PROTEINS 1.

Amino acids that are normally not essential but

NUTRITION: Ma’am Wynona become essential under certain clinical
OBJECTIVES: indications.
1. To be able to learn and understand the nature of 2. Amino acids that can lower the requirement for
protein an essential amino acid but cannot replace it
2. Categorize the different types of amino acids entirely.
3. See the digestion process and function of protein 3. Taurine, cysteine and tyrosine are essential for
in the body premature babies.
4. Learn the protein sources and health effects of 4. Cysteine and tyrosine, may become essential in
proteins some patients with cirrhosis of the liver.
5. To know the kinds of protein malnutrition 5. Glutamine – severe illness or after severe
6. To know and see the comparison of Kwashiorkor traumatic injury.
and Marasmus 6. Tyrosine, cysteine, glutamine, arginine and
7. Protein requirement and allowance glycine – do not appear to be synthesized at a rate
to meet cellular needs under certain physiologic
DEFINITION AND COMPOSITION: or pathologic conditions.
1. Protein comes from the Greek word “protelos” 7. Arginine – malnourished, septic, or recovering
meaning “of first importance” or “to take the first from injury or surgery
place” 8. Tyrosine – Essential in phenylketonuria (PKU)
2. Complex organic compounds containing carbon, because of genetic disorders or enzyme activity
hydrogen, oxygen and nitrogen arranged into or function.
amino acids linked in a chain by peptide bonds. 9. Arginine and glutamine – during cell
3. The presence of Nitrogen distinguishes protein proliferation and growth. They speed up wound
from carbohydrate and fat. 16% 1g N= 6.25g healing by increasing collagen deposition.
protein
4. A very large nutrient that’s made up of smaller NONESSENTIAL (DISPENSABLE) AMINO ACID:
substances called amino acids. There are 20 1. Amino acids that can be synthesized in the body
amino acids, but your body can only make 9 of from essential amino acid.
them. The other 11 are called essential amino 2. Not a dietary essential.
acids and you can only get them through your
diet. CLASSIFICATION OF AMINO ACIDS BASED ON
ESSENTIALITY:
STRUCTURE: INDISPENSABL CONDITIONALL DISPENSABL
1. The building blocks of proteins are called amino E Y E
acids and they serve as the “currency” of protein INDISPENSABLE
nutrition and metabolism.
Leucine Proline Glutamate
2. All amino acids have the same basic structure: a
central carbon atom to which a hydrogen, a basic Isoleucine Serine Alanine
or amino group (-NH2), an acid or carboxyl group
(-COOH), and a distinctive side group (or side Valine Arginine Aspartate
chain) are attached. Tryptophan Tyrosine Glutamine

CLASSIFICATIN OF AMINO ACIDS: Phenylalanine Cysteine

1. Essential (Indispensable) Amino Acids
Methionine Taurine
2. Semi-essential (Conditionally Indispensable)
Amino Acids Threonine Glycine
3. Nonessential (Dispensable) Amino Acids
Lysine
ESSENTIAL (INDISPENSABLE) AMINO ACIDS: Histidine
1. Amino acids that the human body cannot
synthesize at a rate sufficient to meet growth and
maintenance requirements. CLASSIFICATION OF PROTEINS:
2. Amino acids that results in nutritional or 1. ACCORDING TO METABOLIC
metabolic effects when omitted from the diet. PATHWAY
3. An obligatory dietary requirement exist for 1. Glucogenic Amino Acids – From pyruvate to
tryptophan, leucine, isoleucine, valine, intermediates of the Kreb Cycle which can be
phenylalanine, methionine, lysine, threonine and converted to glucose or glycogen.
histidine. 2. Ketogenic Amino Acids – Give rise to
AcetylCoA resulting in the formation of fate or
SEMI-ESSENTIAL (CONDITIONALLY ketone bodies.
INDISPENSABLE) AMNINO ACIDS: 3. ACCORDING TO CHEMICAL
STRUCTURE
1. Simple Proteins

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1. Yield only amino acids upon complete hydrolysis 2. As hormones, regulate blood glucose level, blood
2. Ex: Albumins, globulins, glutelins, prolamins, calcium level, metabolic rate, fluid and
gliadin, Keratin, collagen, elastin, zein, myosin electrolyte balance and promote growth.
and many others. 3. Transport protein carry nutrients to the
3. Compound or Conjugated Proteins tissues:
1. Simple proteins combined with non-protein. 1. Transferin – transport iron
Could properly perform by itself. 2. Albumin – transports fatty acids, bilirubin, and
2. Ex: Mucoproteins, glycoproteins, nucleoproteins, many drugs
lipoproteins, phosphoproteins, chromoproteins, 3. Hemoglobin – oxygen from lungs to the cells
flavoproteins, metalloproteins 4. Retinol – binding protein – Vitamin A through
3. Derived Proteins the plasma to the cells in the form of retinol
1. Substances resulting from the decomposition of 5. Ceruloplasmin – regulates the plasma copper
simple and combined proteins by the action of and prevents accumulation of toxic levels.
heat and other physical forces or hydrolytic 6. Plasma Proteins Perform Various Functions:
agents. 1. Gamma Globulin – Provides antibodies that
2. Ex: Peptones, proteoses and peptides which are maintain the body’s resistance
formed in the various stages of protein digestion. 2. Albumin – vital importance in the regulation of
3. ACCORDING TO CHEMICAL osmotic pressure and in the maintenance of fluid
COMPOSITION OF THEUR BRANCHED balance.
CHAIN 3. Fibrinogen – blood clotting metabolism
4. Branched AA 4. As Source of Energy and Glucose
1. Additional Amino Acid group ex: lysine, 1. Proteins provide 4kcal/g
arginine, histidine 2. Expensive and are not a recommended source of
2. Acidic AA energy
3. Contain additional carboxyl group Ex: aspartic 3. Glucogenic amino acids serve as a source of
acid, glutamic acid glucose
4. Neutral AA
5. Contain additional acidic or basic group
classified into aliphatic and aromatic or cyclic
amino acids. THE 9 ESSENTIAL AMINO ACIDS PERFROM A
6. ACCORDING TO AMINO ACID CONTENT NUMBER OF IMPORTANT AND VARIED JOBS IN
7. Complete Protein YOUR BODY:
8. Contains all the essential amino acids in 1. Phenylalanine – precursor for the
proportions capable of maintaining life and neurotransmitters tyrosine, dopamine,
supporting a normal rate of growth. epinephrine and norepinephrine. It plays an
9. High Biologic value protein integral role in the structure and functions of
10. All animal proteins except gelatin and complete proteins and enzymes and the production of other
proteins. amino acids.
11. Partially Complete Proteins 2. Valine – one of the three-branched chain amino
1. Contains all essential amino acids but a relatively acids, meaning, it has a chain branching off to one
small amount of one or more of the AA necessary side of its molecular structure. Valine helps
for growth. stimulate muscle growth and regeneration and is
2. Can maintainlife but cannot support a normal involved in energy production.
growth 3. Threonine – Principal part of the structural
3. Low biologic value protein proteins such as collagen and elastin, which are
4. Ex: Gliadin and Hordein important components of th skin and connective
5. Partially Complete Proteins (? Amo an tissue. It also plays a role in fat metabolism and
nakadto ha ppt HAHAHA) immune function.
1. Lack one or more of the essential AA’Low BV 4. Tryptophan – often associated with causing
protein drowsiness, it’s needed to maintain proper
2. Ex: Zein and Gelatin nitrogen balance and is a precursor to serotonin,
a neurotransmitter that regulates your appetite,
FUNCTIONS: sleep and mood.
3. As building materials for growth and repair 5. Methionine – important role in metabolism and
4. Furnish the amino acids require to build and detoxification. Necessary for tissue growth and
repair body tissues. the absorption of zinc and selenium, minerals that
5. Structural components of cells, enzymes, are vital to your health.
hormones, and various body fluids and 6. Leucine – like valine, leucine is a branched-chain
secretions. Tissue proteins comprise amino acid that is critical for protein synthesis
approximately 16% of the human body. and muscle repair. It also helps regulate blood
6. As regulators of body processes sugar levels, stimulates wound healing and
1. As enzymes catalyse chemical reactions and aid produces growth hormones.
in physiologic processes.

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7. Isoleucine – involved in muscle metabolism and pepsinog 9. Activates autocatalys
is heavily concentrated in muscle tissue. It’s also en pepsinog is.
important for immune function, haemoglobin en
production and energy regulation
10. Kills
8. Lysine – plays major roles in protein synthesis,
some
hormones and enzyme production and the
bacteria
absorption of calcium. It’s also important for
energy production, immune function and the 11. Helps in
production of collagen and elastin. the
9. Histidine – used to produce histamine, a absorptio
neurotransmitter that is vital to immune response, n of
digestion, sexual function and sleep-wake cycles. Vitamin
It’s critical for maintaining the myelin sheath, a B12
protective barrier that surrounds yiur nerve cells.
DIGESTION AND ABSORPTION OF PROTEINS:
DIGESTION AND ABSORPTION OF PROTEINS: 1. SMALL INTESTINE
1. Proteins are too large to be absorbed 1. Hydrolyse polypeptides into short peptide chains
2. The Dietary Proteins are hydrolysed to amino (tripeptides, dipeptides and amino acids.
acids by Proteolytic enzymes. 2. A few peptides escape digestion and enter the
3. Proteolytic enzymes - Responsible for degrading blood intact.
proteins are produced by three organs. The 3. The mixture of free amino acids and small
stomach, pancreas and small intestine. peptides is transported to mucosal cells by a
series of carrier systemns for amino acids,
tripeptides, dipeptides each specific for a limited
range of peptide substrate.

1. IN THE MOUTH:
1. Chewing and crushing breaks down into smaller
particles
2. Food particles are mixed with saliva before 4. Absorption of AAs takes place by Active
swallowing Transport mechanism (By Na+ dependent active
transport system).

1. IN THE STOMACH
1. HCl uncoils (denatures) the tangles strands off
protein and activates proteolytic enzymes which
attack the peptide bonds
2. HCl converts pepsinogen (inactive enzymes) to
pepsin (active enzymes)
3. Pepsin cleaves the large polypeptides of proteins
into smaller polypeptides and amino acids
4. FROM MOUTH TO STOMACH

1. In the mouth, chewing starts the mechanical

breakdown of protein
2. In the stomach, the chemical digestion of proteins
begins from hydrochloric acid (HCl) and the
enzyme pepsin
DIGESTION OF PROETIN BEGINS IN THE 3. In the small intestine, polypeptides are broken
STOMACH: down into amino acids, dipeptides and tripeptides
Stomach Hydrochloric Pepsinogen by protein digesting enzymes secreted from the
Secretes Acid (HCl) pancreas.
4. A variety of different transport proteins moves
5. Strong 7. Denature 12. Secreted by the products from protein digestion into the
Acid s proteins Chief cells. mucosal cell. Some amino acids share the same
(HCl) Activated transport system.
8. Decrease
to pepsin 5. Dipeptides and tripeptides can enter the mucosal
6. Proenzym pH (2-3)
by HCl. cell. Once inside, they are broken down into
e-
And single amino acids.

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6. Amino acids pass from the mucosal cell into the 3. Reduces production of antibodies
blood and travel to the liver. The liver regulate the 4. Protein Energy Malnutrition (PEM)
distribution of amino acids to the rest of the body. 1. Class of clinical disorders from varying
7. Small amounts of dietary protein in lost in the combinations and degrees of protein and
feces. energy deficiency
2. Common among infants and young children (1-3
PROTEIN RECOMMENDED INTAKE: years old)
1. 10-15% of the energy value, seldom 20% 3. Infection accompanied by other nutritional
2. Food protein is the only source of essential amino deficiencies such as severe Vitamin A
acids and it is the only practical source of N deficiency
3. The DRI (Dietary Reference Intake) is 0.8g 4. Serious from: Kwashiorkor and Marasmus
grams of protein per kilogram of body weight, or MARASMUS:
0.35 grams per pound. 1. Greek word “Dying away” which looks
This amounts to: like “little old people”
56 grams per day for the average sedentary man
2. Predominantly Calorie Deficiency
46 grams per day for the average sedentary
woman 3. Characterized by stunted growth, muscle
wasting,
FOOD SOURCES:
1. All foods of animal origin (meat, fish, poultry, 4. Absence of subcutaneous fat.
egg, seafood, milk and dairy products) 5. Occurs mostly in Children 6-18 months.
2. Plant food – legumes, nuts, seeds, cereals, grains,
fruits, vegetables and processed vegetables KWASHIORKOR:
proteins (tofu, vegemeats and others) 6. Acute PEM due to inadequate protein
intake
ACTION STEPS FOR MONITORING PROTEIN IN 7. Appears in infants and young children in
YOR DIET the late breastfeeding and post-weaning
1. Choose a variety of nutrient-dense protein foods, phases
such as beans and peas, eggs, fat-free (skim) or 8. Characterized by hypoalbuminemia and
low-fat (1%) dairy products, lean meats and enlarges fatty liver “pot belly”
poultry, seafood, soy products and unsalted nuts 9. Subcutaneous fat is usually preserved,
and seeds. but muscle wasting is often masked by
2. Choose seafood and plant sources of protein edema.
(such as beans and peas, soy products and
unsalted nuts and seeds) in place of some meats MARASMIC KWASHIORKOR:
and poultry. 1. Deficiency of both protein and energy
3. Substitute fat-free (skim) or low-fat (1%) dairy 2. Characterized by the edema of Kwashiorkor with
products (such as cheese, milk and yogurt) or the wasting of marasmus.
fortified soy beverages for regular/full-fat Researchers believe that Kwashiorkor and marasmus
(whole) dairy products. are two stages of the same disease.
4. Select fresh meats, poultry and seafood rather
than processed varieties.
5. Trim or drain fat from meats before or after
cooking and remove poultry skin before cooking
or eating.
6. Try baking, broiling, grilling or steaming. These
cooking methods do not add extra fat.

PROTEIN NUTRITURE:
1. Protein Excess
1. Among young infants – elevation of BUN and
Creatinine and may lead to metabolic COMPLIMENTARY PROTEINS:
acidosis 1. Two or more dietary proteins whose amino acid
2. Excess amino acids are not stored. patterns compliments each other in such a ways
3. Protein Deficiency that the essential amino acids missing in one are
1. Accompanies a deficiency of calories and other supplied by the other.
nutrients. Wasting of muscles tissue and loss Type of food Tends to be low Combine with
of weight. in
2. Anemia, delayed healing of wounds and
Legumes (except Methionine Grains, nuts, seeds
fractures, edema, fatty liver, dermatitis,
soy)
weakness and loss of vigor

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 Grains (except Lysine, threonine legumes
quinoa)
Nuts/seeds lysine legumes
corn Tryptophan, legumes
lysine
VEGETARIANISM:
2. Defined as the abstinence from animal products
3. Eat only plant foods. Makes diet planning
essential to ensure adequate intakes of calories,
Vit B12, Vitamin D, Iron and Calcium

Types of Vegetarians:
1. Lacto-ovo vegetarian – eats egg and dairy
2. Lacto-vegetarian – east dairy products but not
eggs
3. Ovo-vegetarian – eats eggs but not dairy
products
4. Vegan – do not eat dairy, eggs or any type of
animal product or by-product

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