chromoproteins.
● Glycoproteins - Glycoproteins contain carbohydrates or derivatives of carbohydrates as
a prosthetic group.
● Phosphoproteins - These are conjugated proteins in which the prosthetic group contains
a phosphate group or a complex molecule such as 5′-phospho-DNA.

● Lipoproteins - The prosthetic group in lipoproteins is lecithin, kephalin, etc.

● Metalloproteins - These contain a metal that is an integral part of the structure. Many
metals such as iron, manganese, copper, and magnesium formed metalloproteins. For
example, hemoglobin and chlorophyll contain iron and magnesium metal.

Derived proteins
Derived proteins are degradation products obtained by the action of acids, alkalies, and
enzymes on protein. These are classified into two types such as primary and secondary.
Primary proteins are insoluble in water but soluble in acids and alkalis. Secondary proteins are
soluble in water and coagulated by heat.

Function of Proteins

Proteins are made up of amino acids that build and repair cells and tissues, supply
energy, and control bodily functions. This is due to the fact that our vital organs, blood
cells, muscles, and antibodies are protein in nature while our skeletal system, as well as
hair, nails, and skin cannot be formed without protein. An available proper amount of
essential amino acids forms a specific protein molecule that aids the growth of all living
things. Also, all enzymes are protein and only some hormones are protein. All body
fluids and secretions have protein, except bile. This makes about 1/5 or 20% of an adult
body weight to be protein of which 1/3 is in the muscles, 1/5 in bones and teeth, 1/10 in
the skin, and the rest is body fluids and other tissues (Claudio, 1982).

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 ● Source of Energy

The main sources of energy are fats and carbs, but protein is also present. It is
claimed to be more practical in meal planning to consume fats and carbs than
carbohydrates in order to save energy for cell and tissue growth and repair. This is
because it is the protein's primary and unique role, and being a source of energy is only
one of its capacities (Claudio, 1982).

For instance, if an individual consumes more protein than they require, the cells in their
bodies use it for energy for tissue maintenance and repair. When extra protein is not
required for energy, their bodies use it to produce fat. It then forms a component of fat
cells. If they do not get enough calories and protein in their diets, protein in food and
bodies be used for energy. If this occurs, protein is not taken for its intended purpose.
The primary goal is to keep the body in good condition. Having enough. Protein and a
well-balanced diet with enough calories are essential. Protein will thus be employed for
tissues and other purposes. Proteins perform various tasks. To achieve the
requirements, fat and carbohydrates will be needed to meet energy requirements
(Hermann, 2019).

● Regulator of Body Processes

Protein influences the level of osmotic pressure, which helps to maintain water
and acid-base homeostasis. It acts as a buffer, facilitating your body in maintaining
proper pH levels in blood and other bodily fluids. When a person has low plasma
proteins, fluids accumulate between tissues, which causes edema, which is a clinical
sign of hypoproteinemia. This is a type of severe protein malnutrition which occurs when
a person consumes enough calories but not enough protein.

Proteins are responsible for transporting nutrients such as lipids, vitamins,

minerals, and oxygen throughout the body, while others store them. Protein transporters
only bind to certain molecules. To put it another way, a protein transporter that transfers
glucose will not transport cholesterol. Proteins can also be used for storage. Ferritin and
Casein stores protein of which Ferritin is an iron storing protein while the latter is the
main protein in milk that helps newborns grow (Claudio, 1982; Van De Walle, 2023).

8
 ● Specific Roles of an Amino Acid

Each amino acid performs a specific purpose, and when combined, they serve as
the building blocks for protein molecules. A person requires twenty (20) distinct amino
acids for them to develop and function effectively, although only nine (9) are considered
essential- namely, phenylalanine, valine, threonine, tryptophan, methionine, leucine,
isoleucine, isoleucine, lysine, and histidine. This is because your body cannot
synthesize the nine essential amino acids, you must obtain them from your food.
Conditionally essential amino acids are non-essential amino acids that become
necessary under particular conditions, such in disease or pregnancy (Richter, 2023)

-Methionine is a methylating agent and helps form the heme of red blood cells
and choline. It contributes the methyl radical (-CH3) to metabolic reactions that need it.
It’s also necessary for tissue growth and the absorption of zinc and selenium, minerals
that are vital to your health (Claudio, 1982; Richter, 2023).

-Phenylalanine is the precursor for tyrosine. Both are important in the production
of two hormones: thyroxine and epinephrine. It plays an integral role in the structure and
function of proteins and enzymes and the production of other amino acids (Claudio,
1982; Richter, 2023).

-Tryptophan is a precursor for niacin (a B-vitamin) and the neurotransmitter

serotonin that regulates your appetite, sleep and mood (Claudio, 1982; Richter, 2023).

While glycine combines with toxic substances to render them harmless. It is also a
precursor of porphyrin like heme.

-Leucine, Isoleucine, and Valine all enter the alanine-glucose cycle— also
referred to in the literature as the Cahill cycle or the alanine cycle that involves muscle
protein being degraded to provide more glucose to generate additional ATP for muscle
contraction to release the nitrogen to other intermediate metabolites that need it
(Claudio 1982; PubChem, n.d.).

-Cysteine, glutamate, and glycine make up the tripeptide glutathione, which is a

most powerful antioxidant in the body, present in every cell. Glutathione protects cells,
and is especially important for liver health (Claudio, 1982). Lastly, aspartate, glycine and
glutamine are precursors of nucleotides.

Some Special Functions of Protein (Claudio, 1982)

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Table 1.2 Examples and Function of mentioned Amino Acids.
Type and examples Occurrence or function
Catalytic protein (enzymes)
Trypsin Hydrolysis of peptide bonds
DNA polymerase Synthesis of DNA
Regulatory proteins (hormones)
Insulin Stimulates glucose metabolism
Growth hormone Stimulates bone growth
Protective proteins
Antibodies Combine with foreign proteins
Interferon Impairs virus replication
Storage proteins
Casein Major protein in milk
Ferritin Iron storage in liver
Transport proteins
Hemoglobin Transports oxygen in blood
Myoglobin Transports/stores oxygen in muscles
Structural proteins
Collagen Fibrous connective tissue
Ribosomal proteins Associated with RNA in ribosomes
Contractile proteins (in muscles)
Myosin Thick filaments of muscle
Actin Thin filaments of muscle
Genetic proteins
Histones Associate with DNA of chromosomes
Repressor Blocks expression of genes
Blood clotting proteins
Prothrombin Converted to Thrombin
Fibrinogen Converted to Fibrin

Determination of Protein Quality

A. Biological Test

1. Biological Value (BV) of protein is one method of measuring protein quality. It refers to the
relative utilization of the protein in the body compared to a standard protein; usually egg albumin
or casein of milk. The proportion of digested and absorbed nitrogen is calculated by subtracting
from the total nitrogen intake what is excreted as fecal and urinary nitrogen.

The biological value of protein is defined as:

Retained Nitrogen / Absorbed Nitrogen x 100

10
Note: When a protein contains the essential amino acids in the right proportion required by
humans, we say that it has high biological value (e.g. meat, poultry, cheese, soya beans, milk,
quinoa, eggs, fish, yogurt, quark, soya beans, quinoa). When the presence of one or more
essential amino acids is insufficient, the protein is said to have low biological value (e.g. peas,
beans, nuts, lentils, cereals (rice, oats, barley, rye, millet, sorghum) and cereal products (bread,
pasta), seeds and gelatine).

2. Net Protein Utilization (NPU) - this is a measure of relative digestibility of proteins which is
defined as:

NPU = Dietary N minus (Urinary N+ Fecal N) / Dietary N × 100

3. Protein Efficiency Ratio (PER) - this refers to change in body weight in relation to the
amount of protein eaten which is defined as:

PER = N wt. (g) / P intake (g)

4. Net Dietary Protein Calories Percent - this relates protein quality to energy intake which is
defined as:

NDP Cal % = Protein kcal / Total kcal intake × 100

B. Chemical Testing

5. Amino Acid Score (AAS) or Chemical Score - this is based on chemical analysis of protein
by comparing its amino acid content with a reference protein which is defined as:

Amino Acid Score = mg of AA in 1 g test protein / mg AA in 1 g reference protein x 100

In protein measurement, the principle of Kjeldahl method is used. This is based on the analysis
of nitrogen multiplied by the factor 6.25 (100% protein divided by 16% nitrogen = the factor of
6.25)

6. Protein Digestibility Corrected Amino Acid Score (PDCAAS) is a method of evaluating

the protein quality based on both the amino acid requirements of humans and their ability to
digest it.

PDCAAS = mg of limiting AA in I g test protein / mg of same AA in 1 g reference protein × 100

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 Figure 2. Protein Quality Comparison Chart

Ways of Improving Protein Quality

To increase the nutritive value of protein foods listed here are the ways on how to increase its
value:

1. Fortification - refers to the addition of amino acids in desirable levels so that food contains
more than what originally exists. (i.e. lysine added to bread)

2. Enrichment - to restore what was lost during the milling process by adding an amino acid
according to Food and Drug standards (i.e. lysine to Cerelac™).

3. Supplementation - refers to the addition of protein rich foods to regular diet so as to increase
total protein content and improve its standards (i.e. High protein milk given in addition to lugao
or fruits or vegetables).

4. Complementation - refers to the combination of food proteins such that one lacking in an
essential amino acid is provided by another rich in that amino acid. Examples are: rice and
monggo; soybean and wheat; soybean and nuts; cottonseed and corn; soybean and corn;
soybean and red kidney bean.
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 Protein Malnutrition
Protein malnutrition is an imbalance between the amount of protein and energy available
and what the body needs in order to grow and operate at its most efficient level (Bhutia, 2014).
Prolonged protein malnutrition will result in PEM (Protein-energy Malnutrition) or CPM
(Calorie-Protein Malnutrition) which is an insufficient protein, calorie, and micronutrient intake or
absorption to meet metabolic requirements. It could also appear when there has been an
excessive loss of nutrients (DermNet NZ, n.d.).

Deficiency Signs
Early signs affected by protein malnutrition includes; general weakness, weight loss,
reduced resistance to infections, lethargy or malaise, and pallor. Edema and dry, scaly skin are
the later signs. There are two forms of protein malnutrition; the kwashiorkor and marasmus.
These forms are caused by poverty which affects the supply of foods and lack of food supply for
protein sources.
● Kwashiorkor
- Kwashiorkor is a condition characterized by extreme protein deficiency and
swelling in both extremities. Infants and toddlers are typically affected, most
frequently between the ages of weaning and 5.
● Marasmus
- A severe sign of protein-energy malnutrition. It happens as a result of not getting
enough calories overall. Adipose tissue and muscle are overtly lost as a result. A
weight-for-height ratio that is more than three standard deviations below the
average for the child's age or gender is possible.

Comparing kwashiorkor and marasmus

● Kwashiorkor and marasmus have both skeletal muscle losses, but much more in
marasmus.
● Kwashiorkor significantly decreases serum protein and has pronounced edema.
● Marasmus resulted in wrinkled and thin skin (old man’s face) due to its significant
loss of adipose tissues.
● Body weight loss in kwashiorkor is not significantly partly due to edema and
partly because there is some adipose tissue left.

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 Figure 2. Difference between Kwashiorkor and Marasmus

Excessive Protein Intake

Extra protein consumption can also lead to higher blood lipids and heart disease
because many high-protein diets are high in total and saturated fat. Extra protein consumption,
which can strain the kidneys, poses an added risk to persons who are prone to kidney disease
(Wempen, 2022). Protein is broken down into amino acids, which then enter the bloodstream.
The liver converts excess amino acids to other usable molecules in a process known as
deamination. Deamination is when an excess of protein is taken, an amine group is removed,
which is subsequently transformed into ammonia and excreted by urination. This deamination
mechanism enables the body to transform surplus amino acids into useful byproducts.

Protein Metabolism
Proteins in food are digested in the stomach and small intestine, by the action of stomach
acid, which denatures proteins, and several enzymes that hydrolyze peptide bonds. Together
they break down proteins into individual amino acids, which are then absorbed and circulated
into the bloodstream and transported to the liver. The amino acids then enter the metabolic pool
and cells to perform various physiological and structural roles.

General Principles of Protein Metabolism

● The amino acids are in a dynamic state. There is constantly an exchange, mixing,
intermingling among them.
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 ● 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 in the right amount
and in the site where the protein is formed.
13
● There is a limited number of amino acids that are labile, they are reserve for immediate
use to maintain nitrogen balance.
● Synthesize of a particular protein is controlled by a genetic material, the DNA. The RNA
has the code or formula for a particular protein to be formed.
● Protein metabolism is closely related with fat and carbohydrate metabolism.

Nitrogen Balance
Nitrogen balance is the traditional method of determining dietary protein requirements.
Determining dietary protein requirements using nitrogen balance requires that all nitrogen inputs
and losses are carefully collected, to ensure that all nitrogen exchange is accounted for. In
short, it is an index of the amount of protein utilized by the body. An individual is said to be in a
nitrogen balance or equilibrium if his nitrogen intake is equal to his nitrogen output. If protein is
being used up for anabolic processes: children, pregnant mother, and convalescing person, he
is in a state of positive nitrogen balance. If the intake is less than the output, the person is
catabolizing protein instead of retaining the nitrogen in tissues. During surgery, fever, shock, and
burns, negative nitrogen balance are experienced, it is when nitrogen losses are greater.

Factors Affecting Nitrogen Balance

● Amino Acid Composition

-to be efficiently utilized for tissue synthesis, the right assortment of amino acids has
definite proportions for the particular tissue to be formed. They should be present at the proper
site and at the same time. The amino acid pattern of egg protein is considered a model for best
growth response.

● Immobility
-a healthy individual who is immobilized or at rest, may lose as much as 18gm of nitrogen
a day. It has been observed in bedridden person, that inactivity causes negative nitrogen
balance even if their diet is adequate with protein.

● Emotional Stress
-emotional stress such as fear, worry, anger, and anxiety will increase secretion of
adrenaline, resulting in loss of nitrogen. Even students under stress of examination could lose
nitrogen appreciably.

● Caloric Intake
-if fat and carbohydrate sources of calories are not sufficient, protein will be deaminated
and used for energy. Nitrogen retention drops at a critical level.
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PROTEIN FOOD SOURCES

As protein plays a vital role with our growth and development it is a must that we supply the
adequate amount of protein that our body needs everyday. With this concept we must also know
the sources to sort out the best quality of protein. Red meat and processed meat increase the
risk of various diseases and early mortality. Lower your risk by eating healthy protein sources
like beans, almonds, fish, or chicken instead.. Here are examples of good protein sources:

Animal based:

Figure 3: Egg Figure 3.1: Poultry

Figure 3.2: Seafoods Figure 3.3: Fish

16
 Figure 3.4: Meat Figure 3.5: Dairy Products

Plant based protein according to Eva Fry (2021):

Figure 4: Nutritional yeast Figure 4.1: Tofu

Figure 4.2: Nuts Figure 4.3: Quinoa

17
Figure 4.4: Seeds Figure 4.5: Chia Seeds

Figure 4.6 Buckwheat Figure 4.7: Beans

Figure 4.8: Broccoli Figure 4.9: Protein powders

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PROTEIN REQUIREMENT AND ALLOWANCE

In the Philippines, protein allowance for adult men and women is calculated at 1.14 g/kg body
weight, considering NPU ( Net Protein Utilization ).
The minimum amino acid requirement is 0.35-0.525g per kilogram desirable body weight
(Nitrogen x 6.35). However, the simplest guide is to use 1 g/kg desirable body weight for normal
adults. To add, another method of expressing protein intake is based on total caloric
requirement. ( Claudio,2010).

Example:

10 %of a 2, 200 kcalories need of an adult Filipina is equivalent to 50 kg protein that is;

( 220 kcal divided by 4 kcal/gram protein).

FACTORS THAT AFFECT PROTEIN REQUIREMENT

1. Body Size
As mentioned, protein needs to be based on the IBW (Ideal Body Weight) of a person on
a given height;and not on actual height. For adults the protein requirement per kg body
weight is considered to be the same for both sexes, at all ages, and for all body weights
within the acceptable range.
In accordance with WHO (2007) the accepted level of or safest level of intake is 0.83
g/kg per day. No safe upper limit has been identified. However, caution is advised to
those contemplating the very high intakes of 3-4 times the safe intake, since such
intakes cannot be assumed to be risk free.

Physical activity does not increase the protein requirements.

2. Effect of growth
Infants do need more protein intake per unit body weight than older children.
Infants require about 1.5-2.2 g protein/kg body weight;
Children need 1.6-2.0 g
Early adolescence about 1.5 g
Older teenagers about 1.25
Adults need 1.14g protein/kg desirable body weight.
3. Effect of pregnancy and lactation
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 Growing fetus and protein synthesis in a pregnant woman increases the factor of protein
requirement.
Philippine RENI suggests an 8g and 18-23g increase of protein intake for pregnancy and
lactation, during lactation as much as 15g protein is secreted daily in the breast milk.
4. Effect of aging
Total caloric requirement is lower and it is recommended that a higher proportion of
protein be supplemented to maintain the nitrogen balance. The Philippine RENI has not
been revised to allow for the effect of aging above 65 years old.
5. State healthy
Any condition that demands protein replacement in the body requires more dietary
protein. In given situations; fevers, burns,surgery, hyperthyroidism, convalescence and
wound healing.
6. Stress factors
Severe environmental conditions and psychological factors are factors other than
physiological and physiological stress factors.
The protein allowance for moderate and severe stress is 1.3-1.4g/kg body weight/day
and 1.5-2.0 g/kg body weight/day.
7. Effect of Physical activity
Exercise or physical activity does not require increased protein intake. Athletes need
more protein than the normal requirement is for the building period of their muscles.
8. Quality of Proteins
19
Proteins in animal foods are eight essential amino acids which are present in optimum
amounts higher than those from plant sources that are lower due to lack of lysine and
methionine, two of the essential amino acids.

20
 Figure 5. Amino Acid Requirement for Adults

Figure 5.1 Amino Acid Requirements of Infants, Children and Adolescents

20

Adequacy of calories
Calories from fats and carbohydrates must be supplied adequately to prevent protein foods
from being deaminized.

Planning the Diet to Meet the Protein Needs

To put it in a more relative way, “ Your Guide to Good Nutrition” and “Food Exchanges” is a
practical method of planning the daily intakes of adequate protein a person needs.

Figure 5.2 Sample Food groups and Recommended servings/day

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 CONCLUSION
Eating meals at a regular time is important. Eating with moderation, variety and
balance are the key words. Observing the nutrient content of the food is essential as well. In
eating it is important to observe the supplements and complementation of the protein content.
Mostly, be sure to consume safe food that can provide satiety.

22
References

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Journal of Family Medicine and Primary Care, 3(1), 63.

https://doi.org/10.4103/2249-4863.130279

Benjamin, O., & Lappin, S. L. (2022). Kwashiorkor. PubMed; StatPearls Publishing.

https://www.ncbi.nlm.nih.gov/books/NBK507876/#:~:text=Kwashiorkor%20is%20a%20disease%

20marked

Claudio, V. (1982). Basic nutrition for Filipinos. http://ci.nii.ac.jp/ncid/BA91288437

Fry, E. (2021). Best Plant Based Sources of Protein - Super Safeway. Super Safeway.

https://supersafeway.com/best-plant-based-sources-of-protein/

Hermann, J., Ph. D. ,. RD/LD. (2019, October). Protein and the Body. Oklahoma State

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Learning Chemistry. (2022). Protein. Learning Chemistry.

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LaPelusa, A. (2022, November 14). Physiology, Proteins. StatPearls - NCBI Bookshelf.

https://www.ncbi.nlm.nih.gov/books/NBK555990/

Protein-energy malnutrition | DermNet NZ. (n.d.). Dermnetnz.org.

https://dermnetnz.org/topics/protein-energy-malnutrition

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