The Effect of Temperature on an Enzyme's Ability to Break Down Fat

The Effect of Temperature on an Enzyme's Ability to Break Down Fat

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The Effect of Temperature on an Enzyme's Ability to Break Down Fat

Aim:

To investigate the effect of temperature on an enzyme’s (lipase)
ability to break down fat.

Hypothesis:

The graph below shows the rate increasing as the enzymes get closer to
their optimum temperature (around 35 degrees Celsius) from room
temperature. The enzyme particles are moving quicker because the
temperature increases so more collisions and reactions occur between
the enzymes and the substrate molecules.

After this the graph shows the rate decreasing as the enzymes are past
their optimum temperature (higher than). They are getting exposed to
temperatures that are too hot and so the proteins are being destroyed.
The shape of the molecules is changing and so the enzyme molecules can
no longer fit into the gaps in the substrate that they need to and
therefore the enzymes have de – natured and can no longer function as
they are supposed to and cannot do their job correctly.

Changing the temperature:

Five different temperatures could be investigated. Water baths were
used to maintain a constant temperature. Water baths were set up at 40
degrees, 60 degrees and 80 degrees (Celsius). Room temperature
investigations were also carried out (20 degrees). Using a Bunsen
burner, tripod and beaker of water 100 degrees could also be tested
and 0 degrees was tested by using ice. (I didn’t investigate the 80
degrees temperature).

Fair test:

Below is a list of things that were kept the same throughout the
investigation:

Volumes of lipase and milk (by using syringes); volumes of
phenolphthalein and sodium carbonate (using pipettes); (best volumes
from the preliminary work were used). Each temperature was repeated
three times to get a good average. The milk and lipase were
equilibrated to the right temperatures before the lipase was added to
the milk.

Equipment list:

Test tubes were used to hold the milk, the lipase and the milk and
lipase solutions. Test tube racks were used to hold the test tubes

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when the test tubes were holding liquid. Stopwatches were used to time
how long the reactions took. Water baths were used to maintain the
temperatures (mentioned above). Ice tested the 0 degrees
investigation. Bunsen burners, tripods and beakers tested the 100
degrees investigation. Thermometers were used to measure the exact
temperatures. Phenolphthalein; sodium carbonate; lipase; milk.
Syringes were used to measure the exact amounts of lipase and milk and
pipettes measured the exact amounts of sodium carbonate and
phenolphthalein.

Preliminary work:

Volume of milk (ml)

Drops of phenolphthalein

Drops of sodium carbonate

Volume of lipase (ml)

Time taken

1

3

9

1

3m29s

1

3

14

1

8m26s

1

3

27

1

19m01s

Experiment number 2’s volumes of sodium carbonate was used when
carrying out the actual experiments because the milk changed from pink
back to it’s original colour (the enzyme broke down the fat) in about
10 minutes, which is the time I was aiming for to make all the tests
fair and still have enough time to carry out the experiment at the
temperatures I needed to.

Methods:

Room temperature:

1 – milk and lipase were measured out into different test tubes using
a syringe;

2 – three drops of phenolphthalein were added to the milk;

3 – fourteen drops of sodium carbonate were added to the milk;

4 – lipase was added to the milk solution;

5 – the stopwatch was started;

6 – the mixture was observed until it returned to the milk’s original
colour;

7 – the stopwatch was stopped and the time was noted.

Water baths:

1 – milk and lipase were measured out into different test tubes using
a syringe;

2 – three drops of phenolphthalein were added to the milk;

3 – fourteen drops of sodium carbonate were added to the milk;

4 – the milk test tube and the lipase test tube were placed in the
chosen water bath and equilibrated to the required temperature;

5 – the lipase was added;

6 – the stopwatch was started;

7 – the mixture was observed until it reached the milk’s original
colour;

8 – the stopwatch was stopped and the time noted.

Beaker (0 degrees Celsius):

1 – milk and lipase were measured out into different test tubes using
a syringe;

2 – three drops of phenolphthalein were added to the milk;

3 – fourteen drops of sodium carbonate were added to the milk;

4 – the milk test tube and the lipase test tube were placed in the
beaker containing the ice and water and equilibrated to the required
temperature (0 degrees Celsius);

5 – the lipase was added;

6 – the stopwatch was started;

7 – the mixture was observed until it returned to the milk’s original
colour;

8 – the stopwatch was stopped and the time noted.

Bunsen burner (100 degrees Celsius):

1 – the milk and lipase were measured out into different test tubes
using a syringe;

2 – three drops of phenolphthalein were added to the milk;

3 – fourteen drops of sodium carbonate were added to the milk;

4 – the milk test tube and the lipase test tube were placed in a
beaker on a tripod above a Bunsen and equilibrated to the required
temperature (100 degrees Celsius).

5 – the lipase was added;

6 – the stopwatch was started;

7 – the mixture was observed until it returned to the milk’s original
colour;

8 – the stopwatch was stopped and the time noted.

We were looking for the milk to change back to its original colour
from the pink the sodium carbonate and phenolphthalein had made it
because when this happened, it meant that the lipase enzyme had broken
down the fat in the milk.

Rate = amount of fat converted to fatty acids and glycerol every
minute.

We measured how long it took to convert all the fat in the tube to
fatty acids and glycerol (in minutes)

So, to calculate rate we use this equation:

Rate (mg/min) = amount of fat in each tube

[IMAGE]


Time taken (minutes)

= volume of milk (ml) x amount of fat in 1ml (mg)

[IMAGE] time taken (minutes)

= there is 33mg in 1ml of milk.

So rate = volume of milk (ml) x 33mg

[IMAGE]


Average time (minutes)

Results:

Temperature (degrees Celsius)

Rate (mg/min)

1

2

3

Average

0

>41m04s

>41m04s

>41m04s

>41m04s

00m80s

20

08m75s

09m01s

08m83s

08m86s

03m72s

40

03m02s

03m04s

03m08s

03m05s

10m82s

60

09m90s

09m79s

10m01s

09m90s

03m33s

100

>52m22s

>52m22s

>52m22s

>52m22s

00m63s

Conclusion:

As I predicted in my hypothesis – the graph shows the rate increasing
as the enzymes get closer to their optimum temperature. This is
because the particles are moving quicker and so more collisions and
reactions occur between the enzymes and the substrate molecule.

After this, the graph shows the rate decreasing as the enzymes are
past (higher than) their optimum temperature. They are getting exposed
to temperatures that are too hot and so the proteins are being
destroyed. The shape of the molecules is changing and so the enzyme
molecules can no longer fit into the gaps in the substrate that they
need to. Therefore, the enzymes have de – natured and can no longer
function as they are supposed to and cannot do their job properly.

Compared to the hypothesis – my graph shows that my hypothesis was
correct but the ascent and the decent of the graph was steeper than I
imagined.

Evaluation:

Limitations – the precise time that all the milk had returned to its
original state can’t be known. The drop sizes of the pipettes may have
differed slightly and so more or less of the chemicals could have been
added without knowing.

Improvements – more accurate ways of dropping the sodium carbonate and
phenolphthalein could have been used during the experiment.

Reliability – I had no anomalous results. The repeats are very close
together – often differing by only 0.02 or 0.03 minutes, proving that
either none of them is out of sync or none of them are accurate. None
of my temperatures produced temperatures that very far apart.
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