SENIOR HIGH SCHOOL

General Biology1
Quarter 1 – Module :
Factors Affecting Enzyme
Activity
Science – Grade 11
Alternative Delivery Mode
Quarter 1 – Module : Factors Affecting Enzyme Activity
First Edition, 2020

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General Biology 1
Quarter 1 – Module ___:
Factors Affecting Enzyme
Activity
Introductory Message
For the facilitator:

Welcome to the General Biology 1 with Grade 11 Alternative Delivery Mode

(ADM) Module on Factors Affecting Enzyme Activity!

This module was collaboratively designed, developed and reviewed by educators

both from public and private institutions to assist you, the teacher or facilitator in
helping the learners meet the standards set by the K to 12 Curriculum while
overcoming their personal, social, and economic constraints in schooling.

This learning resource hopes to engage the learners into guided and independent
learning activities at their own pace and time. Furthermore, this also aims to help
learners acquire the needed 21st century skills while taking into consideration
their needs and circumstances.

In addition to the material in the main text, you will also see this box in the body of
the module:

Notes to the Teacher

This contains helpful tips or strategies
that will help you in guiding the learners.

As a facilitator you are expected to orient the learners on how to use this module.
You also need to keep track of the learners' progress while allowing them to
manage their own learning. Furthermore, you are expected to encourage and assist
the learners as they do the tasks included in the module.

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For the learner:

Welcome to the General Biology 1 Alternative Delivery Mode (ADM) Module on

Factors Affecting Enzyme Activity!

The hand is one of the most symbolized part of the human body. It is often used to
depict skill, action and purpose. Through our hands we may learn, create and
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This module has the following parts and corresponding icons:

What I Need to Know This will give you an idea of the skills or
competencies you are expected to learn in
the module.

What I Know This part includes an activity that aims to

check what you already know about the
lesson to take. If you get all the answers
correct (100%), you may decide to skip this
module.

What’s In This is a brief drill or review to help you link

the current lesson with the previous one.

What’s New In this portion, the new lesson will be

introduced to you in various ways such as a
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What is It This section provides a brief discussion of

the lesson. This aims to help you discover
and understand new concepts and skills.

What’s More This comprises activities for independent

practice to solidify your understanding and
skills of the topic. You may check the
answers to the exercises using the Answer
Key at the end of the module.

What I Have Learned This includes questions or blank

sentence/paragraph to be filled in to process
what you learned from the lesson.

What I Can Do This section provides an activity which will

help you transfer your new knowledge or

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 skill into real life situations or concerns.

Assessment This is a task which aims to evaluate your

level of mastery in achieving the learning
competency.

Additional Activities In this portion, another activity will be given

to you to enrich your knowledge or skill of
the lesson learned. This also tends retention
of learned concepts.

Answer Key This contains answers to all activities in the

module.

At the end of this module you will also find:

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developing this module.

The following are some reminders in using this module:

1. Use the module with care. Do not put unnecessary mark/s on any part of
the module. Use a separate sheet of paper in answering the exercises.
2. Don’t forget to answer What I Know before moving on to the other activities
included in the module.
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If you encounter any difficulty in answering the tasks in this module, do not
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We hope that through this material, you will experience meaningful learning
and gain deep understanding of the relevant competencies. You can do it!

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 What I Need to Know

This module was designed and written with you in mind. It is here to help you
master the nature of Biology. The scope of this module permits it to be used in
many different learning situations. The language used recognizes the diverse
vocabulary level of students. The lessons are arranged to follow the standard
sequence of the course. But the order in which you read them can be changed to
correspond with the textbook you are now using.

After going through this module, you are expected to:

1. identify the properties of an enzyme;
2. determine how pH, temperature, and substrate affect enzyme activity;
3. design a simple experiment that illustrates how pH, temperature, or
amount of substrate affects enzyme activity.

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 What I Know

Choose the letter of the best answer. Write the chosen letter on a separate sheet of
paper.

1. Each enzyme only has 1 substrate that will fit its active site. What is this called?
A. denaturation C. reusability
B. fragility D. specificity

2. How do enzymes speed up chemical reaction?

A. Increasing activation energy C. Increasing deactivation energy
B. Decreasing activation energy D. Decreasing deactivation energy

3. Some people cannot digest milk products because they lack a specific enzyme.
Which enzyme would be used to break down the lactose in milk?
A. Hydroxylase C. Maltase
B. Lactase D. Peroxisomes

4. The part of the enzyme where the substrate binds is called the:
A. active site C. inhibitor
B. catalyst D. large subunit

5. The active site of an enzyme differs from an antibody-antigen binding site in that
the enzyme active site
A. catalyzes a chemical reaction.
B. contains modified amino acids.
C. is complementary to a specific ligand.
D. contains amino acids without sidechains.

6. What happens when an enzyme changes shape?

A. enzyme dies
B. reaction speeds up
C. reaction slows down
D. enzyme has to change back its shape to work

7. The pH at which an enzyme is most efficient is called the _________ pH of an

enzyme.
A. Experimental C. Neutral
B. Minimum D. Optimum

8. What is it called when an enzyme's shape is changed?

A. Delete C. Denature
B. Demolish D. Destroy

9. Which of the factors does NOT affect enzymatic activity?

A. Color C. pH level
B. Concentration D. Temperature

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10. Which of these is NOT true?
A. Extreme pH can denature enzymes.
B. Enzymes speed up chemical reactions.
C. Enzymes can only be used once in a chemical reaction.
D. Enzymes can denature (change shape) when the temperature gets too high.

11. Enzyme A digests proteins in the stomach (environment with a pH of 2).

Enzyme B digests proteins in the small intestine (environment with a pH of 8).
Which of the following is NOT true?
A. Enzyme A works best in acidic conditions.
B. Enzyme A helps in the hydrolysis of proteins.
C. Enzyme A can also work in the small intestine.
D. Enzyme A would be denatured in the small intestine.

12. Trypsin has an optimum temperature of 35°C and an optimum pH of 7.5. What
would happen if the pH changed to 3?
A. Reaction rate will not change.
B. Sucrase would continue to work the same
C. The reaction sucrase catalyzes would speed up
D. The reaction sucrase catalyzes would slow down

13. The diagram provided shows an enzyme that has undergone a sudden change
in pH. What happened to this enzyme?

A. The enzyme has been killed.

B. The enzyme has been destroyed.
C. The enzyme has been denatured.
D. The enzyme has been replicated.

14. Some bacteria live in hot springs. Their cells contain enzymes that function
best at temperatures of 70 °C or higher. At the temperature of 50 °C, how will
the enzymes in these bacterial cells most likely be affected?
A. The enzymes will be destroyed by lysosomes
B. The enzymes will lose their bond structure and fall apart.
C. The enzymes will require less energy to function than at 70 °C.
D. The enzymes will not increase the rate of reactions as much as they would at
70 °C.

15. The human body maintains a temperature of around 98.6 degrees at all times.
Enzymes are involved in almost every chemical reaction in the body. Which of
the following describes the connection between these two statements?
A. Enzymes function best at a specific temperature.
B. The body needs to be warm to prevent hypothermia.
C. There is no connection between the two statements.
D. The body is kept relatively warm to prevent too much enzyme action.

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E.

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 Lesson
Factors Affecting Enzyme
1 Activity
Enzymes are basically protein molecules with a special physiological function. They
catalyze and speed up chemical reactions, thus saving energy use in the cell. Some
enzymes need co-factor such as metal and other molecules. Some examples of
enzymes are amylase that performs partial digestion in our mouth; kinases which
perform signal transduction. By modifying the structure of a certain substrate, the
reaction becomes faster for the cell. They participate both in anabolism and
catabolism.

What’s In

Last module we have learn about oxidation- reduction reaction which is a type of
chemical reaction that involves a transfer of electrons between two species. It is any
chemical reaction in which the oxidation number of a molecule, atom, or ion
change by gaining or losing an electron. Redox reactions are common and vital to
some of the basic functions of life, including photosynthesis, respiration,
combustion, and corrosion or rusting. The two species that exchange electrons in a
redox reaction are given special names. The ion or molecule that accepts electrons
is called the oxidizing agent; by accepting electrons it causes the oxidation of
another species. Conversely, the species that donates electrons is called the
reducing agent; when the reaction occurs, it reduces the other species. In other
words, what is oxidized is the reducing agent and what is reduced is the oxidizing
agent.

Notes to the Teacher

Simple ways to remember this include the mnemonic devices OIL
RIG, meaning "oxidation is loss" and "reduction is gain," and LEO
says GER, meaning "loss of e- = oxidation" and "gain of e- =
reduced." There is no net change in the number of electrons in a
redox reaction. Those given off in the oxidation half reaction are
taken up by another species in the reduction half reaction.

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10
 What’s New

Can You Control Enzymes?

What if enzymes just kept going and converted every molecule in the world?

An organism can create its own molecules to slow down and stop the activity of
enzymes and proteins. At other times, enzymes can be controlled by poisons and
contaminants, such as herbicides. There are many factors that can regulate
enzyme activity including temperature, activators, pH levels, and inhibitors. Try to
accomplish Activity 1 then identify how some environmental factors affects enzyme
activity.

ACTIVITY 1: ENZYME PROPERTIES

1. The effect of temperature on enzyme activity.

Temperature oC Reaction rate

10 1.0
15 1.5
20 2.5
25 3.5
30 5.5
35 7.5
40 9.5
45 8.5
50 7.0
55 4.0
60 0.0

a. Using a graphing paper, draw a line graph of the results of the effects of
temperature on a typical enzyme reaction rate. Use a smooth hand drawn
line to join the points
b. What is the best temperature for this enzyme to work?
c. Most enzymes work at this temperature in humans, why do you think this
is?

2. The effect of pH on enzyme activity.

pH Reaction rate
1.0 8.5
1.5 10.0
2.0 8.5
2.5 7.0
3.0 5.5
3.5 3.0

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a. Draw a line graph of the results of the effects of pH on the enzyme pepsin’s
reaction rate. Use a smooth hand drawn line to join the points
b. What is the best pH for this enzyme to work? (try and be quite accurate)
c. Where is this enzyme found?
d. Why do you think it works best at such an acidic pH?

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 What is It

Like most chemical reactions, the rate of an enzyme-catalyzed reaction increases as

the temperature is raised. A 10ºC rise in temperature will increase the activity of
most enzymes by 50 to 100%. Variations in reaction temperature as small as 1 or 2
degrees may introduce changes of 10 to 20% in the results. In the case of
enzymatic reactions, this is complicated by the fact that many enzymes are
adversely affected by high temperatures. As shown in Figure 1, the reaction rate
increases with temperature to a maximum level, then abruptly declines with
further increase of temperature. Because most animal enzymes rapidly become
denatured at temperatures above 40°C, most enzyme determinations are carried
out somewhat below that temperature.

Figure 1. Effect of Temperature on Enzyme Activity

Source: Source: Western Oregon University

Over a period of time, enzymes will be deactivated at even moderate temperatures.

Storage of enzymes at 5°C or below is generally the most suitable. Some enzymes
lose their activity when frozen. Many enzymes lose function at lower and higher
temperatures. At higher temperatures, an enzyme’s shape deteriorates. Only when
the temperature comes back to normal does the enzyme regain its shape and
normal activity.

Various environmental factors can affect the rate of enzyme-catalysed reactions

through reversible or irreversible changes in the protein structure. Enzymes are
affected by changes in pH. The most favorable pH value - the point where the
enzyme is most active - is known as the optimum pH. This is graphically illustrated
in Figure 2.

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 Figure 2. The pH Profile of β-Glucosidase
Source: Western Oregon University

Extremely high or low pH values generally result in complete loss of activity for
most enzymes. pH is also a factor in the stability of enzymes. As with activity, for
each enzyme there is also a region of pH optimal stability. The optimum pH value
will vary greatly from one enzyme to another, as Table I shows:

Table I: Optimum pH for Selected Enzymes

 Digestive enzymes secreted in the acidic environment, with low pH of the

stomach help break down proteins into smaller molecules. The main
digestive enzyme in the stomach is pepsin, which works best at a pH of
about 1.5 to 2. These enzymes would not work optimally at other pHs.
Trypsin is another enzyme in the digestive system, which breaks protein
chains in food into smaller parts. Trypsin works in the small intestine, which
is not an acidic environment. Trypsin's optimum pH is about 8.

The pH profile is dependent on a number of factors. As the pH changes, the

ionization of groups both at the enzyme’s active site and on the substrate can alter,

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influencing the rate of binding of the substrate to the active site. These effects are
often reversible. For example, if we take an enzyme with an optimal pH (pHopt) of
7.0 and place it in an environment at pH 6.0 or 8.0, the charge properties of the
enzyme and the substrate may be suboptimal, such that binding and hence the
reaction rate are lowered. If we then readjust the pH to 7.0, the optimal charge
properties and hence the maximal activity of the enzyme are often restored.

However, if we place the enzyme in a more extreme acidic or alkaline environment

(e.g. at pH 1 or 14), although these conditions may not actually lead to changes in
the very stable covalent structure of the protein’s primary structure (i.e. its
configuration), they may well produce changes in the conformation (shape) of the
protein such that, when it is returned to pH 7.0, the original conformation and
hence the enzyme’s full catalytic activity are not restored. It should be noted that
the optimum pH of an enzyme may not be identical to that of its normal
intracellular surroundings. This indicates that the local pH can exert a controlling
influence on enzyme activity.

Initially, when the substrate concentration is increased, the rate of reaction

increases considerably. However, as the substrate concentration is increased
further the effects on the reaction rate start to decline, until a stage is reached
where increasing the substrate concentration has little further effect on the
reaction rate. At this point the enzyme is considered to be coming close to
saturation with substrate and demonstrating its maximal velocity (Vmax). Note that
this maximal velocity is, in fact, a theoretical limit that will not be truly achieved in
any experiment, although we might come very close to it.

Figure 3. Relationship Between Substrate Concentration and the Rate of an

Enzyme-Catalyzed Reaction

The relationship described here is a fairly common one, which a mathematician

would immediately identify as a rectangular hyperbola. The equation that describes
such a relationship is as follows:

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The two constants a and b thus allow us to describe this hyperbolic relationship,
just as with a linear relationship (y = mx + c), which can be expressed by the two
constants m (the slope) and c (the intercept). We have in fact already defined the
constant a — it is Vmax. The constant b is a little more complex, as it is the value on
the x-axis that gives half of the maximal value of y. In enzymology we refer to this
as the Michaelis constant (Km), which is defined as the substrate concentration that
gives half-maximal velocity.
Our final equation, usually called the Michaelis–Menten equation, therefore
becomes:

Michaelis constants have been determined for many of the commonly used
enzymes. The size of Km tells us several things about a particular enzyme.
 A small Km indicates that the enzyme requires only a small amount of
substrate to become saturated. Hence, the maximum velocity is reached at
relatively low substrate concentrations.
 A large Km indicates the need for high substrate concentrations to achieve
maximum reaction velocity.
The substrate with the lowest Km upon which the enzyme acts as a catalyst is
frequently assumed to be enzyme's natural substrate, though this is not true for all
enzymes.

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 What’s More

Activity 1.1 Understanding Enzyme Activity

Enzymes are like other chemical catalysts. They partake in the reaction
without getting affected. In other words, they speed up the chemical reactions
inside the cells without getting consumed. Enzymes are affected by the hydrogen
ion concentration (pH) and the temperature. Enzymes are highly specific compared
to other catalysts, and each enzyme is specialized for one reactant substance. This
reactant substance is called substrate, and it is specialized for one type of reaction
or a few reactions. Enzymes lower the activation energy required to get the reaction
started. Collectively, these are the most important properties of the enzyme.
This worksheet covers how temperature and pH affect the rate of enzyme
catalyzed reactions. Write your answers in a blank paper.
1. Consider the graph below:
Label the optimum temperature for the enzyme as ‘A’
Label the point at which the enzyme has been completely denatured as ‘B’

2. Explain why the rate of reaction initially increases with temperature

3. The graph below shows rate of reaction data for 2 different enzymes. One of
these enzymes are found in the stomach, the other is found in the mouth.

a) Which of these lines is more likely to indicate the enzyme found in the
stomach? Explain your answer.
b) Both these enzymes have the same optimum pH, TRUE or FALSE?

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 4. Explain, in terms of bonding, why the rate of reaction gradually falls once the
pH increases above the optimum rather than denaturing straight away
5. An enzyme-controlled reaction was carries out at 36°C. After 3 minutes, 240 cm 3
of product had been produced. Calculate the rate of reaction is cm 3/s.
Rate of reaction = …………… cm3/s

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 What I Have Learned

There are several factors that affect the speed of an enzyme’s action, such as
the concentration of the substrate, temperature, and hydrogen ion concentration
(pH):
 In the presence of a given amount of enzyme, the rate of enzymatic
reaction increases as the substrate concentration increases until a
limiting rate is reached, after which further increase in the substrate
concentration produces no significant change in the reaction rate. At
this point, so much substrate is present that essentially all of the
enzyme active sites have substrate bound to them. In other words, the
enzyme molecules are saturated with substrate. The excess substrate
molecules cannot react until the substrate already bound to the
enzymes has reacted and been released (or been released without
reacting).
 The protein nature of the enzymes makes them extremely sensitive to
thermal changes. Enzyme activity occurs within a narrow range of
temperatures compared to ordinary chemical reactions. As you have
seen, each enzyme has a certain temperature at which it is more
active. This point is called the optimal temperature, which ranges
between 37 to 40°C.
 The enzyme activity gradually lowers as the temperature rises more
than the optimal temperature until it reaches a certain temperature at
which the enzyme activity stops completely due to the change of its
natural composition.
 On the other hand, if the temperature lowers below the optimal
temperature, the enzyme activity lowers until the enzyme reaches a
minimum temperature at which the enzyme activity is the least. The
enzyme activity stops completely at 0°C, but if the temperature rises
again, then the enzyme gets reactivated once more.
 Each enzyme has a pH value that it works at with maximum efficiency
called the optimal pH. If the pH is lower or higher than the optimal
pH, the enzyme activity decreases until it stops working. For example,
pepsin works at a low pH, that it is highly acidic, while trypsin works
at a high pH, that it is basic. Most enzymes work at neutral pH 7.4.

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 What I Can Do

Activity 1.2 Fruits Gone Enzymatic Browning

Have you ever wondered why potato slices turn brown once you cut them, or why a
yellow banana gets dark spots over time? Both of these phenomena have the same
cause: enzymatic browning triggered by an enzyme called polyphenol oxidase (PPO).
In this activity you will find out how this enzyme works by turning a banana from
yellow to brown in just a matter of seconds. Then you will explore how you can
keep your potato slices looking fresh.

Materials:
Banana (yellow with no brown spots)
Stove
Pot
Water
Timer
Adult helper
Potato
Cutting board
Knife
Lemon juice
Distilled vinegar
Milk
Additional one to two bananas (optional)
Fridge (optional)
Tape (optional)
Other fruits and vegetables to test (optional)

Preparation:
16.Fill a pot with tap water.
17.Place the pot on the stove and heat the water until boiling. Always use
caution and adult help when working around very hot water.

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Procedure:
1. Take one of your bananas and look closely at its peel. What color is it? Do
you see any brown spots?
2. Carefully dip the bottom third of the banana into the boiling water for 30
seconds. What happens to the banana when you submerge it in hot water?
3. After the 30 seconds remove the banana from the boiling water and observe
it for another three minutes. What do you notice? Does the banana look
different after a while? How?
4. When the banana has cooled down, peel the banana. Look at the fruit that
was inside the peel. Did you expect the banana to look like that?
5. Cut two slices from the potato on a cutting board. Place each slice onto its
side. How do they look?
6. Pierce one of the potato slices with a fork several times. Then observe both
slices for 15 to 20 minutes. How do the potato slices change over time? Do
you notice a difference between the two slices? If yes, can you explain why?
7. Cut five more slices from the potato and place each slice on its side.
Immediately after cutting, sprinkle milk on top of the first slice, distilled
vinegar on the second slice, lemon juice on the third slice and water on the
fourth slice. Keep the last slice as is. Then pierce each potato slice several
times with a fork. What do you think these liquids will do to the potato?
Observe all five potato slices for another 15 to 20 minutes. How are the
potato slices different after 15 to 20 minutes? What did each liquid do to the
potato slice? Can you explain your results?

Assessment

Multiple Choice. Choose the letter of the best answer. Write the chosen letter on a
separate sheet of paper.
1. Which of these can destroy or permanently deactivate an enzyme?
A. Poison
B. High Acidity
C. Extreme Temperature
D. All of the Above

2. The main reason why rate of enzyme action increases with temperature initially
is?
A. The enzymes become denatured
B. Time passing, allowing more collisions to occur
C. The kinetic energy of enzymes and substrates increases
D. More substrate is produced, therefore the enzymes become saturated

3. Which of the factors does NOT affect enzymatic activity?

A. Color C. pH
B. Concentration D. Temperature

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4. Enzymes need certain environmental conditions in order to function
properly. What happens when enzymes are heated to a high temperature?
A. die C. work better
B. denature D. change their amino acid sequence

5. Which of these is NOT true?

A. Extreme pH can denature enzymes.
B. Enzymes speed up chemical reactions.
C. Enzymes can only be used once in a chemical reaction.
D. Enzymes can denature (change shape) when the temperature gets too
high.

6. Enzyme A digests proteins in the stomach (environment with a pH of 2).

Enzyme B digests proteins in the small intestine (environment with a pH of
8). Which of the following is NOT true?
A. Enzyme A works best in acidic conditions.
B. Enzyme A helps in the hydrolysis of proteins.
C. Enzyme A can also work in the small intestine.
D. Enzyme A would be denatured in the small intestine.

7. Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2.

What would happen if the pH changed to 3?
A. Reaction rate will not change.
B. Sucrase would continue to work the same
C. The reaction sucrase catalyzes would speed up
D. The reaction sucrase catalyzes would slow down

8. Based on the graph shown at the side, at

what temperature would there be the
most enzyme activity?

A. 25°C
B. 30°C
C. 35°C
D. 40°C

9. Which of the following conclusions can

be drawn from the graph shown below?

A. Optimum pH of the enzyme is 5.8

B. Optimum pH of the enzyme is 6.6.
C. Enzyme’s activity is greater around
pH of 8.0
D. Enzyme’s activity increases as pH
increases 5.0 to 9.0

10. The pH at which an enzyme is most efficient is called the _________ pH of an

enzyme.
A. Experimental C. Neutral
B. Minimum D. Optimum

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11. What is it called when an enzyme's shape is changed?
A. Delete C. Denature
B. Demolish D. Destroy

12. What happens when an enzyme changes shape?

A. enzyme dies
B. reaction speeds up
C. reaction slows down
D. enzyme has to change back its shape to work

13. Which of the factors does NOT affect enzymatic activity?

C. Color C. pH level
D. Concentration D. Temperature

14. The graph below shows the rate of an enzyme-controlled reaction compared
to the concentration of substrates. Why does the graph plateau?

A. The enzymes have denatured, and so the reaction has stopped.

B. The products made bind to the active sites, so no more substrates can
bind.
C. There are no more substrates to be broken down, so the rate of reaction
has reached its maximum.
D. There are no available enzymes to bind to more substrates, so the rate
of reaction has reached its maximum.

15. The active site of an enzyme differs from an antibody-antigen binding site in
that the enzyme active site ______?
A. catalyzes a chemical reaction.
B. contains modified amino acids.
C. is complementary to a specific ligand.
D. contains amino acids without sidechains.

23
 Additional Activities

In connection to Activity 1.2 “Fruits Gone Enzymatic Browning” instead of heating

the banana, try exposing it to cold. Place one banana in the fridge for several days.
Take a second banana and cover parts of the banana peel with duct tape. Get
creative with the pattern of the tape! Then put that banana in the fridge as well.
Check on both bananas every day. Do both bananas change color? How does the
second banana look when you remove the tape after a couple of days? What do you
think happened?
Beside bananas and potatoes other fruits can also undergo enzymatic
browning. Test different fruits or vegetables to see if they are prone to enzymatic
browning. Or try the same fruit but test different kinds of that fruit. How do
different kinds of potatoes compare?

24
 Answer Key

What's More

Factors Affecting Enzyme Action

1.

2. As temperature increases the molecules have more

energy so collide more often and with more energy
meaning more successful collisions and a faster rate
(2 marks)

3.

What I Know

1. D
2. B
3. B
4. A
5. A
6. C
7. D
a) The solid black line. As that is at a lower pH and 8. C
9. A
the stomach is very acidic, with a pH of 2. 10. C
11. C
b) False 12. D
13. C
14. D
15. A

25
cont. Assessment

4. The bonds around the active site start to break so 1. D

2. C
the active site changes shape which means that 3. A
4. B
the substrate can no longer fit as well and so less
5. C
enzyme-substrate complexes will form and less 6. C
7. D
product will be made (2 marks) 8. B
9. B
5. Rate of reaction = 240 cm3 ÷ 180 s 10. D
11. C
12. C
= 1.33 cm3/s (2 marks)
13. A
14. D
15. A

26
References
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