Investigating an enzyme-catalyzed reaction

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Investigating an enzyme-catalysed reaction

Introduction

Our experiment involves us testing the rate of reaction by using hydrogen peroxide and the enzyme called catalase. The catalase in this experiment is an enzyme with an active site (place where substrate fits) which fits hydrogen peroxide (a poison produced by all cells). This is an example of a lock and key model where the substrate molecule fits in to the enzyme. Enzymes are used to speed up chemical reactions in the body.

Catalase is found in all living cells and is specific for the breakdown of hydrogen peroxide. The catalase can become denatured through heat and pH. The catalase will be used to break down the hydrogen peroxide into water and oxygen. The equation for this equals:

         

                                                    Catalase

                                                     2H2O2        2H2O+O2

This is another diagram to show how an enzyme (invertase) can break down sucrose into to smaller sugars- glucose and fructose. At the end of the reaction, the enzyme is unchanged and can catalyse the breakdown of another molecule of sucrose:

 

After looking at the scientific understanding of what is required I have thought about what sort of method I would use to get a good set of results. I have also reviewed what I will need to check during my preliminary investigations to make sure that I get the most reliable set of results I can. I have also thought about what change in variable I will make that will be easiest to achieve and to get the best set of results.

Hydrogen Peroxide

Hydrogen peroxide () is a very pale blue , slightly more  than water that appears colorless in dilute solution. It is a weak , has strong  properties, and is a powerful . Nearly all living things possess enzymes known as , which harmlessly and catalytically decompose low concentrations of hydrogen peroxide to water and oxygen.

Variables

There are lots of different factors that can affect the rate of the enzyme reaction. Here are some of them:

pH- Enzymes have a specific 3- dimensional shape which is very sensitive to pH. In very acidic or alkaline conditions the shape of the enzyme can change. If this changes the active site it will no longer fit the substrate and the reaction will no longer take place. The pH at which enzymes work best at vary on the enzymes purpose e.g. enzymes in the stomach work best in acidic conditions, so 1-5.

Temperature- At higher temperatures there are more reactions because there are more collisions between the molecules because they are moving faster. If the temperature is above 40°C the enzyme can become denatured which again leads to the shape of the active site changing. The temperature at which enzymes work best at 37°C.

Surface Area- If there is a larger surface area more of the enzyme is in contact with the substrate, leading to an increased reaction rate.

Concentration- A more concentrated solution has more molecules in a given volume. This leads to more collisions between enzyme and substrate taking place resulting in an increased rate of reactions.

The variable that we will be changing in our experiment is the concentration in the yeast. All the other variables will be staying the same in our investigation. We choose to change the concentration because it is easier to measure and easier to use than the others. I thought that temperature would be harder to measure and that measuring ph and surface area would have been too hard to put together and it would have taken to long. So we decided for concentration to be the variable that we changed. I came to this decision because it was easy to do and was the least time consuming; it was also easier to record the results. We also choose to use the yeast solution over the small solid grains of yeast because it was more evenly distributed and the solid yeast granules were harder to measure small solids accurately.

Preliminary Investigation

Before I start my experiment I must do some preliminary tests to check the sort of equipment I will be using and the way I will perform my experiment. Firstly I needed to choose the source of the catalyse, because without the catalyse there is no experiment. At first I tried to run an experiment using small amounts of potatoes, however I felt that this didn’t go very well because it took me too long to get it all prepared and wasn’t very practical. So I decided to use the yeast solution in the end as they were very easy to prepare and were reliable.

I also had to decide on the variable that I would be testing to do my experiment on. After looking at the different variables I decided to base my experiment on concentration. I came to this decision because it seemed an interesting variable to investigate. I also thought that testing pH, temperature and surface area wouldn’t have been suitable for the level of my investigation. I thought it would be easier measuring the amount of yeast rather than changing the pH or temperature.

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These results I have recorded from are final preliminary results from the experiment that I will be doing for our actual experiment. This is also the table that I will record for my results in for my actual result.

To calculate the % of concentration on diluting the original 2% solution:

Volume of yeast solution

Concentration of Yeast=    Volume of yeast+ Volume of water   X 2%

Now knowing this calculation I know how I can change the concentration and how I can get some good results. I can do this by changing ...

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