Enzyme Concentration’s Affect on the Rate of Enzyme Activity

Mahsa Rezazadeh-shahi

Mrs. Korn

SBI 4U1-04
 Rezazadeh-shahi 2
23 February 2011

Introduction

An enzyme is a protein that has the primary purpose of catalyzing a chemical reaction. It is

composed of amino acid monomers which are arranged in a specific sequence and shape for each

individual enzyme of a particular type. This makes each enzyme specific to a process to which it

pertains to. Because enzymes are proteins, they behave like other proteins as their structure is vital to

the function they perform. There are many factors that can denature the structure of a protein such as

heat and acidity. When exposed to extreme levels, the peptide bonds within the protein are broken and

the protein can no longer perform its specific function. This directly affects the function of enzymes as

they are proteins that serve a particular purpose and must be kept at an optimal environment in order to

serve their specific function.

The function of an enzyme is vital to the metabolic processes of all living organisms. The

enzymes increase the rate of a reaction. The faster a process is completed, the more efficient the

organism's cell activity is. There are many factors that can affect the rate of enzyme activity including

temperature, acidity, the concentration of the enzyme, and the concentration of the substrate. A high

temperature allows for an increase of movement in the substrate"s molecules and promotes contact

with the active site of an enzyme which increases the likelihood of the process. Since unused enzymes

that are waiting for contact with the substrate are being satisfied quicker, more reactions can be carried

through; however, because high temperatures can denature an enzyme, the optimal temperature of an

enzyme in the body is about 37 degrees Celsius, the average body temperature of a human. The pH of

an enzyme must also be kept at a specific pH since a drastic change in acidity can also denature the

enzyme. Different enzymes require different pH levels depending on where in the body the enzyme’s

function takes place. The rate of enzyme activity is most efficient at a specific or optimal pH level. A

higher concentration of the enzyme also increases the rate of the reaction. Since there are more

enzymes in a sample with a higher concentration, there are more enzymes prepared to complete a
 Rezazadeh-shahi 3
reaction and in turn metabolizes the substrate at a faster rate. Like with the concentration of the

enzyme, a higher concentration of the substrate can also increase the rate of a reaction; however, based

on the limited amount of enzymes available to complete a reaction, the rate will plateau at a certain

concentration. If there are too many substrate molecules, each molecule would have to wait until

another enzyme finishes a process; therefore causing the rate of reaction to plateau, as known as

enzyme saturation. These various factors must all be considered when describing an enzymes activity

at the site of the reaction.

These various factors apply to all enzymes, one being catalase, which is used to decompose

hydrogen peroxide in cells. Catalase is an enzyme that is composed of four polypeptide chains, each

composed of over five hundred amino acids. The main significance of the structure of the enzyme is

the presence of four iron groups. This structural characteristic is essential for the enzyme to carry out

its specified function as the iron groups allow the enzyme to bind and react with the hydrogen peroxide.

The presence of the cofactor iron in the quaternary structure of the enzyme allows the enzyme to work

properly, in the case of catalase, to carry out the decomposition of hydrogen peroxide into water and

oxygen.

The hydrogen peroxide which requires the presence of catalase is created by peroxisomes as a

by-product of another reaction. Peroxisomes are membrane bound organelles that break down very

long fatty acid chains to smaller sizes. They act as a filters which rid the body of harmful toxins. They

do this by breaking down the harmful toxins through oxidization, forming hydrogen peroxide; however,

hydrogen peroxide has its harmful affects on the body as well. So this by-product of peroxisomal

activity needs to be further broken down, which is why catalase is present in the peroxisome as well.

Catalase is present to catalyze the decomposition of hydrogen peroxide into water and oxygen

molecules. This must be done because although hydrogen peroxide is produced as a by-product of the

peroxisome, it can cause harmful effects within the body when present in large quantities. These

harmful effects include the oxidization of the cell membrane and other organelles, causing physical
 Rezazadeh-shahi 4
damage to the cell. Therefore, it is important to decompose the hydrogen peroxide as quickly and

safely as possible, hence, the importance of the enzyme catalase. The liver is a primary location where

peroxisomes and the enzyme activity of catalase takes place. Because the liver and kidneys act as a

filtration system for the toxins within the body, the use of the liver in the lab will allow the enzyme to

be extracted and used for lab testing.

The rate at which the reaction takes place is vital to the well-being of the cell as a whole. The

reaction must take place fast enough so that the cell itself is not harmed; however, if the reaction is too

fast, other harmful effects in the body may take place. The catalase is present at an optimal quantity,

concentration, temperature and pH in order to satisfy the needs of the cell and the body, as well as to

create a balanced and functional cell.

 Rezazadeh-shahi 5

Data/Analysis

Factors Affecting Rate of Enzyme Activity

Rate
Concentration_of_Catalase 0.31757214
S1 = correlation ( )

According to the data collected, the results verify the prediction. The trend shows a positive

correlation which implies that as the concentration of catalase increases, the rate of the enzyme activity

also increases. However, the collected data indicates a weak correlation because of the inconsistent

results collected such as the outliers at 0.8g/mL and 1.6g/mL. This suggests that there may be outside

factors that have an affect on the reaction during testing. It is unclear whether or not the rate of enzyme
 Rezazadeh-shahi 6
activity increases exponentially or linearly. The only thing that is proven by the samples used and the

collected data is that there is a positive correlation and that the concentration of the enzyme does cause

the rate of the reaction to increase relatively.

 Rezazadeh-shahi 7
Conclusion

The data proves that as the concentration of the enzyme increases, as does the rate of the

reaction. The results are derived from experiments conducted in a lab setting; however, the application

of the reaction occurs inside a living organism and the internal effects of the reaction must be

considered when describing an optimal concentration for the enzyme concentration. The increased rate

is a desirable result of a higher concentration of enzyme; however, the qualitative results indicate that

along with the reaction, gas is formed as indicated by the bubbles that rise. This may cause undesirable

affects within the body. With a higher concentration of catalase, more bubbles are formed and they are

formed at a faster rate. This suggests that although an infinitely large concentration of the enzyme

would result in a faster rate of reaction, the faster rate may cause other implications. The high amounts

of gas which form as a result of the reaction may cause discomfort and pain within the body during the

reaction; therefore, an infinitely large concentration of catalase is not optimal. The concentration of

catalase within the body should be limited to the needed amounted based on one’s diet. There should

be just enough of the enzyme to induce a reaction at a moderate rate which would control the reaction

and the harmful effects of the reaction.

Reflection
 Rezazadeh-shahi 8
Sources of Error
 Rezazadeh-shahi 9
Works Cited