MODULE IN BIOCHEMISTRY

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 Module 3- Carbohydrates

Learning Outcomes

 Identified the nature of carbohydrates, described its structure, formulated

reactions, discussed the biological functions hexoses, disaccharides,
polysaccharides and showed respect to people particularly on gender
sensitivity issues.

Learning Content

Carbohydrates

Carbohydrates are the body’s major source of energy. There are two main types of
carbohydrates- sugar (found in milk, fruit, table sugar& candy) and starches (which
found in grains breads crackers & pasta): Composed of carbon, hydrogen, and oxygen.
The suffix -ose indicates sugar. For example: 1. Glucose (for the principal sugar in blood);
2. Fructose (for a sugar in fruits and honey); 3. Sucrose (for ordinary table sugar) 4.
Maltose (for malt sugar).

In plants, energy from the Sun is used to convert carbon dioxide and water into the
carbohydrate glucose. About 65% of the foods in our diet consist of carbohydrates. The
body break down carbs in to sugar glucose. Glucose is absorbed in to bloodstream,
which makes the sugar level in the blood go up. As sugar level rises in the body, the
pancreas releases a hormone called insulin. Insulin is needed to move glucose from the
blood in to cells, where it can be used as source of energy. In plants, a polymer of
glucose called cellulose builds the structural framework. Cellulose has other important
uses, too. The wood in our furniture, the pages in your notebook, and the cotton in our
clothing are made of cellulose.

Classification of Carbohydrates

Carbohydrates are classified according to the number of subunits that make them up.

There are 4 Types of Carbohydrates:

1. Monosaccharides. [Greek monos = single; sacchar = sugar] or simple sugars consist of

one sugar unit that cannot be further broken down into simpler sugars. Examples of
monosaccharides in foods are glucose, fructose and galactose. Over 200 different
monosaccharides are known. Monosaccharides are classified according to: 1. The
number of carbon atoms present in the molecule; 2. Whether they contain an aldehyde
or ketone group. A monosaccharide containing three carbon atoms is called a triose;
one containing four carbon atoms is called a tetrose. A monosaccharide containing an
aldehyde group is called an aldose; one containing a keto group is called a ketose.
2. Oligosaccharides. These are compound sugars that yield 2 to 10 molecules of the same
or different monosaccharides on hydrolysis. Accordingly, an oligosaccharide yielding 2
molecules of monosaccharide on hydrolysis is designated as a disaccharide, and the one
yielding 3 molecules of monosaccharide as a trisaccharide and so on.
3. Polysaccharides. Containing 10 or more monosaccharide units attached together.
Examples 1. Starch- digestible, 2. Glycogen- digestible, 3. Fiber- indigestible Long chains
of glucose units form these polysaccharides. Cellulose gives structure to plants, fiber to
our diet. Glycogen is an energy storage sugar produced by animals. Liver cells
synthesize glycogen after a meal to maintain blood glucose levels.

Functions of Carbohydrates

Carbohydrates have eight major functions within the body:

1. Blood sugar and insulin

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 2. Provides energy
3. Trigger appetite, hunger and fullness
4. In influences our mood
5. For digestion
6. Prebiotics and colon health
7. Brain functionality
8. It gives us weight

Sources of Carbohydrates: Dairy (milk, yogurt, and ice cream), Fruit (whole fruit and fruit
juice), Grains (bread, rice, crackers, and cereal), Legumes (beans and other plant-based
proteins), and Starchy Vegetables (cassava, potatoes and sweetcorn).

Recommended Dietary Allowance (RDA) of Carbohydrates

The Dietary Guidelines recommends that carbohydrates make up 45 to 65 % of your total daily
calories. So, if you get 2,000 calories a day, between 900 and 1, 300 calories should be from
carbohydrates. That translates to between 225 and 325 grams of carbohydrates a day.

Deficiency and Excess of Carbohydrates

Deficiency:

1. Weight loss if carbohydrate intake is also reduced

2. Body feels cold quickly (not enough insulation)
3. Body bruises easily (not a thick enough cushion of fat to prevent damage to blood
vessels and bones)
4. Body will not receive enough Vit A, D, E, K (found in foods that contain fat)

Excess of Carbohydrates: Weight gain or obesity. Being overweight or obese raises the risk of
serious health problems such as: Type 2 diabetes, High blood pressure, and Heart disease.
Foods containing fats are energy dense – fat provides 37 kilo Joule (kJ) energy per gram. So,
foods high in fat are high in energy too. Obesity develops if you combine eating too many
energy rich foods with a lack of exercise. If the energy from fatty foods is not all used in physical
activity each day it will be stored by the body under the skin and elsewhere around the organ.

Biologically Active Carbohydrates

According to recent researches carbohydrates promise to be a major source of drug discovery.

The diversity and complexity of carbohydrates explain their wide range of biological functions.
There are several established carbohydrates-based products with “biopharmaceutical”
application, as well as, other new products with potential application in medicine, e.g.,
development of specific cancer vaccines, new non- steroidal anti-inflammatory drugs, and many
other examples.

1. Antibiotics. This class of useful and potential therapeutics has gained attention with the
appearance of complex nucleoside antibiotics, which exhibit a variety of biological
activities. Of these are natural the thiosugars, aminoglycosides and macrolide antibiotics
produced by various species of bacteria and fungi.
2. Antitumor agents. Only some non-toxic antitumor polysaccharides derived from
bacteria, fungi, and algae have demonstrated good antitumor activity. Example (1-3)- β-
D-glucans, such as lentinan isolated from the fruiting body of Lentinus edodes. It is
useful in combination with other antineoplastic treatments in the management of
carcinomas of the lungs, stomach, uterus and breasts.
3. Laxatives: Lactulose is used in treatment of chronic constipation.
4. Sucralfate is an aluminum hydroxide complex of sucrose sulfate that is used in the
therapy of duodenal ulcers.
5. Sweeteners. Carbohydrates play an important factor in increasing the incidence of
diabetes, obesity and dental caries. There is increasing need for other alternatives to
sucrose as sweetening agents for medical purposes, especially in case of diabetes, and
for diet improvement. These agents should have high solubility in water, good stability,

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 and a relative sweetness close or equivalent to that of sucrose. They should be safe, low
caloric, and non-carcinogenic.

Learning Assessment

Name: __________________Course/Year: _________ Biochemistry, Module 3

Briefly Explain:

1. What are Carbohydrates? What are the types of carbohydrates required in the human
body?
2. How Carbohydrates function on a low carb diet?
3. What are the diseases caused by deficiency of carbohydrates?

Module 4- Amino Acids, Peptides and Proteins

Learning Outcomes
 Classified and describe the physical and chemical properties of
proteins, identified structures, reactions and functions
Learning Content

Amino Acids, Peptides and Proteins

 Structural Proteins – all made from Amino Acids
 Amino Acids: Building Blocks of Protein
 Proteins are linear heteropolymers of amino acids. Amino acids have properties
that are well-suited to carry out a variety of biological functions such as:
– Capacity to polymerize
– Useful acid-base properties
– Varied physical properties
– Varied chemical functionality

Amino Acids: Classification

Common amino acids can be placed in five basic groups depending on their R substituents. R
substituents represents straight or branched carbon chains:

1. Nonpolar, aliphatic (7)

2. Aromatic (3)
3. Polar, uncharged (5)
4. Positively charged (3)
5. Negatively charged (2)

CLASSIFICATION BY SHAPE & SOLUBILITY

1. FIBROUS PROTEINS- these proteins have a rod like structure. They are not
soluble in water. (a) These are made up of polypeptide chain that are parallel to
the axis & are held together by strong hydrogen and disulphide bonds. (b) They
can be stretched & contracted like thread. Examples: -Collagen, Keratin,
Fibrinogen, and Muscle protein.

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 2. GLOBULAR PROTEINS- these proteins more or less spherical in nature. Due to
their distribution of amino acids (hydrophobic inside, hydrophilic outside) they
are very soluble in aqueous solution. Examples Myoglobin, albumin, globulin,
casein, hemoglobin, all of the enzymes, and protein hormones.
3. MEMBRANE PROTEINS These are protein which are in association with lipid
membranes. Those membrane proteins that are embedded in the lipid bilayer
have extensive hydrophobic amino acids that interact with the non-polar
environment of the bilayer interior. Membrane proteins are not soluble in
aqueous solution.
CLASSIFICATION BY COMPOSITION
1. SIMPLE PROTEINS are those which on hydrolysis yield only amino acids and no
other major organic or inorganic hydrolysis products. They usually contain about
50% carbon,7% hydrogen, 23% oxygen, 16% nitrogen and 0–3% sulphur.
Example: Egg (albumin), Serum (globulins), Wheat (Glutelin), and Rice
(Coryzenin).
2. CONJUGATED PROTEINS are those which on hydrolysis yield not only amino
acids but also organic or inorganic components. The non-amino acid part of a
conjugated protein is called prosthetic group. Conjugated proteins are classified
on the basis of the chemical nature of their prosthetic groups.
NUTRITIONAL BASIS
1. COMPLETE PROTEINS A complete protein contains an adequate amount of all of
the essential amino acids that should be incorporated into a diet. Some protein
contains all the amino acids needed to build new proteins, which generally come
from animal and fish products. A complete protein must not lack even one
essential amino acid in order to be considered complete. Sources: The following
foods are examples of complete proteins, which need not be combined with any
other food to provide adequate protein: Meat, Fish, Poultry, Cheese, Eggs,
Yogurt, Milk.
2. INCOMPLETE PROTEINS An incomplete protein is any protein that lacks one or
more essential amino acids in correct proportions. These can also be referred to
as partial proteins. Even if the protein contains all the essential amino acids,
they must be in equal proportions in order to be considered complete. If not, the
protein is considered incomplete. Sources of Incomplete Proteins: Grains, Nuts,
Beans, Seeds, Peas, Corn.
COMBINING INCOMPLETE PROTEINS TO CREATE COMPLETE PROTEINS
By combining foods from two or more incomplete proteins, a complete
protein can be created. The amino acids that may be missing from one type of food can
be compensated by adding a protein that contains that missing amino acid. When eaten
in combination at the same meal, you are providing your body with all the essential
amino acids it requires. These are considered complementary proteins when they are
combined to compensate for each other's lack of amino acids.
PROPERTIES OF PROTEINS
1. PHYSICAL PROPERTIES
 contains carbon, hydrogen, oxygen, nitrogen and small amount of
sulphur.
 Composed of amino acids that are linked together by peptide bonds.
 Act as catalysts, enzymes that speed up the rate of chemical reactions.

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  Provides structural support for cells
 Transport substances across cell membrane
 Provides a defense mechanism against pathogens (antibodies)
 Responds to chemical stimuli
 Secretes hormones
2. CHEMICAL PROPERTIES
Denaturation is a process in which proteins or nucleic acids lose the quaternary
structure, tertiary structure and secondary structure which is present in their
native state, by application of some external stress or compound such as a
strong acid or base, a concentrated inorganic salt, an organic solvent (e.g.,
alcohol or chloroform), radiation or heat. The most common observation in the
denaturation process is the precipitation or coagulation of the protein. Heat can
be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This
occurs because heat increases the kinetic energy and causes the molecules to
vibrate so rapidly and violently that the bonds are disrupted. The proteins in
eggs denature and coagulate during cooking. Other foods are cooked to
denature the proteins to make it easier for enzymes to digest them. Medical
supplies and instruments are sterilized by heating to denature proteins in
bacteria and thus destroy the bacteria.

Learning Assessment:

Name: ________________ Course/Year: ____________ Biochemistry, Module 4

Briefly Answer.

1. Classify and describe the physical and chemical properties of proteins, identified
structures, reactions and functions in living organism (10 points)

Module 5- Lipids

Learning Outcome
 Identified the physical and chemical properties of lipids and fatty acids and
classified it by structures and functions

Learning Content
Chemistry of Lipids
 Lipids are organic compounds formed mainly from alcohol and fatty acids
combined together by ester linkage.
 Lipids are insoluble in water, but soluble in fat or organic solvents (ether,
chloroform, benzene, acetone).
 Lipids include fats, oils, waxes and related compounds.
 They are widely distributed in nature both in plants and in animals.
Biological Importance of Lipids
 They are more palatable and storable to unlimited amount compared to
carbohydrates.

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  They have a high-energy value (25% of body needs) and they provide more
energy per gram than carbohydrates and proteins but carbohydrates are the
preferable source of energy.
 Supply the essential fatty acids that cannot be synthesized by the body.
 Supply the body with fat-soluble vitamins (A, D, E and K).
 They are important constituents of the nervous system.
 Tissue fat is an essential constituent of cell membrane and nervous system. It is
mainly phospholipids in nature that are not affected by starvation.
 Stored lipids “depot fat” is stored in all human cells acts as: (a) A store of
energy; (b) A pad for the internal organs to protect them from outside shocks;
and (c) A subcutaneous thermal insulator against loss of body heat
Lipoproteins -is a complex of lipids and proteins that are important cellular constituents.
It is present both in the cellular and subcellular membranes. Cholesterol enters in
membrane structure and is used for synthesis of adrenal cortical hormones, vitamin D3
and bile acids. Lipids provide bases for dealing with diseases such as obesity,
atherosclerosis, lipid-storage diseases, essential fatty acid deficiency, and respiratory
distress syndrome.
Classification of Lipids
1. Simple lipids (Fats & Waxes)
2. Compound or conjugated lipids
3. Derived Lipids
4. Lipid-associating substances
Fatty alcohols Glycerol- It is a trihydric alcohol (i.e., containing three OH groups) and has
the popular name glycerin. It is synthesized in the body from glucose. It has the
following properties:
1. Colorless viscous oily liquid with sweet taste.
2. On heating with sulfuric acid or KHSO4 (dehydration) it gives acrolein that has
a bad odor.
3. This reaction is used for detection of free glycerol or any compound
containing glycerol.
4. It combines with three molecules of nitric acid to form trinitroglycerin (TNT)
that is used as explosive and vasodilator.
5. On esterification with fatty acids, it gives:
a) Monoglyceride or monoacyl-glycerol: one fatty acid + glycerol.
b) Diglyceride or diacyl-glycerol: two fatty acids + glycerol.
c) Triglyceride or triacyl-glycerol: three fatty acids + glycerol.
6. It has a nutritive value by conversion into glucose and enters in structure of
phospholipids.
Simple Lipids
Neutral Fats and oils (Triglycerides)- They are called neutral because they are
uncharged due to absence of ionizable groups in it. The neutral fats are the most
abundant lipids in nature. They constitute about 98% of the lipids of adipose tissue,
30% of plasma or liver lipids, less than 10% of erythrocyte lipids. They are esters of
glycerol with various fatty acids. Since the 3 hydroxyl groups of glycerol are
esterified, the neutral fats are also called “Triglycerides”.
Esterification of glycerol with one molecule of fatty acid gives monoglyceride, and
that with 2 molecules gives diglyceride.

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 Types of triglycerides
1. Simple triglycerides- If the three fatty acids connected to glycerol are of the
same type the triglyceride is called simple triglyceride, e.g., tripalmitin.
2. Mixed triglycerides- if they are of different types, it is called mixed
triglycerides, e.g., stearo-diolein and palmito-oleo- stearin. Natural fats are
mixtures of mixed triglycerides with a small number of simple triglycerides.
Physical properties of fat and oils
1. Freshly prepared fats and oils are colorless, odorless and tasteless. Any color,
or taste is due to association with other foreign substances, e.g., the yellow
color of body fat or milk fat is due to carotene pigments (cow milk).
2. Fats have specific gravity less than 1 and, therefore, they float on water.
3. Fats are insoluble in water, but soluble in organic solvents as ether and
benzene.
4. Melting points of fats are usually low, but higher than the solidification point.
Chemical Properties of fats and oils
1. Hydrolysis-They are hydrolyzed into their constituents (fatty acids and glycerol) by
the action of super-heated steam, acid, alkali or enzyme (e.g., lipase of pancreas).
During their enzymatic and acid hydrolysis glycerol and free fatty acids are
produced.
2. Saponification- Alkaline hydrolysis produces glycerol and salts of fatty acids (soaps).
Soaps cause emulsification of oily material this help easy washing of the fatty
materials
3. Halogenation -Neutral fats containing unsaturated fatty acids have the ability of
adding halogens (e.g., hydrogen or hydrogenation and iodine or iodination) at the
double bonds. It is a very important property to determine the degree of
unsaturation of the fat or oil that determines its biological value.
4. Hydrogenation or hardening of oils- It is a type of addition reactions accepting
hydrogen at the double bonds of unsaturated fatty acids. The hydrogenation is done
under high pressure of hydrogen and is catalyzed by finely divided nickel or copper
and heat. It is the base of hardening of oils (margarine manufacturing), e.g., change
of oleic acid of fats (liquid) into stearic acid (solid). It is advisable not to saturate all
double bonds; otherwise, margarine produced will be very hard, of very low
biological value and difficult to digest.
5. Oxidation (Rancidity)- It is a Physico-chemical change in the natural properties of
the fat, leading to the development of unpleasant odor or taste or abnormal color,
particularly on aging after exposure to atmospheric oxygen, light, moisture, bacterial
or fungal contamination and/or heat. Saturated fats resist rancidity more than
unsaturated fats that have unsaturated double bonds. This toxic reaction of
triglycerides leads to unpleasant odor or taste of oils and fats developing after
oxidation by oxygen of air, bacteria, or moisture. Also, this is the base of the drying
oils after exposure to atmospheric oxygen. Example is linseed oil, which is used in
paints and varnishes manufacturing.
Types and causes of Rancidity
1. Hydrolytic rancidity- It results from slight hydrolysis of the fat by
lipase from bacterial contamination leading to the liberation of free
fatty acids and glycerol at high temperature and moisture.
2. Volatile short-chain fatty acids have unpleasant odor.
3. Oxidative Rancidity
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  It is oxidation of fat or oil
 catalyzed by exposure to oxygen, light and/or heat
 producing peroxide derivatives which on decomposition give
substances, e.g., peroxides, aldehydes, ketones and
dicarboxylic acids that are toxic and have bad odor.
 This occurs due to oxidative addition of oxygen at the
unsaturated double bond of unsaturated fatty acid of oils.
4. Ketonic Rancidity
 It is due to the contamination with certain fungi such as
Asperigillus Niger on fats such as coconut oil.
 Ketones, fatty aldehydes, short chain fatty acids and fatty
alcohols are formed.
 Moisture accelerates ketonic rancidity.
Prevention of rancidity
1. Avoidance of the causes (exposure to light, oxygen, moisture, high
temperature and bacteria or fungal contamination).
2. By keeping fats or oils in well-closed containers in cold, dark and dry
place (i.e., good storage conditions).
3. Removal of catalysts such as Pb and Cu that catalyze rancidity.
4. Addition of anti-oxidants to prevent peroxidation in fat (i.e.,
rancidity).
5. They include phenols, naphthols, tannins and hydroquinones. The
most common natural antioxidant is vitamin E that is important in
vitro and in vivo.
Hazards of Rancid Fats
1. The products of rancidity are toxic, i.e., causes food poisoning and
cancer.
2. Rancidity destroys the fat-soluble vitamins (vitamins A, D, K and E).
3. Rancidity destroys the polyunsaturated essential fatty acids.
4. Rancidity causes economical loss because rancid fat is inedible.
Waxes
Waxes are solid simple lipids containing a monohydric alcohol (with a higher
molecular weight than glycerol) esterified to long-chain fatty acids. Examples of
these alcohols are palmitoyl alcohol, cholesterol, vitamin A or D.
Properties of waxes:
 Waxes are insoluble in water, but soluble in fat solvents and are negative for
acrolein test.
 Waxes are not easily hydrolyzed as the fats and are indigestible by lipases
and are very resistant to rancidity. Thus, they are of no nutritional value.
Type of Waxes: Waxes are widely distributed in nature such as:
 the secretion of certain insects as bees-wax,
 protective coatings of the skins and furs of animals and leaves and fruits of
plants.
 They are classified into true-waxes and wax-like compounds as follows:

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 True waxes: include: Bees-wax is secreted by the honeybees that use it to
form the combs. It is a mixture of waxes with the chief constituent is mericyl
palmitate.
Wax-like compounds- Cholesterol esters: Lanolin (or wool fat) is prepared
from the wool-associated skin glands and is secreted by sebaceous glands of the
skin. It is very complex mixture, contains both free and esterified cholesterol, e.g.,
cholesterol-palmitate and other sterols.
Phospholipids or phosphatides are compound lipids, which contain phosphoric acid
group in their structure.
Importance:
1. They are present in large amounts in the liver and brain as blood.
2. Every animal and plant cell contains phospholipids.
3. The membranes bounding cells and sub cellular organelle composed
mainly of phospholipids.
4. Thus, the transfer of substances through this membrane is influenced
by properties of phospholipids.
5. They are important components of the lipoprotein coat essential
secretion and transport of plasma lipoprotein complexes.
6. Myelin sheath of nerves is rich with phospholipids.
Sources: They are found in all cells (plant and animal), milk and egg- yolk in the form
of lecithin.
Structure: phospholipids are composed of:
1. Fatty acids (a saturated and an unsaturated fatty acid).
2. Nitrogenous base (choline, serine, threonine, or ethanolamine).
3. Phosphoric acid.
4. Fatty alcohols (glycerol, inositol or sphingosine).
Glycolipids -They are lipids that contain carbohydrate residues with sphingosine as the
alcohol and a very long-chain fatty acid (24 carbon series). They are present in cerebral
tissue, therefore are called cerebrosides.
Classification: According to the number and nature of the carbohydrate
residue(s) present in the glycolipids
1. Cerebrosides -They have one galactose molecule (galactosides).
2. Sulfatides -They are cerebrosides with sulfate on the sugar (sulfated
cerebrosides).
3. Gangliosides -They have several sugar and sugar amine residues.
Lipoproteins -are lipids combined with proteins in the tissues. The lipid component is
phospholipid, cholesterol or triglycerides.
Structural lipoproteins- These are widely distributed in tissues being present in
cellular and sub cellular membranes. In lung tissues acting as a surfactant in a
complex of a protein and lecithin. In the eye, rhodopsin of rods is a lipoprotein
complex.
Transport lipoproteins-These are the forms present in blood plasma. They are
composed of a protein called apo lipoprotein and different types of lipids.

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 (Cholesterol, cholesterol esters, phospholipids and triglycerides). As the lipid content
increases, the density of plasma lipoproteins decreases.
Types of Transport lipoproteins
a. Chylomicrons- They have the largest diameter and the least density.
They contain 1-2% protein only and 98-99% fat. The main lipid
fraction is triglycerides absorbed from the intestine and they contain
small amounts of the absorbed cholesterol and phospholipids.
b. Very low-density lipoproteins (VLDL) -Their diameter is smaller than
chylomicrons. They contain about 7-10% protein and 90-93% lipid.
The lipid content is mainly triglycerides formed in the liver. They
contain phospholipid and cholesterol more than chylomicrons.
c. Low-density lipoproteins (LDL) -They contain 10-20% proteins in the
form of apo lipoprotein B. Their lipid content varies from 80-90%.
They contain about 60% of total blood cholesterol and 40% of total
blood phospholipids. As their percentage increases, the liability to
atherosclerosis increases.
d. High-density lipoproteins (HDL) -They contain 35-55% proteins in the
form of apolipoprotein A. They contain 45-65% lipids formed of
cholesterol (40% of total blood content) and phospholipids (60% of
total blood content). They act as cholesterol scavengers, as their
percentage increases, the liability to atherosclerosis decreases. They
are higher in females than in males. Due to their high protein content,
they possess the highest density.
Cholesterol
Importance:
 It is the most important sterol in animal tissues as free alcohol or in an
esterified form (with linoleic, oleic, palmitic acids or other fatty acids).
 Steroid hormones, bile salts and vitamin D are derivatives from it.
 Tissues contain different amounts of it that serve a structural and metabolic
role, e.g., adrenal cortex content is 10%, whereas, brain is 2%, others 0.2-
0.3%.
Source: It is synthesized in the body from acetyl-CoA (1gm/day, cholesterol does not
exist in plants) and is also taken in the diet (0.3 gm/day as in, butter, milk, egg yolk,
brain, meat and animal fat).
Steroids - constitute an important class of biological compounds. Steroids are usually
found in association with fat. They can be separated from fats after saponification since
they occur in the unsaponifiable residue. They are derivatives of cholesterol that is
formed of steroid ring or nucleus.
Biologically important groups of substances, which contain this ring, are:
1. Sterols
2. Adrenal cortical hormones
3. Male and female sex hormones
4. Vitamin D group
5. Bile acids
6. Cardiac glycosides.

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Bile acids-They are produced from oxidation of cholesterol in the liver, producing cholic
and chenodeoxycholic acids that are conjugated with glycine or taurine to produce
glycocholic, glycochenodeoxycholic, taurocholic and taurochenodeoxycholic acids. They
react with sodium or potassium to produce sodium or potassium bile salts.
Their functions
1. Emulsification of lipids during digestion.
2. Help in digestion of the other foodstuffs.
3. Activation of pancreatic lipase
4. Help digestion and absorption of fat-soluble vitamins.
5. Solubilizing cholesterol in bile and prevent gall stone formation.
6. Choleretic action (stimulate their own secretion).
7. Intestinal antiseptic that prevents putrefactions

Enrichment Activity

Conduct this simple experiment:

Good and Bad Lipids

This project focuses on saturated and unsaturated lipids (fats and oils). Diets high in
saturated fat are linked to high blood cholesterol levels and heart disease. High-fat diets can
also increase the risk for obesity and cancer. The research aspect of this experiment is to use
a simple iodine test to determine if several common lipid products are saturated or
unsaturated. This will be done by adding tincture of iodine (betadine solution) to various
substances. If the iodine changes from brown to clear the lipid is unsaturated. If the iodine
does not change its color, the lipid is saturated. The practical application from the results of
this experiment is to reinforce the idea that as part of a healthy diet we should try to reduce
the amount of saturated lipids and trans-fats we eat and replace them with unsaturated
lipids.

Materials: tincture of iodine (betadine solution), 7- glasses, pre-boiled water, coconut oil, oil
from animal fats (pork, fish oil, chicken oil), margarine, cooking oil.

Procedure:

1. Allow the solid fats to melt into liquids. The margarine will melt just by placing them
in the warmth of the radiant heat produced by sunlight. For animal fats, extract
their oils by placing these into pan containing small amount of water just enough to
obtain their oils. Allow them to cool off.
2. Place about 10 ml of each test oil and fat into 6 glasses. Prepare a control by pouring
10 ml of pre-boiled water into the last glass. Label it properly.
3. To each glass slowly and carefully add Tincture of iodine drop by drop, shaking the
glass after each addition.

If the iodine changes from brown to clear the

lipid is unsaturated. If the iodine does not change colors the lipid is saturated. Record the results
in a table similar to the one shown.

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 Test Sample Name Test Sample Name
1. Pre-boiled water /distilled (control)
2. Pork oil
3. Chicken oil
4. fish oil
5. margarine
6. Coconut oil
7. cooking oil

Questions:

1. What is a lipid?
2. What is the difference between a saturated and an unsaturated fat?
3. Which oil do you think is the healthiest?

Your Conclusion:

Module 6- Nucleic Acid

Learning Outcomes

 Identified the structure, composition and functions of nucleic acid, illustrated decoding
of DNA template and explained genetic diseases.

Learning Content

NUCLEIC ACIDS

 are the largest and the most complex organic molecules.

 are macromolecules, found in all cells, which precipitate in the storage, transmission
and translation of genetic information.
 are found in abundance in all living things, where they create, encode, and then store
information of every living cell of every life-form on Earth.
 POLYPEPTIDES are the building blocks of nucleic acids.
 Friedrich Miescher who discovered nucleic acids in 1871

There are two types of nucleic acids:

1. Deoxyribose Nucleic Acid (DNA)- found only inside the nucleus of the cell. Contains the
organism’s genetic information, including instructions for how to make proteins.
DNA.
 Deoxyribonucleic acid is a nucleic acid that contains the genetic instructions
used in the development and functioning of all known living organisms.
 The main role of DNA molecules is the long-term storage of information and
DNA is often compared to a set of blueprints, since it contains the instructions
needed to construct other components of cells, such as proteins and RNA
molecules.
 The DNA segments that carry this genetic information are called genes, but
other DNA sequences have structural purposes, or are involved in regulating the
use of this genetic information.
 Deoxyribose is present in the nucleic acid found in the yeast cell nuclei, while
ribose is contained in the nucleic acid obtained from pancreas. There are cases
also were both of nucleic acids are found together. So that it is now definitely
accepted that both the ribose and deoxyribose nucleic acids are found in plants

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 and animals; and that while the deoxyribose type is found in the nucleic of the
cells (white) the ribose type predominate in the cytoplasm.
 Some amounts of DNA are also housed in the cell’s mitochondria, whose main
function is to generate the energy needed for the cell functioning, it couldn’t be
in the cell wall, because human cells are bound by membrane and lack the cell
walls that plants have.
 There are DNA viruses, like herpes but some of the most prevalent, like the
common cold or influenza, as well as other well-known viruses like hepatitis C
and are RNA viruses.

Functions of DNA (deoxyribonucleic acid)

a) DNA is a permanent storage place for genetic information.

b) DNA controls the synthesis of RNA (ribonucleic acid).
c) The sequence of nitrogenous bases in DNA determines the protein
development in new cells.
d) The function of the double helix formation of DNA is to ensure that no
disorders occur. This is because the second identical strand of DNA that runs
anti-parallel to the first is a backup in case of lost or destroyed genetic
information. Ex. Down’s Syndrome or Sickle Cell Anemia.
2. Ribose Nucleic Acid (RNA)- found both inside and outside of the nucleus. Directs the
building of proteins, primarily concerned with the synthesis of protein. Ribonucleic acid
is found only in plants while the deoxyribonucleic acid is exclusive of animal products.
 Ribonucleic acid (RNA) functions in converting genetic information from genes
into the amino acid sequences of proteins.
 The three universal types of RNA include transfer RNA (tRNA), messenger RNA
(mRNA), and ribosomal RNA (rRNA). Messenger RNA acts to carry genetic
sequence information between DNA and ribosomes, directing protein synthesis.
Ribosomal RNA is a major component of the ribosome, and catalyzes peptide
bond formation.

Functions of RNA (ribonucleic acid)

1. RNA is synthesized by DNA for the transportation of genetic information to the protein
building apparatus in the cell.
2. RNA also directs the synthesis of new proteins using the genetic information it has
transported. -mRNA (messenger ribonucleic acid) is used to transfer genetic information
through plasma membranes.
3. Nucleic acids (specifically DNA) carry out a vital role in the human body.
4. In particular, nucleic acids play an essential role in Mitosis, and Meiosis.
5. Nucleic acids can be used to create energy in the form of ATP (adenosine triphosphate -
C10H16N5O13P3). ATP is formed with the nitrogenous bases’ adenosine and ribose

Kinds of RNA

1. Transfer RNA
 serves as the carrier molecule for amino acids to be used in protein synthesis,
and is responsible for decoding the mRNA. In addition, many other classes of
RNA are now known.
 Transfer RNA occupies 10 to 15% of the nuclei
 small, about 80 nucleotides long.
 transport amino acids to site of protein synthesis.
 exhibits extensive inter chain of bonding represent by clover leaf structure.
2. Ribosomal RNA – 75 to 80%
 several kinds, variable in size
 combines with proteins to form ribosome's, the site of CHON synthesis.
 molecules to be quite large.
3. Messenger RNA

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  variable size (its size varies with the size of CHON)
 directs amino acids sequence of proteins - extent of it bonding is very little.
 in most cells it constitutes not more than 5% to 10% of the total cellular RNA.

Composition of Nucleic Acids

Nucleic acids are substances with high molecular weight ranging from 1,286 to 3,000,000. They
are made up of carbon, hydrogen, oxygen, nitrogen and phosphorus. Nitrogen is from 15 to 16%
while phosphorus is from 9 to 10%. On hydrolysis with either an enzyme or by heating with
dilute acids or alkali, nucleic acids yield a group of compounds known as nucleotides

Properties of Nucleic Acids:

 Nucleic acids are insoluble in alcohol, slightly soluble in cold water, but readily dissolved
in hot water and dilute alkalis’, forming alkali salts. They are precipitated by HCL and by
excess of acetic acid. Feulgen Test differentiates the DNA from RNA, if the deoxyribose
sugar is present, a red color is produced with the dye. Ribose sugar do not exhibit this
reaction.

Hydrolysis of nucleic acids gives nucleotide, which can be considered the units that make up the
polymer. A nucleotide consists of three parts: (1) Heterocyclic base; (2) sugar and (3) phosphoric
acids

The sugar in nucleotide, and so in nucleic acids, is a PENTOSE. In RNA and its nucleotide, the
sugar is RIBOSE, whereas in DNA and its nucleotide it is DEOXYRIBOSE. The prefix deoxy - means
“without oxygen”. Nucleotides can be hydrolyzed to yield nucleosides and phosphoric acid.

Nucleic acids and their derivatives

 Are not dietary essentials.

 They can be synthesized in vivo from amino acids and other substances.
 They influence the general pattern of metabolism (in chromosomes, viruses and other
cells) and act as cytoplasmic regulations of protein synthesis.

Levels of structure in Nucleic acids

1. Primary structure of nucleic acids is the order of bases in the polynucleotide sequence.
2. Secondary structure is the 3-dimensional conformation of the backbone.
3. Tertiary structure is specifically the super coiling of the molecule.

 In the early 1950s, four scientists, James Watson and Francis Crick at Cambridge
University and Maurice Wilkin and Rosalind Franklin at King's College, determined the
true structure of DNA from data and X-ray pictures of the molecule that Franklin had
taken. In 1953, Watson and Crick published a paper in the scientific journal. Nature
describing this research. Watson, Crick, Wilkins and Franklin had shown that not only is
the DNA molecule double-stranded, but the two strands wrap around each other
forming a coil, or helix. The true structure of the DNA molecule is a double helix, as
shown below.

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Figure 11. The structure of DNA molecule

 The double-stranded DNA molecule has the unique ability that it can make exact copies
of itself, or self-replicate. When more DNA is required by an organism (such as during
reproduction or cell growth) the hydrogen bonds between the nucleotide bases break
and the two single strands of DNA separate. New complementary bases are brought in
by the cell and paired up with each of the two separate strands, thus forming two new,
identical, double- stranded DNA molecules.
 Secondary structure of DNA - double helix
 DNA consists of 2 polynucleotide chains wrapped around each other to form a
helix.
 the sugar PO4 backbones, run in antiparallel directions on the 2 strands, lie on
the outside of the helix.
 pairs of bases, one on each strand, are held in alignment hydrogen bonds. The
bases pairs lie in a plane perpendicular to the helix axis.
 no twists in it other than the helical twists.
 Tertiary structure of DNA:
 super coiling
 further twisting & coiling of double helix. Ex: prokaryotes and eukaryotes

 RNA Ribonucleic acid, or RNA, gets its name from the sugar group in the molecule's
backbone - ribose. Several important similarities and differences exist between RNA and
DNA. Like DNA, RNA has a sugar-phosphate backbone with nucleotide bases attached to
it. Like DNA, RNA contains the bases adenine (A), cytosine (C), and guanine (G);
however, RNA does not contain thymine, instead, RNA's fourth nucleotide is the base
uracil (U)
 Unlike the double-stranded DNA molecule, RNA is a single-stranded molecule. RNA is
the main genetic material used in the organisms called viruses, and RNA is also
important in the production of proteins in other living organisms. RNA can move around
the cells of living organisms and thus serves as a sort of genetic messenger, relaying the
information stored in the cell's DNA out from the nucleus to other parts of the cell
where it is used to help make proteins.

Figure 12. The RNA

NUCLEOPROTIENS

 Properties of Nucleoprotein: Nucleoproteins are frankly acidic and are soluble in alkalis
with which they form salt. They precipitated from their solutions by acetic acid -are

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 redissolved by dilute HCL. They are not coagulated by -- but exhibit the precipitation
and color reactions characteristic of protein substances.
 Importance of nucleoproteins:
1. Their importance lies in the increasing evidence that they are closely associated
with the chromosomes of the cells.
2. In the bacteria cells, substances have been demonstrated, which can transform
one genetic type of bacteria into another genetic strain. They have been proven
to be deoxyribonucleic acid

MUTATION

Mutations can involve large sections of DNA becoming duplicated, usually through genetic
recombination. These duplications are a major source of raw material for evolving new genes,
with tens to hundreds of genes duplicated in animal genomes every million years. Most genes
belong to larger families of genes of shared ancestry. Novel genes are produced by several
methods, commonly through the duplication and mutation of an ancestral gene, or by
recombining parts of different genes to form new combinations with new functions.

Nucleoprotein, conjugated protein consisting of a protein linked to a nucleic acid, either DNA
(deoxyribonucleic acid) or RNA (ribonucleic acid). The protein combined with DNA is commonly
either histone or protamine; the resulting nucleoproteins are found in chromosomes. Many
viruses are little more than organized collections of deoxyribonucleo proteins. Little is known
about the proteins linked with RNA; unlike protamine and histone, they appear to contain the
amino acid tryptophan. The term nucleo is derived from the early erroneous belief that
nucleoproteins occur only in the nucleic cells.

Nucleotides and Nucleosides

 Nucleotides are the building blocks of all nucleic acids. Nucleotides have a distinctive
structure composed of three components covalently bound together:
 a nitrogen-containing "base" - either a pyrimidine (one ring) or purine (two rings)
 a 5-carbon sugar - ribose or deoxyribose
 a phosphate group.

 The combination of a base and sugar is called a nucleoside. Nucleotides also exist in
activated forms containing two or three phosphates, called nucleotide diphosphates or
triphosphates. If the sugar in a nucleotide is deoxyribose, the nucleotide is called a
deoxynucleotide; if the sugar is ribose, the term ribonucleotide is used.

Module 7: Enzymes

Learning Outcome

 Identified and discussed the biological roles of enzymes in the body.

Learning Content

Enzyme Properties / Mode of Action / Classification

 Enzymes are macromolecular biological catalysts that speed up the rate of the
biochemical reaction. Most enzymes are three-dimensional globular proteins (tertiary
and quaternary structure). Some special RNA species also act as enzymes and are called
Ribozymes

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  These are proteins or RNA produced by living cells, which is highly specific and highly
catalytic to its substrates. Due to the action of enzymes, chemical reactions in organisms
can also be carried out efficiently and specifically under mild conditions.
 The term ‘enzyme’ was coined in 1878 by Friedrich Wilhelm Kuhne, previously been
called ‘ferments’; a “manifestations of nature’s impatience”. The name ‘enzyme’ (en
(G) = in ; zyme (G) = yeast) literally means ‘in yeast’ because of most recognizable
reaction popularly known as alcohol fermentation by zymase enzyme in yeast

Difference from catalysts

 Like catalysts, the enzymes do not alter the chemical equilibrium point of a reversible
reaction but only the speed of the reaction is changed
 Differ from catalysts in being the biological products, i.e., produced from the living cells.
 The enzymes are all protein and, unlike catalysts, cannot last indefinitely in a reaction
system since they, being colloidal in nature, often become damaged or inactivated by
the reactions they catalyze. they must be replaced constantly by further synthesis in the
body.
 Unlike catalysts, most individual enzymes are very specific in that they act either on a
single or at the most on some structurally related substrates.

Classification of Enzymes

The 7 major classes of enzymes with some important examples from some subclasses are
described below:
1. Oxidoreductases
This class comprises the enzymes which were earlier called dehydrogenases, oxidases,
peroxidases, hydroxylases, oxygenase etc. The group, in fact, includes those enzymes
which bring about oxidation-reduction reactions between two substrates.
2. Transferases
Catalyze the transfer or exchange of certain groups among some substrates. In these are
included the enzymes catalyzing the transfer of one-carbon groups, aldehydic or ketonic
residues and acyl, glycosyl, alkyl, phosphorus or sulfur-containing groups: Choline
acetyltransferase, Phosphorylase, Hexokinase
3. Hydrolases
Accelerate the hydrolysis of substrates. These catalyze the hydrolysis of their substrates
by adding constituents of water across the bond they split. The substrates include ester,
glycosyl, ether, peptide, acid-anhydride.
4. Lyases
Promote the removal of a group from the substrate to leave a double bond reaction or
catalyze its reverse reaction. Facilitate the conversion of isomers, geometric isomers or
optical isomers.

5. Isomerases. Facilitate the conversion of isomers, geometric isomers or optical isomers

6. Ligases or Synthetases
Catalyze the synthesis of two molecular substrates into one molecular compound with
the release energy. These are the enzymes catalyzing the linking together of two
compounds utilizing the energy made available due to simultaneous breaking of a
pyrophosphate bond in ATP or a similar compound.
7. Translocases
Catalyze the movement of ions or molecules across membranes or their separation
within membranes. Translocases are the most common secretion system in Gram
positive bacteria. Translocase of the outer membrane (TOM) can work in conjunction
with translocase of the inner membrane (TIM) to transport proteins into the
mitochondrion

Properties of Enzymes

1. Colloidal Nature

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 On account of their large size, the enzyme molecules possess extremely low rates of
diffusion and form colloidal systems in water. Being colloidal in nature, the enzymes are
nondialyzable although some contain dialyzable or dissociable component in the form of
coenzyme.
2. Catalytic Nature or Effectiveness
A universal feature of all enzymatic reactions is the virtual absence of any side products
They are recovered as such without undergoing any qualitative or quantitative change.
This is the reason why they, in very small amounts, are capable of catalyzing the
transformation of a large quantity of substrate.
3. Specificity of Enzyme Action
With few exceptions, the enzymes are specific in their action. Their specificity lies in the
fact that they may act (a) on one specific type of substrate molecule (b) on a group of
structurally-related compounds (c) on only one of the two optical isomers of a
compound (d) on only one of the two geometrical isomers.

CHARACTERISTICS

 Enzymes speed up the reaction by lowering the activation energy of the reaction.
 Their presence does not affect the nature and properties of end product.
 They are highly specific in their action that is each enzyme can catalyze one kind of
substrate.
 Small number of enzymes can accelerate chemical reactions.
 Enzymes are sensitive to change in pH, temperature and substrate concentration. 
Turnover number is defined as the number of substrate molecules transformed per
minute by one enzyme molecule. Catalase turnover number = 6 x106/min

Coenzymes

 Enzymes functional groups takes part in acid-base reaction, to form transient bonds
with substrate or take part in charge – charge interactions. They are less stable for
catalyzing Redox reaction or transfer of a chemical group.
 Such reactions are carried out by small molecules called cofactors
 Cofactors may be metal ions, such as the Zn2+ required for the catalytic activity of
carboxypeptidase A, or organic molecules known as coenzymes, such as the NAD+ in
YADH
 Some cofactors, for instance NAD+, are but transiently associated with a given enzyme
molecule, so that, in effect, they function as co-substrates.
 Other cofactors, known as prosthetic groups, are essentially permanently associated
with their protein, often by covalent bonds.
 For example, the heme prosthetic group of hemoglobin is tightly bound to its protein
through extensive hydrophobic and hydrogen bonding interactions together with a
covalent bond between the heme Fe2+ ion and His F8.
 Coenzymes are chemically changed by the enzymatic reactions in which they
participate. Thus, in order to complete the catalytic cycle, the coenzyme must be
returned to its original state. For prosthetic groups, this can occur only in a separate
phase of the enzymatic reaction sequence.
 For transiently bound coenzymes, such as NAD+, however, the regeneration reaction
may be catalyzed by a different enzyme.
 A catalytically active enzyme–cofactor complex is called a holoenzyme (Greek: holos,
whole).
 The enzymatically inactive protein resulting from the removal of a holoenzyme’s

𝐀𝐩𝐨𝐞𝐧𝐳𝐲𝐦𝐞 𝐢𝐧𝐚𝐜𝐭𝐢𝐯𝐞 + 𝐜𝐨𝐟𝐚𝐜𝐭𝐨𝐫 ⇔ 𝐡𝐨𝐥𝐨𝐞𝐧𝐳𝐲𝐦𝐞 (𝐚𝐜𝐭𝐢𝐯𝐞

cofactor is referred to as an apoenzyme (Greek: apo, away)

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