[SASBADI, SECTION A, QUESTION 1]

Answer:
(a) (i) A: enzyme (sucrase); B: substrate (sucrose); C: fructose; D: glucose
(ii) 1. Enzyme is specific
2. Enzyme is sensitive to temperature/pH

(b) (i) Enzyme-substrate complex

(ii) Subtrate molecules fits into the active site of the enzyme molecule

(c) (i) Lock-and-key hypothesis

(ii) Enzymes are specific

(d) (i) Rate of reaction will decrease

(ii) Enzyme molecule is denatured at high temperatures.

[SASBADI, SECTION A, QUESTION 2]

Answer:
(a) (i) Enzyme X: pH 1-pH 7; Enzyme Y: pH 4-pH 8
(ii) Enzyme X: pH4; Enzyme Y: pH 6

(b) (i) Enzyme X

(ii) X has a bigger range of 6, but Y has a smaller range of 4

(c) (i) pH 4 to pH 7
(ii) pH 5

(d) Excess H+ and OH- on the active site prevents the formation of the enzyme-substrate
complex.

(e)
Diagram pg 585

[SASBADI, SECTION B, QUESTION 3]

Answer:
(a) - Are protein molecules [1 m]
- Synthesized in ribosomes of living cells [1 m]
- Acting as catalysts that speed up the rate of reaction in a body [2 m]

(b) Metabolic enzymes

- are intracellular enzymes [1 m]
- synthesized in a cell and catalyses reaction within a cell [1 m]
- for example – the DNA polymerase catalyses the synthesis of DNA in a nucleus [1 m]

Digestive enzymes
- are extracellular enzyme [1 m]
- are synthesized in cells and then excreted out to catalyse reactions, particularly as
digestive enzymes
[1 m]
- for example – the salivary amylase catalyses the conversion of starch to maltose in the
buccal cavity
(inside the mouth) [1 m]
(c) - Figure 3 is a graph of the rate of reaction against temperature (from 15oC to 40oC. [1
m]
- From A to B, the rate of reaction increases as temperature increases from 15oC to
o
40 C. [1 m]
- Temperature rise increases kinetic energy, which increases the number of collisions
between enzymes and substrate, increasing the rate of reaction. [2 m]
o
- The rate of reaction achieves a maximum at B (40 C). [1 m]
- All the enzyme molecules are involved in the catalysis of substrate per unit time. [1 m]
- From B to C, the rate of reaction decreases as the temperature increases from 40oC to
45oC.
[1 m]
- The more the temperature increases, the more the enzyme molecules denature,
leading to a gradual decrease in rate of reaction. [2 m]

[SPM 2005, PAPER 2, SECTION A, QUESTION 4]

Answer:
(a) P: Golgi apparatus
R: Secretory vesicles

(b) (i) Produces energy

(ii) Q stores genetic information in the DNA and this information is transferred to the
RNA
which then carries it out to the cytoplasm.

(c) (i) Protease enzyme softens the meat

(ii) Cellulase breaks down cell walls of seaweed and frees agar-agar contained in it.

(d)

[SPM 2006, PAPER 2, SECTION A, QUESTION 2]

Answer:

(a) (i) Ileum

(ii) Lipase
(iii)
(b) (i) The pancreas secretes an amylase into the duodenum which hydrolyses starch to
maltose.
(ii) - The duodenum medium becomes acidic
- Which is not suitable for the action of the amylase on starch
- Slows down the digestion of starch

(c) - Papaya contains papain/protease

- The pieces of meat and papaya strips increase the total surface area
- To increase enzyme action
- Protease will tenderize the meat
- Takes place in water at 40oC, which is the optimum temperature for enzyme reaction

[SASBADI PAPER 2, SECTION C, QUESTION 4]

Answer
1.(a) (i) Pepsin does not digest the cell wall of the stomach because:
• The stomach is protected by a mucus lining [1
m]
• Mucus consists of mainly lipid (fat) and carbohydrate (polysaccharide) on which
pepsin (digesting only proteins) has no effect [1
m]
• Pepsin is synthesised in an inactive form (pepsinogen) [1
m]
• It only turns into active pepsin when proteins from a meal enter the stomach[1
m]

(ii) The action of the enzymes causes the responses to take place
• Enzymes break chlorophyll down so that the fruit skin changes colour from
green to yellow
[1 m]
• Pectinase breaks the pectin (pectin glues the cells together) down, so they can
slip past each other, making the banana soft [1
m]
• Amylase hydrolyses starch into sugar, increasing its juiciness and sweetness [2
m]
• Enzymes break down large organic molecules into smaller ones so that they
become volatile (evaporate into the air) and we can detect the aroma [1
m]

(b) Biological detergents

• Detergents proteases degrade coagulated proteins into soluble short-chain
peptides
 [1m
]
• Detergent lipase degrade fat or oil stains into soluble fatty acids and glycerol[1
m]
• Detergent amylase degrade starch stains into soluble shorter-chained
polysaccharides and sugars [1
m]

Baking industry
• Protease is used in the breakdown of proteins in flour for biscuit manufacture [1
m]
• Amylase is used in the breakdown of some starch to glucose in flour for white
bread, buns and rolls [1
m]

Medical
• Trypsin is used to remove blood clots and in cleaning wounds [1
m]
• Various enzymes are used in biosensors [1
m]

Enzymes are used in industries for these reasons:

• Enzymes are effective [1
m]
• Enzymes are cheap and easy to use [1
m]
• Enzymes can be re-used, so only small amounts are needed [1
m]
• As enzymes do not need high temperatures to work, this reduces fuel costs [1
m]

[SASBADI PAPER 3]
Answer
Aim of investigation: To investigate how different enzyme concentrations affect the rate
of enzyme-catalysed reaction

Statement of hypothesis:In the presence of excess starch, increasing the concentration of

amylase will increase the rate of reaction proportionately

Variables:
Manipulated variable: Concentration of amylase solution
Responding variable: Rate of reaction
Constant variable: pH, temperature (room temperature) and amount of starch

Materials: 1% starch solution, iodine test solution

Apparatus: Dropper, beaker, test tubes in a rack, labeling stickers, a

stopwatch, a white cavity tile

Technique used: time taken by amylase to catalyse the hydrolysis of a starch

 solution is determined by sing the iodine test solution

Procedure:
1. Mouth is rinsed with water and 5ml of saliva is collected in a small beaker
2. The same amount of distilled water is added into the small beaker to make a salivary
amylase solution
3. Six test tubes are labeled as A, B, C, E, and F.
4. The amount of saliva solution and distilled water which is poured into each test tube
are shown in the table below.
Test tube A B C D E F
Amount of saliva solution (ml) 0.5 1.0 1.5 2.0 2.5 3.0
Amount of distilled water (ml) 3.5 3.0 2.5 2.0 1.5 1.0

5. Two drops of iodine solution is put into all the cavities of a white cavity tile.
6. 5ml of starch solution is poured into test tube A and the stopwatch is started.
7. A dropper is used to transfer a drop of mixture from A into a cavity of the while tile.
8. Any changes in colour of the iodine solution are observed.
9. Steps 7-8 is repeated in one-minute intervals until the blue-black colour of the
iodine solution in the cavity disappears.
10. The time taken for the blue-black colour to disappear is recorded in the table.
11. Steps 5-10 are repeated for test tube B to F.

Collected data:
1. The experimental data are tabluted in the table below.
2. The rate of reaction for each amylase concentration is calculated.

Presentation of data:
A graph of the rate of reaction against amylase concentration is plotted using data from the
table below.
Test tube Time for the blue-black iodine Rate of reaction, 1/t (min-1)
colour to disappear, t(min)
A
B
C
D
E
F

Conclusion:
If the graph for the rate of reaction against amylase concentration shows a linear relation,
accept the hypothesis. Otherwise, reject the hypothesis.

[SPM 2006, PAPER 3, QUESTION 1]

Answer:
(a) (i) 1. The albumen suspension of concentration 10% becomes clear at 7 minutes.
2. The albumen suspension of concentration 20% becomes clear at 13 minutes.

(ii) 1. The albumen has been hydrolised by the enzyme/pepsin.

2. The albumen has been hydrolised by the enzyme/pepsin.
(b) 10% - 7 minutes
15% - 10 minutes
20% - 13 minutes

(c) (i)
Variable
Manipulated variable
Concentration of the albumen suspension
Responding variable
Time taken
Controlled variable
Enzyme concentration
Method to handle the variable
Use albumen suspensions of
different concentrations
Measure and record the time
taken for the cloudiness of the
albumen suspension to clear,
by using stopwatch
Using the same enzyme
concentration, i.e 1%

(ii)
Variable Apparatus Material
Manipulated Syringe Albumen suspension
Responding variable Stopwatch Pepsin
Controlled variable Thermometer Water bath

(d) The higher the concentration of the albumen suspension is, the longer the time taken
for the enzyme reaction will be.

(e) (i)
Percentage of albumen (%) 10 15 20
Time (minutes) 7 10 13
Rate of enzyme reaction as the 1.43 1.50 1.54
percentage of albumen
converted per minute

(ii)
 (iii) - When the concentration of albumen suspension increases, the rate of pepsin
reaction increases
- Because the number of substrate molecules/albumen molecules increase
- Causing the collision between the enzyme molecules and the substrate molecules
to increase

(f) - Enzyme/pepsin hydrolyses the albumen suspension

- The cloudy suspension turns clear
- The rate of pepsin reaction is affected by the albumen concentration

(g) R, because the enzyme used has been boiled. Hence, it is denatured and cannot act on
the substrate/albumen

[SPM 2009, PAPER 3, QUESTION 2]

Answer
Problem statement: What is the effect of temperature on the activity of salivary
amylase on starch?

Objective: To study the effect of temperature on the rate of enzyme reaction

Hypothesis: When the temperature increases, the rate of enzyme reaction

increases

Variables:
Manipulated variable: Temperature of the reaction
Responding variable: The rate of enzyme reaction / The time taken for the hydrolysis of
starch
Constant variable: Volume of enzyme / Concentration of enzyme

Materials: Starch suspension, saliva, water bath, ice cubes, iodine solution
Apparatus: Beakers, tile with grooves, test tube, thermometer, syringe,
stopwatch, Bunsen burner, tripod stand, wire gauze, glass rod

Technique used: Use a stopwatch to record the time taken for the complete
hydrolysis of starch

Procedure:
1. Use a syringe to put 1 ml of 0.1% starch suspension into each of the test tubes
labeled A1 and B1.
2. Use another syringe to put 2 ml of saliva into each of the test tubes labeled A2 and
B2.
3. Immerse test tube A1 and A2 into a water bath of cold water (10oC)
4. After 5 minutes of immersion, pour the starch suspension from test tube A1 into test
tube A2. Stir the mixture, using a glass rod.
5. Start the stopwatch.
6. Use a dropper to put a drop of mixture from test tube A2 onto the iodine solution in
the first groove of the white tile.
7. Repeat the iodine test every minute for 10 minutes.
8. Rinse the dropper after each sampling
9. Record the time taken for the hydrolysis of starch.
10. Keep the test tubes with the mixtures in their respective water baths throughout the
experiment.
11. Repeat the experiment with warm water (37oC).
12. Repeat the experiment to get average readings.
13. Record the results in a table.

Tabulation of data:
Temperature/oC Time taken for the starch to Rate of reaction (min-1)
disappear/minutes
10
37

Conclusion:
When the temperature increases, the rate of amylase reaction increases.