Catalyze Enzyme Activity

I. Objectives
In conducting this experiment, the following objectives are followed:
1. To observe the breakdown of hydrogen peroxide toxin by potato's enzyme
catalase.
2. To determine if temperature and pH affect enzyme effectiveness.
II. Procedures
1. Prepare the potato wedges.
1.1 Potato 1 – normal 2 cm size.
1.2 Potato 2 – normal 2 cm size but boiled.
1.3 Potato 3 – small bits of potato.
1.4 Potato 4 – normal 2 cm size.

2. Prepare four test tubes and a rack.

2.1 Put hydrogen peroxide to test tubes 1, 2, and 3.
2.2 Put vinegar to test tube 4.
3. Observe for 10 minutes.

4. Look at the bubbles produced, which shows the oxygen produced from the
chemical reaction
III. Experimental Setup and Materials

Before

After

Materials:
Picture/Image Name Function
Marker Marker – used to mark the potato in order
Ruler to cut it properly.
Chopping Ruler – used to measure the potato.
Board Chopping Board – used to protect the
Knife surface of the table and to ensure that the
potato is cut properly.
Knife – used to precisely cut the potato.
Test Tubes
Test Tubes – used to be the place where
the chemical reaction takes place.
Test Tube Test Tube Rack – used to hold the test
Rack tubes in place.

Hydrogen It decomposes slowly in light to produce

Peroxide oxygen and water and was sped up by the
enzyme catalase found in potatoes.
 Vinegar Used to differentiate the product in the
chemical reaction when it comes to the
pH level.

Hot water Used to differentiate the product in the

chemical reaction when it comes to the
exposure to heat.

IV. Data & Findings

Test Tube 1 Test Tube 2 Test Tube 3 Test Tube 4

Appearance Medium number Little to a small A large number of Small to a

of bubbles number of bubbles medium number
bubbles of bubbles

V. Analysis
Test Tube 1 Test Tube 2 Test Tube 3 Test Tube 4

Appearance Medium number Little to a small A large number of Small to a

of bubbles number of bubbles medium number
bubbles of bubbles

Analysis There is a There are a There is a large There are a small

medium number minimal number number of to a medium
of bubbles of bubbles bubbles produced number of
produced from produced from from the chemical bubbles produced
the chemical the hydrogen reaction and the from the vinegar
reaction between peroxide and the bits of potato. and the boiled
the hydrogen boiled 2cm-sized Test Tube 3 got 2cm-sized potato.
peroxide and the potato. This is the largest This is because
normal 2cm-sized because the number of the enzymes
potato. enzymes inside bubbles due to inside the potato
the potato were the fact that the were already
already potatoes got a denatured by the
 denatured by the surface area. vinegar, which is
heat. a bit more acidic
than hydrogen
peroxide.
VI. Conclusion
Through this experiment, I observed how the potato enzyme catalase
accelerates the hydrogen peroxide's breakdown into oxygen and water.
However, I could also discern the various effects of potato exposure to the
surface area, acid, and heat in this activity. The results demonstrate that there
are more bubbles created in Test Tube 3 due to the potatoes being sliced into
smaller pieces, which increases their surface area and speeds up the breakdown
process. Additionally, the fact that the potato had previously been boiled and
created a small number of bubbles in Test Tube 2 indicated that the quantity of
decomposition would also be small because the potato had already been
denatured by heat. Similar results were found in Test Tube 4. Because vinegar
was added, small to medium amounts of bubbles were created, demonstrating
that only a small amount of decomposition had taken place because the potato
had already been denatured by the vinegar's acid, which has a slightly higher
acidity level than hydrogen peroxide. Overall, Test Tube 3 produced the best
findings of the four setups conducted.
Enzyme Inhibition Activity
I. Objectives
In conducting this experiment, the mentioned objectives are followed:
1. To investigate the effect of inhibitors on enzyme activity.
2. To distinguish what type of inhibition occurred in each setup.
II. Procedures
1. Label two test tubes with A and B.

2. Put chemicals in each test tube.

 2.1 Test Tube A – 5 cubic cm of urea solution, five drops of bromothymol blue
indicator, and five drops of mercuric chloride solution.
2.2 Test Tube B- 5 cubic cm of urea solution, five drops of bromothymol blue
indicator, and five drops of distilled water.

3. Add 2 cubic cm of urease solution to each test tube and shake well.

4. Leave both test tubes for 30 minutes.

 5. Note the color changes.

III. Experimental Setup and Materials

Before

After

Materials:
Picture/Image Name Function
Pipette Dropper Used to collect and
drop the chemicals
being used.
Urea Solution Used to test as an
inhibitor
Bromothymol Blue Used as an
Indicator indicator
Mercuric Chloride Used to test as an
Solution inhibitor
Distilled Water Used to test as an
inhibitor

Urease Solution Used to be the

enzyme
 Test Tubes Where the
chemicals are
being mixed and
tested
Test Tube Rack Used to keep the
test tubes in place.

IV. Data & Findings

Tube Color of bromothymol blue indicator
Original Color Final Color
A Yellow Yellow
B Yellow Blue
V. Analysis
Tube Color of bromothymol blue Analysis
indicator
Original Color Final Color
A Yellow Yellow Due to the fact that the
final color does not
change from its original
color, it only means that
the inhibitors used in
this setup can be
considered as non-
competitive enzyme
inhibitors.
B Yellow Blue Since from yellow it
changed to blue, the
inhibitors in this setup
can be considered as
competitive enzyme
inhibitors. This is proved
by the change in color,
which indicates that it
binds the active site and
prevents the substrate
from binding there.
VI. Conclusion
Through this experiment, I discovered that competitive enzyme inhibitors
compete with the substrate for the enzyme's active site by having a similar shape
to the substrate molecule. As a result, enzyme-substrate complexes cannot form.
As a result, the enzymes may attach to fewer substrate molecules, which slows
 down the reaction rate. With this information, I could determine that Tube B had
a competitive enzyme inhibitor due to the color change from yellow to blue. On
the other hand, since no color change took place in Tube A, it must contain a
non-competitive enzyme inhibitor.
Questions
1. The enzyme catalase, which is present in potatoes, converts hydrogen peroxide into
water and oxygen gas. This causes the hydrogen peroxide to break down more
quickly and create water and oxygen gas. This was demonstrated in the experiment
by the formation of bubbles, which revealed the presence of oxygen.
2. 2H2O2 -------------------> 2H2O + O2
catalase

3. Most proteins become inactive once they are coupled to mercury. In its most basic
form, mercury binds irreversibly to an enzyme, altering its conformation and
inhibiting the binding of its typical substrate.

4. A. Competitive inhibition - When molecules that are very identical to the substrate
molecules bind to the active site, they hinder the actual substrate from binding.
B. Mixed type inhibition - When the inhibitor attaches to the enzyme in a different
position than the one where the substrate will bind, this is known as mixed
inhibition.
C. Non-competitive inhibition - It is a particular kind of enzyme inhibition where an
inhibitor binds to an allosteric location and reduces the enzyme's effectiveness.
5. When hydrogen peroxide had a contact with its substrate, enzyme catalase, it starts
to decompose into water and oxygen.
References (for both)
education.com. (2013, November 18). Catalase and Hydrogen Peroxide Experiment.

Education.com. Retrieved October 20, 2022, from

https://www.education.com/science-fair/article/activator/

Oxford Mastering Biology 牛津基礎生物學. (2020, September 22). Practical 4.4

Investigation of the effect of inhibitors on enzyme activity. YouTube. Retrieved

October 20, 2022, from https://www.youtube.com/watch?v=U2It7pEZLo8

Professor Revell. (2020, September 7). Enzyme Potato Experiment [Video]. YouTube.

Retrieved October 20, 2022, from https://www.youtube.com/watch?

v=3PYdMaClUmw