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Enzyme Peroxidase Experiment

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Enzyme Peroxidase Experiment
The experimental results were different from the hypothesis because while the enzyme appeared to not work as well, I expected a more significant change. Most of the time, there was only a millimeter of difference of the foam between the two samples while I expected a greater difference such as 10 millimeters. Enzymes speed up chemical reactions and at the active site, a substrate can be broken down or two substrates can form a larger molecule. Hydrogen peroxide is broken down by peroxidase into water and oxygen which is released in the form of gas bubbles. If there is a large amount of bubbles, it means there is a large quantity of peroxidase breaking down the hydrogen peroxide. Denatured enzymes are enzymes whose shape has been altered and are no longer active (Wiggins). Ethanol is able to denature enzymes and caused the enzymes in the potato piece to be unable to function. This caused the ethanol-soaked potato to have less activity than the water-soaked potato since it did not have its enzymes denaturized like the one soaked in ethanol. …show more content…
This would have messed up the experiment since you would have been measuring the activity of both potatoes instead of comparing the activities of the potatoes in different test tubes. I would have been incapable of measuring whether or not the enzyme peroxidase worked as well a regular after being soaked in ethanol since I would also be measuring the activity of the regular potato. Further research is needed to know if ethanol denatures enzymes at the same rate in different substances. I could soak different foods like potatoes or pineapples in ethanol before placing them into test tubes filled with hydrogen peroxide. If there is a difference in the amount of foam, then I would know that ethanol affects enzyme activity at different rates in different

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