SIR M.

RAMISH ANSARI
ST
BS POULTRY SCIENCE, 1 YEAR

LIPIDS:
Lipids are a diverse group of organic compounds that are hydrophobic or insoluble in water. They
are primarily composed of carbon (C), hydrogen (H), and oxygen (O) atoms. Lipids play crucial
roles in biological systems. The lipids are a group of substances found in plant and animal tissues.
They are insoluble in water but soluble in common organic solvents such as benzene, ether and
chloroform. They act as electron carriers, as substrate carriers in enzymatic reactions, as
components of biological membranes and as sources and stores of energy. Lipids are made up of a
glycerol molecule attached to three fatty acid molecules. Such a lipid is called triglyceride.

In animals, lipids are the major form of energy storage, mainly as fat, which may constitute up to 97
per cent of the adipose tissue of obese animals. The yield of energy from the complete oxidation of
fat is about 39 MJ/kg DM, compared with about 17 MJ/kg DM from glycogen the major
carbohydrate form of stored energy. In addition, stored fat is almost anhydrous, whereas stored
glycogen is highly hydrated. Weight for weight, fat is, therefore, about six times as effective as
glycogen as a stored energy source. The structural lipids of animal tissues, mainly
Phosphoglycerides, constitute between 5 and 10 g/kg of muscle and adipose tissue; the
concentration in the liver is usually between 20 and 30 g/kg. The most important non-glycerides,
neutral lipid fraction of animal tissue, is made up of cholesterol and its esters, which together make
up 0.6 to 0.9 g/kg of muscle and adipose tissue.

Key Characteristics of Lipids:

 Hydrophobic Nature: Lipids do not mix well with water, which allows
them to form membranes and store energy efficiently.
 Energy Storage: They are a major source of energy, providing more
than double the energy per gram compared to carbohydrates and
proteins.
 Structural Components: Lipids, especially phospholipids and
cholesterol, are essential components of cell membranes, contributing
to membrane fluidity and integrity.
 Biological Signaling: Many lipids serve as signaling molecules,
influencing various physiological processes (e.g., hormones,
eicosanoids).
 Insulation and Protection: Lipids provide insulation against heat loss
and protect vital organs in animals.
FUNCTIONS OF LIPIDS:

1. Energy Storage:
o Store energy efficiently as triglycerides, providing more energy per gram than
carbohydrates.

2. Structural Components:
o Form cell membranes (phospholipids and cholesterol) that regulate what enters and
exits the cell.

3. Insulation and Protection:

o Provide thermal insulation and cushion vital organs from injury.

4. Signaling Molecules:
o Act as hormones (e.g., steroids) and signaling molecules (eicosanoids) involved in
various physiological processes.

5. Transport of Nutrients:
o Aid in the absorption and transport of fat-soluble vitamins (A, D, E, K).

6. Cell Signaling:
o Participate in cell communication and signaling pathways.

7. Flavor and Aroma:

o Enhance taste and aroma in foods.

8. Essential Fatty Acids:

o Provide essential fatty acids necessary for health, such as omega-3 and omega-6.
CLASSIFICATION OF LIPIDS:
Glycerol-Based Lipids
Definition: These lipids contain a glycerol backbone, to which fatty acids or other groups are
attached. They are the most common type of lipids in animal and plant tissues.

1. SIMPLE LIPIDS:

FATS:

 Definition: Fats are lipids that are generally solid at room temperature due to their
structure. They are typically derived from animal sources, although some plant fats (like
coconut and palm oils) are also solid.
 Sources:
o Animal sources: butter, lard, beef tallow, and dairy products.
o Plant sources: coconut oil, palm oil, and cocoa butter.
 Functions:
o Energy Storage: Fats are a dense energy source, providing 9 calories per gram.
They are stored in adipose tissue and used as a reserve energy source.
o Insulation and Protection: Fats help insulate the body against temperature
changes and cushion vital organs.
o Nutrient Absorption: Fats aid in the absorption of fat-soluble vitamins (A, D, E, and
K) and provide essential fatty acids necessary for various bodily functions.
 Health Impacts:
o Diets high in saturated fats can raise LDL (low-density lipoprotein) cholesterol
levels, potentially increasing the risk of cardiovascular disease.
o However, saturated fats are also essential in moderate amounts, supporting
hormone production and cellular structure.

OILS:

 Definition: Oils are lipids that are generally liquid at room temperature. They are primarily
derived from plant sources but can also come from certain fish and other marine animals.
 Sources:
o Plant sources: olive oil, canola oil, sunflower oil, soybean oil, and flaxseed oil.
o Marine sources: fish oil, cod liver oil, and krill oil.
 Functions:
o Heart Health: Unsaturated fats, particularly monounsaturated and polyunsaturated
fats, have been associated with improved cardiovascular health. They can help
reduce LDL cholesterol levels and increase HDL (high-density lipoprotein)
cholesterol levels.
o Anti-Inflammatory Properties: Omega-3 fatty acids, a type of polyunsaturated fat
found in oils like flaxseed and fish oil, have anti-inflammatory effects and are
beneficial for brain health, joint health, and immune function.
o Essential Fatty Acids: Oils provide essential fatty acids (omega-3 and omega-6),
which the body cannot produce but requires for functions like cell membrane
formation and hormone production.
  Health Impacts:
o Oils rich in omega-3 and omega-6 fatty acids support brain and heart health and
may help lower the risk of chronic diseases.
o However, an imbalance in omega-6 to omega-3 intake can promote inflammation, so
balanced consumption is key.
o While healthier than saturated fats, oils are also calorie-dense, so portion control is
essential.

TRIGLYCERIDES:
Triglycerides (also known as triacylglycerols) are the most common type of lipid found
in the body and in food. They serve as a primary form of energy storage in animals and
plants and are also crucial for insulation and protection.

Structure of Triglycerides: Triglycerides consist of three fatty acid molecules attached to a

glycerol molecule (a three-carbon alcohol). The fatty acids are linked to the glycerol backbone by
ester bonds, formed through a dehydration synthesis reaction where water is released.

FATTY ACIDS:

Fatty acids are carboxylic acids with long hydrocarbon chains that can be saturated or
unsaturated. They are fundamental components of lipids, especially triglycerides and
phospholipids, and play diverse roles in energy storage, cellular structure, and various
physiological processes.

Types of Fatty Acids

Based on the presence or absence of double bonds in their hydrocarbon chains, fatty acids
are classified as either saturated or unsaturated.

1. Saturated Fatty Acids:

o Definition: Saturated fatty acids have no double bonds between the carbon atoms
in the hydrocarbon chain, meaning each carbon is “saturated” with hydrogen atoms.
o Sources: Commonly found in animal fats (butter, lard) and tropical oils (coconut oil,
palm oil).
 o Examples: Palmitic acid, stearic acid, arachidic acid, capric, caproic, caprylic acid
and butyric acid.
o Health Effects: High intake of saturated fatty acids is associated with elevated LDL
(bad) cholesterol levels, which may increase the risk of heart disease.

2. Unsaturated Fatty Acids:

o Definition: Unsaturated fatty acids have one or more double bonds between
carbon atoms in the hydrocarbon chain. These double bonds cause bends or
"kinks" in the structure, preventing tight packing and resulting in a liquid
form at room temperature.
o Types:
 Monounsaturated Fatty Acids (MUFA): Contain only one double bond.
 Polyunsaturated Fatty Acids (PUFA): Contain two or more double bonds.

Sources:

 MUFA: Olive oil, avocados, nuts, seeds, canola oil.

 PUFA: Fatty fish (salmon, mackerel), flaxseeds, chia seeds, walnuts, vegetable oils
(sunflower, safflower).

Health Benefits:

 Heart health: Lowers bad cholesterol (LDL) and reduces the risk of heart disease.
 Brain function: Omega-3s (DHA, EPA) improve cognitive health.
 Anti-inflammatory: Reduces inflammation, helping with conditions like arthritis.
 Mental health: May ease symptoms of depression and anxiety.
 Skin health: Improves skin barrier and reduces dryness.

Examples: Palmitoleic, oleic, linoleic, linolenic, archidinoic acid

3. Essential Fatty Acids (EFAs)

 Definition: These are fatty acids that the body cannot synthesize on its own and
must be obtained from the diet. They are crucial for various physiological functions,
including cell membrane integrity, brain function, and inflammatory response.
 Types:
o Omega-3 Fatty Acids: These have a double bond three carbons from the end
(omega) of the carbon chain. Important omega-3 fatty acids include:
 Alpha-Linolenic Acid (ALA): Found in plant oils like flaxseed, chia seeds,
and walnuts.
 Eicosapentaenoic Acid (EPA) and Docosahexaenoic Acid (DHA): Found
in marine sources, such as fish oil and algae. EPA and DHA are derived from
ALA and are essential for cardiovascular and brain health.
o Omega-6 Fatty Acids: These have a double bond six carbons from the omega end.
Important omega-6 fatty acids include:
 Linoleic Acid (LA): Found in vegetable oils (such as sunflower, safflower,
and soybean oils), nuts, and seeds. It can be converted into arachidonic acid
(AA), which is involved in inflammation and immune responses.
 Arachidonic Acid (AA): An omega-6 fatty acid derived from LA. It is also
found in animal products and is essential for cellular signaling and
inflammatory respons
4. Non-Essential Fatty Acids

 Definition: These are fatty acids that the body can synthesize from other fats or
dietary sources. Although they are not required from the diet, they still perform
essential functions within the body.
 Types:
o Saturated Fatty Acids: These fatty acids have no double bonds between carbon
atoms, allowing them to be fully “saturated” with hydrogen atoms. They are
generally solid at room temperature. Examples include:
 Palmitic Acid: Commonly found in palm oil, animal fats, and dairy products.
 Stearic Acid: Found in animal fats, cocoa butter, and certain plant oils.
o Monounsaturated Fatty Acids (MUFAs): These fatty acids have one double bond,
making them more flexible. They are typically liquid at room temperature. Examples
include:
 Oleic Acid: Found in olive oil, canola oil, and avocados.
o Certain Polyunsaturated Fatty Acids (PUFAs): While most polyunsaturated fatty
acids are essential, some can be synthesized by the body, such as:
 Gamma-Linolenic Acid (GLA): Although not essential, it can be derived
from linoleic acid and is found in borage oil and evening primrose oil.
2. COMPOUND LIPIDS:

GLYCOLIPIDS:

 Definition: Glycolipids are lipids with one or more carbohydrate groups attached.
They play key roles in cell recognition, signaling, and membrane stability.

Types:

1. Glucolipids: These glycolipids contain glucose as the carbohydrate component. They are
found in various cell membranes and play a role in cellular communication and signaling.

2. Galactolipids: These glycolipids contain galactose as the carbohydrate component. They are
particularly abundant in plant cells, especially in chloroplast membranes, where they play a role in
photosynthesis.

 Functions:
o Cell Recognition: Glycolipids on the cell surface act as recognition sites for
interactions with other cells or molecules, important for immune response and
tissue formation.
o Stability of Cell Membranes: They contribute to the stability and structure of cell
membranes, helping to maintain the membrane's integrity.
o Signal Transduction: Glycolipids participate in cell signaling processes, such as
those involved in the immune response and cell differentiation.

PHOSPHOGLYCERIDES: (Phospholipids)

 Definition: Phosphoglycerides, a type of phospholipid, are compound lipids

containing a phosphate group. They are major components of cell membranes and
are involved in forming lipid bilayers that enclose cells.

Types:

1. Lecithin (Phosphatidylcholine): Contains a choline group attached to the phosphate

group. Found in high amounts in egg yolks, soybeans, and other foods. Lecithin Plays a crucial role
in cell membrane integrity, lipid metabolism, and as a precursor for acetylcholine (a
neurotransmitter).

2. Cephalin (Phosphatidylethanolamine): Contains an ethanolamine group attached

to the phosphate group. Commonly found in brain and nerve tissues. Cephalin Involved in cell
membrane formation, blood clotting, and cellular signaling.

 Functions:
 o Membrane Structure: Phosphoglycerides are fundamental components of cell
membranes, forming lipid bilayers that provide structural integrity and create a
semi-permeable barrier.
o Facilitating Transport: The amphipathic nature (having both hydrophobic and
hydrophilic regions) of phospholipids allows them to form membranes that regulate
the movement of substances in and out of cells.
o Cell Signaling: Phosphoglycerides are involved in signaling pathways. For example,
phosphatidylinositol is a phosphoglyceride involved in intracellular signaling.
o Lipid Metabolism: Lecithin and cephalin participate in lipid metabolism, playing
roles in the transport and breakdown of fats within the body.

NON GLYCEROL BASED LIPIDS:

Non-glycerol-based lipids are lipids that do not contain glycerol as a backbone. Instead,
they have other structural components, such as sphingosine, long-chain alcohols, or
complex ring structures. These lipids play critical roles in cell membranes, signaling, and
various biological processes. Here’s a breakdown of some major types:

1. Sphingolipids

 Sphingomyelins:
o Function: Found in the myelin sheath surrounding nerve cells,
sphingomyelins play a role in nerve cell insulation and signal transmission.
o Location: Predominantly in the nervous system, especially in the
membranes of nerve cells (neurons).
 Cerebrosides:
o Function: Important in the structure of brain cell membranes, cerebrosides
contribute to cell recognition and signaling.
 o Location: Found in high concentrations in the brain and nervous tissues,
particularly in the myelin sheath.

2. Waxes

 Function: Waxes provide waterproofing and protection. In animals, they are found
on skin, feathers, and fur to repel water. In plants, they coat leaves to prevent water
loss and protect against environmental damage.
 Examples: Beeswax, lanolin (from wool), and cuticle waxes on plant leaves.

3. Steroids

 Types and Functions:

o Cholesterol: Essential for cell membrane structure, providing fluidity and
stability. It also serves as a precursor for steroid hormones, bile acids, and
vitamin D.
o Steroid Hormones: Includes sex hormones (e.g., estrogen, testosterone) and
corticosteroids (e.g., cortisol), which regulate various physiological processes
like metabolism, immune response, and reproduction.
o Bile Acids: Derived from cholesterol, they aid in the digestion and
absorption of dietary fats in the intestine.

4. Terpenes

 Function: Terpenes are involved in a variety of biological functions and are also
important as natural flavors, scents, and colors in plants. They can have antioxidant,
anti-inflammatory, and antimicrobial properties.
 Examples:
o Carotenoids: Pigments found in plants that have antioxidant properties and
are important for vision (precursors of vitamin A).
o Menthol: A monoterpene that provides the characteristic scent and cooling
effect of mint.

5. Eicosanoids

 Types and Functions:

o Prostaglandins: Involved in regulating inflammation, pain, and fever. They
also play roles in blood flow, blood clotting, and reproductive processes.
o Thromboxanes: Aid in blood clot formation and vascular constriction, which
is important for wound healing and controlling blood flow.
o Leukotrienes: Contribute to immune responses, especially in allergic and
inflammatory reactions.
 Roles: Eicosanoids act as signaling molecules, regulating inflammation, immune
response, and other cellular functions. They are typically produced on-demand and
have short half-lives, acting locally near their site of production.
BETA OXIDATION OF FATTY ACIDS:
DEFINITION:
Beta oxidation is a catabolic process by which fatty acid molecules are broken down in the
mitochondria (or peroxisomes) to generate acetyl-CoA, the key building block used in the citric
acid cycle (Krebs cycle) to produce energy in the form of adenosine triphosphate (ATP). Fatty
acids, particularly those stored as triglycerides in the body, serve as a significant energy source,
especially during periods of fasting, intense physical activity, or prolonged low carbohydrate intake.
The "beta" in beta oxidation refers to the beta carbon, which is the second carbon atom from the
carboxyl group of a fatty acid. The breakdown occurs through successive removal of two-carbon
fragments, a process highly efficient in generating ATP, making beta oxidation a central mechanism
in energy metabolism.

Where Does Beta Oxidation Occur?

Beta oxidation occurs in two main cellular organelles depending on the type of fatty acid being
oxidized: the mitochondria and the peroxisomes. For most fatty acids, particularly short- and
medium-chain fatty acids, beta oxidation takes place in the mitochondria, the powerhouse of the
cell, where the acetyl-CoA generated can directly feed into the citric acid cycle for further oxidation
and ATP production. However, for very long-chain fatty acids (those with more than 22 carbons),
the process begins in peroxisomes. These organelles are specialized to handle longer-chain fatty
acids that are too large to be processed by mitochondrial enzymes. Once partially oxidized, the
shorter fatty acid chains are transferred to the mitochondria for complete oxidation. This
compartmentalization is essential for managing the different physical and chemical properties of
fatty acids of varying chain lengths.

Steps of Beta Oxidation:

The process of beta oxidation involves a series of enzymatic steps that break down fatty acids two
carbons at a time, producing acetyl-CoA, NADH, and FADH₂.

Beta oxidation consists of four main steps:

1. Dehydrogenation – In this step, acyl CoA is oxidized by the enzyme acyl CoA
dehydrogenase, which catalyzes the removal of two hydrogens between carbons 2 and 3
(C2 and C3), forming a double bond between the alpha and beta carbons in the fatty acyl-
CoA molecule. The end product of this reaction is trans-delta 2-enoyl CoA.

2. Hydration – In this step, the double bond between C2 and C3 of trans-delta 2-enoyl CoA is
hydrated in a reaction catalyzed by the enzyme enoyl CoA hydratase. The addition of water
(H2O) results in the formation of L-β-hydroxyacyl CoA, which has a hydroxyl group (-OH)
in C2, in place of the double bond.

3. Oxidation – The third step involves another dehydration reaction, which is similar to that
in the first step but occurs at a different position on the fatty acyl-CoA molecule. During this
reaction, 2 hydrogen atoms are removed from the beta carbon, which now contains a
hydroxyl group from Step 2. This reaction is catalyzed by the enzyme 3-hydroxyacyl-
CoA dehydrogenase, which generates NADH+ H and beta-ketoacyl CoA.

4. Thiolysis – In this final step, the enzyme thiolase cleaves the terminal acetyl-CoA group
(between the alpha and beta carbons), resulting in the formation of a new acyl-CoA, which is
shortened by 2 carbon atoms. The shortened acyl-CoA chain can re-enter the beta-oxidation
cycle, repeating the series of reactions until the entire fatty acid has been broken down into
acetyl-CoA molecules. Acetyl-CoA molecules enter the citric acid cycle to generate ATP.

End Products

 1 Acetyl-CoA: Enters the citric acid cycle for further energy production.
 1 FADH₂: Contributes to the electron transport chain to produce ATP.
 1 NADH: Also contributes to the electron transport chain.
2. Energy Yield

3. Total ATP Yield

 Total ATP produced from one molecule of palmitic acid is approximately:

o 108 ATP (10.5 + 17.5 + 80)
STORAGE OF FAT:
The storage of fat in the body primarily occurs in the form of triglycerides within
specialized cells called adipocytes, or fat cells. When we consume dietary fats, they are
broken down into fatty acids and glycerol during digestion. These components can then be
reassembled into triglycerides, which are stored in adipose tissue. There are two main
types of adipose tissue: white adipose tissue (WAT) and brown adipose tissue (BAT). WAT
serves as the primary storage site for triglycerides, providing a concentrated energy
reserve and insulation for the body. In contrast, BAT is involved in thermogenesis and is
found mainly in infants and in smaller amounts in adults. The process of storing fat, known
as lipogenesis, occurs when excess nutrients, such as glucose and fatty acids, are converted
into triglycerides, regulated by hormones like insulin. When the body needs energy,
triglycerides can be broken down through lipolysis, releasing glycerol and free fatty acids.
This process is stimulated by hormones like glucagon and epinephrine. Overall, fat storage
plays a critical role in energy regulation, serving as a highly efficient energy reserve while
also providing insulation and protecting vital organs, as well as secreting hormones that
help regulate appetite and metabolism.
PROTEIN:
What is Protein?
Proteins are very large molecules composed of basic units called amino acids. Proteins
contain carbon, hydrogen, oxygen, nitrogen, and sulphur.

Protein molecules are large, complex molecules formed by one or more twisted and folded
strands of amino acids. Proteins are highly complex molecules that are actively involved in
the most basic and important aspects of life. These include metabolism, movement,
defense, cellular communication, and molecular recognition.

Proteins are complex organic compounds of high molecular weight and consist of long chains of
amino acids. In common with carbohydrates and fats, they contain carbon, hydrogen and oxygen,
but in addition they all contain nitrogen and sometimes sulphur. Proteins are found in all living
cells, where they are intimately connected with all phases of activity that constitute the life of the
cell. Each species has its own specific proteins, and a single organism has many different proteins in
its cells and tissues. It follows, therefore, that a large number of proteins occur in nature.

What is an Amino acid?

“Amino Acids are the organic compounds that combine to form proteins, hence they are referred
to as the building components of proteins. These biomolecules are involved in several biological
and chemical functions in the human body and are the necessary ingredients for the growth and
development of human beings. There are about 300 amino acids that occur in nature.”

There are 20 naturally occurring amino acids and all have common structural features – an
amino group (-NH3+), a carboxylate (-COO-) group and a hydrogen-bonded to the same
carbon atom. They differ from each other in their side-chain called the R group. Each amino
acid has 4 different groups attached to α- carbon.

These 4 groups are:

 Amino group,
 COOH,
 Hydrogen atom,
 Sidechain (R).

The general structure of Amino acids is H2NCH RCOOH,

and it can be written as:
CLASSIFICATION OF PROTEINS:
Proteins are classified into three main types based on their composition and what they yield
when broken down (hydrolysis): simple proteins, conjugated proteins, and derived proteins.

1. Simple Proteins

Simple proteins are proteins that, when hydrolyzed, yield only amino acids. They do not contain
any non-protein components. Some key examples include:

 Albumin and Globulins: Found in milk and eggs, these proteins are highly nutritious. In
blood, albumin and globulins are two of the main plasma proteins.
 Histones: Basic proteins that are rich in the amino acid histidine. Histones are found in
association with nucleic acids in chromosomes and in the globin part of hemoglobin.
 Scleroproteins: These are the most resistant proteins, forming protective and supportive
structures in the body. Examples include:
o Collagen: Found in tendons, cartilage, bones, and connective tissues.
o Elastin: Present in elastic fibers in the lungs and large arteries.
o Reticulin: Found in reticular connective tissues of the liver, spleen, and kidney.
o Keratin: Found in hair, nails, and skin.

2. Conjugated Proteins

Conjugated proteins yield amino acids and a non-protein part, known as the prosthetic group,
when hydrolyzed. Examples include:
  Phosphoproteins: Proteins that are combined with phosphoric acid. An example is
caseinogen found in milk.
 Glycoproteins: Proteins combined with carbohydrates (mucopolysaccharides). They
occur in mucous secretions, cartilage, bone, and connective tissues. Examples include
chondroitin sulfate, mucoitin sulfate, and heparin.
 Chromoproteins: These contain a pigment as the prosthetic group. For example,
hemoglobin in blood and myoglobin in muscles are composed of a protein part (globin)
and a non-protein part (heme).
 Lipoproteins: Proteins combined with lipids. Plasma lipoproteins help transport lipids in
the bloodstream.
 Nucleoproteins: Composed of basic proteins, like histones, and nucleic acids (DNA),
they are found in chromosomes.

3. Derived Proteins

Derived proteins are products that result from the breakdown or decomposition of proteins. They
are formed from the chemical or enzymatic modification of simple or conjugated proteins.

Classification of amino acids on the basis of

nutrition

 Essential amino acids (Nine)

Nine amino acids cannot be synthesized in the

body and, therefore, must be present in the diet
in order for protein synthesis to occur. These
essential amino acids are histidine, isoleucine,
leucine, lysine, methionine, phenylalanine,
threonine, tryptophan, and valine.

 Non-essential amino acids (Eleven)

These amino acids can be synthesized in the

body itself and hence do not necessarily need
to be acquired through diet. These non-
essential amino acids are Arginine, glutamine,
tyrosine, cysteine, glycine, proline, serine,
ornithine, alanine, asparagine, and aspartate.
Classification of amino acids on the basis of
Structure (Side Chain Nature)
Amino acids can be classified based on the chemical properties of their side chains (R groups),
which determine their behavior and function.

a. Nonpolar (Hydrophobic) Amino Acids

These amino acids have side chains that are hydrophobic (repel water) and are usually
found in the interior of proteins. Examples include:

 Glycine
 Alanine
 Valine
 Leucine
 Isoleucine
 Methionine
 Proline
 Phenylalanine
 Tryptophan

b. Polar (Hydrophilic) Amino Acids

These have side chains that are hydrophilic (attract water) and are often found on the
exterior of proteins, interacting with water. Examples include:

 Serine
 Threonine
 Cysteine
 Tyrosine
 Asparagine
 Glutamine

c. Acidic Amino Acids

These amino acids have side chains that contain carboxyl groups (-COOH), making them
negatively charged at physiological pH. Examples include:

 Aspartic acid
 Glutamic acid

d. Basic Amino Acids

These have side chains that contain amino groups (-NH2), making them positively charged
at physiological pH. Examples include:
  Lysine
 Arginine
 Histidine

Classification of amino acids Based on Metabolic Fate

Amino acids can be classified based on how they are metabolized in the body.

a. Glucogenic Amino Acids

These amino acids are broken down into compounds that can be used to produce glucose
(through gluconeogenesis). Examples include:

 Alanine
 Arginine
 Asparagine
 Aspartic acid
 Cysteine

b. Ketogenic Amino Acids

These amino acids are broken down into ketone bodies, which can be used for energy.
Examples include:

 Leucine
 Lysine

c. Both Glucogenic and Ketogenic Amino Acids

Some amino acids can be metabolized into both glucose and ketone bodies. Examples
include:

 Isoleucine
 Phenylalanine
 Tyrosine
 Tryptophan

Classification of amino acids on the basis on Polarity

Amino acids can also be classified based on the polarity of their side chains:

 Nonpolar Amino Acids: Hydrophobic, usually found inside proteins.

 Polar Amino Acids: Hydrophilic, usually found on protein surfaces interacting with the
environment.
 Functions of Amino acids
1. In particular, 20 very important amino acids are crucial for life as they contain peptides
and proteins and are known to be the building blocks for all living things.
2. The linear sequence of amino acid residues in a polypeptide chain determines the three-
dimensional configuration of a protein, and the structure of a protein determines its
function.
3. Amino acids are imperative for sustaining the health of the human body. They largely
promote the:
Production of hormones
• Structure of muscles
• Human nervous system’s healthy functioning
• The health of vital organs
• Normal cellular structure
4. The amino acids are used by various tissues to synthesize proteins and to produce
nitrogen-containing compounds (e.g., purines, heme, creatine, epinephrine), or they are
oxidized to produce energy.
5. The breakdown of both dietary and tissue proteins yields nitrogen-containing substrates
and carbon skeletons.
6. The nitrogen-containing substrates are used in the biosynthesis of purines, pyrimidines,
neurotransmitters, hormones, porphyrins, and nonessential amino acids.
7. The carbon skeletons are used as a fuel source in the citric acid cycle, used for
gluconeogenesis, or used in fatty acid synthesis.

General properties of Amino acids:

 They have a very high melting and boiling point.
 Amino acids are white crystalline solid substances.
 In taste, few Amino acids are sweet, tasteless, and bitter.
 Most of the amino acids are soluble in water and are insoluble in
organic solvents.

Deficiency of Amino acids

As mentioned above, amino acids are the building blocks of proteins and proteins play a
fundamental role in almost all life processes. Therefore, it is necessary to include all nine
essential amino acids in our daily diet to maintain a healthy and proper function of our
body. The deficiency of amino acids may include different pathological disorders, including:
Edema, Anemia, Insomnia, Diarrhea, Depression, Hypoglycemia, Loss of Appetite, Fat
deposit in the liver, Skin and hair related problems, Headache, Weakness, Irritability, and
Fatigue.
NAMES OF 20 DIFFERENT AMINO ACIDS:
STRUCTURES OF PROTEIN:
For convenience, the structure of proteins can be considered under four basic headings

Primary structure:

The primary structure of a protein is its unique sequence of amino acids, linked by peptide
bonds to form a polypeptide chain. This sequence is essentially the blueprint that dictates all
subsequent levels of the protein's structure. Even a small change in this sequence, such as the
replacement of one amino acid with another, can dramatically alter the protein's shape and
function. A well-known example is sickle cell anemia, which arises from a single amino acid
substitution in the hemoglobin protein. The primary structure, therefore, holds the key to the
protein’s identity and its biological role.

Secondary Structure

The secondary structure refers to local folding patterns within the polypeptide chain, stabilized
by hydrogen bonds between the backbone atoms of the amino acids. The two most common
forms of secondary structures are the alpha helix and the beta-pleated sheet. In an alpha helix,
the polypeptide chain coils into a spiral, stabilized by hydrogen bonds every fourth amino acid.
In contrast, beta-pleated sheets form when strands of the polypeptide lie side by side, held
together by hydrogen bonds. These structures are crucial for providing stability and flexibility,
serving as the building blocks for more complex folding.

Tertiary Structure

The tertiary structure represents the three-dimensional shape of a single polypeptide chain. It
arises from various interactions between the side chains (R-groups) of amino acids, including
hydrogen bonds, hydrophobic interactions, ionic bonds, and disulfide bridges. The tertiary
structure is crucial for a protein’s functionality, as it determines the protein’s overall shape and
the positioning of key functional areas, such as enzyme active sites or receptor binding sites.
Proper folding at this level is essential for the protein’s activity, and misfolding can lead to loss
of function or diseases like Alzheimer's, which is associated with protein misfolding.

Quaternary Structure

The quaternary structure applies to proteins that consist of more than one polypeptide chain,
known as subunits. These subunits are arranged in a specific manner to form a functional protein
complex. The interactions between the subunits are similar to those found in tertiary structures,
involving hydrogen bonds, ionic bonds, and other forces. The quaternary structure is essential for
the activity of many complex proteins. For example, hemoglobin, the oxygen-carrying protein in
red blood cells, is made up of four subunits, and its function depends on the precise arrangement
and interaction of these subunits.
CLASSIFICATION OF PROTEIN:
Proteins are essential biological molecules, and they can be classified into two main groups:
simple proteins and conjugated proteins.

1. Simple Proteins

Simple proteins are those that yield only amino acids upon hydrolysis. They are further
subdivided into two groups based on their shape, solubility, and chemical composition: fibrous
proteins and globular proteins.

 Fibrous Proteins

Fibrous proteins are typically structural proteins that play critical roles in animal cells and
tissues. These proteins are insoluble in water and resistant to digestion by enzymes. They consist
of long, filamentous chains held together by cross-linkages. Some key examples of fibrous
proteins include:

 Collagens: These are the main proteins in connective tissues, making up around 30% of
the total protein in mammals. Collagen is rich in the amino acid hydroxyproline, which
requires vitamin C for its production. A deficiency in vitamin C weakens collagen fibers,
leading to gum and skin issues. Collagens lack the essential amino acid tryptophan.
 Elastin: Found in elastic tissues like tendons and arteries, elastin is composed of flexible
polypeptide chains rich in alanine and glycine. Cross-links between lysine side chains
give elastin its ability to stretch and return to its original form.
 Keratins: Keratins are divided into two types: α-keratins, found in hair and wool, and β-
keratins, found in feathers, beaks, and scales of birds and reptiles. They are rich in
cysteine, a sulfur-containing amino acid.

 Globular Proteins

Globular proteins have compact, folded polypeptide chains. This group includes enzymes,
antigens, and protein-based hormones. Important types of globular proteins include:

 Albumins: Water-soluble and heat-sensitive, albumins are found in milk, blood, eggs,
and some plants.
 Histones: These are basic proteins found in the cell nucleus, where they bind to DNA.
They are rich in arginine and lysine and are soluble in salt solutions.
 Protamines: Low molecular weight proteins, protamines are found in male germ cells
and are rich in arginine. They lack tyrosine, tryptophan, and sulfur-containing amino
acids.
 Globulins: These proteins occur in milk, eggs, and blood and serve as reserve proteins in
seeds.
2. Conjugated Proteins

Conjugated proteins contain both amino acids and a non-protein component called a prosthetic
group. Some important types of conjugated proteins include:

 Glycoproteins: These proteins have carbohydrate prosthetic groups, often including

glucosamine or galactosamine. Glycoproteins are found in mucous secretions, where they
act as lubricants.
 Lipoproteins: Proteins bound to lipids, such as cholesterol or triacylglycerols.
Lipoproteins are important for cell membranes and for transporting lipids in the
bloodstream. They are classified by their density into categories like chylomicrons,
VLDL, LDL, and HDL.
 Phosphoproteins: These proteins contain phosphoric acid as a prosthetic group.
Examples include caseins in milk and phosvitin in egg yolk.
 Chromoproteins: These proteins have a pigment as their prosthetic group. Hemoglobin
and cytochromes, which contain iron in their heme groups, are examples of
chromoproteins. Flavoproteins, which contain flavins, are also chromoproteins.

NUCLEIC ACIDS:
Nucleic acids are high-molecular-weight compounds that play a fundamental role in living
organisms as a store of genetic information; they are the means by which this information is
utilised in the synthesis of proteins. On hydrolysis, nucleic acids yield a mixture of basic
nitrogenous compounds (purines and pyrimidines), a pentose (ribose or deoxyribose) and
phosphoric acid. The main pyrimidines found in nucleic acids are cytosine, thymine and uracil.
Adenine and guanine are the principal purine bases present in nucleic acids.
PROTEIN QUALITY:
Protein
Proteins are large, complex molecules made up of amino acids. They play essential roles in
the body, including building and repairing tissues, supporting immune function, acting as
enzymes, and serving as hormones. Proteins are found in a wide variety of foods, especially
in animal products, legumes, nuts, and some grains.

Protein Quality
Protein quality refers to how well a protein supplies the essential amino acids needed by
the body. High-quality proteins contain all the essential amino acids in the right amounts
and are easily digestible, allowing the body to use them effectively. Animal proteins (e.g.,
eggs, meat, milk) are generally considered higher quality compared to most plant proteins,
as they contain all essential amino acids.

Importance of protein quality:

Protein quality is important because:

 The body requires essential amino acids for growth, repair, and normal functioning,
and these must come from dietary proteins.
 High-quality proteins provide all the essential amino acids in the right proportions,
ensuring optimal health, especially for growth in children, pregnant women, and
those recovering from illness.
 Low-quality proteins may lack some essential amino acids, which can lead to protein
deficiency or impaired growth and repair in the body.

Measures of Protein Quality

Several methods are used to measure protein quality, including:

1. Biological Value (BV): Measures how efficiently the body uses the protein
absorbed. The higher the BV, the better the protein is utilized.
2. Protein Digestibility-Corrected Amino Acid Score (PDCAAS): This method
evaluates protein quality based on both the amino acid profile and digestibility. A
score of 1.0 (like for eggs or milk) indicates complete protein quality.
3. Digestible Indispensable Amino Acid Score (DIAAS): Similar to PDCAAS but
more accurate, it measures the digestibility of individual amino acids rather than the
entire protein.
 4. Net Protein Utilization (NPU): Measures how much of the protein consumed is
used by the body for growth and maintenance.
5. Protein Efficiency Ratio (PER): Evaluates the growth rate of animals fed a
particular protein source, commonly used for infant formulas.

Factors That Influence Protein Quality

Several factors affect protein quality:

1. Amino Acid Composition: High-quality proteins provide all essential amino acids
in adequate amounts; low-quality proteins may lack some.
2. Digestibility: Easily digestible proteins are higher quality, with animal proteins
generally more digestible than plant proteins.
3. Processing and Cooking: Heat treatments can reduce digestibility and amino acid
availability, affecting quality.
4. Source of Protein: Animal proteins are typically higher quality than plant proteins,
which may lack some essential amino acids.
5. Anti-Nutritional Factors: Compounds like phytates and tannins in plants can
reduce protein absorption, lowering quality.