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Chapter 4g

1. The rate of an enzyme-catalyzed reaction increases with increasing substrate concentration until all the enzyme's active sites are occupied, at which point the rate reaches its maximum. 2. Increasing the temperature increases the reaction rate until the enzyme's optimum temperature is reached, above which the rate decreases as heat denatures the enzyme. 3. The reaction rate also depends on pH, with each enzyme functioning best at its own optimum pH level. Deviations from this pH can alter the enzyme's structure and charges, preventing substrate binding.

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0% found this document useful (0 votes)
78 views33 pages

Chapter 4g

1. The rate of an enzyme-catalyzed reaction increases with increasing substrate concentration until all the enzyme's active sites are occupied, at which point the rate reaches its maximum. 2. Increasing the temperature increases the reaction rate until the enzyme's optimum temperature is reached, above which the rate decreases as heat denatures the enzyme. 3. The reaction rate also depends on pH, with each enzyme functioning best at its own optimum pH level. Deviations from this pH can alter the enzyme's structure and charges, preventing substrate binding.

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wienna1987
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ENZYME

FACTORS AFFECTING ENZYME


ACTIVITY
The Lock and Key analogy
The Lock and Key analogy
ACTIVATION ENERGY
At low temperatures,
an enzyme-catalysed
reaction takes place
Reaction rate / arbitrary units

slowly. This is because


the substrate molecule
are moving at slow rate

Temperature / oC
10 20 30 30 40 50 60
As the temperature
increases, the
substrate and
molecules move
Reaction rate / arbitrary units

faster

Temperature / oC
10 20 30 30 40 50 60
Collisions between the substrate and enzyme
molecules occur more frequently

Random movement of molecules and more


frequent collisions between the substrate and the
enzyme molecules increase the chances of the
substrate molecules coming into contact with the
active sites of the enzymes.

At higher temperatures, the rate of reaction


between the substrate and enzyme increases.

Each 10C rise in temperature- rate of enzymatic


reaction in a cell is doubled- only true until
optimum temperature is reached.
Optimum
temperature
Reaction rate / arbitrary units

Temperature / oC
10 20 30 30 40 50 60
As the surrounding temperature increases, the
rate of reaction is increased until it reaches the
optimum temperature.

-Optimum temperature:
-the temperature at which an enzyme catalyses a
reaction at the maximum rate

- each enzyme has an optimum temperature at which


its reaction rate is the fastest
-Most enzymes in humans and animals have an
optimum temperature of about 37C
Rate of reaction
decrease
Reaction rate / arbitrary units

Temperature / oC
10 20 30 30 40 50 60
Beyond the optimum temperature, any increase
in temperature causes the rate of reaction to
decrease sharply until it stops completely at about
60C

At very high temperature, the chemical bonds


holding the enzyme molecules in their precise
shape begin to break. This alters the 3D shape of
the enzyme molecules and eventually destroys the
active sites

This means that the substrate can no longer fit


the active sites of the enzyme. The enzyme is said
to be denatured.
Denaturation of enzymes- irreversible. It is
important to maintain our body temperature at an
optimum level.

Most organisms cannot survive at temperatures


above 40C.

There are some organisms that can live at higher


temperatures. Ex: bacteria living in hot springs
have optimum temperatures of between 80C and
100C or higher.
pH
The activity of enzymes is affected by the acidity or
alkalinity of the solutions in which they act

A slight change in pH can decrease the rate of


enzyme-catalysed reactions as each enzyme can only
function optimumly at a particular pH.

Optimum pH: pH at which the rate of enzymatic


reaction is at its fastest. Most enzymes function
optimally at a pH that ranges from 6 to 8.
- H+
H+ + +
- H+ + +
- H+ +
H+ +

The charges on the active site and the


In an acidic condition
surface of the substrate undergo
charges

+ +
+ +
+ +

The enzyme-substrate
complex cannot be
formed
A change in the pH value can alter the
charges on the active sites of an enzyme
and the surface of a substrate.

This can reduce the ability of both


molecules to bind with each other.

At a low pH value, excess hydrogen ions


attach themselves to the active site of the
enzyme. When this happens, ionic charges
on the active site are altered.

The substrate is unable to bind to the


enzyme and the reaction cannot takes
place.
In extreme pH conditions (acidic or alkaline),
the configuration of the enzyme is altered and the
enzyme structure is altered, destroying its
normal function.

Exceptions:
- pepsin: only function optimumly in an acidic
condition (pH 2) in the stomach.
- trypsin: function optimumly in an alkaline
condition (pH 8.5) in the duodenum.

Effects of heat on the active sites of enzymes are


normally reversible.

When pH in the environment returns to the


optimum level for the enzyme, the ionic
charges on the active sites are restored-
enzyme resumes its normal function.
Enzymes and pH
ALL GROUPS:

DRAW GRAPHS ON THE EFFECTS OF


TEMPERATURE AND Ph ON THE ENZYMES
ACTIVITY.

CHOOSE ONE LEADER, TWO SECRETARY TO


WRITE DOWN ALL THE TASKS.

EXPLAIN AND DISCUSS IN YOUR GROUPS


BASED ON THE GRAPHS.
Initial reaction rate /
arbitrary units
Enzymes and [S]

[S]
Enzymes and [S]
Increasing [S]
increases collision
rate and increases
reaction rate
Initial reaction rate /
arbitrary units

[S]
Enzymes and [S]
All active sites are
occupied. Enzymes
are working at
maximum rate.
Initial reaction rate /
arbitrary units

All active sites are


not occupied

[S]
Initial reaction rate /
arbitrary units
Enzymes and [S]

[S]
SUBSTRATE CONCENTRATION
The rate of enzyme-catalysed reaction
increases in direct proportion to the
substrate concentration until maximun
rate

Any increases in substrate concentration-


has no effect on the rate of reaction

All the active sites of enzyme molecules are


fully occupied by the substrate molecules
Low substrate concentrations- few substrate
molecules are present

Many active sites are present

The rate of reaction increases in direct


proportion to the substrate concentration

Increase in substrate concentration: more substrate


molecules are available

More chances of collision between the


substrate molecules and enzyme molecules for
catalytic reaction

More substrate molecules fill the active sites,


more products are formed per unit time
High substrate conc., more substrate molecules than
enzyme molecules

Excess substrate molecules- compete with one another for


active site.

Active sites- only available after enzyme molecules have


finished catalysing the substrate molecules

When all active sites are engaged in the catalysis of



substrate, an increase in substrate concentration will not
alter the rate of reaction

The rate of reaction becomes constant.

Now, enzymes concentration becomes a limiting factor.

Rate of reaction- increased if the enzyme concentration is


increased. Cells- producing more enzymes.
Increase in substrate concentration- lead to an increase in the
rate of reaction if there are enough enzyme molecules to
catalyse the additional substrate molecule.

at a certain substrate conc., the rate of reaction will not


increase further , becomes constant= maximum rate

All active sites are filled and engaged in catalysis- enzyme


molecules are said to be saturated

When products leave the active site, another substrate


molecule enters the active site
SUBSTRATE
MOLECULE

ENZYME
MOLECULE
SUBSTRATE
MOLECULE

ENZYME
MOLECULE
Enzymes and [enzyme]
-maximum number of reaction
- The concentration of substrate
becomes a limiting factor
Initial reaction rate /
arbitrary units

What factor is
limiting here?

[Enzyme]
The rate of an enzyme-catalysed reaction increases when the
enzyme concentrations increased. It is only if
a) no other factors limiting the rate of reaction
b) the substrate molecules available are in excess-
because more active sites are available for enzyme action.

The rate of enzyme-catalysed reaction is directly


proportional to the concentration of the enzyme present until
maximum rate is achieved.

Beyond the maximum rate of reaction: substrate


concentration- limiting factor.

The enzyme concentration is doubled- the rate of


reaction/ the number of substrate molecules that are
converted to products per unit time- doubled.
Initial reaction rate /
arbitrary units

4X

2X

1X
conc.
Enzyme
TYPES OF INDUSTRY ENZYMES USED USES
APPLICATION

1) Food
processing
industry
a) Meat products Protease Tenderises meat
b) Starch products Amylase and Change starch to sugar in the making
amyloglucoxidase of syrup
Production of high fructose syrup:
Glucose Glucose is converted into fructose-
isomerase used in slimming products as only
small amount needed
c) Fish products Protease Removes the skin of fish
d) Dairy products Lipase Ripening of cheese
Lactase Hydrolyses lactose to glucose and
galactose in the making of ice-cream
Rennin Solidifies milk protein
e) Alcoholic drinks Zymase Converts sugars to ethanol
(beer, wine)
f) Bread and other Amylase Converts starch flour into sugar in the
bakery products making of bread
g) Cereal grain Cellulase Break down cellulose and removes
products seed coats from cereal grains
h) Seaweed Cellulase Extracts agar from seaweed
products
TYPES OF INDUSTRY ENZYMES USED USES
APPLICATION

2) Leather Trypsin Removal of hair from


products animal hides

3) Textile products Amylase Removes starch that


is used as stiffeners
from fabrics

4) Medical/ - Pancreatic trypsin -Treats inflammation


pharmaceutical - Microbial trypsin -Dissolves blood
products clots

5) Biological Protease and -Dissolve proteins


washing powder amylase and starch stains in
or detergents clothes
IMPORTANCE OF CHEMICAL
COMPOSITION IN CELLS

Chemical substances in the cell- enable the cells to


function optimally
Lack of proteins: new tissues and cells cannot be
formed to replace the damaged ones- inhibit body
growth
Enzymes and hormones- made up of proteins
Without enzyme- all biochemical reactions will
proceed too slowly

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