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How does temperature affect the rate of an enzyme controlled reaction_

The document investigates how temperature affects the activity of catalase, an enzyme that breaks down hydrogen peroxide. It outlines that enzyme activity increases with temperature up to an optimal point (around 37°C for catalase), after which denaturation occurs, leading to decreased activity. Experimental results show that catalase produced the most foam at 26°C, demonstrating the critical role of temperature in enzymatic reactions.

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Jayden Poon
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22 views

How does temperature affect the rate of an enzyme controlled reaction_

The document investigates how temperature affects the activity of catalase, an enzyme that breaks down hydrogen peroxide. It outlines that enzyme activity increases with temperature up to an optimal point (around 37°C for catalase), after which denaturation occurs, leading to decreased activity. Experimental results show that catalase produced the most foam at 26°C, demonstrating the critical role of temperature in enzymatic reactions.

Uploaded by

Jayden Poon
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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How does temperature affect the rate of an enzyme

controlled reaction?

Research Question:

How does temperature affect the relative rate at which catalase breaks down hydrogen
peroxide?

Scientific Background:

The experiment investigates the effect of temperature on the activity of catalase, an


enzyme found in living organisms that facilitates the breakdown of hydrogen peroxide into
water and oxygen.

Enzymes are biological catalysts that speed up chemical reactions by lowering the
activation energy required for the reaction to occur. Temperature plays a crucial role in
enzyme activity because it influences the kinetic energy of the enzyme and the molecules
they react with. At lower temperatures, the kinetic energy is lower, resulting in a slower
molecule speed. As a result, fewer enzyme-substrate collisions occur, and the rate of the
reaction is relatively low. As the temperature increases, the kinetic energy of the molecules
also increases. This leads to more frequent and energetic collisions between the enzyme and
molecules, resulting in an increased rate of reaction. The enzyme and other molecules have
more energy to overcome the activation energy barrier, facilitating the formation of the
reaction products.

However, enzymes are sensitive to changes in temperature. They have an optimal


temperature range at which they exhibit maximum activity. This optimal temperature is
specific to each enzyme and corresponds to the temperature at which the enzyme's structure is
most stable. In the case of catalase, the optimal temperature is typically around 37°C (body
temperature for many organisms). When the temperature exceeds the optimal range, the
increased kinetic energy can disrupt the enzyme's structure. The enzyme molecules may
denature or lose their shape, leading to a loss of catalytic activity. (Denaturation involves the
disruption of the non-covalent bonds that maintain the enzyme's specific shape, such as
hydrogen bonds and hydrophobic interactions.) Additionally, when the temperature is lower
than the optimum temperature, the enzyme functions slower as the kinetic energy of the
molecules decreases.

As a result, the active site of the enzyme, where the molecules bind with, may become
distorted or inaccessible, impairing the catalytic function. In the experiment, by varying the
temperature of the hydrogen peroxide and measuring the height of the foam produced, you
are indirectly measuring the rate of the reaction. The foam height corresponds to the amount
of oxygen gas produced, which is a byproduct of the reaction. By recording the foam height
at different temperatures, you can observe how the rate of the reaction changes with
temperature. Typically, the rate will increase as the temperature rises until it reaches the
optimal temperature for catalase. Beyond this point, the rate will decrease as denaturation and
loss of enzyme activity occur.

(Picture showing the optimum temperature of function for an enzyme)

(Diagram showing catalase)

Hypothesis:

I predict that the catalase will function the best and produce the most foam at 26 degrees, as
that temperature is closest to the optimum temperature of the enzyme (37 degrees).

Variables:

Independent Variable: Temperature (5, 26 and 60 degrees)

Dependent Variable: Amount of Foam Produced

Control Variables:
1. Amount of Detergent used
2. Time taken for Foam to Develop
3. Amount of Hydrogen Peroxide used
4. Potato Used

Data/Observations/Results:
Table of Results:

Temperatur Average Average Average Average Average


e/C Height of Foam Foam Foam height of
Foam after Height Height Height foam per
5 minutes/ (Trial (Trial (Trial minute/mm
mm 1)/mm 2)/mm 3)/mm

5 11 11 9 13 2.2

26 20 20 18 21 4

60 7.3 6 6 10 1.5

General Observations:

Observations (5 degrees):

- Slow foam formation.


- Low foam height.
- Gradual increase in foam height over time.

Observations (26 degrees):

- More rapid foam formation compared to 20 degrees.


- Increased foam height.
- Steady increase in foam height over time.

Observations (60 degrees):

- Foam formation is faster at the start.


- Foam height is lower compared to previous temperatures.

Safety:
- Wear appropriate PPE, including lab coats, gloves or safety goggles. This will help
protect your skin if the hydrogen peroxide is spilled.
- Be careful when handling sharp items such as scalpels and cork borers. It is easy to
cut yourself if you are careless while cutting the potato.
- Hydrogen Peroxide is highly corrosive and it burns the skin.

Conclusion:
The experiment investigated the effect of temperature on the enzymatic activity of
catalase, which catalyzes the decomposition of hydrogen peroxide into water and oxygen gas.

By varying the temperature of the hydrogen peroxide and measuring the height of the
foam produced, I explored the relationship between temperature and activity of catalase. The
results of the experiment demonstrated that temperature has a significant impact on the
catalytic activity of catalase. As the temperature increased from 5°C to 26°C, the rate of the
catalase-catalyzed reaction increased steadily. This can be attributed to the higher kinetic
energy of the enzyme and substrate molecules, leading to more frequent and energetic
collisions between them. The increased collisions facilitated the breakdown of hydrogen
peroxide, resulting in faster foam formation and higher foam heights. However, as the
temperature exceeded the optimal range, the rate of the reaction started to decline. This
decrease in activity can be attributed to the denaturation of the catalase enzyme, caused by
the disruption of its three-dimensional structure at higher temperatures. Denaturation led to a
loss of catalytic activity and a decrease in foam height.

The experiment's findings highlight the importance of temperature in enzymatic


reactions. Enzymes exhibit maximum activity within a specific temperature range, known as
the optimal temperature. Deviations from this range can significantly impact enzyme activity.
In conclusion, the experiment demonstrated that temperature plays a critical role in the
activity of catalase, and it is the most effective at 26 degrees when compared to other
temperatures we used.

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