CHAPTER 4

4.1

CHEMICAL COMPOSITION OF THE CELL

ELEMENTS IN THE CELL

Class of
element
s
Essentia
l
element
(96%)
Trace
element
(< 4%)

Element and its

composition in the
cell (%)
Oxygen (O) = 65

Function in

Form the main groups of chemical compounds

Carbon (C) = 18.5

in the cell eg: water, proteins, nucleic acids,

Hydrogen (H) = 9.5

carbohydrates, lipids, vitamins and other

Nitrogen (N) = 3.3

Calcium (Ca) = 1.5

compounds
1-Contraction of

1-Formation of middle

muscle cells

lamella of cell wall

2- Formation of bone

2- Maintain the semi-

cells

permeability of the

Animal cell

Plant cell

Phosphorous (P) =
1.0
Potassium (K) = 0.4

PM
Same as calcium
Aids in cell division
Synthesizing ATPs and nucleic acids
Transmission of
Formation of the cell

Sulphur (S) = 0.3

nervous impulses
1- Aids in cell division

wall

2- Helps in well-functioning of enzymes

Sodium (Na) = 0.2

3- Synthesizing amino acids/protein

1- Maintaining the
Not required
osmotic pressure in
cells
2- Transmission of

Chlorine (Cl) = 0.2

nervous impulses
1-Synthesizing

Not required

stomach hydrochloric
acid
2- Transmission of
Magnesium (Mg) =
0.1
Ultra-

Ferum (Fe)

nervous impulses
Synthesizing protein

Synthesizing protein

and chlorophyll
Activators for certain enzymes
1- Formation of
1- Formation of
1

trace
element
(<0.1%)

haemoglobin in RBC

chlorophyll

2- Formation of

2- Activator for

Copper (Cu), Zinc

respiratory enzymes
certain enzymes
Essential for many biological processes eg:

(Zn),

enzyme activator, coenzymes etc

Manganese (Mn),
Cobalt (Co), Boron
(B),
CHEMICAL COMPOUNDS IN THE CELL

INORGANIC CHEMICAL COMPOUNDS (ICC)

ICC without carbon
ICC with carbon

ORGANIC CHEMICAL

- do not contain carbon

-contain inorganic

COMPOUND (OCC)
- contain organic carbon

-usually smaller and

carbon

-usually macromolecules

simpler than OCC

Eg: CO2, sodium

-usually found in and

Eg : water (H2O), acids

hydrogen carbonate

originated from living

(HCl), alkalis & mineral

(NaHCO3)

organisms

salts

-Eg : carbohydrates, lipids,

proteins and nucleic acids

BODY WEIGHT PROPORTION

Water = 65 % - 90%
*Dry weight = 10% - 35%
DRY WEIGHT PROPORTION
Chemical compound
Percentage (%)
Protein
50
Nucleic acids
18
Carbohydrates
15
Lipids
10
Others OCC (eg: Vitamins) and ICC
7
THE IMPORTANCE OF ORGANIC COMPOUNDS IN THE CELL
A

THE IMPORTANCE OF CARBOHYDRATES (GLUCOSE)

Animal
1- Energy and food storage
Glucose can be converted into
glycogen by insulin. Glycogen

Plant
1- Energy and food storage
Glucose can be converted into
starch and kept in storage organs
2

then
is stored in the liver and skeletal
muscles.

eg: stem, fruits, roots etc

Glycogen (in the liver)can be

reconverted into glucose by
glucagon
insulin
Glucose
glycogen
(blood) glucagon (liver & muscle)
2- Support & structure
Chitin, a modified glucose forms
the
cell wall of fungi & exoskeleton of
insects and mollusks.

2- Support & structure

Cellulose cell walls of plants which
gives support and shape to the cell

3- Energy production by cell respiration

Glucose is oxidized by oxygen in the mitochondria to produce energy
(ATPs &
heat energy), CO2 and water during cell respiration
Glucose + Oxygen

Energy
+ carbon dioxide + water
(ATPs & heat)

4- Synthesizing of ribose sugar of the nucleic acids

Ribose, a five-carbon sugar forms part of the nucleotide of the DNA and
RNA
B
THE IMPORTANCE OF LIPIDS
1- Energy and food storage in form
1- Energy and food storage in form of
of
fatty acids and stored in fruits and
fatty acids and stored in the
seeds
adipose
tissue
2- Essential in synthesizing hormones
3- Insulate body as the adipose
tissues
line the entire skin and help in
maintaining body temperature at
37oC
C
THE IMPORTANCE OF PROTEINS
1- Formation of the PM and membranous protein molecules
2- Provide shape & structure eg:
i -collagen, a fibrous protein found in bones, skins and cartilage
3

ii-keratin, a tough insoluble protein found in nails, hair, horns and hooves
3- Essential in defence system by formation of antibodies, specific proteins
against pathogen
45678-

Form enzymes to catalyze biochemical reaction

Form hormones for biochemical processes and body coordination
Involve in the formation of ATPs
Form haemoglobin in the RBC to transport oxygen
Form the coagulative proteins eg: fibrinogen that helps in blood clotting
Mechanism

9- Energy storage as proteins can be used during starvation

D
THE IMPORTANCE OF NUCLEIC ACIDS
1- Genetic information storage
Genetic info. can be stored by using the combination of four nitrogenous
bases of the nucleic acids
2- Provide a stable genetic info. storage within the lifetime of an organism
3- Enable the inheritance of genetic info. from generation to generation
Structure of a nucleotide

Structure of DNA
(consists of 2 poly

nucleotides)
P
RS
Keys :
P = Phosphate group
RS = Ribose sugar
NB = Nitrogenous base
4 types of NBs
A = adenine
T = thymine
G= guanine
C=cytosine
A pairs with T
G pairs with C

NB

THE IMPORTANCE OF WATER

1- As a solvent for most substances necessary for biochemical reaction
2 As a transport medium as water forms 50% of the blood composition
4

3 As a coolant / gives cooling effect as water absorbs heat from the body,
evaporates (during perspiration) and cools the body
4 As a reaction as water takes part in biochemical reaction eg: the hydrolysis of
food
5 As a medium of biochemical reaction
6 Regulates body temperature as water transport heat from heat generating
sites/organs eg: liver and heart to the heat releasing sites/organs like skin
7 Gives support and structure as 65 70% of the body mass is water

4.2

UNDERSTANDING CARBOHYDRATES Made up of carbon, hydrogen and oxygen elements

Monosaccharides

Type
Aspect
Known as
Molecular
formula
Examples

Taste
Solubility
in water
Reducing
sugar (RS)
Confirmati
on test
Formation

Disaccharides

Polysaccharides

Simple sugars (Monomer)

C6 H12 O6

Twins sugars
C12 H22 O11

Complex sugars (Polymer)

(C6 H10 O5) n

Glucose (grape sugar)

Fructose( fruits & honey
sugar)
Galactose (milk sugar)

Maltose (Malt sugar)

Sucrose (sugar cane & sugar
beet)
Lactose (milk sugar)

Cellulose (cell wall)

Starch (plants food storage)
Glycogen (animals food
storage)

Sweet
Soluble

Sweet
Soluble

Tasteless
1. Soluble starch
2. Insoluble glycogen &
cellulose
Yes
1. Reducing (RS) maltose & Non-reducing
2+
+
RS reduce Cu (blue) to Cu
Lactose
(brick red precipitate)
2. Nonreducing (NRS)
Sucrose
Benedict test
Hydrolisis (using dilute HCl)
Iodine test for starch
Benedict solution is alkaline
(NRS becomes RS) followed by
solution of CuSO4
Benedict test
Hydrolysis of Polysaccharides By Condensation Reaction :
By Polymerization which is a
Eg:
condensation of many
Starch + water
2 monosaccharides are bond
monomers to form a large
amylase
together with a glicosidic bond /chain of polysaccharides
Maltose
to form a disaccharide and a
and water molecules are
water molecule is removed.
removed
Maltose + water
Eg:
maltase
Glucose + Glucose
Glucose
Maltose +
water
6

Glucose + Fructose
Sucrose + water
Glucose + Galactose
Lactose + water
Breakdown Glucose can be broken down / Disaccharides can be broken
oxidized by oxygen to
down to 2 monosaccharides by
produce energy, CO2 and
Hydrolisis Reaction (a process
water during cell respiration.
which involves the addition of
water as a hydrolytic substance)
Glucose + oxygen
Eg:
Energy + water +
Maltose + Water
CO2
Glucose + glucose

Polysaccharides can be
broken down into
monosaccharides by
Hydrolysis Reaction.
Eg :
Starch + water
(Glucose)n

CONFIRMATION TEST
Test : Benedict test
Test : Iodine test
Aim : To detect the presence Reducing Sugar
Aim : To detect the presence of starch
Reagent : Benedict / Fehling solution
Reagent : Iodine solution
Materials: Benedict solution, food sample, dH20
Materials : Iodine solution, food sample
Apparatus : Beaker, test tube, reagent bottle, dropper,
Apparatus : Reagent bottle, dropper, white tile
measuring cylinder, Bunsen burner, tripod stand, wire
Technique: Observe & record colour changing
gauze
Method :
Technique : Observe & record colour changing
Method :
1- Put food sample onto the w/tile.
2- Drop a droplet of iodine solution.
1- Fill 1ml of food sample into a t/ tube. Add 1 ml of
3- Observe colour change.
Benedict solution.
2- Heat mixture in the t/tube in the boiling water bath
for 5 minutes.
3- Observe colour change.
Observation

Inference /
7

Observation
Mixture turns
green/brown/brick red
precipitate
Mixture remains blue

Inference /
conclusion
RS present.

Yellowish turns
dark blue
Remains yellow

conclusion
Starch present
Starch absent

RS absent

Test : Non-Reducing Sugar Test

Aim : To detect the presence of Non-Reducing Sugar
Reagent : Benedict / Fehling solution
Materials: Reagent, food sample, dH20, dilute HCl,
NaHCO3 powder
Apparatus : Beaker, test tube, reagent bottle, dropper,
measuring cylinder, filter paper, Bunsen burner, tripod
stand, wire gauze
Technique : Observe & record colour changing
Method :
1- Carry out Benedict Test first. If the mixture remains
blue, it means no Reducing Sugar.
2- Fill 1ml of food sample into a test tube. Add 1 ml of
dilute HCl.
3- Heat mixture in the test tube in the boiling water
bath for 5 minutes.
4- Place the mixture in the test tube under running
water to cool it down.

Test : Grease Spot Test

Aim : To detect the presence of fats
Reagent : Materials : Filter paper, food sample, dH20
Apparatus : Dropper, test tube
Technique: Observe & record the present of grease
spot
Method :
1- Drop a few droplets of food sample onto the
filter paper.
2- Dry up the filter paper.
3- Observe the presence of grease spot.

Observation

Inference /
8

5- Put spatula of NaHCO3 powder into the mixture.

4- Add 1 ml of Benedict solution.
6- Heat mixture in the t/tube in the boiling water bath
for 5 minutes
7- Observe colour change.
Observation
Mixture turns
green/brown/brick red
precipitate
Mixture remains blue

Inference /
conclusion
Non -RS present

Shows
presence of
grease spot.
Shows absence
of grease spot

conclusion
Fats present
Fats absent

Non-RS absent

Test : Millon Test

Aim : To detect the presence of protein
Reagent : Millon reagent
Materials: Millon reagent, food sample, dH20
Apparatus : Beaker, test tube, reagent bottle, dropper, measuring cylinder, Bunsen burner, tripod stand, wire
gauze
Technique : Observe & record colour changing
Method :
1- Fill 1ml of food sample into a t/ tube. Add 1 ml of Millon Reagent
2- Heat mixture in the t/tube in the boiling water bath for 5 minutes.
3- Observe colour change.
Observation
Mixture turns red precipitation
No colour change

Inference / conclusion
Protein present.
Protein absent

4.3

UNDERSTANDING PROTEIN Made up of C, H, O, N, P and S

Peptide / monomer (Amino
acid)

Dipeptides

Polypeptides

Digestion of protein by protease

enzyme
Eg:
Protein + water

By Condensation
Reaction:
2 peptides/amino acids
are bond together with a
peptide bond to form a
dipeptide and a water
molecule is removed
Eg:
Amino acid + amino acid
Dipeptide +
water

By polymerization which is a
condensation of many amino acids
with peptide bond (and involves
removal of water molecules) to form
a large / long chain of polipeptides
molecules.

By Hydrolysis Reaction :
Dipeptides can be broken
down to 2 amino acids by
the addition of water (as
the hydrolytic agent)
Eg :
Dipeptides + water
Amino acids

By Hydrolisis Reaction
Eg:
Polypeptides + water
(amino acid)n

Type
Aspect
Formatio
n

protease
Amino acids

Breakdo
wn

10

CLASSIFICATION OF AMINO ACIDS

ESSENTIAL AMINO ACIDS

1- Cannot be synthesized by human
body
2- Can be obtained from protein
food class
3- Required for protein synthesis in
the body eg: enzymes, hormones,
membranous protein molecular.
4- Examples :
Essential AA
Leucine

Abbreviation
Leu

NON-ESSENTIAL AMINO ACIDS

1- Can be synthesized by human
body
2- Are also required for protein
synthesis in the body.
3- Examples:
Non-essential
AA
Glutamic acid

Abbreviation
Glu

CLASSIFICATION OF PROTEINS

FIRST CLASS PROTEINS

1- Known as complete proteins /
animal proteins
2- Contain all essential AA
3- Examples are all animal proteins
eg: eggs, milk, meat and soy
beans
4- Normally with high
fats/cholesterols content

SECOND CLASS PROTEINS

1- Known as incomplete proteins /
plant proteins
2- Lack of essential AA
3- Examples are beans, nuts, seeds,
grains except soy beans
4- Normally low fats/cholesterols
content

11

THE PROTEIN STRUCTURES

PRIMARY
STRUCTURE

SECONDARY
STRUCTURE

A linear
polypeptides chain

4.4

TERTIARY
STRUCTURE

Folded or coiled
polypeptides chain

QUARTENARY
STRUCTURE

2 or more tertiary
A folded secondary structured proteins
structured protein
which join together
Eg: Lysozyme
Eg: pore proteins,
(found in tears)
haemoglobin

UNDERSTANDING LIPIDS Made up of C, H and O

TYPE OF LIPIDS
1- Triglycerides (fats and
oils)
-composed of a glycerol and 3
fatty acids molecules which are
bond together by Condensation
Reaction (with the removal of
water molecules)
- are true fats

A glycerol

3 fatty acids

1234-

FUNCTION
Supply energy
Food storage store in adipose tissues
beneath the skin
Insulate body, prevent excessive heat loss
and maintain body temperature
Solvent for lipid soluble vitamins

Notes:
1- Fatty acid is an organic acid. Its molecular
structure has a long chain of hydrocarbon
with a carboxyl group (COOH)
2- There are many types of fatty acids.
Different types of fatty acids and no. of
fatty acids molecules form different types
of fats/oils
3- Glycerol is an alcohol which is colourless,
odourless and tastes sweet.
4- Naming of lipids/fats/oils
No. of
glycerol
molecule
s
1
1
1

2- Phospholipids
Composed of a diglyceride

No. of
fatty
acids
molecules
1
2
3

Name of the lipid

formed
Monoglyceraldehyde
Diglyceraldehyde
Triglyceraldehyde

1- Construct the structure of PM

2- Provide the semi-permeability
12

which is bond to phosphate

group

characteristic of the PM

3- Waxes

1- form a waterproof cuticle layer on the

followings mainly to prevent water loss and
provide waterproof characteristic
a- epidermal layer of the plants
b- exoskeleton (chitin) of insects
c- feathers of birds

4-Steroids
Eg:
a- Cholesterol
b- Sex hormones ie:
oestrogen,
progesterone and
testosterone
c- Bile

1- Cholesterol provides flexibility to the PM

2- Sex hormones stimulate and control the
development of secondary sexual
characteristics
3- Bile emulsifies fats

COMPARISON BETWEEN SATURATED FATS AND UNSATURATED FATS

SATURATED FATS
Fats with no double covalent
bond of carbon. Carbon
covalent bonds are saturated
with H atoms

Single covalent bond

Solid
High
Animal fat sources and
coconut oil
High LDL (Low-density
lipoprotein - bad cholesterol)
content

DIFFERENCES
Definition

UNSATURATED FATS
Fats with one / more double
covalent bond of carbon
(C=C)
1 double bond present
monounsaturated fats
2 or more double bonds present
polyunsaturated fats
Single and double bond

Type of
chemical bond
between C
atoms
State of matter Liquid (oil)
at room
temperature
Melting point
Low
Source
Plant source except coconut oil
Cholesterol
content

Low LDL content

High HDL content

Low HDL (High-density

lipoprotein good
cholesterol) content.
13

SIMMILARITIES
12345-

4.5

Both are glycerides / glyceraldehydes

Both are composed of glycerol and fatty acids
Both have hydrocarbon chains
Formed by Condensation Reaction.
Broken down by hydrolysis.

ENZYMES
1. Metabolic reactions are all biochemical reactions carried out within
the body.
2. Classification of metabolic reaction

ANABOLIC REACTION

CATABOLIC REACTION

Refers to processes of synthesizing of

complex molecules from simpler
molecules eg : synthesizing proteins
like enzymes, hormones, antibodies etc

Refers to processes of breaking down

complex molecules to form simpler
molecules eg: cell respiration, food
digestion etc.

3. Metabolic reactions are catalyzed by specific enzymes.

4. Enzyme is an organic substance made of protein produced by living
cells and acts as a biochemical catalyst that speeds up the rate
biochemical reaction within the body.
5. The importance of enzymes :
energy level
Enzymes lower the activation
energy needed for carrying
out biochemical processes
so that the processes occur
optimally at body temperature.

B
Notes :
A = activation energy required in
uncatalyzed reaction
B = activation energy required in
enzyme-catalyzed reaction
GENERAL CHARACTERISTICS OF ENZYMES
1.

progress of reaction

Made up of proteins
14

2.

Speed up the rate of biochemical reactions.

3.

Required in small amount to catalyze reactions.

4.

Catalyze specifically on particular substrate and reaction. The specificity of

an
enzyme can be shown by `lock & key hypothesis.
5.

Not being used up or destroyed in the reaction that they catalyze (remain
unchanged after carrying out reaction), they can be reused to catalyze the
same reaction.

6.

Catalyzed reversible reaction

Eg:

enzyme Y
X
+
(substrate)

water
enzyme Y

Z
(simpler product)

In living cell/organism, enzyme catalyzes forward reaction because Z is not

allowed to form X
, as Z will be removed as soon as Z is produced.

7.

Highly affected by changes in temperature and pH value.

8.

Able to be well-functioned in the presence of coenzyme/cofactor.

NAMING OF ENZYMES
1.

Standardization of naming of enzymes done by the International Union of

Biochemistry (IUB) in 1961.

2.

An enzyme is named by using its substates name and adding the suffix `-

ase.
Substrate

Class of
enzyme

Protein
Amylose
(starch)
Lipids
Sucrose
Hydrolase
Polymerase
Oxyreductase

Examples of
enzymes
Protease eg : pepsin,
tripsin, erepsin
Amylase

Type of reaction
catalyzed
Hydrolysis

Lipase
Sucrase
All digestive enzymes
DNA polymerase, RNA
polymerase
Dehydrogenase,
oxydase

Hydrolysis
Hydrolysis
Hydrolysis
Polymerization
(Condensation)
Oxidation & reduction

Hydrolysis

15

Transferase

Transaminase,
phosphorilase

Transferring functional
group of a particular
substrate to another
molecule

THE MECHANISM OF ENZYME REACTION

1. Shows the way an enzyme catalyzes a substrate
2. The enzyme has active site which binds to (fits with) a specific substrate
3. The equation shows the idea of enzyme reaction
(Substrate) (Enzyme)
S
+
E

(simpler products)
P1 + P2

E-S
(Enzyme-substrate
complex).

4.Can be explained by the Principal / Hypothesis of `lock and key which shows :
i- the specificity of an enzyme to a particular substrate.
ii- enzyme is not used up/ reacted during the reaction and can be reused
Enzyme = lock

Specific substrate = key

a- Substrate fits into the enzyme at the enzymes active site to form
enzyme-substrate complex.
b- Enzyme-catalyzed reaction takes place at the active/binding site to
form simpler products
c- The enzyme can be reused to catalyze the particular substrate
CLASSIFICATION OF ENZYMES
INTRACELLULAR ENZYMES
Produce in the living cells.
Catalyze reactions within the cell.
Normally found in cytoplasm, nucleus,
mitochondria and chloroplast.

INTER/EXTRACELLULAR ENZYMES
Produced in the living cells but then,
leave the cell and catalyze reactions
outside.
Found in lumen of alimentary tubes.
Examples : All digestive enzymes i.e:
amylase, protease, lipase etc.

Example : DNA polymerase, ATP

synthetase, ATPase
THE PRODUCTION OF INTER/EXTRACELLULAR (EC) ENZYMES
Organelle
involved
Nucleus

Function
Contains DNA which has the information for producing enzymes
16

mRNA (messenger RNA) in the nucleus copies the information

from the DNA
Next, mRNA goes out of the nucleus ( via nuclear pore) and
attaches itself to the ribosome on the rough ER.
Ribosome

Interprets information/ instruction carried by mRNA and starts

joining amino acids to form the instructed enzyme and a long
polypeptides chain is formed.
Amino acids are taken from the cytoplasm and carried to the
ribosome by the tRNA (transfer RNA)
The product is called raw enzyme.

Rough ER

Golgi apparatus

Provides pathway to the mRNA to attach to the ribosome on it.

Transports raw enzyme to the Golgi apparatus by forming
transport vesicles.
Modifies the raw enzyme until the enzyme is completely
produced.
Forms secretion vesicles so that the enzyme will be transported
to the PM..

Mitochondria

Secretion vesicles which contain enzyme fuse with the PM and

the EC enzyme is released out of the cell as an EC enzyme.
Generates energy (ATPs) required as the production of EC
enzyme requires a lot of energy.

THE PRODUCTION OF INTRACELLULAR(IC) ENZYMES

Organelle
involved
Nucleus

Function
Contains DNA which has the information for producing enzymes
mRNA (messenger RNA) in the nucleus copies the information
from the DNA
Next, mRNA goes out of the nucleus ( via nuclear pore) and
attaches itself to the free ribosome in the cytoplasm.

Ribosome
(found freely in
the cytoplasm)

Interprets information/ instruction carried by mRNA and starts

joining amino acids to form the instructed enzyme and a long
polypeptides chain is formed.
17

Amino acids are taken from the cytoplasm and carried to the
ribosome by the tRNA (transfer RNA)
The product is called raw enzyme.
Rough ER
Golgi apparatus

Forms transport vesicles and transports raw enzyme to the Golgi

.
Modifies the raw enzyme until the enzyme is completely
produced.
Forms secretion vesicles so that the enzyme will be secreted in
the cytoplasm as an IC enzyme

Mitochondria

Generates energy (ATPs) required as the production of IC enzyme

requires a lot of energy.

FACTORS AFFECTING THE RATE OF ENZYMESS REACTION

Factor
Temperature
Rate of enzyme reaction
max _ _ _ _ _ _ _ _
i
i
I
i
i
i
i
i
optimal temp.
Temperature
(oC)

pH value

Effect on the rate of enzymes reaction

1- At low temperature, enzyme is less active.
( Enzyme molecules posses less kinetic
energy
Less collision occurs between enzyme &
substrate molecules
Less enzyme-substrate complex is formed
Less simpler product is produce)
Rate of enzyme reaction is low
2- At optimal temperature (37o C), enzyme is
most active.
Rate of enzyme reaction is maximum
3- At higher temperature than optimal temp.,
enzyme is denatured.
No enzyme-substrate complex is formed/
No enzyme reaction occurs
Rate of enzyme reaction is decreased.
An enzyme has optimal pH value which its rate
of reaction is the fastest /maximum
Eg : Pepsin = pH 2
Amylase = pH 7

rate of enzyme reaction

Acidity is determined by the presence of
hydrogen ion (H+) which has positive charge.
18

pepsin amylase
max

Alkalinity is determined by the presence of

hydroxyl ion (OH-) which has negative charge.

pH
2

14

The enzymes active site must have

complement charge with the substrate so that
the enzyme-substrate complex can be formed
and reaction takes place.
Eg :
Charge of
Charge of
Formation of
enzymes
substrate
enzymeactive site
substrate
complex
+ve
+ve
No
-ve
+ve
Yes
neutral
+ve
No
Acidity and alkalinity affect/change the charge
of the enzymes active site so the enzymesubstrate complex is not formed.

Concentration of enzyme
Rate of enzyme reaction

The higher the concentration of enzyme used,

the higher the rate of enzyme reaction.
Then, the rate of reaction remains at constant
as the concentration of substrate which is
fixed becomes the limiting factor.
The rate of enzyme reaction refers to
1- the amount of substrate catalyzed per
unit time.
2- the amount of product(s) formed per unit
time

Concentration of enzyme

Concentration of substrate
Rate of enzyme reaction

The higher the concentration of substrate

used, the higher the rate of enzyme reaction.
Then, the rate of reaction remains at constant
as the concentration of enzyme which is fixed
becomes the limiting factor.
The rate of enzyme reaction refers to
1- the amount of substrate catalyzed per
19

unit time.
2- the amount of product(s) formed per unit
time.
Concentration of substrate

THE USES OF ENZYMES

Application
Dairy industry

Enzyme used
Rennin

Uses
Coagulate milk protein in cheese

Lipase
Protease
Amylase

manufacturing
Used in ripening cheese
Removes skin/scales of fishes
Breaks down of starch to

Protease

glucose/maltose
Breaks down of proteins in flour for

Biological

Protease /lipase/

biscuits and cakes manufacturing

Removes organic stains (blood / oily

detergents
Leather tanning

amylase
Protease
Lipase

stains / starch residues) from clothes

Removes hair and softens the leather
Breaks down adipose tissue

Amylase

Breaks down starch in order to

Trypsin (protease)

produce threads
Removes blood clots and cleans

Fish industry
Confectionery

industry
Textile industry
Medical analysis

wounds

20