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Think about
4.1 Metabolism
4.2 Properties and actions of enzymes
4.3 Factors affecting the rate of
enzymatic reactions
4.4 Applications of enzymes
Recall Think about
Summary concept map
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enzyme
enzyme
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enzyme
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3
enzyme
4.1 Metabolism
different chemical reactions take place
in living cells
respiration
protein
synthesis
lipid
synthesis
4.1 Metabolism
different chemical reactions take place
in living cells
sum of the chemical
reactions that take place in
an organism
= metabolism ( )
10
4.1 Metabolism
Metabolism
Catabolism
( )
Anabolism
( )
11
4.1 Metabolism
1 Catabolism
complex
molecule
energy
simple
molecules
breaking-down reactions
release of energy
12
4.1 Metabolism
1 Catabolism
example: respiration
carbon
water +
dioxide
glucose
energy
13
4.1 Metabolism
Metabolism
Catabolism
( )
Anabolism
( )
14
4.1 Metabolism
2 Anabolism
simple
molecules
energy
building-up reactions
requires energy
complex
molecule
15
4.1 Metabolism
2 Anabolism
example: condensation of glucose
starch
glucose
energy
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4.1 Metabolism
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18
reacting
molecules
product
( )
energy barrier
( )
19
reacting
molecules
product
( )
Energy supplied
energy to
barrier
overcome the
energy barrier( )
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energy barrier
product
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By increasing the
temperature?
smaller
energy barrier
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By increasing the
temperature?
Not possible
smaller
because
high barrier
energy
temperature
kill the body cells!
energy level raised
energy barrier is easier to overcome
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lower
energy barrier
27
energy
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4.1
Demonstration of the breaking-down
action of enzymes
1 Prepare liver extract.
a Grind fresh liver with cold distilled water.
cold distilled
water
fresh pig
liver
29
4.1
b Filter the ground
tissue with filter
paper.
filter paper
liver extract
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4.1
c Dilute the liver extract by 50% with cold
distilled water.
distilled water
liver extract
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4.1
2 Set up 3 test tubes A to C. Observe for the release
of gas and the gas given off with a glowing splint.
hydrogen
peroxide
+ liver
extract
distilled
water +
liver
extract
hydrogen
peroxide +
distilled
water
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4.1
Results and discussion
A gas is released from tube A.
The gas is oxygen because
re-lights
a
glowing
splint.
it
No oxygen is released from
the control set-ups (tubes B
and C).
33
4.1
Results and discussion
Fresh liver tissues can break down
hydrogen peroxide possibly due to the
presence of catalase in the liver tissue.
Catalase speeds up the breakdown of
hydrogen peroxide.
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shapes fit
together!
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enzyme
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enzyme
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Properties of enzymes
1) Biological catalysts
act as catalysts ( ) in
organisms
speed up metabolic reactions
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Properties of enzymes
2) Reusable
enzyme returns to its original form
after reaction
before
reaction
same!
after
reaction
43
Properties of enzymes
3) Required in small amount
large amount of products produced
reusable
reusable
reusable
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Properties of enzymes
4) Proteins
enzymes are denatured ( )
at high temperatures and extreme
pH
45
Properties of enzymes
5) Specific action
different shape!
46
Properties of enzymes
5) Specific action
each enzyme combines with a specific
substrate
each enzyme catalyses only one
type of reaction
47
Properties of enzymes
5) Specific action
can be explained by
lock-and-key
hypothesis
( )
48
Lock-and-key hypothesis
specific
shape
fit only a particular lock
49
Lock-and-key hypothesis
active sites of
specific shape
53
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temperature
pH
inhibitor
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Temperature
reaction rate
0C
low kinetic energy
enzyme inactive
temperature()
10
20
30
40
50
60
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Temperature
reaction rate
temperature rises
more kinetic energy
temperature()
10
20
30
40
50
60
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Temperature
more kinetic energy
molecules vibrate more
rapidly
collide more frequently
have higher chance to
form an enzymesubstrate complex
60
Temperature
reaction rate
temperature rises
10
20
Temperature
reaction rate
maximum rate
optimum temperature
rate of enzymatic
reaction reaches
maximum
temperature()
0 10 20 30 40 50 60
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Temperature
reaction rate
temperature higher
than optimum
temperature
enzyme denatured
reaction rate
decreases
temperature()
0 10 20 30 40 50 60
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4.2
Simulation
2 Leave the different pairs of test tubes in water baths at different temperatures for
10 minutes.
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4.2
ice
A
starch solution
B
4.2
3 Pour the amylase solution into starch solution. Put the tube of mixture back to its
beaker. Record the time as zero.
amylase solution
A
1
starch solution
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4.2
4 At 2-minute intervals, transfer a drop of each mixture to an iodine drop. Record the
time it takes for the blue-black colour to disappear.
amylase
and starch
mixture
iodine drops
spot plate
69
4.2
Results and discussion
The time it takes for the blue-black colour
to disappear is the shortest at 60C.
4.2
Results and discussion
At low temperature, the enzymatic reaction
rate is low because amylase is inactive.
Its activity increases with temperature until
it reaches a maximum (around 60C).
71
4.2
Results and discussion
The enzyme activity is the highest at 60C.
Above the optimum temperature, the
enzyme activity decreases and the reaction
rate decreases until the enzyme becomes
denatured and can no longer work.
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temperature
pH
inhibitor
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pH
reaction rate
pepsin
many enzymes in
mammals (e.g.
salivary amylase)
pancreatic
lipase
14
12
10
pH
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pH
reaction rate
each enzyme
works in a narrow
range of pH
14
12
10
pH
75
pH
optimum pH for
most enzymes:
pH 5 pH 9
each enzyme
have their own
optimum pH
unsuitable pH
causes
denaturation
reaction rate
14
12
10
pH
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4.3
Simulation
Benedicts
solution
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4.3
2 Add sucrose solution to another 6 test tubes A to F. Then add citratephosphate buffer solution at different pH values to the tubes as shown.
Tube
pH of buffer
solution
4.3
3 Add invertase solution to test tubes A to F.
Leave at room temperature for 5 minutes.
sucrose solution
+ citratephosphate buffer
+ invertase
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4.3
4 Pour the Benedicts solution in test tubes 1 to 6 into test
tubes A to F respectively. Shake the tubes gently. Put
the test tubes into a boiling water bath for 10 minutes.
boiling water
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4.3
5 Allow the tubes to stand for 15 minutes.
Measure the depth of any brick-red
precipitate settled in the test tubes.
81
4.3
Results and discussion
Precipitate is formed in tubes A, B, C and
D. The largest amount of precipitate is
settled in tube C. No precipitate is formed
in tubes E and F.
The results show that invertase works in an
acidic medium. It has an optimum pH
value around pH 5.2.
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temperature
pH
inhibitor
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Inhibitors
inhibitors ( ) are chemicals that
slow down or stop the activities of
enzymes
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Inhibitors
Competitive
inhibitors
( )
Non-competitive
inhibitors
( )
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1 Competitive inhibitors
Animation
competitive
inhibitor
substrate
similar
shape!
86
1 Competitive inhibitors
compete with substrates for active sites
substrate
inhibitor
active site
enzyme
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1 Competitive inhibitors
reaction rate
decreases
enzyme
inhibitor prevents
binding of substrate
chance to form
enzyme-substrate
complex lowered
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1 Competitive inhibitors
enzyme
reversible binding
substrate can bind
when inhibitor
leaves
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1 Competitive inhibitors
more substrates,
greater chance
of binding
reaction rate
increases
90
Inhibitors
Competitive
inhibitors
( )
Non-competitive
inhibitors
( )
91
2 Non-competitive inhibitors
substrate
noncompetitive
inhibitor
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2 Non-competitive inhibitors
active site
changes
shape
93
2 Non-competitive inhibitors
not fit together!
reaction rate
decreases
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2 Non-competitive inhibitors
2 Non-competitive inhibitors
examples:
cyanide
heavy
metals
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4.4
Video
4.4
3 Add 10 drops of invertase solution to test tubes A to
C. Leave the tubes at room temperature for 5 minutes.
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4.4
4 Pour Benedicts solution in test tubes 1 to 3 into test
tubes A to C respectively. Shake the tubes gently. Put
the test tubes into a boiling water bath for 10 minutes.
boiling water
99
4.4
5 Allow the tubes stand for 15 minutes.
Measure the depth of any brick-red precipitate settled in the test tubes.
100
4.4
Results and discussion
Precipitate is formed in control set-up (tube C).
No precipitate is formed in tubes A and B.
The results show that copper(II) ion and silver ion
are inhibitors of enzyme invertase. Their presence
slows down the action of invertase on sucrose.
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Enzymes
2 Effect of pH on enzymes:
pH
Enzymes
Optimum pH
Work best
Extreme pH
Denatured
103
Action
NonCompetitive
competitive
Compete Change the
What is their
shape of
for active
mode of action?
enzyme
site
105
107
example:
lipases and proteases
to remove stains
containing lipids and
proteins
biological washing
powder
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example:
a protease extracted
from papaya
papain
to soften meat
meat tenderizer
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example:
cheese
example:
enzymes
to modify starch to
keep the bread soft
bread
111
example:
fruit juice
enzymes
to break down plant
cell walls so that the
juice looks less
cloudy
112
example:
leather
enzymes
to remove hairs from
hides ( )
to soften leather
113
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Specific in action
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4.5
Investigation of protease activities in
different fruit juices
1 Heat the end of a cork borer in a Bunsen flame and allow it to cool.
118
4.5
2 Gently press the borer down into the milk-agar plate to make five wells. Replace
the lid quickly.
cork
borer
well
119
4.5
3 Use a clean dropper to fill the wells AD with pineapple juice, kiwi fruit juice, papaya
juice and guava juice. Fill well E with distilled water.
4.5
4 Replace the lid. Incubate the plate at 35C for one hour.
incubator
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4.5
5 Measure the diameter of the clear zones around the wells by placing the plate on
graph paper and examining against light.
122
4.5
Results and discussion
Clear zones are observed around the wells
containing fruit juices and their diameters are
different.
123
4.5
Results and discussion
The results show that pineapple, kiwi fruit, papaya and guava contain
proteases that can break down proteins, but the activities of the proteases
differ from one another.
124
4.6
Video
enzyme
127
enzyme
129
Enzymes
lower the
energy barrier
therefore speed up
metabolic reactions
include
anabolic catabolic
reactions reactions
130
Enzymes
have an
active site
shows
specificity
can be explained by
lock-and-key hypothesis
131
Enzymes
activities affected by
temperature pH inhibitors
too low too high
causes causes
extreme values
cause
inactivation denaturation
of enzymes of enzymes
132
inhibitors
may be
competitive
non-competitive
133