The Enzyme Catalase Experiment

The Enzyme Catalase Experiment

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The Enzyme Catalase Experiment

Aim

A series of experiments involving the enzyme Catalase has been
performed in order to determine some of the enzyme's properties. The
enzyme had its reaction rate found in different conditions. Variation
of enzyme concentration, variation of pH, variation of temperature,
and the effect of different concentrations of inhibitors were all
tested.

Increasing the enzyme concentration increased the reaction rate. An
optimum pH and temperature were found for the enzyme, outside of this
optimum the reaction rate would be lower. As inhibitor concentration
rose, the reaction rate fell.

Introduction

Virtually all of the complex biochemical reactions that take place in
animals, plants, and micro organisms are regulated by enzymes. Most
enzymes are Proteins. Each enzyme is able to catalyse only one type
(or a small number) of chemical reactions. Enzymes may only catalyse
reactions which can happen naturally; the substrates do not require
the enzyme but the reaction is much faster in its presence.

In 1965 a theory was created by biologists describing an 'induced fit'
- where the structure of an enzyme is altered by its substrate, by the
movement of charges and hydrophobic/hydrophilic interactions, so the
substrate fits perfectly on the active site in such a way that its
reaction can be catalysed. Once the reaction has ended, the enzyme
returns to its original shape which uses up the least energy to hold
together. It was the work by chemists on the strong and weak chemical
bonds which allowed for this theory to be created. Catalase was
discovered to produce this induced fit in the presence of Hydrogen
Peroxide.

Catalase promotes the breakdown of Hydrogen Peroxide (H2O2) into
non-harmful products, Water and Oxygen by the equation:

CATALASE

2H2O2 ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯>2H2O + O2


Model of catalase structure


As can be seen in the diagram, the Catalase molecule is a very complex
protein. Its structure is held together by a variety of bonds

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including covalent, hydrogen and ionic bonds, Van der Waals forces,
and Hydrophobic interactions - the arrangement of the polar and
non-polar molecules.


Temperature, pH and the presence of inhibitors can all alter the
structure of the molecule thus causing differences in reaction rate of
the enzyme. Since one molecule of Catalase can break 40 million
molecules of hydrogen peroxide per second (at room temperature), I
will test the effect of enzyme concentration on reaction rate also.

Hypothesis

Reaction rate will increase as enzyme concentration increases.

Reaction rate will reach an optimum value at a pH of between 7 to 8.

Reaction rate will increase as temperature increases up to a
temperature of between 35-40 °C where reaction rate will peak. After
this point, the reaction rate will decrease as the temperature rises.

Reaction rate will fall as the concentration of inhibitors rises.


Procedure

[IMAGE]

Apparatus was set up as in the above diagram.

A pH 7 buffer is produced as shown in the table on the next page. This
is the buffer used in all experiments but experiment 2 where the
buffer pH is altered.

A 4% Yeast solution is made up by mixing 1g of Yeast powder with
distilled water. The concentration of the solution of Yeast is never
changed. The Yeast produces the Catalase enzyme very quickly when in
an environment with a high concentration of Hydrogen Peroxide.

For each experiment, once the syringe has been fully depressed the
stop clock is started. Each experiment is repeated three times so a
fair average can be obtained.

Volume of Oxygen produced from the reaction is measured using the gas
syringe.

Experiment 1 - The Effect of Variation of Enzyme Concentration

The reaction mixture is made up of 10ml pH 7 buffer mixed with 5ml of
10 Moll¯¹Hydrogen peroxide solution. Enzyme concentration is altered
by varying the volume of Yeast solution added to the reaction mixture
via the syringe. The experiment is performed with 0, 1, 2 and 3ml of
Yeast solution added. The volume of Oxygen produced is measured every
ten seconds for a period of ninety seconds.

Experiment 2 - The Effect of Variation of pH

Buffers of different pH values are produced using the volumes of
solution shown below:

Solution A: 0.2M NaH2PO4

Solution B: 0.2M Na2HPO4

Solution C: 0.1M Glycine

0.1M NaCl

Solution D: 0.1M NaOH

Buffer Type

pH

A (ml)

B (ml)

C (ml)

D (ml)

0.1M Phosphate Buffer

4.5

100

0

-

-

0.1M Phosphate Buffer

6

87.7

12.3

-

-

0.1M Phosphate Buffer

7

39

61

-

-

0.1M Phosphate Buffer

8

5.3

94.7

-

-

Sorensen-Walbaum's Buffer

8.5

-

-

95

5

Sorensen-Walbaum's Buffer

9

-

-

85

40

Sorensen-Walbaum's Buffer

10

-

-

60

40

Sorensen-Walbaum's Buffer

11

-

-

50.5

49.5

Sorensen-Walbaum's Buffer

12

-

-

45

55

Note that the Phosphate buffers must have 100ml distilled water added
to each mixture.

The reaction mixture is made up using 10ml of buffer of a particular
pH with 5ml 10 Moll¯¹Hydrogen Peroxide. For each experiment 1ml Yeast
solution is added to start the reaction.

Experiment 3 - The Effect of Variation of Temperature

To perform this experiment the use of a water bath is employed to
raise the temperature. To lower the temperature, cooled water or ice
is used in a basin. The conical flask is partially submerged in either
to cool/ heat the reaction mixture. The reaction mixture is made up of
10ml pH 7 buffer mixed with 5ml 10 Moll¯¹Hydrogen Peroxide. 1ml Yeast
solution is used to start the reaction. Only temperature is altered in
the experiment. Temperatures of 0, 10 ,20, 30, 40, 50 and 60°C are
used.

Experiment 4 - The effect of inhibitors

Using the same apparatus as in experiment 1 and 2, a reaction mixture
of 9ml pH 7 buffer, 5ml 10 Moll¯¹Hydrogen Peroxide and 1ml inhibitor
solution is produced and reacted with 1ml Yeast solution. Inhibitor
solutions of different concentrations are used; 1, 0.75, 0.5, 0.25 and
0.1 Moll¯¹solutions are used. The inhibitor I chose was Copper (II)
Sulphate solution.


Results

Experiment 1 - The Effect of Variation of Enzyme Concentration

Time (s)

Volume of Oxygen Produced (cm³)

0

Yeast

1 cm³ Yeast Solution

2 cm³ Yeast Solution

3 cm³ Yeast Solution

A

B

C

Av

A

B

C

Av

A

B

C

Av

10

0

1

1

0.5

0.8

2.5

4

2

2.8

4

5

3

4

20

0

2

2

1.5

1.8

5

7

4

5.3

6

8

7

7

30

0

3

3

3

3

6.5

10

5.5

7.3

9

12

9

10

40

0

4

4

4

4

8

13

7

9.3

12

15

13

13.3

50

0

5

4

5

4.7

10

15

9

11.3

13

19

15

15.7

60

0

6

5

5.5

5.5

12

18

11

13.7

15

23

17

18.3

70

0

7

6

6

6.3

14

20

12

15.3

18

28

19

21.7

80

0

7

6

7

6.7

15

22

14

17

19

33

21

24.3

90

0

8

7

8.5

7.8

17

24

15

18.7

20

38

22

26.7

[IMAGE]

Experiment 2 - The Effect of Variation of pH

pH

Volume of Oxygen Produced in 60 Seconds (cm³)

Experiment A

Experiment B

Experiment C

Average Result

4.5

5

6

5

5.33

6

6

6

5

5.67

7

6

5

6

5.67

8

7

5.5

5

5.83

8.5

8

6

7

7

9

8

8

9

8.33

10

7

7

5

6.33

11

6.5

5

7

6.17

12

6

5

5.5

5.5

[IMAGE]

Experiment 3 - The Effect of Variation of Temperature

Temperature (°C)

Volume of Oxygen Produced in 60 Seconds (cm³)

Experiment A

Experiment B

Experiment C

Average Result

0

1

2

1

1.33

10

3

4

4

3.67

20

5

5

4

4.67

30

7.5

7

8

7.5

40

14

13

15

14

50

19

17

17

17.67

60

33

32

30

31.67

[IMAGE]

Experiment 4 - The effect of inhibitors

Concentration of Copper (II) Sulphate Solution (Moll¯¹)

Volume of Oxygen Produced in 60 Seconds (cm³)

Experiment A

Experiment B

Experiment C

Average Result

0

5.5

6

5.5

5.67

0.25

5

6

5

5.33

0.5

4.5

4

4

4.17

0.75

3

4.5

3.5

3.67

1

2

2.5

2.5

2.33

[IMAGE]

Discussion

Conclusion

Most of the results showed the hypothesis to be correct. Reaction rate
increased as the enzyme concentration increased by varying the volume
of 4% Yeast solution added. The reaction rate was optimum at a pH of
9, which was close to the hypothesis of between 7 and 8. This
hypothesis was made due to the fact that blood is slightly alkaline
and Catalase must work efficiently in these conditions to prevent the
cells of the body being contaminated by Hydrogen Peroxide. The results
showed that reaction rate increased continuously as temperature rises.
This is a scientific impossibility since the Catalase enzyme denatures
above 45°C and so there would be no reaction (and therefore no oxygen
produced) above this temperature. This will be further discussed in
the evaluation. Reaction rate fell as the inhibitor concentration
rose.

Evaluation

Experiment 3 (The Effect of Variation of Temperature) did not work as
planned since a gas was produced at the higher temperatures which were
not anticipated in the planning of the investigation. The gas was due
to evaporation of the reaction mixture at the higher temperatures. The
expansion of the air inside the conical flask could also create this
effect. This could be seen easily by the steam rising from the
contents of the conical flask. Accurate results could only be obtained
knowing the exact rate of evaporation of the reaction mixture and the
degree of expansion of air inside the conical flask.

In general, the other experiments produced good results which were
made more accurate by the two repeats of every experiment, then an
average found.

There would have been some small inaccuracies in the results due to
occasional poor washing of the apparatus after use. For example when
the conical flask was not washed out several times some Yeast/Catalase
would remain on the bottom. This could be seen when small bubbles
formed when Hydrogen Peroxide was added (this was performed as an
experiment after only two cleans of the conical flask - a deliberate
error to find out how thorough a wash was required).

For all measurements of solutions, different sizes of pipettes were
used. There were some inaccuracies in the actual measurement to the
liquids (human error) due to poorly checking the position of the
bottom of the meniscus against the line of the volume required. Only
two granulated pipettes were required, a 1ml and a 10ml pipette. Since
many chemicals were used, each time a pipette was used it had to be
washed out several times with distilled water. Before the pipette was
then reused, it had to be washed out with the chemical it was going to
measure. These procedures insured no contamination and inaccuracies in
many of the measurements by systematic error.

Once the syringe containing the Yeast solution was depressed, the
conical flask was not moved e.g. to swirl the contents around, since
this would create too many inaccuracies such as the length of time and
force with which the flask was swirled.

The yeast solution was made up each day and disposed of afterwards to
ensure a constant 4% solution.

References/Bibliography

Books

Rose, S (1966) The Chemistry of Life, Penguin, p97-107.

Wynn, C. H. (1973) The Structure and Function of Enzymes (Studies in
Biology No. 42), Edward Arnold, p43

Websites

Roy B. Clariana (1991) Enzyme Action, Carnegie Institution. Visited
March 2003.

URL:
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Enzymes.html

P. Keusch (2000) Kinetics: Enzymatic Decomposition of Hydrogen
Peroxide, University of Regensburg Visited March 2003.

URL:
http://www.uniregensburg.de/Fakultaeten/nat_Fak_IV/Organische_Chemie/Didaktik/Keusch/cassylab_kat-e.htm

Acknowledgements

I would like to take this opportunity to thank Mr X and the Technician
Staff for their great help during this investigation.
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