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Anthony Araracap

Period 4 AP Biology

Enzyme Action: Testing Catalase Activity Lab Report

Background:

Enzymes are globular proteins responsible for most chemical activities in living
organisms and act as catalysts. Enzymes are efficient and reusable; temperature and
pH at which enzymes function are extremely important. Most organisms have a
preferred temperature range in which they function in and work best within that
temperature range. If the environment of the enzyme is too acidic or too basic the
enzyme may irreversibly denature.

Purpose:

The purpose of this lab was to study the rates of enzyme-catalyzed reactions
through rate of appearance of product, disappearance of substrate, and pressure of
the product as it appears.

Hypothesis:

If H2O2 is added to the enzyme as a substrate, then the enzyme reaction rate
will double (from 5 drops to 10 drops the slope will double and from 10 to 20 the
slope will double once more) and if the enzyme is placed in an ideal temperature,
then the reaction rate will further increase.

Materials:

● Computer
● Vernier computer interface
● Logger Pro
● Vernier O2 gas sensor
● 400mL beaker
● 10mL graduated cylinder
● 250mL Nalgene bottle
● (3) dropper pipettes
● 3.0% H2O2
● Enzyme suspension
● (3) 18x150mm test tubes
● Ice
● pH buffers
● test tube rack
● thermometer
Procedure:

The Enzyme Action: Testing Catalase Activity Computer 6A procedures were


followed by our group.

Data & Observations:

Part 1 Data Table

Test tube label Slope, or rate (%/min)


5 drops .049%/min
10 drops .106%/min
20 drops .2814 %/min

In this lab several things were observed. Firstly, once the substrate (H2O2) was
added to the enzyme oxygen bubbles were formed and led to an increased rate of
reaction based on the amount of drops placed into the test tube with the enzyme.
Also, when the enzyme in the test tube was placed in a hot bath, the enzyme
denatured due to the temperature being too high, which was observed from the graph
produced on the computer showing no reaction occurring. Another observation was
that the color of the catalase was light brown and it was a liquid from potatoes.

Analysis:

(See graph in lab notebook)


Error Analysis:

During the lab, a few errors may have occurred. For example, when placing
drops into the test tubes, the amount of drops placed may have been too many if not
done carefully. Also, when placing the drops into the test tube, bubbles may have
came out instead of the H2O2 causing there to be not enough dropped into the test
tube. Another error may have been in temperature, when the hot water began to cool
down and become room temperature.

Discussion:

In this lab the hypothesis was “If H2O2 is added to the enzyme as a substrate,
then the enzyme reaction rate will double (from 5 drops to 10 drops the slope will
double and from 10 to 20 the slope will double once more) and if the enzyme is
placed in an ideal temperature, then the reaction rate will further increase” was
proven true. The lab group tested the enzyme’s reaction to a substrate (H2O2). When
several drops were added, the rates of reaction increased by almost double each 5-10
drops, this was expected as the H2O2 catalyzed the reaction, when the data was
shown on the graph, it was clearly visible of the exponential group between the drops
and amount of oxygen produced. Next, the group used a beaker with boiling water as
a hot bath, and then lowered the temperature to about 55 degrees, then the test
tube with the substrate and enzyme was placed into the hot bath. After, the solution
was placed into a bottle to record the amount of oxygen produced over three minutes
for the tests of 5, 10, and 20 drops of substrate. In part two, the enzymes were
heated, a clear decline in slope when placed in a hot bath was noticeable—most likely
due to denaturing of the protein. Thus, the hypothesis was accepted for this lab,
although the enzyme was denatured it demonstrated that it was not at its ideal
temperature.

Discussion Questions:

1. Changing the concentration of enzyme affects the rate of decomposition of


H2O2 because the rate should be highest when the concentration of enzyme is
highest. With higher
concentration of enzyme, there is a higher chance of an effective collision between
the
enzyme and H2O2 molecule.
2. At twenty-five drops, the reaction rate will most likely increase, since the
rate doubles when the concentration of enzyme doubles. Since the data are
almost linear, the rate is proportional to the concentration. At a concentration of 5
drops,
the rate in the experiment should be about 0.049 %/min. For 30 drops the rate will
most likely double the rate of reaction for 20 drops.
3. The temperature at which the rate of enzyme activity is the highest should
be close to 30°C.
The lowest rate of enzyme activity should be at 60°C. This is due to the temperature
being ideal for the enzyme (too high or too low temperatures cause denaturing).
4. The rate increases as the temperature increases, until the temperature
reaches about 50°C, but above this temperature, the rate decreases. This is what I
would expect since denaturing would occur at temperatures too high or too low.
5. At high temperatures enzymes lose activity as they are denatured and can’t
function as they normally would.

6. The activity for the enzyme is highest at pH 10 and lowest at pH 4, since


this is the ideal pH for the enzyme. If the enzyme is too acidic or too basic the
enzyme will denature.

7. Usually, the enzyme activity increases from pH 4 to 10 when at low


pH values, the protein may change its structure. This may affect the enzyme’s
ability to recognize a substrate or it may change its polarity within a cell.

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