Lesson Plan March 29, 2019 Biochemistry Chapter 5 Topic: Enzymes Pp. 43-47

LESSON PLAN
March 29, 2019
Biochemistry Chapter 5 Topic: Enzymes pp. 43-47

I. Objectives
At the end of the period, 85% of the students should be able to:
1. Define enzyme;
2. Explain the mechanism of enzyme action.
3. Determine the different factors that affect the rate of enzyme reaction.
4. Distinguish between competitive inhibitors and non-competitive inhibitors.
5. Appreciate the catalytic actions of enzyme in many metabolic processes by
citing examples.
II. Content
1. Enzymes are special proteins that are catalytic in action. This means that they
hasten or speed up chemical reactions without being directly used up in the
reactions. Enzymes are highly specific. Specificity is the ability of an enzyme to
discriminate between two competing substrates.
2. Mechanism of Enzyme Action
The first step in enzyme catalysis involves the formation of an enzyme-
substrate complex (ES complex) due to the binding of the substrate to an
enzyme's active site. The amino acid side chains present in active site interact
with the substrate and hold it in place. A reaction takes place faster in the
presence of appropriate enzyme than in its absence because the substrate is
held in proper orientation and near other atoms that are involved in the bond
making or bond breaking process that goes on during the reaction. Once the
product has formed, it leaves the enzyme, which is restored to its original form,
ready for another cycle of catalysis.
3. Factors that Affect the Rate of Enzyme Reaction.
 pH level- low pH or high pH values can cause denaturation and
inactivation of enzyme. Each enzyme has its own optimum pH. The
optimum pH is hydrogen ion concept traction in which the enzyme could
act best.
 Temperature- thermal denaturation of the enzyme protein with
increasing temperature will decrease the effective concentration of an
enzyme, thus decrease the reaction rate. The optimum temperature for
most enzymes is about 40°C.
 Concentration of substrates- the concentration of an enzyme is fixed but
the concentration of the substrate is variable. With fixed enzyme
concentration, an increase in substrate will result at first in a very rapid
rise in velocity or reaction rate. As the substrate concentration continues
to increase, however, the increase in the rate of reaction begins to slow
down until with a very large substrate concentration, no further change
in velocity is observed.
4. Enzyme inhibition
The action of enzyme can be inhibited or retarded in several ways. There
are two most common types of inhibitors.
 Competitive inhibitors are substances that have structure similar to that
of substrate.
 Non-competitive inhibitors- combine with free enzymes or the enzyme-
substrate complex, thus, inferring with the action of one or both.
III. Procedure
Activity: Enzymatic Browning of Apples
Background information
The purpose of this experiment is to monitor the level of enzymatic browning of
apple slices. Apples contain an enzyme called polyphenol oxidase (phenolase). In the
presence of oxygen from air, this catalyses the formation of brown pigments called
melanins.
Treatment of the apple slices with ascorbic acid, citric acid or acetic acid will
reduce the level of browning. The reduction in Browning is dependent on the type of
substance and its concentration. Soaking in water alone will temporarily reduce the
level of browning by restricting the amount of oxygen in contact with the apple slices.
Materials: 1 piece of apple and calamansi.
Procedures:
1. Ask each student to bring an apple and a piece of calamansi.
2. Let them bite two sides of the apple.
3. Ask them to put calamansi on one of the bitten side of the apple. Then, leave
the other bitten side as it is.
4. Leave the apple for 10-15 minutes.
5. Observe the changes that will occur between the two bitten sides of the
apple.
6. Compare the result between the bitten side of an apple with calamansi, and
the other side without calamansi and note the time it takes before the
changes occur.
Guide Questions
1. What changes occur between the two bitten sides of the apple? Which side
shows changes?
2. Why do you think does the bitten side of the apple without calamansi extract
turns into brown color?
3. What do you think is the role of the calamansi extract in the experiment?
IV. Evaluation
Multiple Choice. Choose the best answer.
1. These are special proteins that hasten or speed up chemical reactions without being
directly used up in the reaction.
A. Hormones
B. Enzymes
C. DNA
D. Glucose
2. The ability of an enzyme to discriminate between two competing substrates.
A. Specificity
B. Catalytic action
C. Inhibition
D. Neutralization
3. The first step in enzyme catalysis wherein the amino side chains present in active site
interact with the substrate and hold it in place results in the formation of
A. Substrate complex
B. Product
C. Enzyme-substrate complex
D. New enzyme
4. Which of the following is/are true about the relation of pH level to the rate of enzyme
reaction?
A. It can cause denaturation
B. It can inactivate the enzyme.
C. Each enzyme has its own optimum pH in which the enzyme could act best.
D. All of the above statements are true.
5. A type of enzyme inhibitor that combines with the free enzyme or the enzyme-substrate
complex, thus, interfering with the action of one or both.
A. Competitive inhibitors
B. Non-competitive inhibitors
C. Chemotherapeutic drugs
D. None of the above
V. Agreement
1. Illustrate the mechanism of enzyme action through a comic strip.
2. Cite instances where enzyme inhibition is beneficial. Use graphic organizer (bubble
map).
Prepared by: Ms. Evangeline L. Martinez

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Lesson Plan March 29, 2019 Biochemistry Chapter 5 Topic: Enzymes Pp. 43-47

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LESSON PLAN

March 29, 2019

Biochemistry Chapter 5 Topic: Enzymes pp. 43-47

Prepared by: Ms. Evangeline L. Martinez

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