UNIT 5: CHEMISTRY OF NATURALLY OCCURRING

BIOORGANIC COMPOUNDS
 Carbohydrates
 Proteins and Amino acids
 Fats and Oils
 Nucleic Acids
Introduction

 Proteins, carbohydrates, nucleic acids, and lipids are the four major classes of biological
macromolecules—large molecules necessary for life that are built from smaller organic
molecules.
 Macromolecules are made up of single units known as monomers that are joined by
covalent bonds to form larger molecules - polymers.
 Carbohydrates and lipids both contain carbon (C), hydrogen (H), and oxygen (0); proteins
contain these three elements plus one or more from nitrogen (N), sulphur (S) and
phosphorous (P).
1. Carbohydrates
 Carbohydrates are defined as biomolecules containing a group of naturally occurring
carbonyl compounds (aldehydes or ketones) and several hydroxyl groups.
 It consists of carbon (C), hydrogen (H), and oxygen (O) atoms, usually with a hydrogen-
oxygen atom ratio of 2:1 (as in water).
 It’s represented with the empirical formula C m(H2O)n (where m and n may or may not be
different) or (CH2O)n.
 But some compounds do not follow this precise stoichiometric definition, such as uronic
acids. And there are others that, despite having groups similar to carbohydrates, are not
classified as one of them, e.g., formaldehyde
Function of Carbohydrates
 A storage form of energy in the body.
 Cell surface recognition receptors (by other cells, hormones, viruses)
 Cell surface antigens, e.g. blood groups.
 Gastric glycoprotein (mucin) contains more than 60% carbohydrate.
 A structural component of many organisms:
a) cell walls of bacteria
b) exoskeleton of insects
c) cellulose of plants.
 intermediates in the biosynthesis of other basic biochemical entities (fats and proteins)
 associated with other entities such as glycosides, vitamins and antibiotics)
 participate in biological transport, cell-cell recognition, activation of growth factors,
modulation of the immune system, lubrication of skeletal joints
Classification of Carbohydrates
 Carbohydrates are divided into four major groups based on the degree of polymerization:
monosaccharides, disaccharides, oligosaccharides, and polysaccharides.
 The carbohydrates may also be classified as either reducing or nonreducing sugars. All
those carbohydrates which reduce Fehling’s solution and Tollens’ reagent are referred to
as reducing sugars. All monosaccharides whether aldose or ketose are reducing sugars.
A. Monosaccharides
 Monosaccharides are the simplest carbohydrates and cannot be hydrolyzed into other
smaller carbohydrates. The “mono” in monosaccharides means one, which shows the
presence of only one sugar unit.
 They are the building blocks of disaccharides and polysaccharides. For this reason, they are
also known as simple sugars. These simple sugars are colorless, crystalline solids that are
soluble in water and insoluble in a nonpolar solvent.
 Monosaccharides are further classified on the basis of number of carbon atoms and the
functional group present in them. If a monosaccharide contains an aldehyde group, it is
known as an aldose and if it contains a keto group, it is known as a ketose. Number of
carbon atoms constituting the monosaccharide is also introduced in the name as is evident
from the examples given below
Different Types of Monosaccharides
  Monosaccharides may exist as a linear chain or as ring-shaped molecules; in aqueous
solutions, they are usually found in the ring form.
 Monosaccharides are simple carbohydrates composed of one molecule of sugar and are the
building blocks (monomers) of larger molecules of carbohydrates: polysaccharides
(polymers).
 Glucose, fructose and galactose are the most commonly known monosaccaride
 Glucose

 The chemical formula for glucose is C 6H12O6. In most living species, glucose is an
important source of energy. During cellular respiration, energy is released from glucose,
and that energy is used to help make adenosine triphosphate (ATP).
 Plants synthesize glucose using carbon dioxide and water by the process of
photosynthesis, and the glucose, in turn, is used for the energy requirements of the plant.
The excess synthesized glucose is often stored as starch that is broken down by other
organisms that feed on plants.
The exact spatial arrangement of different —OH groups of glucose was given by Fischer’s
formula as shown below

 Glucose is correctly named as D (+)-glucose. ‘D’ before the name of glucose represents the
configuration whereas ‘(+)’ represents dextrorotatory nature of the molecule. It should be
remembered that ‘D’ and ‘L’ have no relation with the optical activity of the compound.
 The letters ‘D’ or ‘L’ before the name of any compound indicate the relative configuration of a
particular stereoisomer of a compound with respect to configuration of some other compound,
configuration of which is known. In the case of carbohydrates, this refers to their relation with
a particular isomer of glyceraldehyde. Glyceraldehyde contains one asymmetric carbon atom
and exists in two enantiomeric forms as shown below.

 (+) Isomer of glyceraldehyde has ‘D’ configuration. It means that when its structural
formula is written on paper following specific conventions the –OH group lies on right
hand side in the structure.
 All those compounds which can be chemically correlated to D (+) isomer of
glyceraldehyde are said to have D-configuration whereas those which can be correlated
to ‘L’ (–) isomer of glyceraldehyde are said to have L—configuration. In L (–) isomer –
OH group is on left hand side as you can see in the structure.

 Glucose is found to exist in two different crystalline forms which are named as α and
β. The α -form of glucose (m.p. 419 K) is obtained by crystallisation from concentrated
solution of glucose at 303 K while the β -form (m.p. 423 K) is obtained by
crystallisation from hot and saturated aqueous solution at 371 K.
 This behaviour could not be explained by the open chain structure for glucose. It was
proposed that one of the —OH groups may add to the —CHO group and form a cyclic
hemiacetal structure.
 It was found that glucose forms a six-membered ring in which —OH at C-5 is involved in
ring formation. This explains the absence of —CHO group and also existence of glucose
in two forms as shown below. These two cyclic forms exist in equilibrium with open
chain structure
 The two cyclic hemiacetal forms of glucose differ only in the configuration of the hydroxyl
group at C1, called anomeric carbon.
 The six membered cyclic structure of glucose is called pyranose structure ( α – or β–), in
analogy with pyran. Pyran is a cyclic organic compound with one oxygen atom and five
carbon atoms in the ring. The cyclic structure of glucose is more correctly represented by
Haworth structure as given below.
 In the α- form, the exocyclic O group at the anomeric center is on the opposite face to the -
CH2OH group, and
 In the β- form, the exocyclic O group at the anomeric center is on the same face as the -
CH2OH group.
 In general the two forms are stable solids, but in solution they rapidly equilibrate

The anomeric carbon or the anomeric center can be recognised by looking for the C that is
attached to two O atoms by single bonds.
 Glucose is an aldohexose and is also known as dextrose. It is the monomer of many of
the larger carbohydrates, namely starch, cellulose. It is probably the most abundant
organic compound on earth

Fructose

 Fructose is an important ketohexose. It is obtained along with glucose by the hydrolysis of

disaccharide, sucrose. It is a natural monosaccharide found in fruits, honey and
vegetables. In its pure form it is used as a sweetner. It is also an important ketohexose.
 Fructose also has the molecular formula C 6H12O6
 Its open chain structure is as shown below.

 It also exists in two cyclic forms which are obtained by the addition of —OH at C5 to
the ( ) group. The ring, thus formed is a five membered ring and is named as
furanose with analogy to the compound furan. Furan is a five membered cyclic
compound with one oxygen and four carbon atoms.
The cyclic structures of two anomers of fructose are represented by Haworth structures
as given below
Galactose
It is a sugar found in dairy products,in the form of Lactose.
It is a disaccharide formed of Glucose & Galactose.
It forms part of glycolipids and glycoproteins in several tissues of the body

Cyclic forms of galactose

Chair conformation of D-Galactopyranose
B. Disaccharides

 Disaccharides are formed when two monosaccharides are joined together by an oxide
linkage formed by the loss of a water molecule. Such a linkage between two
monosaccharide units through oxygen atom is called glycosidic linkage.
 In disaccharides, if the reducing groups of monosaccharides i.e., aldehydic or ketonic
groups are bonded, these are non-reducing sugars, e.g., sucrose.
 On the other hand, sugars in which these functional groups are free, are called reducing
sugars, for example, maltose and lactose.
(i) Sucrose: One of the common disaccharides is sucrose which on hydrolysis gives
equimolar mixture of D-(+)-glucose and D-(-) fructose
 These two monosaccharides are held together by a glycosidic linkage between C1 of a-D-
glucose and C2 of b-D-fructose. Since the reducing groups of glucose and fructose are
involved in glycosidic bond formation, sucrose is a non reducing sugar.
 Sucrose is dextrorotatory but after hydrolysis gives dextrorotatory glucose and
laevorotatory fructose. Since the laevorotation of fructose (–92.4°) is more than
dextrorotation of glucose (+ 52.5°), the mixture is laevorotatory. Thus, hydrolysis of sucrose
brings about a change in the sign of rotation, from dextro (+) to laevo (–) and the product is
named as invert sugar.
(ii) Maltose:
 Another disaccharide, maltose is composed of two α-D-glucose units in which C1 of one
glucose (I) is linked to C4 of another glucose unit (II). The free aldehyde group can be
produced at C1 of second glucose in solution and it shows reducing properties so it is a
reducing sugar.
(iii) Lactose:
 It is more commonly known as milk sugar since this disaccharide is found in milk. It is
composed of b-D-galactose and b-D-glucose.
 The linkage is between C1 of galactose and C4 of glucose. Free aldehyde group may be
produced at C-1 of glucose unit, hence it is also a reducing sugar.
C. Polysaccharides

 Polysaccharides contain a large number of monosaccharide units joined together by

glycosidic linkages. These are the most commonly encountered carbohydrates in nature.
They mainly act as the food storage or structural materials
 They are a long chain of monosaccharides linked by covalent bonds.
 The chain may be branched or unbranched, and it may contain the same or different
types of monosaccharides.
 Starch, glycogen, cellulose, and chitin are examples of polysaccharides.
(i) Starch:
 Starch is the main storage polysaccharide of plants. It is the most important dietary
source for human beings.
 High content of starch is found in cereals, roots, tubers and some vegetables.
 It is a polymer of α-glucose and consists of two components— Amylose and
Amylopectin.
 Amylose is water soluble component which constitutes about 15-20% of starch.
Chemically amylose is a long unbranched chain with 200-1000 α-D-(+)-glucose units
held together by C1– C4 glycosidic linkage.
 Amylopectin is insoluble in water and constitutes about 80- 85% of starch. It is a
branched chain polymer of α-D-glucose units in which chain is formed by C1–C4
glycosidic linkage whereas branching occurs by C1–C6 glycosidic linkage.
(ii) Cellulose:
 Cellulose occurs exclusively in plants and it is the most abundant organic substance in plant
kingdom. It is a predominant constituent of cell wall of plant cells.
 Cellulose is a straight chain polysaccharide composed only of β-D-glucose units which are
joined by glycosidic linkage between C1 of one glucose unit and C4 of the next glucose
unit.
(iii) Glycogen:
 The carbohydrates are stored in animal body as glycogen. It is also known as animal starch
because its structure is similar to amylopectin and is rather more highly branched.
 It is present in liver, muscles and brain. When the body needs glucose, enzymes break the
glycogen down to glucose. Glycogen is also found in yeast and fungi.
 In glycogen the chain are much more highly branched and the molecular weight is very
high.
 Glucose (from glycogen) is highly water soluble and as an ideal Source of “ready energy”.
Polymer of α- 1→4 linked subunit and branching at α- 1→6 (similar to amylopectine)
Highly branched

 The size and structure of glycogen suits its function:

(1) Its size makes it too large to cross cell membranes.
(2) The structure of glycogen solves the enormous of osmotic pressure within the cell.
(3) The high branch structure of glycogen simplify the cell’s logistical problems.
Fibers
 Found in food derived from plants
 Includes polysaccharides such as cellulose, hemicellulose, pectins, gums and
mucilages
 Also includes non-polysaccharides such as lignin, cutins and tannins
 Fibers are not a source of energy in non ruminants because digestive enzymes cannot
break down fibers but ruminants can do
 The bacteria in nonruminanats GI tract can breakdown some fibers.
classification of fibers based on their solubilities in water
(1)Soluble fibers: includes gum,pectin, some hemicellulose and mucilages found in fruits, oats,
barley and legumes .
Actions on body:
(i) Delay GI transit (benefits digestive disorders)
(ii) Delay glucose absorption (benefits diabetes)
(iii) Lowers blood cholesterol(benefits heart disease)

(2) Insoluble fibers: includes cellulose, many hemicellulose, lignin found in wheat bran ,
corn bran, whole grain bread, cereals and vegetables (carrot, cabbage)
Actions in body:
(i)Accelerates GI transit and increases fecal weight(promotes bowel movement)
(ii) Slows starch hydrolysis and delays glucose absorption(Benefits diabetes)
Other polysaccharides
 Chitin (poly glucose amine), found in fungal cell walls and the exoskeletons of insects.
 Dextran (poly 1-2, 1-3 and 1-4 glucose), the storage polysaccharide in fungi and bacteria.
 Inulin (poly fructose), a plant food store. β- 1→2 linkage
 Agar (poly galactose sulphate), found in algae and used to make agar plates.
 Murein (a sugar-peptide polymer), found in bacterial cell walls.
 Lignin (a complex polymer), found in the walls of xylem cells, is the main component of
wood.
2. Proteins and Amino acids

 Proteins are the most abundant biomolecules of the living system.

 Chief sources of proteins are milk, cheese, pulses, peanuts, fish, meat, etc.
 They occur in every part of the body and form the fundamental basis of structure and
functions of life.
 They are also required for growth and maintenance of body.
 The word protein is derived from Greek word, “proteios” which means primary or of
prime importance. All proteins are polymers of a-amino acids.
Amino Acids

Amino acids contain amino (–NH2 ) and carboxyl (–COOH) functional groups. Depending
upon the relative position of amino group with respect to carboxyl group, the amino acids can
be classified as α, β , ϒ, and so on. Only α-amino acids are obtained on hydrolysis of
proteins. They may contain other functional groups also.
 All α -amino acids have trivial names, which usually reflect the property of that compound
or its source. Glycine is so named since it has sweet taste (in Greek glykos means sweet)
and tyrosine was first obtained from cheese (in Greek, tyros means cheese.)

 Amino acids are generally represented by a three letter symbol, sometimes one letter
symbol is also used. Structures of some commonly occurring amino acids along with their
3-letter and 1-letter symbols are given below
͙
Classification of Amino Acids

 Amino acids are classified as acidic, basic or neutral depending upon the relative number
of amino and carboxyl groups in their molecule.
 Equal number of amino and carboxyl groups makes it neutral; more number of amino than
carboxyl groups makes it basic and more carboxyl groups as compared to amino groups
makes it acidic.
 The amino acids, which can be synthesised in the body, are known as non essential amino
acids. On the other hand, those which cannot be synthesised in the body and must be
obtained through diet, are known as essential amino acids
Q. Write the names of essential AA and nonessential AA
 20 Amino Acids and their Functions

Glycine (G/Gly).

 Slices DNA in order to produce different amino acids. One of the three most important
glycogenic amino acids.
Alanine (A/Ala)

 Important source of energy for muscle. One of the three most important glycogenic am
acids. The primary amino acid in sugar metabolism. Boosts immune system by produc
antibodies
  Valine (V/Val). Essential for muscle
development.

 Leucine (L/Leu). Beneficial for skin, bone and tissue wound healing.

 Isoleucine (I/Ile). Necessary for the synthesis of hemoglobin.

Proline (P/Pro). Critical component of cartilage; aids in joint health, tendons and ligaments.
Keeps heart muscle strong.

 Phenylalanine (F/Phe). Beneficial for healthy nervous system. It boosts memory and
learning.

 Tyrosine (Y/Tyr). Precursor of dopamine, norepinephrine and adrenaline. Increases energy,

improves mental clarity and concentration, can treat some depressions.
 Tryptophan (W/Trp). Necessary for neurotransmitter serotonin (synthesis). Effective sleep
aid, due to conversion to serotonin. Reduces anxiety and some forms of depression. Treats
migraine headaches. Stimulates growth hormone.

 Serine (S/Ser). One of the three most important glycogenic amino acids, the others being
alanine and glycine. Maintains blood sugar levels, and boosts immune system. Myelin
sheaths contain serine.
 Threonine (T/Thr). Required for formation of collagen. Helps prevent fatty deposits in
liver. Aids in antibodies' production

 Cysteine (C/Cys). Protective against radiation, pollution, and ultra-violet light. Detoxifier;
necessary for growth and repair of skin.

 Asparagine (N/Asn). One of the two main excitatory neurotransmitters.

Glutamine (Q/Gln). Essential for helping to maintain normal and steady blood sugar levels.
Helps muscle strength and endurance. Gastrointestinal function; provides energy to small
intestines

 Lysine (L/Lys). Component of muscle protein, and is needed in the synthesis of enzymes and
hormones. It is also a precursor for L-carathine, which is essential for healthy nervous system
function.
Arginine (R/Arg). One of the two main excitatory neurotransmitters. May increase endurance
and decrease fatigue. Detoxifies harmful chemicals. Involved in DNA synthesis.

Histidine (H/His). Found in high concentrations in hemoglobin. Treats anemia; has been used
to treat rheumatoid arthritis.

Aspartate (D/Asp). Increases stamina and helps protect the liver; DNA and RNA
metabolism; immune system function.
Glutamate (E/Glu). Neurotransmitter that is involved in DNA synthesis.
 Amino acids are usually colourless, crystalline solids. These are water-soluble, high melting
solids and behave like salts rather than simple amines or carboxylic acids. This behaviour is
due to the presence of both acidic (carboxyl group) and basic (amino group) groups in the
same molecule.
 In aqueous solution, the carboxyl group can lose a proton and amino group can accept a
proton, giving rise to a dipolar ion known as zwitter ion. This is neutral but contains both
positive and negative charges.

 In zwitter ionic form, amino acids show amphoteric behaviour as they react both with
acids and bases.
Structure of Proteins

 proteins are the polymers of α -amino acids and they are connected to each other by
peptide bond or peptide linkage. Chemically, peptide linkage is an amide formed
between –COOH group and –NH2 group.
 The reaction between two molecules of similar or different amino acids, proceeds through
the combination of the amino group of one molecule with the carboxyl group of the other.
This results in the elimination of a water molecule and formation of a peptide bond
–CO–NH–.

.
 The product of the reaction is called a dipeptide because it is made up of two amino acids

 During the reactions that occur, the resulting CO-NH bond is the peptide bond, and the
resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called an
amide group or a peptide group.
For example, when carboxyl group of glycine combines with the amino group of alanine we
get a dipeptide, glycylalanine.
 If a third amino acid combines to a dipeptide, the product is called a tripeptide. A
tripeptide contains three amino acids linked by two peptide linkages. Similarly
tetrapeptide, pentapeptide or hexapeptide, etc. When the number of such amino acids is
more than ten, then the products are called polypeptides.
 A polypeptide with more than hundred amino acid residues, having molecular mass higher
than 10,000u is called a protein. However, the distinction between a polypeptide and a
protein is not very sharp. Polypeptides with fewer amino acids are likely to be called
proteins if they ordinarily have a well defined conformation of a protein such as insulin
which contains 51 amino acids.
• Proteins are a large number of linear combination of amino acid monomers- polymers
Proteins can be classified into two types on the basis of their molecular shape.

Fibrous proteins and globular proteins

(a) Fibrous proteins

 When the polypeptide chains run parallel and are held together by hydrogen and
disulphide bonds, then fibre–like structure is formed. Such proteins are generally
insoluble in water. Some common examples are keratin (present in hair, wool, silk) and
myosin (present in muscles), etc

(b) Globular proteins

 This structure results when the chains of polypeptides coil around to give a spherical
shape. These are usually soluble in water. Insulin and albumins are the common
examples of globular proteins.
Structure and shape of proteins

 Structure and shape of proteins can be studied at four different levels, i.e., primary, secondary,
tertiary and quaternary, each level being more complex than the previous one.
(i) Primary structure of proteins:
Proteins may have one or more polypeptide chains. Each polypeptide in a protein has
amino acids linked with each other in a specific sequence and it is this sequence of amino acids
that is said to be the primary structure of that protein. Any change in this primary structure i.e.,
the sequence of amino acids creates a different protein.
ii) Secondary structure of proteins:
The secondary structure of protein refers to the shape in which a long polypeptide chain can
exist. They are found to exist in two different types of structures viz. α--helix and b-pleated
sheet structure. These structures arise due to the regular folding of the backbone of the
polypeptide chain due to hydrogen bonding between and –NH– groups of the peptide
bond.
 α-Helix is one of the most common ways in which a polypeptide chain forms all possible
hydrogen bonds by twisting into a right handed screw (helix) with the –NH group of each amino
acid residue hydrogen bonded to the C O of an adjacent turn of the helix as shown below

α - Helix structure of proteins

 In β-pleated sheet structure all peptide chains are stretched out to nearly maximum
extension and then laid side by side which are held together by intermolecular hydrogen
bonds. The structure resembles the pleated folds of drapery and therefore is known as β--
pleated sheet.

β-Pleated sheet structure of protein

(iii) Tertiary structure of proteins:
 The tertiary structure of proteins represents overall folding of the polypeptide chains i.e.,
further folding of the secondary structure. It gives rise to two major molecular shapes viz.
fibrous and globular. The main forces which stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.
(iv) Quaternary structure of proteins:
 Some of the proteins are composed of two or more polypeptide chains referred to as sub-units.
The spatial arrangement of these subunits with respect to each other is known as quaternary
structure
 The quaternary structure of a protein is the association of several protein chains or subunits
into a closely packed arrangement. Each of the subunits has its own primary, secondary, and
tertiary structure.
Summary of Protein Structure

 The primary structure of protein is the hierarchy’s basic level, and is the particular linear
sequence of amino acids comprising one polypeptide chain.
 Secondary structure is the next level up from the primary structure, and is the regular
folding of regions into specific structural patterns within one polypeptide chain. Hydrogen
bonds between the carbonyl oxygen and the peptide bond amide hydrogen are normally held
together by secondary structures.
 Tertiary structure is the next level up from the secondary structure, and is the particular
three-dimensional arrangement of all the amino acids in a single polypeptide chain. This
structure is usually conformational, native, and active, and is held together by multiple
noncovalent interactions.
 Quaternary structure is the next ‘step up’ between two or more polypeptide chains from the
tertiary structure and is the specific spatial arrangement and interactions.
A diagrammatic representation of all these four structures is given below where each colored
ball represents an amino acid.
 Denaturation of Proteins

 Protein found in a biological system with a unique three-dimensional structure and

biological activity is called a native protein. When a protein in its native form, is
subjected to physical change like change in temperature or chemical change like
change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix
get uncoiled and protein loses its biological activity. This is called denaturation of
proteins

 Denaturation involves the breaking of many of the weak linkages, or bonds (e.g.,
hydrogen bonds), within a protein molecule that are responsible for the highly ordered
structure of the protein in its natural (native) state. Denatured proteins have a looser,
more random structure; most are insoluble.
 During denaturation secondary and tertiary structures are destroyed but primary
structure remains intact. The coagulation of egg white on boiling is a common
example of denaturation. Another example is curdling of milk which is caused due to the
formation of lactic acid by the bacteria present in milk.

Denaturation : the loss of shape in a protein

as a result of changes in temperature, pH, or
exposure to chemicals
Proteins have multiple functions, including:
 acting as enzymes and hormones, maintaining proper fluid and acid-base balance, providing
nutrient transport, making antibodies, enabling wound healing and tissue regeneration, and
providing energy when carbohydrate and fat intake is inadequate.
That is
 Some proteins are hormones, which are chemical messengers that aid communication
between your cells, tissues and organs.
 Some proteins are fibrous and provide cells and tissues with stiffness and rigidity.

Keratin is a structural protein that is found in your skin, hair and nails.
 Proteins in your blood maintain the fluid balance between your blood and the surrounding
tissues.
 Some proteins are enzymes which catalyzes biochemical processes.
  Proteins form antibodies to protect a body from foreign invaders, such as disease-causing
bacteria and viruses.

 Some proteins transport nutrients throughout an entire body, while others store them.
eg. Ferritin is a storage protein that stores iron and casein another storage protein , which
is the principal protein in milk that helps babies grow.

 Proteins can supply your body with energy.

3. Fats and oils
Introduction.
 Lipids along with proteins and carbohydrates constitute the principal structural
components of all living cells. Some of these are important energy storage compounds
especially in animals and human beings.
 During the past few decades, role of lipids in diet has come into focus due to their
connection with blood cholesterol and consequently heart diseases. They exhibit unique
physical and chemical properties which play a significant role in their diverse functional
properties.
Fats and oils are used in our diets to provide us with energy. They play an important role in
the transport of vitamins which are soluble in fats around the human body
 Fats and oils are commonly added to the diets of domestic animals. Nutritionally, fats and
oils are a source of essential fatty acids and energy.
 Generally, the natural feedstuffs consumed by domestic animals will fulfill their dietary
fatty acid requirement. Therefore, the primary nutritional function of fats and oils is to
provide energy.
 Fats and oils are concentrated energy sources; one unit provides approximately 2.25
times more digestible energy than either carbohydrates or proteins. In addition to
providing energy, fats and oils are also added to the diet for other reasons. As a result of
the relatively low heat increment during digestion, fats and oils aid animals during heat
stress.
 In addition, fats and oils are also digestible and may improve overall digestibility of the
ration. Addition to the ration also improves the efficiency of feed processing. Fats and oils
act as lubricants, aid in pelleting, bind smaller feed particles, and reduce dust.
 Addition of fats and oils to the diet will increase the palatability of the ration and promote
feed intake.
 Feeding fats originate from a variety of sources. The discarded animal fats from processing
and rendering plants are a source of animal feed fats. The primary animal feed fats are
tallow, lard, mixed fats, and grease.
 Grease is an animal fat with a lower melting point compared to tallow. Animal fats and
vegetable oils are used to prepare human foods, are recycled, and used as animal feeds.
Generally, cost prohibits the use of the original vegetable oils.
 Examples of common vegetable oils include corn, cottonseed, soybean, olive, safflower,
sunflower, canola, and peanut oil.
 Fats and oils also influence the absorption of lipid soluble compounds. They will increase
the absorption of lipid soluble vitamins and may decrease the absorption of minerals such
as phosphorus. As fats and oils are an expensive feed source, cost is often the factor that
limits inclusion into the ration.
Fats and oils are the most abundant lipids in nature. They provide energy for living
organisms, insulate body organs, and transport fat-soluble vitamins through the blood.

Lipids : a class of macromolecules that are nonpolar and insoluble in water

On the basis of their structure, lipids are generally classified into three main classes. These are
as given below:
• simple lipids
• complex lipids
• derived lipids
 Chemically, simple lipids are esters of fatty acids with alcohols.
 Oils and fats are common examples of this class of lipids which are the esters of long
chain fatty acids with glycerol. These esters called triglycerides or triacylglycerols,
compose one of the major food groups of our diet.
 The triglycerides that are solids or semisolids at room temperature are classified as fats
and occur predominantly in animals. These are generally the triglycerides containing
saturated fatty acids. On the other hand the triglycerides that are liquids are called oils.
These originate primarily in plants; however triglycerides from fish are also largely oils.
These are the esters of unsaturated fatty acids with glycerol.
 Fatty acids are carboxylic acids, obtained from fats and oils, having carbon chains
containing 4 to 25 carbon atoms. For example, butyric acid is a short-chain fatty acid,
responsible for the characteristic flavour in butter. Linoleic acid plays an important role in
lowering cholesterol levels.
Stearic acid, oleic acid, α-linolenic acid, and linoleic acid
IUPAC Names of fatty acids
 Carboxylic carbon is taken as carbon-1; prefixes such as tetra (4), penta (5),……….deca
(10),…..dodeca (12), ……icosa (20),……doicosa (22) are used as to describe the length of
the carbon chain; endings such as enoic, dienoic, trienoic, and tetraenoic are used to
indicate the number of double bonds. The number(s) given at the beginning of the IUPAC
name indicates the location(s) of the double bond(s).
 For example, the IUPAC name of the unsaturated fatty acid, oleic acid
CH3(CH2)7CH=CH(CH2)7COOH is:
cis-9-octadecaenoic acid.
This name indicates that the acid has 18 carbons with one double bond between carbons 9 and
10. Naturally occurring fatty acids generally have the cis-configuration around the double
bond.
Fats are made of fatty acids & they have various function in the body:
 Lubrication of body surfaces
 Components of cell membrane structures
 Formation of steroid hormones
 Energy storage
 Insulation from cold
 Carrying fat-soluble Vitamins A, D, E, K.
 Waxes are also simple lipids and are esters of fatty acids with long chain monohydric
alcohols. These are widely distributed in nature. For example, the leaves and fruits of
many plants have waxy coatings, which protect them from dehydration and small
predators. The feathers of birds and the fur of some animals have similar coatings which
serve as a water repellent. Waxes are usually inert due to the saturated nature of the
hydrocarbon chain
 Fats and oils are called triglycerides (or triacylglycerols) because they are esters
composed of three fatty acid units joined to glycerol, a trihydroxy alcohol
 A triglyceride is called a fat if it is a solid at 25°C; it is called an oil if it is a liquid at that
temperature. These differences in melting points reflect differences in the degree of
unsaturation and number of carbon atoms in the constituent fatty acids.
 Triglycerides obtained from animal sources are usually solids, while those of plant origin are
generally oils. Therefore, we commonly speak of animal fats and vegetable oils.
 Fats and oils are known as triglycerides or triacylglycerols (TAG) and both terms mean
triesters of glycerol (propane-1,2,3-triol). At room temperature a fat is solid and oil is
liquid.
 Most triglycerides in animals are fats, while those in plants tend to be oils; hence the
terms animal fats (butterfat) and vegetable oils (coconut oil, corn oil) are used.
Triglycerides have lower densities than water (they float on water), and at normal room
temperatures may be solid or liquid.
 Glycerol is a trihydric alcohol (containing three hydroxyl groups) and it can combine
with three fatty acids to form triglycerides while releasing three water molecules. Given
below is the structure of tristearin, a triglyceride with three stearic acid residues.
 The structure of tristearin formed from glycerol and stearic acid
Hydrogenation of unsaturated fats
 When exposed to air, unsaturated fats tend to get oxidised and to have an unpleasant odour
and flavour.
 By hydrogenating, i.e. treating the fat with hydrogen gas in the presence of a catalyst (Ni), the
degree of unsaturation can be decreased (partial hydrogenation) or completely removed. Fully
saturated fats are too waxy and solid to be used as food or food additives. Major problem with
partial hydrogenation of fats is the conversion of some of the natural cis-double bonds to
trans-double bonds. It is known that dietary trans-fats raise the level of low-density
lipoproteins (LDL) increasing the risk of coronary heart diseases. trans-fats also reduce high
density lipoproteins (HDL) and raise the level of triglycerides in the blood.
Soap and detergents
 Soaps are sodium or potassium salts of long chain fatty acids found in plants and animals.
Potassium soaps (soft soaps) tend to be liquids and are used in shaving creams while those
containing sodium are usually solid (hard soaps). When we boil fats or oils with sodium
hydroxide (NaOH), the sodium salts of the fatty acids (soap) and glycerol are formed as
shown below.
Formation of soap
 This is an example of alkaline hydrolysis of an ester and is called saponification.
 The four steps in the manufacture of soap are
(i) Saponification,
(ii) removal of glycerine,
(iii) soap purification, and
(iv) addition of perfumes and colour.
Detergents
 A detergent is a cleaning agent that will remove grease and grime from surfaces. However,
it is more common for liquid cleaning agents to be called detergents and solids to be called
soaps. Common soaps are prepared from natural fatty acid but detergents are made using
synthetic acids such as alkylsulphonic acids and alkylbenzenesulphonic acids.
 The reason why detergents are so useful is that they do not give precipitates with metal ions
such as Ca2+ or Mg2+ which are responsible for the hardness of water. Ordinary soap
gives a precipitate with hard water; this is scum. Detergents do not give a scum even with the
hardest water. The cleansing action of detergents is similar to that of soap. The long alkyl
chains (or the non-polar tail/ hydrophobic tail) take out the oily dirt forming micelles with the
solubility of polar heads/ hydrophilic head (sulphonate/carboxylate groups) in water as shown
below.
Structure of a soap molecule
 The early polymer chains used for detergent manufacture suffered a great deal of branching.
The hydrocarbon side chains did not interfere with the cleaning power of the detergent, but
they did prevent bacteria from attacking and breaking the chains. This meant that detergent
molecules containing branched chains degraded very slowly and they are not
environmentally friendly.
How soap works?
 Soap is a mixture of salts of medium chain length carboxylic acids, with a combination of
ionic and organic characteristics. They have an uncharged hydrocarbon tail (non-polar) and a
charged head (polar head).
 The hydrocarbon tail is likely to be hydrophobic (water hating), and the head hydrophilic
(water loving). Grease and dirt is mainly organic in nature, so the hydrophobic tails will be
able to mix happily with it and the polar heads can be solvated by water molecules instead.
.
 When you add soap or detergent to fat or greasy dirt, the non polar tails mix with non
polar dirt. By adding more soap there comes a point at which the molecules gather
together into clumps called micelles. The tails stick inwards into the roughly spherical
oil/grease balls and the heads stick outwards into the water medium

Micelle formations due to soap action on grease

4. Nucleic Acids

 Every generation of each and every species resembles its ancestors in many ways. How
are these characteristics transmitted from one generation to the next?
 It has been observed that nucleus of a living cell is responsible for this transmission of
inherent characters, also called heredity.
 The particles in nucleus of the cell, responsible for heredity, are called chromosomes which
are made up of proteins and another type of biomolecules called nucleic acids. These are
mainly of two types, the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
Since nucleic acids are long chain polymers of nucleotides, so they are also called
polynucleotides
 Nucleic acids are large biomolecules that play essential roles in all cells and viruses. A
major function of nucleic acids involves the storage and expression of genomic
information. Deoxyribonucleic acid, or DNA, encodes the information cells need to make
proteins. A related type of nucleic acid, called ribonucleic acid (RNA), comes in different
molecular forms that play multiple cellular roles, including protein synthesis

 Nucleic acids, deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), carry genetic
information which is read in cells to make the RNA and proteins by which living things
function. The well-known structure of the DNA double helix allows this information to be
copied and passed on to the next generation.
 Chemical Composition of Nucleic Acids

 Complete hydrolysis of DNA (or RNA) yields a pentose sugar, phosphoric acid and
nitrogen containing heterocyclic compounds (called bases). In DNA molecules, the sugar
moiety is β- D-2-deoxyribose whereas in RNA molecule, it is β- D-ribose
 DNA contains four bases viz. adenine (A), guanine (G), cytosine (C) and thymine (T).
 RNA also contains four bases, the first three bases are same as in DNA but the fourth one
is uracil (U)
Features of DNA and RNA
Structure of Nucleic Acids

 A unit formed by the attachment of a base to 1¢ position of sugar is known as

nucleoside. In nucleosides, the sugar carbons are numbered as 1C’, 2C’, 3C’, etc. in
order to distinguish these from the bases (a). When nucleoside is linked to phosphoric
acid at 5C’-position of sugar moiety, we get a nucleotide (b).

Structure of (a) a nucleoside and (b) a nucleotide

 Nucleotides are joined together by phosphodiester linkage between 5¢ and 3¢ carbon atoms of
the pentose sugar. The formation of a typical dinucleotide is shown below

Formation of a dinucleotide
 A simplified version of nucleic acid chain is as shown below.

 Information regarding the sequence of nucleotides in the chain of a nucleic acid is called its
primary structure. Nucleic acids have a secondary structure also.
 James Watson and Francis Crick gave a double strand helix structure for DNA. Two nucleic
acid chains are wound about each other and held together by hydrogen bonds between pairs of
bases.
 The two strands are complementary to each other because the hydrogen bonds are formed
between specific pairs of bases. Adenine forms hydrogen bonds with thymine whereas
cytosine forms hydrogen bonds with guanine.
 Ribonucleic acid, or RNA, is mainly involved in protein synthesis. Like DNA, RNA is
made of nucleotides linked by phosphodiester bonds. However, the nucleotides in RNA
contain ribose sugar instead of deoxyribose and the nitrogenous base uracil (U) instead of
thymine (T).
 Unlike DNA, RNA is usually single-stranded. However, most RNAs show internal base
pairing between complementary sequences, creating a three-dimensional structure essential
for their function.
 Structure of DNA

DNA structure looks like a twisted ladder

DNA Fingerprinting
 It is known that every individual has unique fingerprints. These occur at the tips of the
fingers and have been used for identification for a long time but these can be altered by
surgery.
 A sequence of bases on DNA is also unique for a person and information regarding this
is called DNA fingerprinting.
 It is same for every cell and cannot be altered by any known treatment.
 DNA fingerprinting is now used
(i) in forensic laboratories for identification of criminals.
(ii) to determine paternity of an individual.
(iii) to identify the dead bodies in any accident by comparing the DNA’s of parents or
children.
(iv) to identify racial groups to rewrite biological evolution.
Biological Functions of Nucleic Acids

 DNA is the chemical basis of heredity and may be regarded as the reserve of genetic
information.
 DNA is exclusively responsible for maintaining the identity of different species of
organisms over millions of years.
 A DNA molecule is capable of self duplication during cell division and identical DNA
strands are transferred to daughter cells. Another important function of nucleic acids is
the protein synthesis in the cell.
 Actually, the proteins are synthesised by various RNA molecules in the cell but the
message for the synthesis of a particular protein is present in DNA.
 Hormones are molecules that act as intercellular messengers. These are produced by
endocrine glands in the body and are poured directly in the blood stream which
transports them to the site of action
 In terms of chemical nature, some of these are steroids, e.g., estrogens and androgens;
some are poly peptides for example insulin and endorphins and some others are amino
acid derivatives such as epinephrine and norepinephrine.
 Hormones have several functions in the body. They help to maintain the balance of
biological activities in the body. The role of insulin in keeping the blood glucose level
within the narrow limit is an example of this function. Insulin is released in response to
the rapid rise in blood glucose level. On the other hand hormone glucagon tends to
increase the glucose level in the blood. The two hormones together regulate the glucose
level in the blood. Epinephrine and norepinephrine mediate responses to external stimuli.

 Growth hormones and sex hormones play role in growth and development. Thyroxine
produced in the thyroid gland is an iodinated derivative of amino acid tyrosine.
Abnormally low level of thyroxine leads to hypothyroidism which is characterised by
lethargyness and obesity. Increased level of thyroxine causes hyperthyroidism.
 Low level of iodine in the diet may lead to hypothyroidism and enlargement of the
thyroid gland. This condition is largely being controlled by adding sodium iodide to
commercial table salt (“Iodised” salt).
 Steroid hormones are produced by adrenal cortex and gonads (testes in males and ovaries
in females). Hormones released by the adrenal cortex play very important role in the
functions of the body. For example, glucocorticoids control the carbohydrate metabolism,
modulate inflammatory reactions, and are involved in reactions to stress.
 The mineralocorticoids control the level of excretion of water and salt by the kidney. If
adrenal cortex does not function properly then one of the results may be Addison’s
disease characterised by hypoglycemia, weakness and increased susceptibility to stress.
The disease is fatal unless it is treated by glucocorticoids and mineralocorticoids.
 Hormones released by gonads are responsible for development of secondary sex
characters. Testosterone is the major sex hormone produced in males. It is responsible
for development of secondary male characteristics (deep voice, facial hair, general
physical constitution) and estradiol is the main female sex hormone.
 It is responsible for development of secondary female characteristics and participates
in the control of menstrual cycle. Progesterone is responsible for preparing the uterus
for implantation of fertilised egg.