Bios Biochemistry PDF

Contents
Contents .................................................................................................................................................. 1
BIOCHEMISTRY ........................................................................................................................................ 4
(BIOLOGICAL CHEMISTRY, THE CHEMISTRY OF LIFE) .......................................................................... 4
COMMON TECHIQUES AND METHODS USED IN BIOCHEMISTRY. ...................................................... 5
OBJECTIVES OF BIOCHEMISTRY .......................................................................................................... 6
SCOPE OF BIOCHEMISTRY ................................................................................................................... 6
NATURAL ELEMENTS IN LIVING THINGS. ............................................................................................ 7
CARBOHYDRATES ................................................................................................................................ 8
CLASSIFICATION OF CARBOHYDRATES (CATEGORIES OF CARBOHYDTRATES) ................................... 8
1. CLASSIFICATION OF CARBOHYDRATES ON THE BASIS OF BEHAVIOUR ON HYDROLYSIS. .............. 9
MONOSACCHARIDES (also called single sugar) .................................................................................. 9
POLYSACCHARIDES............................................................................................................................ 10
REDUCING SUGAR AND NON- REDUCING SUGARS .......................................................................... 10
MONOSSACCHARIDES ....................................................................................................................... 10
GENERAL PROPERTIES OF MONOSACCHARIDES............................................................................... 11
CLASSIFICATION OF MONOSACCHARIDES BASED ON FUNCTIONAL GROUP ................................... 11
CLASSIFICATION OF MONOSACCHARIDES ON THE BASIS OF NUMBER OF CARBON ATOMS. ......... 11
DESIGNATION OF MONOSACCHARIDES............................................................................................ 12
MESOMERISM IN CARBOHYDRATES ................................................................................................. 15
THE D AND L ISOMERS ...................................................................................................................... 15
STEREOISOMERISM ........................................................................................................................... 15
CONFORMATION (STRUCTURES) OF BIOLOGICALLY IMPORTANT MONOSACCHARIDES ................. 17
FORMATION OF HEMIACETALS AND HEMIKETAL ............................................................................. 17
GLUCOSE (C6H12O6) ........................................................................................................................... 19
LINEAR AND RING STRUCTURE OF GLUCOSE. ................................................................................... 19
THE PYRANOSE AND FURANOSE RING OF FRUCTOSE ...................................................................... 21
FRUCTOSE (C6H12O6) .......................................................................................................................... 21
OLIGOSACCHARIDES, ESPECIALLY DISACCHARIDES ........................................................................ 23
PROPERTIES OF DISSASSHARIDES ..................................................................................................... 23
STRUCTURE OF BIOLOGICALLY IMPORTANT OLIGOSACCHARIDES ................................................... 24
A: STRUCTURE OF MALTOSE ............................................................................................................. 24
B: STRUCTURE OF LACTOSE .............................................................................................................. 25
C: STRUCTURE OF SUCROSE .............................................................................................................. 26
POLYSACCHARIDES............................................................................................................................ 26
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Yusuph Nsaze: Kasulu TC

PROPERTIES OF POLYSACCHARIDES.................................................................................................. 26
CLASSIFICATION OF POLYSACCHARIDES ........................................................................................... 27
BASED ON FUNCTION ....................................................................................................................... 27
STRUCTURE OF COMMON POLYSACCGARIDES (STARCH, GLYCOGEN AND CELLULOSE) ................. 27
STARCH (PLANT CARBOHYDRATE) .................................................................................................... 27
GLYCOGEN (ANIMAL POLYSACCHARIDES) ........................................................................................ 29
CELLULOSE ........................................................................................................................................ 29
ROLES OF CARBOHYDRATE IN LIVING ORGANISMS.......................................................................... 31
LIPIDS (FATS AND OIL AND WAXES) .................................................................................................. 32
COMPONENTS OF LIPIDS (FAT and OIL) ............................................................................................ 32
GENE-RAL PROPERTIES OF LIPIDS ..................................................................................................... 33
CLASSIFICATION OF LIPIDS ................................................................................................................ 33
COMPONENTS OF FATS AND OIL ...................................................................................................... 34
GLYCEROL/GLYCERINE ...................................................................................................................... 34
PROPERTIES OF GLYCERAL ................................................................................................................ 34
FATTY AC IDS ..................................................................................................................................... 34
SATURATED FATTY CID...................................................................................................................... 34
UNSATURATED FATTY ACID .............................................................................................................. 34
FORMATION OF LIPIDS...................................................................................................................... 36
SIMPLE LIPIS ...................................................................................................................................... 36
PROPERTIES OF WAXES ..................................................................................................................... 37
FUNCTIONS OF WAXES ..................................................................................................................... 37
COMPLEX LIPIDS (COMPOUND LIPIDS) ............................................................................................. 37
PHOSPHOLIPIDS ................................................................................................................................ 37
FUNCTIONS OF PHOSPHOLIPIDS ....................................................................................................... 38
GLYCOLIPIDIS..................................................................................................................................... 38
FUNCTION OF GLYCOLIPIDS .............................................................................................................. 38
STEROIDS........................................................................................................................................... 38
FUNCTIONS OF STEROIDS. ................................................................................................................ 39
ROLES OF LIPIDIS AS IMPORTANT COMPONENT OF THE CELL MEMBRANE .................................... 40
THE FLUID MOSAIC MODEL OF THE CELL MEMBRANE..................................................................... 40
GEERAL FUNCTIONS OF LIPIDS.......................................................................................................... 43
AMINO ACIDS AND PROTEINS........................................................................................................... 44
FORMATION OF ZWITTER ION .......................................................................................................... 44
THE D – AND L – CONFIGURATION OF AMINO ACIDS....................................................................... 45
CLASSIFICATION OF AMINO ACIDS ................................................................................................... 46
ESSENTIAL AND NON ESSENTIAL AMINO ACID ................................................................................. 46

NON ESSENTIAL AMINO ACIDS (DISPENSABLE AMINO ACIDS) ......................................................... 46
ESSENTIAL AMINO ACIDS (INDESPENSABLE AMINO ACIDS) ............................................................. 46
PEPTIDES AND PEPTIDE BOND .......................................................................................................... 47
POLYPEPTIDES ................................................................................................................................... 48
CHARACTERISTICS OF PLOYPEPTIDES ............................................................................................... 48
STRUCTURE OF POLYPEPTIDES ......................................................................................................... 49
PROTEINS AND THEIR CLASSIFICATION............................................................................................. 49
STRUCTURE OF AMINO ACIDS .......................................................................................................... 50
GENERAL PROPERTIES OF PROTEINS ................................................................................................ 51
CLASSIFICATION OF PROTEINS .......................................................................................................... 51
CLASSIFICATION OF PROTEINS ON THE BASIS OF CHEMICAL COMPOSITION .................................. 51
CLASSIFICATION OF PROTEINS ON THE BASIS OF MOLECULAR STRUCTURE ................................... 52
DIFFERENCES BETWEEN GLOBULAR AND FIBROUS PROTEINS ......................................................... 52
CLASSIFICATION OF PROTEINS ON THE BASIS OF SOLUBILTY. .......................................................... 52
CLASSIFICATION OF PROTEINS ON THE BASIS OF FUNCTIONS ......................................................... 53
LEVELS OF PROTEIN ORGANIZATION ................................................................................................ 53
(STRUCTURES OF PROTEINS)............................................................................................................. 53
PROTEIN DENATURATION ................................................................................................................. 55
FACTORS CAUSING PROTEINS DENATURATION ............................................................................... 56
ROLES OF PROTEINS IN LIVING ORGANISM ...................................................................................... 57
THE NATURE AND PROPERTIE OF ENZYMES ..................................................................................... 58
PROPERTIES OF ENZYMES ................................................................................................................. 58
ENZYMES STRUCTURE AND FUNCTIONS........................................................................................... 59
ENZYMES AND ACTIVATION ENERGY ................................................................................................ 59
MECHANISM OF ENZYME ACTION (Mechanism of enzyme catalysis).............................................. 60
LOCK AND KEY MODEL OF ENZYME ACTIVITY ................................................................................. 61
INDUCED FIT MODEL OF THE ENZYME ACTION ................................................................................ 61
FACTORS GOVRNING ENYZYEM ACTIVITY ........................................................................................ 64
THE GRAPHY TO SHOW EFFECT OF TEMPERATURE ON ENZYME ACTIVITY ..................................... 65
THE GRAPHY TO SHOW THE EFFCT OF CHANGE IN PH ON ENZYME ACTIVITY ................................. 66
THE GRAPHY TO SHOW EFFECT OF SUBSTRATE CONCENTRATION ENZYME ACTIVITY. ................... 68
THE GRAPH TO SHOW EFFECT OF TEMPERATURE ON ENZYME ACTIVITY ....................................... 68
THE GRAPH TO ENZYME INHITION REACTION............................................................................ 71
ENZYME COFACTORS ........................................................................................................................ 71
CLASSIFICATION OF ENZYMES .......................................................................................................... 72
THE SIX MAJOR GROUPS OF ENZYMES ............................................................................................. 72
REFERENCE ........................................................................................................................................ 75

BIOCHEMISTRY
(BIOLOGICAL CHEMISTRY, THE CHEMISTRY OF LIFE)
INTRODUCTION: The term Biochemistry was first of all introduced by a German chemist,
Car Neuberg, in 1903.
Biochemistry is relatively young science. Biochemistry in its broad aspects is the most
comprehensive of all the branches of chemistry, since it includes organic, in organic and
physical chemistry to the extent to which each of the chemistry of living things.
Biochemistry encompasses a study of chemical nature of all living matter from the smallest
viruses and microorganism to the most complex and highly evolved plants (flowering
plants) and animals (human being).
NOTE: Biochemistry is a branch of both Chemistry and biology.
The term biochemistry is the combination of two words, Bio = Life, and chemistry = Which
is the study of composition and decomposition of matter.
Matter is anything that has weight and can occupy the space (All living and non – living
things).
Matter is made of tiny particles of an element called Atom. Atoms combine to form
molecules (compound)
Atom is the smallest particle of an element that has characteristics of that element or are
building block of an element.
NOTE: Composition = Nature of something ingredients or constituents or made up
Decomposition = Break down into pieces, or break down into smaller parts or break down
into constituents’ parts.
So, everything whether living e.g. human being, plants or non-living e.g. rock is made of
substances called elements. Element is a substance that cannot be broken down into simpler
chemical substances.
By definition; Biochemistry is the study of chemical process within and relating to living
organisms.
Biochemistry is the study of the chemical substances and vital process occurring in all
living organisms.
Biochemistry is the study of chemistry of life. It seeks to understand the relationship
between the structure and functions of the molecules that make up living organisms.
Biochemistry may be defined as the science of chemistry, of living matter in different phase
of activity.

Biochemistry, study of the substances found in living organisms, and of the chemical
reactions underlying life processes.
Biochemistry probes into the chemical changes involved in origin of the living matter.
follows the changes involved in its own, and studies the process not only until death but
thereafter until dissolution of the matter following its death.
It involves relationship of the process by which an exchange of chemical substances takes
place between the living organism and its environment through the process of digestion,
absorption and excretion. The process by which the absorbed materials are utilized for
synthetic reactions leading to growth and replishment of tissues and multiplication of the
cell and species, the metabolic break down (catabolism) of the materials to supply energy
for all the above, the mechanism which regulates with precision all these processes by
means of hormonal and neuro-regulatory stimuli – all these come under the biochemistry.
This is not easy task because of the enormous diversity and complexity of life process. There
is a broad overlap between biochemistry and all the sciences that study living organisms
from simplest to the most complex.
Areas as diverse of all cell and molecular biology, molecular genetics, physiology,
toxicology, drugs design, nutrition, forensic science, and environmental science all use
the biochemistry techniques and methods.
NOTE: Biochemistry genetics is the field that has stimulated a lively interest, is a field of
biochemistry.
Some biochemistry tries to explain how the molecules that make up the human body
function. They identify the molecules and determine how molecules are produced, how
they interact with each other, and the results of the chemical reactions they undergo.
Note: No matter what the area of specialization, biochemistry basically applies the tool of
biology, chemistry, physics and mathematics using special techniques.
COMMON TECHIQUES AND METHODS USED IN BIOCHEMISTRY.

TECHNIQUE DESCRIPTION PURPOSE
Cell structure techniques The growing of microorganisms, Obtaining specific materials
cells, or tissue in especially for study
prepared nutrient medium
Microscopy Magnification of structures too Visualization and
small to be seen by the naked identification of cells,
eyes tissues, and biomolecules
Centrifugation Mechanical separation of Separation of the
mixture placed in compartment components of a mixture
spun about a central axis to
separate components of different
weights.
Chromatography Separation method that use Purification of biomolecules
columns filled with gels that
separate a mixture of molecules
into individual components by
size or charge

Kinetic experiments Measurement of the biochemical Understanding the nature or
reactions yields a product function of the reaction
X – ray crystallography Use of x-rays to record the Identification of the atomic
structure of a molecule crystal constituents of a
biomolecule and of its 3D
structure.
Nuclear magnetic Monitoring of the response of Identification of the 3D
resonance protons to radiation when placed structure of biomolecules in
in magnetic field solution.
Radioisotope labelling Incorporation of radioactive Characterization of
label into a compound biomolecules components
tracing reaction path ways.
OBJECTIVES OF BIOCHEMISTRY
 To study the structure and properties of substances which enter the cell as the
source of energy or leave the cell as waste products.
 To study the catalytic activity of enzymes
 To study the processes that convert diet into compound which are characteristics of
the cells of a given species.
 To study the manifold-energy requiring process of the living cell.
 To study the chemistry of inheritance
SCOPE OF BIOCHEMISTRY
A knowledge of the broad chemical principles is desirable for the biochemists. The objective
of the present text is to provide biochemical facts and principles to the students of teacher
education. These involves:
 Study of cell structure and its components
 Chemistry of: Carbohydrates
: Proteins and amino acids,
: Lipids
 Chemistry of inorganic elements and their deficiency manifestations
 Study of enzymes
 Study of vitamins and their deficiency manifestations
 Water metabolism, their source, regulation etc.
 Metabolism of carbohydrates and the metabolic dis orders e.g. Diabetes mellitus a
disease in which the body is either unable to produce enough insulin or the cell cannot
use the insulin to remove glucose from the blood.
 Metabolism of proteins and amino acids and their metabolic disorders e.g. Sickle cell
anaemia disease of the blood that affect haemoglobin. The haemoglobin is a protein
which contains iron in red blood cells.

 Metabolism of lipids and their metabolic disorders e.g. Atherosclerosis – Diseases
that involves the accumulation of lipid containing molecules in arteries which cause
inflammation and narrowing of the artery that may lead into heart attack.
 Chemistry of nucleic, recombinant DNA technology, nucleoproteins and metabolism
of nucleic acids and their metabolic disorders e.g. Genetic diseases and disorders.
 Immunochemistry
 Detoxification mechanism
 Hormones and their biochemical roles in in the body.
NATURAL ELEMENTS IN LIVING THINGS.
Of the naturally occurring element on the earth, only about 25 elements are essential to living
things: Some elements that make up the body of living organisms are: Carbon, oxygen,
hydrogen, nitrogen, sulphur, phosphorus, calcium, potassium, sodium, chlorine, iron,
iodine, zinc, copper manganese, fluorine etc. About 60-90 percent of the body weight is
water. From the elements above it is not surprised that most of the body mass is oxygen.
Carbon, is the building block of organic compounds, take second place. together, the six
body elements – oxygen, carbon, hydrogen, nitrogen, calcium and phosphorus accounts
for about 99% of the body’s mass.
Notice that four elements – Carbon, hydrogen, oxygen, and nitrogen – together make up
more than 96 percent of the mass of the human body. Consider the following percentage of
elements in human body. Oxygen 65% carbon, 18.5%, nitrogen 3.3%, hydrogen, 0.5%,
sulphur 0.3% and calcium 1.5% of the body mass.
Atoms of an element combine to form both organic and inorganic substances. These
substances are also found in living things. Carbon is the fundamental element in all forms of
life.
The chief goal of biochemistry is to understand the structure and behaviour of
Biomolecules (biological molecules).
Biomolecules: Are molecules which are found in living organisms. But mainly we shall
consider biomolecules that contains carbon atom. These are the carbon-containing
compounds that make up the various parts of the living cell and carry out the chemical
reactions that enable it to grow, maintain and reproduce itself, and use and store energy.
Note: The simplest organic compounds from which living organisms are constructed are
unique to life and do not otherwise occur on the earth today except as the product of
biological activity.
A vast array of biomolecules is present in the cell. The structure of each biomolecule
determines what chemical reactions it is able to participate, and hence what role it plays in
the cell's life processes.
Just as there is a great diversity of living organisms, there is also a wide variety of
molecules essential for life. These biomolecules are usually classified in four major groups:
Carbohydrates, lipids, proteins and nucleic acids. These groups differ in chemical
structure, reactivity and functions.
Proteins are one of the most constituents of the cells. the study of proteins includes two
important areas of biochemical specialization, namely protein synthesis and enzymology
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(the study of enzymes). Other specialization areas include cell membrane transport study of
how biomolecules pass into and out of the cell.
Another source: All living things are composed of a large variety of lifeless molecules. Each
such molecule has a specific function in the life-cycle of the living things. Living systems
interact with their surroundings through these molecules. Plants use sun light as the source of
energy to synthesize various compounds, while animals drive energy needed by them from
the breakdown of the molecules present in food. The various types of compounds which are
found to be essential for life are:
Carbohydrates, lipids, proteins, vitamins and hormones. Thus, the molecules of the above
listed compounds form the basis of life. Such molecules of organic compounds which build
up living systems and are required by for their growth and maintenance are called
Biomolecules.
Generally, biochemistry is the super chemistry which help to understand the structure and
properties of substances constituting the framework of cell and tissue.
Where there is life there is Biochemistry
Biochemistry is important in many fields of science in addition to medicine. For example,
biochemists investigate food by studying molecules such as vitamins, fatty acid, glucose and
various minerals and water, all of which are dietary requirements for health nutrition.
But in this curriculum, the following biomolecules should be covered.
- Carbohydrates
- Lipids
- Proteins and
- Enzymes
CARBOHYDRATES
QN: What are carbohydrates?
Carbohydrates are naturally- occurring organic compounds, containing chemical elements
carbon, hydrogen and oxygen.
The general formula of carbohydrates is CyH2yOy. or (CH2O) y, where y is the variable
number e.g. 1,2,3 …….
In carbohydrates, the hydrogen and oxygen being in the same ratio as in water, but these are
not present as water molecules. The oxygen is present in carbohydrate in the form of
aldehydic, Ketonic, and or hydroxyl group. Hydrogen is either present as the – OH group
or directly linked to the carbon.
The polyhydroxy aldehydes, polyhydroxy ketones or large polymeric molecules which on
hydrolysis produce polyhydroxy aldehydes or ketones are called carbohydrates.
Starch and sugar are the most important carbohydrates. Carbohydrates are mainly derived
from plants, where they make up about 70 percent of the solid plant materials.
CLASSIFICATION OF CARBOHYDRATES (CATEGORIES OF CARBOHYDTRATES)
Carbohydrates can be classified on the basis of,

a) Behaviour on hydrolysis and
b) Taste
1. CLASSIFICATION OF CARBOHYDRATES ON THE BASIS OF BEHAVIOUR ON

HYDROLYSIS.
Carbohydrates are classified into three (03) classes according to their behaviour on
hydrolysis.
i. Monosaccharides
ii. Oligosaccharides and
iii. Polysaccharides.
MONOSACCHARIDES (also called single sugar)
Monosaccharides are the simplest carbohydrates which cannot be hydrolysed into any
smaller simpler molecules. Thus, each molecule of monosaccharides represents a complete
carbohydrate unit.
Monosaccharides are sugars which contains 3 to 7 carbon atoms in their molecules. About 20
monosaccharides occurs naturally.
Simply monosaccharides are carbohydrates which are made up of a single molecule of sugar.
General formula: The general formula of monosaccharides is (CH2O) n, where n=3 to 7.
Examples of common monosaccharides are: Glucose (C6H12O6), fructose (C6H12O6),
galactose (C6H12O6) and ribose (C5H10O5).
I. OLIGOSACCHARIDES (Oligo from Greek = means few)
Oligosaccharides are carbohydrates whose molecules give 2 to 10 molecules of
monosaccharides (same or different) upon hydrolysis.
Depending upon the number of molecules of monosaccharides produced upon hydrolysis,
the oligosaccharides are further classified as follows:
a) Disaccharides (Double sugar). Carbohydrates which on hydrolysis produce 2
molecules of monosaccharides (same or different). The molecular formula of
disaccharides is (C12H22O11).
The common examples of disaccharides are: Maltose (C12H22O11), lactose (C12H22O11) and
sucrose (C12H22O11).
b) Trisaccharide: Carbohydrates which on hydrolysis produce three (03) molecules of

monosaccharides (Same or different). The molecular formula of trisaccharide is
C18H32O16.
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Examples; Raffinose a typical trisaccharide. One molecule of raffinose gives one molecule
of each glucose, fructose and galactose on hydrolysis.
c) Tetra saccharides: The carbohydrates which upon hydrolysis gives four molecules of
monosaccharide (same or different). The molecular formula of tetra saccharide is
C24H42O21. Example is stachyrose, one molecule of stachyrose upon hydrolysis gives
one molecule of each of glucose, fructose and two molecules of galactose.
POLYSACCHARIDES
Polysaccharides are carbohydrates which upon hydrolysis gives a large number
monosaccharide. General molecular formula of polysaccharides is (C6H10O5), where n =
100-3000. Examples of common polysaccharides are Starch, cellulose and glycogen
H
(C6H10o5) n + n H2O  n C6H12O6
CLASSIFICATION OF CARBOHYDRATES ON THE BASIS OF TASTE.

Carbohydrates are classified further on the basis of taste into two classes:
Sugars: Carbohydrates which are sweet in taste and dissolve in water. Generally, are
crystalline in nature.
Note: All monosaccharides and disaccharides are sweet in taste so are called sugars
Non – sugars. Are tasteless carbohydrates, insoluble in water, generally amorphous.
Note: Polysaccharides are non-sugars examples: Starch and cellulose.
REDUCING SUGAR AND NON- REDUCING SUGARS
Sugars (Carbohydrates) may also be classified on the basis of chemical nature as:
a) Reducing sugars and
b) Non – reducing sugar
All sugars which contain free aldehyde or ketonic group are called reducing sugars.
All monosaccharides whether contains aldehyde (-CHO) or ketonic (>C=O) functional
group are reducing sugars.
All disaccharides whether contains aldehyde (-CHO) or ketonic (>C=O) free functional
group are reducing sugar for example Maltose, and lactose. All disaccharides in which the
reducing group of the constituent monosaccharides i.e. Aldehyde or ketonic group, are
bonded (not free) are non – reducing sugar. For example, sucrose.
Reducing sugars reduce cupric ion (Cu2+ = blue in colour) from Fehling’s solution to
cuprous ion (Cu+ = reddish in colour)
MONOSSACCHARIDES
Monosaccharides are the simplest carbohydrates. These cannot break down into simpler
carbohydrates by hydrolysis. Monosaccharides are classified as follows:
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GENERAL PROPERTIES OF MONOSACCHARIDES
Some general characteristics of monosaccharides are described below:
 Monosaccharides are readily soluble in water.
 They are small molecules
 Monosaccharides are sweet substances
 They are crystalline solid at room temperature
 Two molecules of monosaccharides combine with elimination of water
(condensation) to give a disaccharide; many monosaccharides combine to form
polysaccharides.
 Exist in ring or open chain structures
 Monosaccharides have asymmetric carbon atoms, as the result exhibit optical activity.
Thus, all monosaccharides have two optical isomers these are, D – and L – forms.
Most of the naturally occurring monosaccharides have D – configuration. In solution
these sugar show mutarotation
 When heated monosaccharides get charred
 Can be reduced to sugar alcohols
 Monosaccharides are reducing agents can reduce Cu++ from Fehling solution to Cu+.
e.tc.
CLASSIFICATION OF MONOSACCHARIDES BASED ON FUNCTIONAL GROUP
In addition to hydroxyl group monosaccharides either an aldehydic (- CHO) or ketonic
(>C=O) group. The monosaccharides containing aldehydic group are termed as aldose,
while that containing a keto group is called ketose.
The aldehyde group (-CHO) being monovalent is always present at the end the carbon
chain. The ketonic group (>C=O) being divalent can be present anywhere in the carbon
chain. In naturally -occurring monosaccharides, the keto group is present at carbon number
CLASSIFICATION OF MONOSACCHARIDES ON THE BASIS OF NUMBER OF CARBON
ATOMS.
Monosaccharides are further classified on the basis of number of carbon atoms in their
chains. These are named on the basis of number of carbon atoms in their molecules as
follows:
No of carbon atoms General name of the Examples
monosaccharide
3 Triose Glyceraldehyde
4 Tetrose Erythrose
5 Pentose Ribose, arabinose
6 Hexose Glucose, fructose
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DESIGNATION OF MONOSACCHARIDES
Depending upon the nature of the functional group and the number of carbon atoms present
in the molecules of monosaccharide, these are designated as follows:
The sugar containing aldehyde group are classified by writing the word aldo followed by the
general name depending upon the number of carbon atoms in it. For example, glucose
(C6H12O6) is an aldehyde sugar containing six carbon atoms. So, it is classified as an
aldohexose
The sugar containing ketonic group are classified by writing the word keto followed by the
general name depending upon the number of carbon atoms in it. For example, fructose
(C6H12O6) is a sugar containing six carbon atoms. So, it is classified as a ketohexose, Pentose
contains five carbon atoms and aldehyde group so it is names as aldopentose.
12

13

IMPORTANT POINTS TO USE:
ISOMERS: Compounds with the same chemical molecular formula but with different
structures. or compounds with the same chemical formula but atoms in the compounds are
arranged differently. for example, in Triose (C3H6O3) two isomeric structures are possible.
On looking at the structure of glyceral aldehyde more closely you can see that it contains
chiral centre carbon
chiral centre carbon (asymmetry carbon) is a carbon which is bonded to four different
atoms or groups. For example, see figure below.
Molecule which contains chiral centre (asymmetry carbon) is called asymmetry molecule.
Asymmetry of a molecule cause is the cause of the optical activity of such molecule.
Optical activity: Is the property of rotating the plane of polarized light through a certain
angle.
Molecule which because optical activity is called optical active compound
Note: The molecules which cause the rotate the plane of polarized light to toward right is
called dextro –rotatory (+) where as those rotate the plane of polarized left towards left are
called Laevorotatory (-).
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For example
MESOMERISM IN CARBOHYDRATES
THE D AND L ISOMERS
Naturally occurring sugars are in D- isomers and the specific enzyme is responsible for
metabolism of this figure.
For example,
The presence of chiral centre carbon in a compound produce the following effects:
 Give rise to stereoisomerism in the compound
 It confers the optical activity of the compound
STEREOISOMERISM
Stereoisomerism: Are isomers that differ in only in the position of atoms in space. For
example, cis and trans-compound
Cis molecule Trans molecule

A. ENANTIOMER: These are stereoisomers which are mirror image of one another or are
optical isomers.
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B. DIASTREOISOMERS: These are isomers which are not mirror image of one another.
For example, D erthyrose and D threose
ANOMERISM:
Anomers are two isomers which differ only in the configuration of carbon 1- atom and this
carbon 1- atom is called anomeric carbon atom.
For examples: alpha glucose and beta glucose
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The stereochemistry of carbon 1 is very important because carbon -1 involved in the
polymerization of sugars into polysaccharides.
The carbon – 1 can affect the shape of the polysaccharide chain therefore it is of biological
NOTE: Sugars in solution exist in ring form and not in chain form
EPIMERISM: Are isomers formed due to variation in the configuration of OH and H around
a single carbon atom in a sugar molecule.
CONFORMATION (STRUCTURES) OF BIOLOGICALLY IMPORTANT MONOSACCHARIDES

FORMATION OF HEMIACETALS AND HEMIKETAL
Formation of ring structure is the result of general reaction between alcohol and aldehyde or
ketones to form derivatives called hemiacetals and hemiketal which contains additional
asymmetry carbon atom thus can exist in two stereoisomers.
The six membered carbon cyclic (ring) structure of monosaccharide are known as
PYRANOSE since they are similar to six –carbon cyclic and the five carbon membered
cyclic is called FURAN Since they resemble the five-member ring called FURAN
17

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GLUCOSE (C6H12O6)
Glucose is the simplest sugar and main source of energy in our body.
Glucose is an aldohexose. Naturally glucose occurs in foods substances like ripened sweet
fruits (e.g. banana, grapes, pineapples etc.), honey, sweet corn and sold in shop in powder
form.
The ripe grapes contain approximately 20%, glucose. Glucose is known as the grape sugar
or dextrose.
In the combined it is a major component of many disaccharides (e.g. Sucrose, maltose and
lactose) and polysaccharides (e.g., Starch, cellulose and glycogen).
Reduction action. Glucose reduce Fehling’s solution to reddish brown cuprous oxide.
It reduces Cu2+ (blue in colour) from Fehling solution to Cu+ (reddish in colour).
Glucose is the most common monosaccharides in biological system it is easily absorbed
and oxidized in biological system hence act as the major source of energy in form of ATP.
Straight or linear chain of monosaccharide is represented by Fischer Projection formula
but Cyclic or ring structure is represented by Haworth Projection formula.
LINEAR AND RING STRUCTURE OF GLUCOSE.
NOTE: The lower thickened edge of the ring in the Haworth structure is near to the
observer.
During the formation of the ring structure groups projected to the right in fisher projection
formula correspond to the those written below the plane of the ring in Haworth structure,
and those on the left in the Fischer Projection correspond to those written above the plane
of the ring.
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OR
20

THE PYRANOSE AND FURANOSE RING OF FRUCTOSE
FRUCTOSE (C6H12O6)
Fructose is a ketohexose. It is found in fruits and honey. It melts with slight decomposition
at 102 degrees of Celsius. It is twice as ordinary sugar and is a reducing agent.
Note: In ring form fructose can exist as both fructopyranose which is based on six
membered ring and fructofuranose which is based on five membered ring.
FRUCTOPYRANOSE:
21

22

GALACTOPYRANOSE:
OLIGOSACCHARIDES, ESPECIALLY DISACCHARIDES

Disaccharides have a formula of C12H22O11 are carbohydrates formed through condensation
of two monosaccharides. The most common examples of disaccharides are Maltose, Lactose
and Sucrose
They are composed of two monosaccharides units bound together by a covalent bond
known as glyosidic linkage formed via dehydration reaction resulting in the loss of a
hydrogen atom from one monosaccharides and hydroxyl group from another. Although there
are numerous kinds of disaccharides, Sucrose is the main the most abundant disaccharides
and the main form in which carbohydrates are transported in plants. BECAUSE it is a non –
reducing sugar hence chemically very stable it does not react with any materials in phloem
during transport.
PROPERTIES OF DISSASSHARIDES
 They are small molecules made up with two molecules of monosaccharides
 They are sweet
 Readily soluble in water
 Some are reducing sugar for example Maltose, and lactose some are non-reducing
sugar for sucrose
 They are crystalline solid at room temperature
NOTE: Maltose occurs in malt, germinating seed and cereals. Is also called malt sugar. It
is the intermediate product in the breakdown of starch by diastase enzyme found in malt
(sprouted barley seed) and amylase in the alimentary canal
Sucrose mainly found in sugar cane and so is called cane sugar
Lactose occurs mainly in milk and so is called milk sugar
Disaccharides are formed by two monosaccharides through condensation reaction (involve
the removal of water)
23

STRUCTURE OF BIOLOGICALLY IMPORTANT OLIGOSACCHARIDES
Disaccharides are formed by two monosaccharides through condensation reaction (involve
the removal of water)
A: STRUCTURE OF MALTOSE
OR
Maltose is made up of two α -D-glucose units. The linkage in maltose occurs between
carbon – 1 in one ring and carbon – 4 of the second ring the bond formed is called Glyosidic
linkage. This bond in maltose is called α-1,4 – glycosidic linkage (bond)
24

NOTE: Maltose is the reducing sugar because the glucose ring on the right have free
anomeric carbon atom that can open to give free aldehyde group
B: STRUCTURE OF LACTOSE
Lactose is formed by joining β -D – galactose and β –D- glucose through β – 1,4 – glyosidic
linkage.
NOTE: Lactose is a reducing sugar
25

C: STRUCTURE OF SUCROSE
Sucrose is formed by joining α- D – Glucose and Beta – D – fructose through α-1, β -2-
glyosidic linkage.
NOTE: During the formation of sucrose, fructose turns up down causing bond formation to
occur between carbon 1 of glucose and carbon 2 of fructose giving 1-2-glycosidic linkage.
POLYSACCHARIDES
Polysaccharides are polymers of monosaccharides.
They are carbohydrates in which large number of monosaccharides are joined together by
glyosidic linkage.
Upon hydrolysis polysaccharides produce large number of monosaccharides units.
A polysaccharide contains many monosaccharides joined to each other by glyosidic linkage
in a long linear or branched structure.
Common examples of polysaccharides are Starch, cellulose and glycogen other
polysaccharides are like chitin, murein, dextrins.
NOTE: Chitin is found in exoskeleton of arthropods while murein is found in bacteria cell
walls.
Polysaccharides are the most common carbohydrates in nature.
PROPERTIES OF POLYSACCHARIDES
 They are not sweet or tasteless
 They are insoluble in water
 They are non-crystalline solid at room temperature
 Can be linear or branched
 On hydrolysis produce many number of monosaccharides
26

CLASSIFICATION OF POLYSACCHARIDES
Polysaccharides can be classified based on Composition and Based on function
a) BASED ON COMPOSITION
Based on nature of monosaccharides present polysaccharides can be classified as:
 Homopolysaccharies: Made up of single kind of monosaccharides units: e.g. Starch,
glycogen, chitin, cellulose
 Heteropolysaccharides – Made up two or more different monosaccharide derives
for example Glycoproteins, heparin.
BASED ON FUNCTION
Based on function polysaccharides can be classified as:
- Structural polysaccharides for example cellulose, chitin, murein
- Storage polysaccharides for example starch and glycogen
STRUCTURE OF COMMON POLYSACCGARIDES (STARCH, GLYCOGEN AND CELLULOSE)
STARCH (PLANT CARBOHYDRATE)
Starch is a polymer of alpha glucose, tasteless, white amorphous and insoluble in water.
Starch occurs in the form of granules which vary in their size and shape depending upon the
source plant. When boiled with water its granules swell and burst to form a colloidal solution
called Starch paste. Starch solution gives blue colour with iodine solution.
Starch may be obtained from starchy materials such as corn (maize), wheat, sweet potatoes,
rice cassava, Irish potatoes, yams, finger millet etc.
Note: Starch is not a reducing sugar indicating that all hemiacetals hydroxyl groups of
glucose unit (C- 1). are linked with glyosidic linkage.
Starch is a polymer of alpha glucose and consists of two components:
Amylose and amylopectin
Amylose make up about 30 percent of starch and consists of unbraces chains in which the
monomers are joined by 1,4 – glyosidic bonds.
Amylopectin constitutes about 70 percent of starch, consists of chain of glucose monomers
linked with 1,4 glyosidic bonds. It has branches that arise from these chains and are linked to
the main chain with 1,6 glyosidic bonds.
Starch is a food reserve in plants.
27

Figure: Highly branched amylopectin starch
28

GLYCOGEN (ANIMAL POLYSACCHARIDES)
Glycogen is the animal polysaccharide. Glycogen is a branched polymer of alpha glucose.
It is soluble in water.
Glycogen is the short term food reserve found in all animal cells mainly in liver, also is
stored in muscle cells. It gives alpha glucose on hydrolysis.
When the body has shortage of glucose, glucagon hormone converts stored glycogen back to
blood glucose for uses.
Glycogen resembles amylopectin in its structure but one major difference is that glycogen
chains contain about 10-14 glucose units in its chain as compared to about 20-25 glucose
units in amylopectin.
he linkage helps
CELLULOSE
Cellulose is the polymer of beta glucose. Cellulose is the major structural polysaccharides in
higher plants where it constitutes bulk of the cell wall. Over 50% of the total organic matter
in the living world is cellulose. Wood is a combination of cellulose and lignin. Cotton is an
example of almost pure cellulose (99 – 95% cellulose). Cellulose is insoluble in water.
Cellulose is a linear polymer of β - glucose. Many beta glucoses are connected via β -1,4 –
glyosidic bond. Many chains in cellulose run parallel to each other and cross linked between
them. The linkage helps its stability which makes its valuable structure. This structure
prevent cell from bursting when water enter by osmosis and help to determine the shape of
cell depending on the way the layers are arranged.
From the structure of cellulose every second glucose is flipped over (turn over) so that the
formation of β -1,4 –glyosidic linkage creates almost a linear molecule with a rigid shape
Many chains run parallel to each other and have cross-linked between them.
29

You can see from the structural formula how every second glucose unit is flipped over so that
the formation of β – 1,4 – glyosidic linkage creates an almost linear molecule with a rigid
conformation.
OR:
Cellulose is a polysaccharide that is made up of β – glucose. It differs from starch and
glycogen in one major respect. It is made up of monomers of β – glucose rather α – glucose.
This small variation produces fundamental difference in the structure and functions of this
polysaccharides. The main reason for this is that in the β – glucose the –OH group is above
rather below, the ring.
This means that in order to form 1,4-glycosidic link each β – glucose must be rotated by 180
degrees compared to its neighbour. The result is that carbon atom 6 (The one forming the –
CH2OH) on each β – glucose alternates between being above and below the chain. Cellulose
has a straight, unbranched chain which run parallel to one another allowing hydrogen bonds
to form linkage between adjacent chains, while each individual hydrogen adds very little to
the strength of the molecules. The alignment of chains and the bonding between them are
responsible for high mechanical strength of the cellulose.
30

Other polysaccharides are like Chitin, murein, agar etc.
ROLES OF CARBOHYDRATE IN LIVING ORGANISMS
31

Another source
LIPIDS (FATS AND OIL AND WAXES)

Lipids are organic food substances which contains carbon (C), hydrogen (H) and oxygen
(O).
Lipids are ester of higher aliphatic alcohols
NOTE: Lipids may contain other elements like sulphur and nitrogen. The most common
lipids are Fats and oil. For example
Fats: Normally found in animals for example beef fat
Lipids: Normally found in plants e.g. corn oil, sunflower oil, coconut oil, ground nut oil
and palm boil, avocado oils etc.
So natural food source of
Fats: meat
Oils: Coconut seed, avocado, corn ground nut seed, palm oil seed, sunflower seed,
fish etc.
NOTE: oil may be found in some animals for example fish oil. Some fats are found in plants
for example cocoa butter.
COMPONENTS OF LIPIDS (FAT and OIL)
Fats and oil are made up of two chemical compounds which are GLYCEROL and FATTY
ACID
Lipids are formed by condensation reaction between GLYCERAL and FATTY ACID
32

GENE-RAL PROPERTIES OF LIPIDS
 Lipids are relatively insoluble in water
 They are soluble in non – polar solvent like ether, chloroform and methanol
 Some are solid at room temperature for example fat other are liquid at room
temperature for example oils
 Lipids have greasy feeling in nature
 Are bad conductor of heat so act as insulator they are found below adipose tissue of
the skin and around of the axon of myelinated neuron.
 May be saturated or un saturated
 On hydrolysis produce glycerol and fat acid
 Produce more energy in form of ATP and metabolic water than carbohydrates and
proteins because have more number of hydrogen atoms than carbohydrates and
proteins.
 Form emulsion when mixed with water. Emulsification is the breakdown of lipid
mass into small lipid droplets.
QN: Explain why birds can fly across the countries without drinking water
How animals living in the extreme cold climatic conditions are adapted to prevent heat loss?
NOTE: Oil are liquid at room temperature while Fatty acid are solid at room temperature.
CLASSIFICATION OF LIPIDS
Generally:
Lipids are classifying as:
 Simple lipids
 Complex lipids and
 Steroids
Note: Lipoids though not true are included here they resemble fats in physiological
properties and extracted with fat solvents. Carotenoids are sometimes included with lipids.
33

COMPONENTS OF FATS AND OIL
Each molecule of fat or oil is composed of two components which are:
 Glycerol and
 Fatty acids
GLYCEROL/GLYCERINE
Glycerol has a back born of three carbon atoms each carrying hydroxyl group (OH)
Molecular formula of glycerol is (C3H803)
insert
PROPERTIES OF GLYCERAL
 They are liquid with sticky
 They are colourless and odourless
 They are sweet
FATTY AC IDS
Are organic acid of hydrocarbon. They contain hydrogen and carbon atoms in their chain but
their molecules end up with carboxylic group – COOH which is responsible for acidic nature
of fatty acid.
Are carbon chains with methyl group at one end and carboxylic group at another end.
Fatty acid may be saturated or unsaturated
SATURATED FATTY CID
Have single bond in their chain
Forms fats examples of saturated fatty acids are stearic acid in animals
They are solid at room temperature, have high melting point
Note: The most abundant saturated fatty acids are stearic acids and palmitic acid. Stearic
acid is the one constitutes the Adipose tissues.
UNSATURATED FATTY ACID

Have one or more than one double bond between carbon atoms in their chain
Presence of double bond lower melting point so they are liquid at room temperature
They form Oil
34

Examples of Unsaturated fatty acids are Linoleic acid which is one of the essential Fatty
acid in our deity since our body cannot synthesize it. It is obtained from the deity we eat.
NOTE: Unsaturated fatty acid may be monosaturated – if contains one double bond in
their chain or polysaturated – if contains more than one double bonds in their chains.
Polyunsaturated fatty acid. Contains two or more than two double bond in their chains. For
example
35

FORMATION OF LIPIDS
OR
Lipid is formed by combining Glycerol and three fatty acid molecules through an ester
bond.
Bond formation involves the removal of water (Condensation reaction)
SIMPLE LIPIS
For example, WAXES
Waxes are formed by a combination of fatty acid with an alcohol other than Glycerol. The
alcohol used is much larger than glycerol. Waxes have a complex chemical structure.
36

For example, bee wax is an ester compound formed by combining palmitic acid with an
alcohol containing 30 Carbon atoms.
PROPERTIES OF WAXES
 Waxes are closely packed together
 Are chemically in active because their chain lack double bond
 Contains other alcohol than glycerol
 They are insoluble in water and difficult to hydrolyse
 They are solid at room temperature
FUNCTIONS OF WAXES
 Act as water proofing in plants and animals.
 Act as food storage in few organisms e.g. in castor oil
 Provide habitat for living organisms for example bee waxes
 Used for making candles
 Used for external drugs as an ointment e.g. Linolin wax from sheep
COMPLEX LIPIDS (COMPOUND LIPIDS)
Examples: Phospholipids and Glycolipids
PHOSPHOLIPIDS
37

Figure: Phospholipids
FUNCTIONS OF PHOSPHOLIPIDS
 Structural role, they are major components the cell membrane
 They are source of choline used during transmission of nerve impulse
GLYCOLIPIDIS
Are lipids which are associated with carbohydrates. In the structure of glycolipid
carbohydrates form a polar head of the molecule.
FUNCTION OF GLYCOLIPIDS
 Structural components of the cell membrane
STEROIDS
Steroids are monohydroxyl alcohols found in animals.
Do not contain fatty acid yet they are classified as lipids or are related to lipids. The best
known steroids are cholesterol and terpenes.
NOTE: Steroids are based on a structure composed of four rings.
The formula of the steroids oestrogen, testerone and cholesterol are given below.
Note: Progesterone and cortisone are steroids.
- Cholesterol is often esterified in the body to form a waxy material. It is obtained from
deity for example egg – yolk, butter milk and liver but the body can synthesize it from
the carbohydrates and proteins. Cholesterol is abundant in the brain, adrenal cortex
and sex glands, it is also present in small amount in blood and in the walls of some
blood vessels. It is said to be associated with some vascular disease such as
thrombosis and hardening of the arterioles.
- Cholesterol is an important of the cell membrane. From cholesterol animals
synthesize other steroids including vitamins D and bile acids.
38

- Food that rich in cholesterol promotes strokes and heart attacks.
FUNCTIONS OF STEROIDS.
 Produce sex hormone e.g. testerone and oestrogen
 Found in myelin sheath help in nerve impulse transmission
 Source of vitamin D
39

 Components of the cell membrane example cholesterol
ROLES OF LIPIDIS AS IMPORTANT COMPONENT OF THE CELL MEMBRANE
THE FLUID MOSAIC MODEL OF THE CELL MEMBRANE
Cell membrane contains lipids and proteins. The phospholipids which are chiefly
present in the cell membrane are phospholipids.
The correct phospholipid by arrangement is
THE FLUID MOSAAIC MODEL OF THE CELL MEMBRANE

Cell membrane is a semipermeable membrane surrounding the cytoplasm of a cell.
The fluid mosaic model of a cell membrane state that the cell membrane consists of a bi-
layer of phospholipids molecules in which protein molecules are imbedded. The two bi-
layer of cell membrane are arrange in a such a way that the head which is polar and hydro-
philic (attract or love water) point outside while the tail which non-polar and hydrophobic
(repel water) points in side, some proteins in cell membrane are intrinsic (integral) these
run through the cell membrane from one surface of the membrane to another, and some pro-
teins are extrinsic (peripheral) these are found outside or attached to the surface of the
membrane (or associate with cell membrane outside). Some carbohydrates associates with
the phospholipids to form glycolipids, also some carbohydrates associates with proteins
in the cell membrane to form glycoprotein. The membrane contains cholesterol and protein
channels.
40

Fig: Fluid mosaic model of the cell membrane
FIG: The fluid mosaic model of the cell membrane
Or
41

Fig: The fluid mosaic model of the cell membrane
42

GEERAL FUNCTIONS OF LIPIDS
or
- Are source of bouyans (provide ability to float in water) – lipid is less dense than
water hence it is used as bouyans of aquatic vertebrates such as shark and whale.
- Prevent water loss in plants and animals for example insect have wax cuticle to
prevent evaporation and reduce transpiration in plants.
43

QN: 2. DESCRIBE THE FLUID MOSAIC MODEL OF THE CELL MEMBRANE
AMINO ACIDS AND PROTEINS
Amino acids are building blocks of proteins.
The carboxylic acid containing amino (- NH2) attached to any carbon atoms other than the
carboxylic carbon are called Amino acid.
The naturally occurring amino acids however containing amino group (– NH2) attached to
only alpha carbon atom (Carbon atom adjacent to the – COOH groups).
Figure: Structure of amino acid

With exception of two amino acids contained at least one amino - NH2 and one carboxylic –
COOH) group. Amino acids are soluble in water where they form ions.
Ions are formed by the loss of hydrogen ions from the carboxylic group, making it
negatively charge. This hydrogen atom associates with the amino acid group making it
positively charged. The formed ion is therefore Dipolar having negative and negative pole
such ion is called ZWITTER ION.
FORMATION OF ZWITTER ION
Amino acid contains both an acidic carboxylic group (- COOH) group a basic amino group (-
NH2) group loses a proton to form carboxylate (- COO-) ion and the amino (- NH2) group
gains one proton to form +NH3 ion. Thus in aqueous solution, amino acid molecule exists as
dipolar ion, such a dipolar ion of amino acid is called zwitter ion.
44

Note: Amino acids are amphoteric (having both acidic and basic properties) being
amphoteric means that amino acids acts as the buffer solution.
Buffer solution is the solution that resist to alter its pH even when small amount of acid or
alkali are added to it. Such property is essential in biological system where any sudden
change in pH could adversely affect the performance of enzymes.
Amino acid in the dipolar ions form are amphoteric i.e. amino acid in zwitter form can
react with both acid and bases.
In aqueous solution amino acid can react as.
 An acid, a proton donor
 A base, a proton acceptor
NOTE: The higher the pH The more the ionisation (1) occurs. The lower the pH the more
the ionisation (2) occurs. There is certain pH at which two ionizations are exactly balanced
and the amino acid is entirely in the form of the of the zwitter ion, this pH the isoelectric
point. There is no net charge on the amino acid at this pH, and the dipolar ion will not
move in electric field.
THE D – AND L – CONFIGURATION OF AMINO ACIDS
The alpha carbon of all amino acid except glycine is asymmetric (chiral). A s the result all
naturally occurring amino acids except glycine are optically active can exist in two
stereoisomeric form i.e. D and L forms.
The two stereo isomeric forms are mirror image of each other
Assignment of D – and L – configuration is done with reference to glyceraldehyde as shown
below:
NOTE: A all naturally occurring amino acids are L – isomer. Proteins consists of only L –
amino acids.
Fischer projection formula of amino acid are written with – COOH at the top. When NH2 is
on right hand side of alpha carbon of the amino acid the amino acid is called D – amino acid
but when is on left hand side of the alpha carbon atom of amino acid the amino acid is called
L – amino acid.
45

CLASSIFICATION OF AMINO ACIDS
Depending on the relative number of amino (- NH2) and carboxylic (- COOH) groups the
amino acids are classified as acidic, basic and neutral
 Acidic amino acid, when the number of carboxylic group is larger than amino
group in any molecule of amino acid
 Basic amino acid, when the number of – amino group is large than the number of
carboxylic group molecule of amino acid
 Neutral amino acid, when the number of carboxylic group is equal to the number of
amino group molecule of amino acid.
ESSENTIAL AND NON ESSENTIAL AMINO ACID
This is the classification of amino acid based on diet criteria.
In 26 different alpha amino acids which have been isolated out of these 20 amino acids are
required for protein synthesis. The human body can synthesize only 10 amino acids. These
10 amino acids that can be synthesized in our body are called Non – essential amino acids
so the remaining 10 amino acids are obtained in diet we eat; these amino acids are called
essential amino acids.
NON ESSENTIAL AMINO ACIDS (DISPENSABLE AMINO ACIDS)
Non-essential amino acids – are amino acids that are required by the body in small amount.
They are obtained in our diet we eat and cannot be synthesized in our body.
Deficit of these amino acids does not necessarily result into nutritional disorder.
ESSENTIAL AMINO ACIDS (INDESPENSABLE AMINO ACIDS)
Essential amino acids are amino acids that are requires by the body in large quantity.
Are obtained in diet and cannot be synthesized in our body, they have crucial role in the
physiological functioning of the body such as growth and development. Deficit of these
amino acids leads to malnutrition disorder such as kwashiorkor in children which
associated with change in skin, hair colour, oedema (Swelling of ankles, feet, bell)
46

NOTE: Based on essential and non-essential amino acids proteins are classified as:
ANIMAL PROTEINS: Obtained in animals contains most of essential amino acids than
plants, therefore are described as first class proteins. For example, are obtained in meat,
fish, egg etc.
PLANT PROTEINS: Obtained in plants, contains most of non-essential amino acids and
they are described as second class proteins.
PEPTIDES AND PEPTIDE BOND
PEPTIDES
Peptides are compound formed by the condensation of two or more same or different
amino acids through peptide bond.
During the formation of peptides, the amino (- NH2) group of one alpha amino acid and
carboxylic (- COOH) group of another molecule of the same or different alpha amino acids
group are condensed with the elimination of water molecule. During condensation a bond of
type – CONH is formed between the two amino acids. This amide linkage the type - CONH
is called a PEPTIDE LINKAGE or PEPTIDE BOND or AMIDE LINKAGE.
NOTE: The peptide formed due to the condensation of only two molecules of the same or
different amino acid is called DIPEPTIDE.
47

POLYPEPTIDES
Polypeptide is a peptide containing very large molecules amino acids.
NOTE: Peptides, polypeptides and proteins are the universal constituents of the biosphere.
They are responsible for the structural and functional integrity of the cell. They differ from
one another by the number and sequence of the constituent amino acids. Generally, a
molecule comprised of few amino acid is called an oligopeptides and that with many amino
acid is a polypeptide (molecular weight below 10 000). Proteins contains a large number of
amino acid
CHARACTERISTICS OF PLOYPEPTIDES
 Are amphoteric – can be titrated as the base or acid
 Each has its own isoelectric point
 Most are toxic in venoms and in plants sources. Minimum quantity of some
oligopeptides with as few as three modifies amino acids are effective hormones.
Some biological important peptides are:
a) Oxytocin it is nanopeptide
b) Vasopression it is also nanopeptide
c) Angiotensin it is an octapeptide
48

NOTE: Dipeptides have free functional both the ends. These free functional groups can
further react with relevant group of the other amino acids forming higher peptides.
A peptide is called tripeptide or tetrapeptide depending upon if it is obtained by
condensation three or four amino acids molecules respectively.
A peptide containing very large number molecules of amino acids residue is called
polypeptide. The shorter polypeptides are called oligopeptides.
The polypeptide containing very large number of amino acid is known as PROTEINS
however the distinction between a polypeptide and a protein is not sharp.
STRUCTURE OF POLYPEPTIDES
The main chain of amino acids which make up a polypeptides have a specific three
dimensional shape. This shape is important in the functioning of the proteins especially
enzymes. The shape of polyketide molecule is due to four different bonding which occur in
between various amino acids in chain.
 Disulphide bond: Arise between sulphur containing groups on the two cysteine molecules.
May arise between cysteine molecules in the same amino acid chain (intra chain), or between
molecules in different chain (inter chain).
 Ionic bond: Amino acid form zwitter ion which have NH3+ and COOH- groups. formation of
peptide bonds when making a polypeptide means that the COOH- and NH2 are not available to form
ion. In the case of acidic amino acids however there are addition of COOH group which may ionize to
give COO-. In the same way basic amino acids may still retain NH3+ group even when combined into
the structure of the polypeptide. In addition, NH3+ and COOH- can occur at the ends of a polypeptide
chain. Any of these available NH3 and COOH groups may form ionic bonds which help to give a
polypeptide molecule its particular shape. These ionic bonds are weak and may be broken by
attractions of pH of the medium around the polypeptide.
 Hydrogen bond: Occurs between certain hydrogen atoms and certain oxygen atoms within the
polypeptides chain. The hydrogen atoms have small positive charges on them (electropositive) and
oxygen have a small negative charges (electronegative). The two charged atoms are attracted together
and form a hydrogen bond. While each bond is very weak the sheer number of bonds means that they
play a considerable role in the shape and stability of a polypeptide chain.
 Hydrophobic interactions: These are interactions between non-polar R groups. These cause the
proteins to fold as hydrophobic side groups are shielded from water.
PROTEINS AND THEIR CLASSIFICATION

Proteins are the polymer of amino acids or are very large molecules of amino acids joined
together via peptide bond.
Proteins are organic food substances that contains chemical elements like carbon, hydrogen,
oxygen and nitrogen. Sometimes they may contain sulphur and phosphorous.
NOTE: The amino acids of proteins differ in nature of the side chain of group (R). The
property of any amino acid depend on the nature of the side chain in it.
49

STRUCTURE OF AMINO ACIDS
Amino acids are the structural unit from which proteins are assembled. The amino acid which
are found in proteins have the amino group attached to the alpha carbon atom (2 – carbon
atom), that is the carbon atom next to the carboxylic group and are therefore named as alpha
amino acids each amino group has a different R group.
The R group may be:
Non – polar and hydrophobic (water hating) E.g. H in glycine and CH3 in alanine
Uncharged and hydrophilic (water loving) e.g. CH2OH in Serine, CH2SH in cysteine
Negatively charged at PH 6 – 7 e.g. CH2CO2H in aspartic acid.
Positively charged at PH 6 – 7 e. g (CH2)4NH2 in lysine.
The alpha carbon atom is asymmetric. In all alpha amino acids except in glycine. There are
two possible stereoisomers foe example in alanine (H2NCH(CH3) CO2H
NOTE: Proteins are formed via condensation reaction of amino acids and on hydrolysis
proteins produce amino acids.
50

GENERAL PROPERTIES OF PROTEINS
 They are colourless and tasteless
 They are partially soluble in water but they form suspension. They can be crystal in
and out of the body.
 They are macro molecules of many monomers of amino acids e.g. egg albumin has
molecular mass of 40,000.
 They perform specific functions e.g. enzymes, hormones
 They are amphoteric (can react both as an acid or a base)
 They can be hydrolysed by enzymes or minerals giving different amino acids and
usually ammonia.
 Mainly exists as ions and carry both positive and negative charges on basic and
acidic part respectively such ion is called Dipolar ion or zwitter ion
 They undergo denaturation, which usually followed by coagulation
 They have variable shapes; they may be simple crystalloid structure to long fibril
structure.
 Their solubility depends on the PH such that solubility increases with increase in
acidity or alkalinity.
 Reacts with corresponding alcohols to give its corresponding esters.
 Free amino acids of proteins react with mineral acids like HCL to form acidic salt.
CLASSIFICATION OF PROTEINS
Proteins can be classified in different ways; these are described below:
CLASSIFICATION OF PROTEINS ON THE BASIS OF CHEMICAL COMPOSITION
Broadly proteins can be classified into three classes depending upon their chemical
composition.
Simple proteins: are proteins which are made up of only alpha amino acid.
Examples: Albumin (in the white eggs), glutenin (in wheat), Keratin (in hair and nails) are
typical simple proteins.
Conjugated proteins: Are proteins which contains other organic and inorganic compounds
in addition to the amino acids. The non-amino acid group is called prosthetic group.
Prosthetic group control biological functions of proteins.
Conjugated proteins are further classified as:
a) Lipoproteins: Contains lipids and amino acid, the prosthetic group in lipoproteins is a
lipid such as, Lipovitelline of egg yolk, serum.
b) Nucleoproteins: Contains nucleic acids in addition to amino acids. Thus the
prosthetic group in nucleoproteins is nucleic acid.
c) Glycoproteins (mucoproteins): Contains amino acids and carbohydrate group in
their molecule the prosthetic group is a carbohydrate. Example mucin of the saliva is
a glycogen.
51

d) Chromoproteins. Contains amino acid and coloured pigments in their molecules,
example haemoglobin, haemocyanin, cytochrome and riboflavin.
e) Phosphoproteins: Contains amino acids and phosphate group in their molecules. the
prosthetic group is phosphate group. Example casein of milk, ovovitellin of the egg.
Derived proteins. The degradation products obtained from the partial hydrolysis of simple
or conjugated proteins is the derived proteins. Example Proteoses, peptones and
polypeptides
CLASSIFICATION OF PROTEINS ON THE BASIS OF MOLECULAR STRUCTURE
On the basis of molecular structure proteins are classified as follows:
 Fibrous proteins: Consists of linear, thread like polypeptide chains which are
arranged or twisted to form long strand (fibres). Polypeptide chains in fibrous
proteins are held together by hydrogen bonds. As a result, the intermolecular forces of
attraction in fibrous proteins are very strong. These are insoluble in water, and quite
stable. example collagen of tendon, Keratin of skin, hair, nails and wool, Fibroin
in silk, myosin in muscles.
 Globular proteins: Are proteins in which polypeptide chains are very tightly folded
into a compact, spherical form. They are water soluble, very sensitive in
temperature and pH. Examples: All enzymes, many hormones such as insulin,
antibodies, haemoglobin, fibrinogen, albumin and venoms of snakes, scorpion,
wasps and bees.
DIFFERENCES BETWEEN GLOBULAR AND FIBROUS PROTEINS
Globular proteins Fibrous proteins
-Have folded ball like structure -Have thread like structure
Soluble in water, acids bases -Insoluble in water, acids, bases
-Have weak intermolecular hydrogen -Have comparatively stronger
bond intermolecular forces
-Have three dimensional shape e.g., egg -Have helical or sheet structure e.g.,
albumin, casein of milk skin, silk, wool.
CLASSIFICATION OF PROTEINS ON THE BASIS OF SOLUBILTY.

On the basis of solubility, the proteins are classified as follows:
 Albumins: Are soluble in water, dilute salt solutions, dilute acids and bases. May
coagulate on heating. Example: Egg albumin, serum albumin and milk albumin
 Globins: Are highly soluble proteins. These can also dissolve in ammonium
hydroxide. Example: Haemoglobin
 Protaminase: Are highly soluble proteins which can be dissolved in ammonium
hydroxide example. Examples: Proteins of fish sperm.
 Histones: Are soluble in water but insoluble in ammonium hydroxide. These do not
coagulate on heating. Example: Nucleoproteins
 Prolamines: These proteins are insoluble in water but soluble 70% ethyl alcohol.
Example: Gliadin of wheat, zein of corn and hardein of barley.
52

 Scleroprotein: Are insoluble in water as well as in all neutral solvents. Example:
Keratins, Collagen of tendon,
CLASSIFICATION OF PROTEINS ON THE BASIS OF FUNCTIONS
Proteins can be classified on the basis of their functions as follows:
 Structural proteins: Are fibrous proteins, most abundant proteins the most familiar
of fibrous proteins are probably keratins, which form the protective covering of
skin, fur, hair, nails, hooves, horns, scales beaks and feather. Also collagen
fibrous proteins which are found in various types of connective tissues such as
cartilage, tendons, bones and ligaments.
 Contractile proteins: These are proteins necessary for all forms of movements.
Muscles contains filament like contractile proteins that, in response to nerve stimuli,
undergo conformation change that involves contraction and relaxation for example
Actin and myosin.
 Hormones: are chemical regulators secreted by endocrine gland or ductless gland.
For example, insulin hormone
 Enzymes: Are complex protein, used as biological catalyst produced in living cells.
For example: Amylase, Invertase, Urease, Pepsin, Trypsin, Nucleases,
 Antibodies (immunoglobulins): These are defensive proteins, which are central to
the functions of the body’s immune system. example is serum glycoproteins.
 Blood proteins (Transport proteins): for example, Haemoglobin: It helps in the
transport of oxygen
LEVELS OF PROTEIN ORGANIZATION
(STRUCTURES OF PROTEINS)
There are four (04) basic structural levels of proteins, these are:
 Primary structure of proteins: This is structure of polypeptide chain having a linear
sequence of amino acids due to polypeptide bond. For example, insulin
 Secondary structure of protein: Is the structure or shape of proteins when
polypeptide chain of amino acids become coiled. It results in the formation of a rigid
and tubular structure called helix. The hydrogen and sulphide are involved to hold the
protein chain in the spiral manner.
or Is the way in which primary structure folds. In structure they form fibres e.g.,
Keratin found in hair, and feathers is two stranded alpha helixes where as keratin
found in silk is a beta pleated sheet.
 Tertiary structure of proteins: Is the structure of protein arise due to folding and
super imposition of various secondary structural element. or is the conformation
(structure) when the chain or sheet of protein are further coiled. or Refers to the
arrangement of secondary structure into three dimensional (fold or super) structure
having peptide, hydrogen, ionic and disulphide bond. The two molecular structure
are fibrous and globular.
Generally: Alpha helical structures and beta pleated structures folds and coil to form
a shape called tertiary. In globular proteins folding is more extensive to give a more
compact tertiary structure e.g., enzymes and hormones.
53

 Quaternary structure of proteins: Is the structure of proteins due to the association
of sub units of proteins structure (polypeptide chain). or is the structure of proteins
made up polypeptide chains locked together.
Many proteins contain molecules consists of two or more polypeptide chains. These
are called oligo metric proteins. e.g., Haemoglobin is oligo metric proteins. The
molecule consists of four sub units. The manner in which sub units are grouped to
form the protein are called quaternary structure of protein. The term also is used to
describe binding of a polypeptide to a non-protein component in a protein structure
unit. The iron (ii) ions in the haem groups bind oxygen and enable haemoglobin to
form its functions of transporting oxygen round the body.
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Fig: Levels of protein organization
PROTEIN DENATURATION
Protein denaturation: Is any change that alter the unique structure of protein
molecule without causing cleaves of peptide bond.
Or Is a process which leads to the change in physical and biological properties
protein without affecting its chemical composition.
For example, when most globular proteins are subjected to temperature above 60 to
70 degree of Celsius become insoluble and lose their biological activity e.g., Egg
white coagulates on heating this is called denaturation of proteins and this
denaturation is irreversible. Denaturation causes changes in the secondary, tertiary
and quaternary structure of protein but the primary structure remain undisturbed.
Note: Denaturation may be permanent or temporary but acidic sequence of
proteins remain unaffected. If denaturation occurs the molecules unfold and can no
longer perform their its biological functions. In some cases, if the factor that causes
denaturation is removed the protein recover its normal physical, chemical and
biological activity, this is called renaturation.
55

FACTORS CAUSING PROTEINS DENATURATION
Denaturation of proteins is caused by the following factors:
Change in pH.
pH is a measure of hydrogen ion concentration. Any change in pH can affectively
denature proteins. Strong acid increases the H+ ions which combine with amino acid to
form the COOH and hence the ionic bonds are broken down e.g., in souring milk by
lactobacillus bacterium produces lactic acid which coagulates by covering pH and
makes milk protein insoluble.
Strong alkalis reduce the relative number of H+ of hydrogen ions and cause NH3 to lose H+
and form NH2 and hence ionic bonds are broken down and cause the proteins to coagulate.
Temperature / heat and ultra – violate rays.
Increasing the kinetic energy to proteins molecules cause the atoms to vibrate more rapidly
and cause the weak hydrogen bonds to break down and change the unique configuration of
protein molecules e.g., Boiling of eggs cause the protein to coagulate or solidify thus
changing from liquid to solid or fibrous and less soluble.
Concentration of heavy metals e.g., Ag, Hg and Pb. The ions of mercury and silver are
highly electropositive and strong bonds with negatively charged carboxylic group and
disulphide ionic bond. Although the electropositive ions e.g., cyanide combine with NH3+
group and disrupt the ionic bond
Metals reduce the protein electrical polarity (overall positive and negative charges) and
increase its solubility. This cause protein to precipitate out of the solution.
Organic solvents and detergent e.g., Alcohol. Disrupt hydrophobic interaction and form
bonds with hydrophobic (non-polar) group. This in turn causes the disrupt of hydrogen bonds
that is why alcohol e.g., alcohol is used as disinfectant in cleaning the skin before infection
since its function is to denature the protein and any bacterial present.
Mechanical forces. Physical movements may break hydrogen bonds e.g., stretching of hair
breaks the hydrogen bonds in the keratin helix.
Enzyme inhibitor. Enzymes are very sensitive to catalytic poisons (inhibitors) some typical
poisons are HCN, H2S, CS2 etc. enzymes lose their activity in presence of these substances
because these molecules tend to get adsorbed on the surface of enzyme strongly.
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ROLES OF PROTEINS IN LIVING ORGANISM
Act as the major structural materials of animal tissues e.g., collagen in tendon, keratin in
skin, hair, nails and feather, Myosin in muscles.
Natural body defence for example antibodies defend body against entry of antigen into the
body systems.
Transport and storage. For example, haemoglobin present in blood is used for transport of
oxygen from lungs to other tissues of the body while myoglobin is used to store oxygen in
muscles.
Help in blood clotting for example Fibrinogen and thrombin are involved in the blood
clotting
Source of hormones. Many proteins are hormone in nature for example insulin hormones
regulate blood sugar.
Act as food reserve for example oval egg albumin of egg white and casein of milk. Oval egg
white albumin is a source of food for growing children, white casein provides nourishment
for young new born mammals.
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Source of biological catalysts (Enzymes). All enzymes found in living organisms are
protein in nature. For example, salivary amylase catalyses the hydrolysis of starch to maltose.
Are major building blocks of body, they activate cell division used for growth and needed
more in young as well as expectant and nursing mothers.
Provide transport carrier across the plasma membrane for example channel and carrier
proteins are involved in the selective transport of polar molecules and ions across the cell
membrane.
Are used by the body to regenerate worn out cells and tissues
THE NATURE AND PROPERTIE OF ENZYMES
Enzymes (Gr: En = in, zyme = yeast). The role of yeast in converting sugar to alcohol is the
earliest recorded example of enzymes.
Life would not be possible without metabolic activities of the cell. This in turn it depends
upon the catalytic molecules called enzymes, without enzymes the dynamic, steady state of
the cell would cease to exist.
Enzymes: Are biological catalysts that speed up the rate of chemical reaction of life without
changing at the end of the reaction.
Enzymes are organics substances that are capable of catalysing specific chemical reactions in
living systems.
Enzymes are proteins that catalyse the biological reactions.
NOTE: The sum of all the chemical reactions going on in cells are known as a
METABOLISM.
Metabolism is divided into two types of reactions
Anabolism is the synthesis of macromolecules from simple molecules usually require energy
and involve condensation reaction (removal of water) - e.g. formation of starch from
glucose, and proteins from amino acids.
Catabolism is the cleavage or splitting of macromolecules into small molecules usually
release energy and involve condensation reaction e.g., Splitting of starch into glucose etc.
All reactions in living cells are catalysed by enzyme. The enzyme which work in side of cell
are called intracellular or endo enzymes e.g., enzymes in respiration and photosynthesis
and those which act out side of the cells is knowns as extracellular or enzymes e.g. Digestive
enzymes.
PROPERTIES OF ENZYMES
Enzymes are protein in nature and their properties should reflect those of proteins.
Biological catalysts. Made up of globular protein with a specific tertiary structure.
Very efficient. They speed up reaction up to 10 million times compared to the uncatalysed
reaction. Very small quantity of any enzyme is needed for catalysing a chemical reaction for
example the enzymes renin coagulates over million times its own weight of milk protein
during cheese making
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Specificity, enzymes catalyses specific reaction. Each enzyme catalyses a particular reaction,
however most of extracellular enzymes work on a wide range of substrate. For example,
invertase enzyme can break up sucrose into glucose and fructose but fail to break up a very
similar disaccharide maltose. Maltose require another enzyme called maltase.
Sensitive to temperature change, enzymes work best in optimum temperature, temperature
above optimum enzymes are denature and temperature below optimum enzymes become in
active because of kinetic energy, for example optimum temperature in human being is 37
degrees of Celsius.
Sensitive to pH (hydrogen ion concentration), every enzyme has got its own pH in which it
works more properly. Some enzymes work better in acid medium while others work better in
basic medium. Excess or less pH cause enzymes not to work properly.
Lower activation energy, which is the energy required for a specific chemical reaction to
occur.
Speed up or slow down metabolic reactions but never used up in the reaction.
The enzymes catalysed reaction is reversible and the direction of reaction depends on the
amount of substrate and product.
Enzymes are colloidal in nature due to thus reason the produce large surface area the
reaction to take place.
Enzymes possess active site where the reaction takes place, these sites have specific shape.
ENZYMES STRUCTURE AND FUNCTIONS
Enzymes have complex three dimensional globular proteins structure, some of which
have other associated molecules.
Enzymes are larger than the substrate molecules it acts upon, only a small part of enzymes
molecule actually comes into contact with the substrate. This region is called the active site
Only a few of the amino acids of the enzyme molecule make up the active site. These are
so called catalytic amino acids are often some distance apart in the protein chain but brought
into close proximity by the folding of the chain.
Insert:
ENZYMES AND ACTIVATION ENERGY
Activation energy is the energy required for a specific reaction to occur.
Before reaction takes place it must overcome an energy barrier by exceeding its
activation energy. Enzymes increase rate of chemical reactions by lowering activation
energy. For example, when urea is hydrolysed in presence of in presence of H+ the
activation energy is 104 Kjmol-1, while when urea is hydrolysed by urease the activation
energy is only 29 Kj-1as heat is the source of activation energy enzymes often dispense with
the need for this heat and allow reaction to take place at lower temperature.
Many reactions which would not ordinarily occur at the temperature of an organisms do so
readily in the presence of enzymes.
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MECHANISM OF ENZYME ACTION (Mechanism of enzyme catalysis)
Enzymes accelerate reaction by providing reaction path way which involve lesser activation
energy. In 1994, Emil Fischer suggested Lock and Key hypothesis to explain the action of
enzymes –catalysed reactions. This hypothesis is still acceptable but in the modified
(modern interruption of the lock and key) as induced fit hypothesis.
There are two major hypotheses (model or theories) about the enzyme action
Lock and Key hypothesis or model
Induced fit hypothesis or model
60

LOCK AND KEY MODEL OF ENZYME ACTIVITY
Substrate shape is directly complementary to the shape of the active site, with the enzyme
acting as the lock and the substrate molecule as the key. or only the correctly sized key
(substrate) fits into the key hole (active site) of the lock (enzyme).
The active site has a rigid shape
Only substrates with the matching shape can fit into the active site of the enzyme.
Note: This is the old model, does not explain clearly the action of enzymes.
NOTE: Active site of an enzyme is region (cavity or hole) within an enzyme where substrate
binds. or Is a depression in enzymes tertiary structure that allows specific substrate to enter.
Substrate is a reactant molecule catalysed by an enzyme.
INDUCED FIT MODEL OF THE ENZYME ACTION
Not all enzymes have a permanent active site. In some develops as substrate molecule
come close with a small change occurring in the enzyme to form a specific active site
The active site is flexible
61

The shape of the enzyme active site and substrate adjust to maximize the fit, which improve
catalysis. There is a great range of substrate specificity. This model is more consistent with
wide range of enzymes.
62

63

FACTORS GOVRNING ENYZYEM ACTIVITY
(Factors affecting rate of enzyme reactions)
Four major factors which affecting an enzymes activity are:
Temperature, the rate of an enzyme activity will increase with increasing temperature up to
an optimum temperature, as the temperature increasing the kinetic energy of enzyme and sub-
strate increase and so they move faster. The faster moving molecules collide more often
forming more enzyme-substrate complex. The temperature above an optimum cause an en-
zyme denaturation by breaking hydrogen bonds and other forces which hold molecule which
hold the molecule in their price shape. The active sites lose its shape and will no longer func-
tion and temperature below an optimum cause the enzyme the enzyme to be inactive and
show very slow
64

THE GRAPHY TO SHOW EFFECT OF TEMPERATURE ON ENZYME ACTIVITY
rate of chemical reaction. The optimum temperature for an enzyme activity in human being is
370C
Or Enzymes work in a narrow temperature range. There is an optimum temperature for each
enzyme reaction. Temperature above or below the optimum reduce the enzyme activity.
Change in PH the rate of an enzyme activity is faster at optimum PH. The amino acids with
acidic or basic side chain have proper charges when the PH is optimum. Changing the PH
that is increasing or decreasing cause the changes of in the charge of enzyme amino acidic
components. This alter attraction and repulsion of enzymes within the enzyme disrupting the
shape of active site (enzyme denatured). The precise three-dimensional molecular shape
which is vital to functioning of enzymes is partly the result of hydrogen bonding, these bonds
may be broken down by the concentration of hydrogen ions present.
Or The enzymes work within a narrow range of PH potential hydrogen atoms. There is an op-
timum at which each enzyme works more efficiently. A PH which is more acidic or alkaline
than the optimal one reduces enzyme activity or may result in enzyme denaturation. Most en-
zymes of the human body have an optimum PH about 7 or 7.4 (Neutral PH). Although some
digestive enzymes work better in low PH or higher PH. For example, pepsin enzymes have
their optimum rate in more acidic condition.
65

THE GRAPHY TO SHOW THE EFFCT OF CHANGE IN PH ON ENZYME ACTIVITY
66

THR GRAPH TO SHOW EFECT OF PH CHANGE ON ENZYME ACTIVITY.
Substrate concentration the rate of enzyme activity or reaction increase with increasing sub-
strate concentration until a plateau or maximum rate of reaction is reached. Maximum rate or
plateau is due to all available active sites becoming occupied by substrate molecules. Increas-
ing substrate molecule will therefore not increase the rate of enzyme activity.
Or The rate of enzyme activity increase with increase in in substrate concentration until a sat-
urated point is reached. This is because at high substrates concentration the active sites of the
enzymes the enzymes become saturated with substrate. Any further increase in substrate will
not increase the rate of enzyme reaction.
Or Low substrate concentration there are many active sites that are not occupied. This means
that the reaction is low. When more substrate molecules are added, more enzymes-substrate
complexes can be formed. As there are more active sites, and the rate of reaction increases.
Eventually increasing substrate concentration yet further will have no effect. The active sites
will be saturated so no more enzyme- substrate complexes can be formed.
67

THE GRAPHY TO SHOW EFFECT OF SUBSTRATE CONCENTRATION ENZYME ACTIVITY.
Enzyme concentration the rate of enzyme activity or reaction increase with increase in en-
zyme concentration if the enzyme is not a limiting factor this is because increasing in enzyme
concentration increase the number of active sites available to catalyze the reaction.
Or Low enzyme concentration there is a great competition for the active sites and the rate of
enzyme is low as the enzyme concentration increases, there are more active sites and the re-
action can proceed at a faster rate. Eventually, increasing the rate of enzyme concentration
beyond a certain point has no effect because the substrate concentration becomes the limiting
factor.
THE GRAPH TO SHOW EFFECT OF TEMPERATURE ON ENZYME ACTIVITY
68

Other factors are:
WATER is very important factor in enzyme activity or reaction. If water is little the enzyme
fail to function properly. The effect is clearly demonstrated in the seed germination when
seed germination cannot take place until unless there is suffient amount of water to activate
enzymes in the cotyledon.
METALS Enzymes colloidal react with metals by absorption the reaction has taken place the
enzymes have no longer able to work. However, there are some enzymes which are activated
by metallic ions such as Mg2+, Zn2+
ACCULATION OF END PRODUCTS

End products reduce the rate action because the accumulation end products hinder the pres-
ence of another substrate. Enzymes become saturated with end product.
STRONG LIGHT Strong light such as ultraviolet rays destroy enzymes and reduce rate of
enzyme activity (reaction)
PRESENCE OF INHIBITORS
INHIBITORS :(I) Are molecules that cause a loss of enzyme activity or are substances that
prevent normal enzyme activity. The rate of enzyme controlled reactions may decrease by the
presence of inhibitors because inhibitors prevents substrate from fitting into the active site of
the enzyme.
E + S = E+P
E+I = EI No product (p) formed
There are two types of inhibitors
Reversible inhibitor
Irreversible inhibitor
REVERSIBLE INHIBITORS
Cause temporary damage to the enzymes because the association of inhibitor and enzyme is
loose and it is easily removed. The removal of inhibitor restores the activity of the enzymes
to normal, shows the inhibitory effect by non-covalent association.
or Reversible inhibitor goes on and off allowing the enzyme to gain activity when inhibitors
leaves.
There are two types of irreversible inhibitors
Competitive reversible inhibitor – have structure like substrate it competes with the sub-
strate for the active site if remained bonded to the active site, reduce the action of enzymes.
Its effect is reversible by increasing substrate concentration. For example, melanoic acid is a
competitive it competes with succinate for the active site of succinic dehydrogenase an im-
portant enzyme in the Krebs cycle.
69

Non-competitive reversible inhibitor has different structure from that of substrate. Do not
attach themselves to the active site of the enzyme but elsewhere on the enzyme molecule (it
binds to the allosteric site). They nevertheless alter the shape of the enzyme molecule in a
such a way that active site can no longer properly accommodate the substrate. As the sub-
strate and inhibitor molecules attaches to different parts of the enzyme they not compete for
the same sites. Increase of substrate concentration will not therefore reduce the effect of the
inhibitor (effect cannot be reversed by adding more substrate). For example, cyanimide is
non –competitive reversible inhibitor. It attaches itself to the copper prosthetic group of
cytorome oxidase, there by inhibiting respiration.
Non-reversible inhibitor – Destroy enzyme structure usually by bonding with side chain
group in the active site. They leave enzyme permanently damaged so unable to carry out its
catalytic functions e.g., Heavy metals ions such as Mercury Hg2+ and silver (Ag+) break di-
sulphide bond maintain the shape of enzyme molecule.
70

THE GRAPH TO ENZYME INHITION REACTION
NOTE: Allosteric enzyme are enzymes which are designed to change shape of an enzyme.
They are regulated by compounds which act as non-competitive inhibitors. Binds to the en-
zyme at specific sites well away from the active site. They modify enzyme activity by caus-
ing a reversible damage in the structure of an enzyme active site. This in turn affects the abil-
ity of a substrate to bind to the enzyme these compound is called allosteric inhibitors.
ENZYME COFACTORS
A cofactor is non – protein substance which is essential for some enzymes to function effec-
tively.
There are three types of enzyme cofactors
Activators
Coenzymes
71

Prosthetic group
ACTIVATORS
Are substances which are necessary for the functioning of certain enzymes. The enzyme
thrombokinase which converts prothrombin into thrombin during blood clotting, is activated
by calcium ions. In the same way salivary amylase requires the presence of chloride (cl-)
ions before it will efficiently convert into maltose. It is possible that these activators assist in
forming enzyme –substrate complex by molding either the enzyme or substrate molecule into
a more suitable shape.
Coenzymes are non-protein organic substances which are essential to the efficient function-
ing of some enzymes but are not themselves bound to the enzyme. Many coenzymes are de-
rived from vitamins e.g., nicotinamide adenine dinucleotide (NAD) is derived from nicotinic
acid a member of the vitamin B complex. NAD act as co enzyme to dehydrogenase by acting
as hydrogen acceptor.
Prosthetic group
Are organic molecules but unlike coenzymes they are bound to the enzyme itself. Perhaps the
best known prosthetic group is haem. It is a ring –shaped organic molecules with iron at Cen-
tre. Apart from its roles is used as oxygen carrier in hemoglobin, it is also the prosthetic
group of the electron carrier cytochrome and of the enzyme catalyze.
CLASSIFICATION OF ENZYMES
THE SIX MAJOR GROUPS OF ENZYMES
It is difficult to estimate the total number enzymes that exist. This is not surprising when you over a
thousand different reactions can take place in individual cell and each reaction has its own specific
enzyme. The classification of enzymes is made more difficult by new enzymes being discovered or
synthesized every day. In 1964, the international Union of Biochemistry introduced a system aimed at
dispelling the confusion. The system is based on the type the reaction the enzyme catalyses: There
are six (06) major classes: Oxidoreductases, Transferases, Hydrolases, Lysases, Isomerase and
Ligase.
OXIDOREDUCTASES. Catalyse redox reactions (biological oxidation and reduction reaction).
Involves transfer of oxygen and hydrogen atoms or electrons from one molecules to another. There
are two type of enzymes, Oxidase – dealing with oxidation and reductases – dealing with reduction.
Both type of reactions is very common.
Example: Ethanal react with NADH in acidic medium to produce ethanol and NAD+ reaction is cata-
lysed by Alcohol Dehydrogenase.
Hydrogen is simultaneously lost from NADH and gained by ethanol. NADH is oxidize to NAD+, and
ethanol is reduced to ethanol. This particular process takes place in aerobic respiration in yeasts and
plants.
TRANSFERASE: Catalyse transfer of a group from one compound to another for example
Glutamic acid react with Pyruvic acid to produce Alpha – keto glutamic acid the reaction is catalysed
by Amino transferase enzyme.
72

The R group on the amino acid, glutamic acid is exchanged with the R group on the keto acid, pyruvic
acid. A new amino acid, alanine, is formed along with a new keto acid, alpha –ketoglutaric acid. This
specific type of process is called transamination and it enable us to make non-essential amino acid
from essential amino acids. other examples of enzymes are: Transaminase and phosphorylase en-
zymes.
HYDROLASES: Catalyse the splitting of a large substrate molecules into two smaller products. Wa-
ter is involved in the reaction or catalyse the decomposition of substrate by hydrolysis attacking spe-
cific linkage. Examples:
Carbohydrase – Catalyse large higher carbohydrates into simple sugars
Lactose hydrolyse to produce Glucose and Galactose the reaction is catalysed by Lactase enzyme.
The disaccharide lactose is broken down into two monosaccharides by the addition of water. Other
enzymes are like maltase act on maltose, salivary amylase act on starch, sucrose act on sucrose
etc.
Esterase- attack organic esters, splitting them into two groups of which is normally acidic. E.g., Li-
pase like steapsin splits fats into aliphatic acids and glycerol etc.
Protease – Attack the peptide linkage – CO-NH- in proteins. E.g., Endopeptidase splits proteins into
smaller units proteoses, peptones and peptides. Thus pepsin and trypsin of animals split proteins into
peptones. etc.
Aminases – attack the – C-NH and – C-NH2 – linkage in non-protein compounds. The NH or NH2
groups is replaced by OH and ammonia is liberated. The enzymes are very important in purine me-
tabolism and in the production of urea. e.g., Adnase deaminates adenine with the formation of hypox-
onthine and ammonia. Arginase hydrolyse orgine to ornithine and urea it plays role in the ornithine
cycle where urea is produced in animals. etc.
LYASES – enzymes that attacking the C-C link. Involves in the addition or removal of group across
a double bond. Sometimes they are known as desmolases. Are important enzyme involved in the part
of complex system especially associated with respiratory process. E.g.,
Pyruvic acid breaks down to produce Ethanol and carbon dioxide the reaction is catalysed by Pyruvic
Decarboxylase enzyme.
Pyruvic acid is converted into ethanal and carbon dioxide by breakage of its double bond and addition
of new group to the freed bond. This particular reaction takes place during the fermentation of sugar
by yeast. The ethanal is converted to ethanol (alcohol) carboxylases activate the decarboxylation of
ketonic acid such as pyruvic acid and oxaloacetic. They are associated with the liberation of carbon
dioxide as a result of cell respiration. Pyruvic carboxylase decarboxylate pyruvic acid to acetaldehyde
and carbon dioxide, Oxaloacetic carboxylase converts oxaloacetic acid to pyruvic with the evolu-
tion of carbon dioxide.
Decarboxylases converts amino acid into the corresponding amines with evolution of carbon dioxide.
They occur principally in amino tissue.
Isomerases catalyse rearrangements within a molecule, converting one isomer into another. Some of
these are important in respiratory process for example.
Glucose 1 – phosphate break down to produce Glucose – 6 phosphates the reaction is catalysed
by Phosphoglucomutase enzyme.
The position of a phosphate group in the glucose 1 – phosphate molecule is changed to form the iso-
mer glucose 6 – phosphate. This reaction takes place during respiration.
73

LIGASES: Catalyse bond formation between two compounds. The reaction use energy that comes
from the hydrolysis of ATP to ADP and phosphate, for Example.
Amino acid react with Specific t RNA to produce Amino acid t RNA complex + ADP + Pi
An amino acid is joined to a tRNA molecule. This particular process is called t RNA activation and it
is an essential step in protein synthesis.
REQUIRED PRACTICAL WORK ON CARBOHYDRATES, LIPIDS, PROTEIN AND FACTORS

AFFECTING ENZYME ACTIVITY (MAINLY TEMEPERATURE AND pH CHANGE)
74

REFERENCE
Kent, M. (2008). Advanced Biology: New York: Oxford University Press.
Laberge, M. (2008). Essential Chemistry. Biochemistry: New York: InfoBase Publishing.

Vulkarn.V., Thonte, S., Rathod, S., Ghiware, B. (2008). Biochemistry. (10thed). Mumbai:
Nirali Prakashan.
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Contents

Yusuph Nsaze: Kasulu TC

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COMMON TECHIQUES AND METHODS USED IN BIOCHEMISTRY.

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1. CLASSIFICATION OF CARBOHYDRATES ON THE BASIS OF BEHAVIOUR ON

b) Trisaccharide: Carbohydrates which on hydrolysis produce three (03) molecules of

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CLASSIFICATION OF CARBOHYDRATES ON THE BASIS OF TASTE.

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Cis molecule Trans molecule

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CONFORMATION (STRUCTURES) OF BIOLOGICALLY IMPORTANT MONOSACCHARIDES

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OLIGOSACCHARIDES, ESPECIALLY DISACCHARIDES

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

NOTE: Lactose is a reducing sugar

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

LIPIDS (FATS AND OIL AND WAXES)

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

UNSATURATED FATTY ACID

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

THE FLUID MOSAAIC MODEL OF THE CELL MEMBRANE

Yusuph Nsaze: Kasulu TC

FIG: The fluid mosaic model of the cell membrane

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Figure: Structure of amino acid

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

Yusuph Nsaze: Kasulu TC

PROTEINS AND THEIR CLASSIFICATION