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1 of 27 10/20/2010 6:19 AM
Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
Talal Syed
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Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
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Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
Lab Report |5
Once all the H₂O₂ had reacted, any more KMnO₄ added would be in excess and therefore did
not decompose. The addition of excess KMnO₄ caused the solution to have a permanent pink or
brown tint. After this had been obtained, no more KMnO₄ was added. The amount of KMnO₄
added was proportional to the measure of the amount of H₂O₂ remaining, therefore allowing us
to calculate how much H₂O₂ had been remaining, and how much had been decomposed. This,
however, is only a general overview of the detailed experiment. The following explains in further
detail.
To observe a general reaction of catalase, 10 mL of 1.5% (0.44 M) H₂O₂ was added into
a 50-ml glass beaker. Into there, a 1 mL extract of fresh catalase was added. To demonstrate
factors of enzymatic activity, 5 mL of catalase was boiled and then cooled. About 1 mL of this
was added to another 10 mL of H₂O₂. Furthermore, catalase was exposed to both an acid (HCl)
and basic (NaOH) environment to see how it functioned. This part of the lab, Exercise 2A, gave
solution. This amount is known as the base line and is the basis for future procedures. Taking a
1.5% solution, 10 mL of H₂O₂ was placed in a clean glass beaker. Instead of enzyme solution, 1
mL of distilled water was added. Then, 10 mL of H₂SO₄ was added, forming a 21 mL solution.
After mixing well, a 5 mL sample was extracted into another beaker for titration. A magnetic
stirring was placed into the beaker, which was in turn placed on a hot plate. Using a burette,
KMnO₄ was added one drop at a time. After measuring the KMnO₄ used, the amount of H₂O₂
was calculated. Another trial of this procedure was conducted to avoid errors.
The following part of the lab called for examining how H₂O₂ decomposed spontaneously.
About 15 mL of H₂O₂ was placed in a beaker. It was stored uncovered at room temperature for
approximately 24 hours. From the remaining solution, a 5 mL extract was titrated to find the
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Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
Lab Report |6
amount of H₂O₂ spontaneously decomposed. This was also repeated several times to ensure
accuracy.
The final portion of the lab observed the rate of enzyme-catalyzed H₂O₂ decomposition.
To observe the rate of reaction, the amount of substrate disappearing was measure over certain
periods of time. For this procedure, 7 clean cups were needed. In each of these cups, 10 mL of
1.5% H₂O₂ was added by a syringe. Along with that, 1 mL of catalase was added into each cup
one at a time, using another clean syringe. For example, one cup was left alone with catalase for
10 seconds. After 10 seconds, all enzymatic activity was halted with the addition of 10 mL of
sulfuric acid, which was added by yet another clean syringe. Another cup had the 1 mL catalase
extracted for 30 seconds. This procedure was consistent for 0, 10, 30, 60, 90, 120, and 180
seconds of catalase activity. From each cup, a 5 mL sample was removed to be titrated. This
allowed us to find out how much H₂O₂ had been remaining after that set time. After this
procedure was completed for all 7 times, it was repeated to ensure maintaining proper results.
RESULTS
For Exercise 2A, an enzyme-catalyzed reaction was observed. The enzyme in the reaction
was catalase. The substrate acted upon was hydrogen peroxide, which was broken down into
water and oxygen gas. The release of the gas was proven as oxygen by a glowing splint test.
When boiling catalase, the reaction does not occur as quickly, since the function of the enzyme
has been altered. Potatoes also have catalase stored in them, as observed when bubbles were
The initial amount of H₂O₂ in a 1.5% solution had to be calculated, which acted as the
basis for the rest of the experiment. In order to find this, the molarity of 2% KMnO₄, which was
used as the titrant, had to be measured as well. The following calculations were made:
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Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
Lab Report |7
KMnO ₄1000 mL H O₂
20 grams KMnO4 1 mole KMnO 1 ₄ L 158.04 grams KMnO ₄ = 0.127 moles KMnO 1 ₄L
µmoles
For Exercise 2C, the spontaneous conversion of H₂O₂ into H₂O and O₂ was observed in
0.0000127 moles KMnO 5₄ moles H O ₂ 2₂ moles KMnO ₄ = 0.0000318 moles or 31.8 µmoles of
H₂O₂ remains
After leaving H₂O₂ uncovered overnight, approximately 1148 µmoles or 97% of the initial
For Exercise 2D, data was obtained by manipulating the time for catalase activity to see
how time would correlate to H₂O₂ decomposition. The following calculations were used to
determine the moles of H₂O₂ remaining from the catalyzed reaction, and how much had been
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Lab Report |8
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Lab Report |9
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Lab 2 Enzyme Catalysis http://www.scribd.com/doc/7624496/Lab-2-Enzyme-Catalysis
L a b R e p o r t | 10
10 30 60 90 120 180
0 sec sec sec sec sec sec sec
Baseline (mL) 3.70 3.70 3.70 3.70 3.70 3.70 3.70
Table 1. This table shows an overview for all of the results for this part of the lab. The manipulated variable was the time
that the catalase was allowed to catalyze. The responding variable would be the amount of H₂O₂ remaining and
decomposed from the reactions. *Calculations for this measurement are shown in the results for 2B (see Lab Report 7)
**Calculations for these measurements are shown above (see Lab Report 8, 9, 10)
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enzyme
ap biology
enzyme catalysis lab
lab 2
ap biology lab 2
lab 2 answers
Science-Biology
decompositions
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Hey. Feel free to use data from mine or leave comments on my lab reports that are
incorrect or whatever. I'm kinda rusty so I can't really help improve them.
01 / 31 / 2010
Reply
02 / 01 / 2010
Note from the author: For some reason, the flash version of this document cuts out a
graph and messes with the formatting. For better viewing, feel free to download this
document.
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10 / 25 / 2009
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his Document for Free
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RogerRC replied:
do you want to publish more like this? i bet it would be of great help to students...
11 / 18 / 2009
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