ENZYME CATALYSIS

ENZYME CATALYSIS
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Title: Enzyme Catalysis

Purpose: The purpose of this activity is to determine the rate for the
enzyme catalyzed decomposition of hydrogen peroxide.
Background Information
Enzymes are proteins are produced by a living cell; they act as a
catalyst in biochemical reaction. A catalyst affect the rate of a
chemical reaction. In an enzyme-catalyzed reaction, the substance to
be acted upon (the substrate) bind reversibly to the active site of the
enzyme. One result of this temporary union is a reduction in the energy
required to activate the reaction of the substrate molecule so that the
products of the reaction are formed. Each enzyme is specific for a
particular reaction because its amino acid sequence is unique and
cause it to have a unique three-dimensional structure. The active site
is the portion of the enzyme that interacts with the substrate. Catalase
is found in all organisms that use oxygen for their metabolism. The
enzyme is found in high concentrations in an organelle in cells called
the peroxisome. One of the functions of catalase is to prevent a toxic
accumulation of hydrogen peroxide (H2O2) in cells. It catalysis the
conversion of hydrogen peroxide to water and molecular oxygen.
Hydrogen peroxide is a byproduct of metabolic processes. It is usually
produced in peroxisomes when they partially oxidize fatty acids.
When catalase is absent, the reaction it catalyzes is spontaneous, but
at very low rates that are not able to reduce the harmful effects of
hydrogen peroxide.

Procedures: Described in the lab manual

Materials: Listed in the lab manual

Data:
Time (seconds)
Baseline Volume

10
3.4

30
3.4

Initial Volume

10.0

Final Volume

7.5

8.4

9.0

9.7

9.9

Amount of KMnO4
Used (Initial Final)

2.5

1.6

1.0

0.3

0.1

Amount of H2O2 used

(baseline- KMnO4
used)

0.9

1.8

2.4

3.1

3.3

10.0

60
3.4

120
3.4

180
3.4

10.0

10.0

10.0

Time Interval (seconds)

Rates

Initial 0
to 10

10 to 30

30 to 60

60 to 120

120 to
180

0.09

0.045

0.02

0.011

0.003

Data must include: (2 tables and 2 graphs)

1. Hydrogen peroxide decomposition by Enzyme Catalysis table
2. Rates table
3. Graph - hydrogen peroxide used
4. Graph rates

Conclusion:
1. What is an enzyme? Substrate? Induced fit?
Enzymes are biological molecules (proteins) that act as
catalysts and help complex reactions occur everywhere
in life. Substrates are chemicals that bind to the enzyme
and become altered (bonds formed and/or broken),
producing a product. the induce fit is the changing in the
shape of the active site of an enzyme so that it binds
more snugly to the substrate, included by entry of the
substrate.
2. What is the independent variable in this activity? Dependent
variable? Some (four) constants?
The independent variable is the amount of time allowed
to catalyze. The dependent variable is the amount of
H202 left. Constants are the temperature of the Kmn04,
the amount of H202 that was started with, the setting of
the experiment and the temperature of the H202.
3. In this activity, what is the enzyme? The substrate? The product?
The enzyme is catalase. The substrate is H2O2. Product
is H2O and O2.
4. What are some (four) factors that affect the rate of enzyme
catalyzed reactions? Describe each one in detail.
Some factors that affect the rate of the reactions is PH
because it either causes the enzyme side groups to gain
or lose H+ denaturing the enzyme. The salt
concentration because if it is too high or too low it
interacts with the side groups denaturing the enzyme.
Temperature because over energizes the bonds past the
optimum level denaturing the enzyme. And activators
and inhibitors because they can unfold the enzyme
reduce the disulphide bridges, or by reacting with the
side chains either blocking them or changing them.
5. What is the function of potassium permanganate in this activity?
The function of potassium permanganate (the titrant) is
to measure how much H2O2 is left.

6. What reaction would you expect if you added boiled catalase to

hydrogen peroxide? Explain your answer.
I think that no signs of a reaction occurring would be
shown. The catalase that occurs naturally would have
been denatured.
7. If you boiled a piece of potato or liver, and added hydrogen
peroxide, what reaction would you expect? Explain why.
I would expect no reaction because boiling denatures
the enzymes and when they are denatured no reaction
can occur.
8. In this activity, when is the rate the highest? Explain why.
The rate is the highest at the beginning because the
concentration of substrate is the highest at the start; the
catalase is fresh and accepts as many substrates (HO)
as possible into its active sites. This makes up for the
exceptionally high rate of reaction.
9. When is the rate slowest? For what reason is the rate slow?
Eventually, after the initial high rate the enzyme
becomes saturated with substrates, and cannot continue
to increase its rate of catalysis, so therefore cannot
increase. As less substrate molecules become available,
reaction rate slows down until it eventually levels off or
reaches 0, when all substrate sources are depleted. This
is when the rate is lowest, near the end of the reaction;
in this case its supposed to be from 120 to 180 seconds.
10. Explain the inhibiting effect of sulfuric acid on the function of
catalase. Relate this to enzyme structure and chemistry.
The inhibiting effect of sulfuric acid (HSO) is mainly
because it lowers the pH of the enzyme. Sulfuric acid is a
very strong acid, so it denatures the protein. If the pH is
lowered, the side chains will begin picking up hydrogen
ions from its environment, which might disrupt its

conformation, ultimately inhibiting its function. The

secondary and tertiary structures of the enzyme become
altered, thus changing the behavior of the enzyme. In
other words, the substrate may not fit or the side chains
will not interact correctly because of the hydrogen added
by the sulfuric acid.
11. Predict the effect lowering the temperature would have on the
rate of enzyme activity. Explain your prediction.
Lowering the temperature will have a negative effect on
an enzyme, since kinetic energy is needed to start the
reaction. If it becomes too cold, the enzyme will denature
and it will no longer function properly.
12. Different enzymes work better under different conditions.
Where in a human body might it be beneficial to have enzymes
that work well in acidic environments?
Our stomach which we have pepsin. Is usually works at
an acidic of pH of 2.
13. There is a large amount of catalase in the human liver. Does
the liver break down more hydrogen peroxide in the summer or
winter? Explain your answer.
The temperature of the external environment would have
no effect on liver catalase. Because the liver is an
internal organ in a warm-blooded creature, the internal
temperature should remain a constant 98.6F.
14. Of the thousands of enzymes known, there is a family of
enzymes called proteases that catalyze a reaction breaking
down proteins. What do you think would happen if you added a
protease to your sample of catalase before proceeding with your
experiment?
A reaction would occur between protease which acts
upon proteins and catalase which is a protein. The
reaction would most likely have caused the catalase in
the experiment to denature and that would have made it
not break down the H2O2.
15. Design an experiment to test the effect of temperature on
catalase activity. Make sure to include the independent variable,

dependent variable, how the dependent variable is going to be

measured and possible results.
Catalase can be used to expedite the breaking down of
H202 into water and oxygen. One can measure the
amount of oxygen produced by the reaction by using a
sensor on top of the flasks that the H2O2 was placed at
first. I would put three set ups with H2O2 and the
catalase added to each flask would have a different
temperature. I predict that the one that would work the
best with he's the one at 37 degrees Celsius. The
independent variable would be the temperatures of each
enzyme. The dependent variable would be how much
product was made after two minutes had passed.
Experimental purposes repeat lab again.

16. Summary- at least 15 lines typed, 20 handwritten.

Enzymes are biological catalysts that speed up reactions
necessary to live. There are different types of enzymes for
different types of reactions. Each enzymes specificity is
determined by the shape of its active sight and clearly
represents the induced fit how a substrate perfectly binds to
the active sight only with a slight change of the enzyme.
Substrates or molecules that require a speedier reaction are
introduced to the active sight of the enzyme where after a
certain amount of time the products are released and the
enzyme may be used over and over again.
This lab was helpful in showing us how enzyme catalysis really
happens in biology. I believe we went wrong in establishing
our baseline; we messed up quite a few times and these
erroneous trials may have been corrected with a repetition of
the lab itself; however, time did not allow us to do so. My

hypothesis was partially correct as the reaction most certainly

did begin quickly and slow as the time moved on, but I was
essentially incorrect in the idea that enough H2O2 would
remain so that the KMnO4 would react. Either way, the lab
represented success in the fact that it taught me an essential
concept to understanding how enzymes work. Reactants have
an energy barrier called the activation energy which must be
surpassed and enzymes serve as a helper to fulfill that energy
goal quicker.