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Running head: The Effect of Peroxidase Concentration on Reaction Rate 1

The Effect of Peroxidase Concentration on Reaction Rate

Student’s Name

Date
The Effect of Peroxidase Concentration on Reaction Rate 2

Abstract

This experiments aims at investigating the rate of enzyme-catalyzed reaction with respect

to an increase in enzyme concentration. Hypothetically, an increase in enzyme concentration

would definitely lead to an increase in the rate of reaction. This test was done using enzyme

extracts of peroxidase on eight trials run at 40 ml, 32 ml, 24 ml, 20 ml, 10 ml, 10 ml, 4 ml, and 2

ml. The enzyme extracts were diluted and mixed with 15 ml hydrogen peroxide. For each trial,

immediately after mixing the enzyme extract with hydrogen peroxide, we recorded the rate of

absorption with the help of spectrophotometer. The recorded data was then plotted on a graph

with significant enzyme activity realized at 1.5% ml hydrogen peroxide.


The Effect of Peroxidase Concentration on Reaction Rate 3

Introduction

Enzymes are protein compounds that carry with them the capability to carry out chemical

reactions. These chemical compounds are catalysts in the living organisms and also regulate the

rate at which the reactions take place. There are a number of enzymes in the body of a living

organism whose functions are entirely dependent on the type of proteins embedded into the

system.

Enzymes are typically crucial for the reactions that take place in the body of an organism.

Specifically for this lab, enzyme peroxidase was use to breakdown hydrogen peroxide.

Peroxidase is available in many forms being able to protect body red blood cells and at times

found in bacteria. Peroxidase is very important owing to its ability decompose great amount of

hydrogen peroxide into oxygen and water within the optimum conditions (Komkova, Karyakina

& Karyakin, 2018).

Materials and Method

This lab consisted of eight beakers containing different concentrations of peroxidase

concentrations which are diluted. The concentrations included: 40 ml, 32 ml, 24 ml, 20 ml, 10

ml, 10 ml, 4 ml, and 2 ml. add distilled water to each beaker reaching a total solution of 40 ml.

immerse a filter paper disc into the peroxidase enzyme and place at the bottom of each substrate

solution of 1.5% hydrogen peroxide. Record the time taken for the disc to rise to the surface of

each solution. This represents the rate of reaction.


The Effect of Peroxidase Concentration on Reaction Rate 4

Collect the time taken for the filter paper to reach the surface of the solution and convert

the information into a rate (rate = 1/s or inverse of seconds).

Findings and Results

In this experiment there were absolute and definite results. For the enzyme concentration,

it was determined that as the concentration of enzyme increased so did the rate of reaction in a

manner to obey laws of proportionality. This data table can be found on figure 1 and a graph be

found on figure 2 as well. This graph demonstrates how the rate of reaction and enzyme

concentration relates. The direct relationship is evident by the linearity of the graph on figure 2

especially before saturation levels.

Enzyme Rate
Concentration (1/second
(units/mL) s)
100 0.8
80 0.5
75 0.286
60 0.217
50 0.2
25 0.143
10 0.154
0 0.161

Figure 1: Table of Results of Effects of Enzyme Concentration on Rates of Reaction


The Effect of Peroxidase Concentration on Reaction Rate 5

Figure 2: Graph of Effects of Enzyme Concentration on Rates of Reaction

Discussion

After data collection and thorough investigation, it was very evident that much of the

objectives and purposes of the lab were attained. This objective was to determine the effects

enzyme concentration on the rate of reaction. The final conclusions made were in congruent with

the fact that rate of reaction increases with an increase in the concentration of enzymes. The

experiment can be modelled as:

2H2O2+ peroxidase2H2O + oxygen + catalase

Peroxidase clearly accelerates the breakdown of hydrogen peroxide into water and

oxygen. The enzyme peroxidase also remains after the reaction occurs because the reactants do

not bind to the active sites of the enzymes according to Küchler et.at. (2016). This reaction is
The Effect of Peroxidase Concentration on Reaction Rate 6

very crucial to the survival of any living organism as it ensures that there is no buildup of

hydrogen peroxide to toxic levels.

Considering carefully the results obtained, a deeper investigation is necessary for clear

understanding of enzyme concentration verses rate of reaction. Each of the eight beakers used

were of different enzyme concentrations. The filter paper was put into the substrate solution that

was 1.5% hydrogen peroxide. The disc rose quickly with an increase in the enzyme

concentration. This can be explained by the fact that as reaction takes place, oxygen is produced

as a product. The disc paper absorbed the oxygen produced and rose as once. Increased enzyme

concentration increased the active sites of the peroxidase lowering the activation energy as well

(Cornish-Bowden, 2014).

The graph and data possibly had room for errors in varied aspects. Human error could

have caused discrepancies in diluting hydrogen peroxide from 6% to 15%. Improper timings

could also cause deviations though very insignificant. However, all the results followed the

expected trend and in total agreement with the hypothesis made. We therefore can conclude that

the results are very valid.

Conclusion

This was relatively a successful lab in determining the effect of enzyme concentration on

the rate of reaction. The objective of the lab were relatively met. All the data that was collected

totally agree with both the hypothesis and objectives of the experiment. The validity of the

results were enhanced by the fact that the experiment was carried out multiple times to verify the

results completely.
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References

Cornish-Bowden, A. (2014). Principles of enzyme kinetics. Elsevier.

Komkova, M. A., Karyakina, E. E., & Karyakin, A. A. (2018). Catalytically Synthesized

Prussian Blue Nanoparticles Defeating Natural Enzyme Peroxidase. Journal of the

American Chemical Society, 140(36), 11302-11307.

Küchler, A., Yoshimoto, M., Luginbühl, S., Mavelli, F., & Walde, P. (2016). Enzymatic

reactions in confined environments. Nature nanotechnology, 11(5), 409.

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