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Catalase Enzyme Reaction Rates Experiment

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38 views5 pages

Catalase Enzyme Reaction Rates Experiment

Uploaded by

baria.najmeddine8
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Catalase enzyme reaction rates experiment

Title: catalase enzyme reaction rates experiment


Aim: the aim of this experiment is to explore the effects of pH, temperature, and
substrate concentration, enzyme concentration and inhibitor on the rate of
hydrogen peroxide breakdown in the presence of the enzyme catalase. This
helped us with understanding how enzymes work and how different conditions
make them work faster or slower.
Intro:
catalase, an enzyme that brings about the reaction by which hydrogen
peroxide is decomposed to water and oxygen. Enzymes are proteins that help
speed up metabolism, or the chemical reactions in our bodies. They build some
substances and break others down. All living things have enzymes. Our bodies
naturally produce enzymes. But enzymes are also in manufactured products and
food. A catalase reaction's rate will rise in response to an increase in substrate
concentration until it reaches its optimum concentration, or saturation point, at
where it will stabilize.

hypothesis:
It is hypothesized that the pH is closest to the optimum pH of the catalase (near
pH7.0 in humans).
Materials:
- A source of catalase; powdered yeast
- 5 cm3 syringe / pipette
- Dropping pipette
- 25ml Measuring cylinder
- Water bath set to 80°C
- Stopwatch
- Solutions of Hydrogen peroxide (20Vol, 15Vol, 10Vol, 5Vol, and 0Vol)
10Vol, 5Vol, and 0Vol)
- Access to an electronic balance
- Access to buffers of pH 2,4,6,8,10 and to water baths of 10, 30, 50, 70,
and 90 °C
Methodology:
Method A: Measuring the Rate of the Reaction
a) 0.1g of yeast powder was measured using an electronic balance. The
yeast cells contained the enzyme catalase.
b) b) 5 cm³ of 20-volume hydrogen peroxide was measured into a boiling
tube.
c) c) The inverted measuring cylinder was set up as shown in the diagram.
d) d) The yeast was added to the boiling tube, and the tube was quickly
connected to the rest of the apparatus.
e) e) Every 10 seconds, the volume of oxygen was recorded until the bubbles
stopped.

Method B: Different concentrations of substrate


Five 0.1g samples of yeast powder were measured using an electronic
balance and placed on carefully folded pieces of paper (or in dry test
tubes).
a) 5 cm³ of each hydrogen peroxide concentration was measured into
separate boiling tubes and labeled as 20 Vol, 15 Vol, 10 Vol, 5 Vol, and 0
Vol.
b) The inverted measuring cylinder was set up as shown in the first
diagram.
c) The yeast was added to the first boiling tube, and the tube was quickly
connected to the rest of the apparatus.
d) After 1 minute, the volume of oxygen produced was recorded.
e) Steps c and d were repeated for each of the five concentrations of
hydrogen peroxide.

Method C: Measuring the Rate with different pH


a) Five 0.1g samples of yeast powder were measured again.
b) b) 5 cm³ of 20 Vol hydrogen peroxide was measured into five separate
boiling tubes.
c) c) Each tube was labeled pH2, pH4, pH6, pH8, and pH10, and five
drops of buffer were added to each to adjust the pH.
d) d) The inverted measuring cylinder was set up as before.
e) e) The yeast was added to the first boiling tube, and the tube was
quickly connected to the rest of the apparatus.
f) f) After 30 seconds, the volume of oxygen produced was recorded.
g) g) This process was repeated for each of the five different pH levels.

Method D: Measuring the Rate at different temperatures.


a. Five 0.1g samples of yeast powder were measured again.
b. 5 cm³ of 20 Vol hydrogen peroxide was measured into five separate
boiling tubes.
c. Each tube was labeled 10°C, 30°C, 50°C, 70°C, and 90°C, and each boiling
tube was placed in a water bath for 5 minutes. The temperature was
checked using a thermometer.
d. The inverted measuring cylinder was set up as before.
e. The yeast was added to the first boiling tube, and the tube was quickly
connected to the rest of the apparatus.
f. After 10 seconds, the volume of oxygen produced was recorded.
g. This process was repeated for each of the five temperatures of hydrogen
peroxide.
Method E: Measuring the Rate at the presence of an inhibitor.
a. Five 0.1g samples of yeast powder were measured again.
b. 5 cm³ of 20 Vol hydrogen peroxide was measured into five separate
boiling tubes.
c. Five tubes were labeled as follows: 0 cm³, 1 cm³, 2 cm³, 4 cm³, and 5
cm³.
d. The specified volume of copper sulfate (the inhibitor) was added to each
of the labeled tubes.
e. The inverted measuring cylinder was set up as before.
f. The yeast was added to the first boiling tube, and the tube was quickly
connected to the rest of the apparatus.
g. After 10 seconds, the volume of oxygen produced was recorded for one
minute.
h. Steps 1–6 were repeated for each of the five concentrations of the
inhibitor.

Results:
1. Effect of substrate concentration

2. PH

3. Temperature
4. Enzyme concentration

5. Inhibitor concentration

Discussion and evaluation:


A limitation to the accuracy of these experiments may be the inaccuracy of the
timing as there may be slight delays in starting the timer or connecting the
apparatus after adding the enzyme, affecting the recorded reaction rate. Another
limitation to the accuracy of these experiments is the change of temperature of
the water may not stay the same throughout the entire experiment as when the
temperature gets higher it can influence enzyme activity. These inaccuracies
make the final data less accurate and reliable. The purpose of this experiment
was to explore the effects of pH, temperature, and substrate concentration,
enzyme concentration and inhibitor on the rate of hydrogen peroxide breakdown
in the presence of the enzyme catalase. The hypothesis I was testing was that
the pH is closest to the optimum pH of the catalase. Some trends and patterns I
can observe in the data related to enzyme activity are as inhibitor concentration
increases, oxygen production and reaction rate decrease. This shows that the
inhibitor slows down catalase activity as expected. Another trend that I observed
was the reaction rate increases with temperature up to 50°C, then decreases at
higher temperatures due to enzyme dehydration. I think I could you improve the
experimental design to minimize errors or obtain more reliable data by using
more precise equipment and repeating the experiment more times to get more
reliable data.

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