Wednesday, December 15, 2010

The Joy of Making Bubbles with Enzymes

Well, we did a little experiment with enzymes to see just how they worked. Our setup was relatively simple: 3 mL of water and 3 mL of hydrogen peroxide. Our enzyme was simply yeast, and the object was to manipulate various variables with the reaction to see what the change would be. My attempt at explaining what was going on is that the yeast breaks off the oxygen from the hydrogen peroxide and releases the oxygen into the atmosphere. This created the pressure we measured with a pressure probe.

Here are the various graphs we managed to draw from the experiment. I'll explain the meaning of each as we go along. 

This graph shows the change in the rate of reaction as we changed the concentration of the enzyme. The slope of this graph is relatively constant, suggesting that the rate of reaction is directly related to the concentration of the enzyme.

This graph (although admittedly bizarre) shows the change of the rate of reaction as the pH level of the solution the reaction was occurring in changed. We used buffers to hold the pH at constant levels of 4, 7, and 10, and found that the highest rate of reaction was when the pH was the pH of water--7.

This graph shows the change of the rate of reaction as we changed the temperature of the solutions that the reaction was occurring in. We used four different temperatures, namely, 0, 25, 38, and 80 (all of which were measured in degrees Celsius). By looking at this graph, we can see that the greatest rate of reaction occurred at slightly warmer than room temperature, but that the enzymes' productivity fell dramatically as the heat increased too much. This was explained when we realized that the heat could cause the enzymes to become denatured (meaning that the shape changed).

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