Peroxidase Lab Report
Effects of Temperature, pH, Boiling, and Hydroxylamine on the Enzyme
Peroxidase Extracted From Brassica rapa
Abstract
In this experiment the enzyme peroxidase was extracted from from a turnip,
Brassica rapa, and tested under different conditions. The effects of temperature, boiling, pH, and a competitive inhibitor were tested. The enzyme was tested at temperatures of 4°C, 24°C, 32°C, and 48°C. As the temperature increased, so did the activity of the enzyme. The enzyme was tested at pH levels of 3, 5, 7, and 9. The optimal pH for peroxidase is 5. If the pH was higher or lower than pH 5 the enzyme activity was significantly decreased. When the enzyme was boiled, the enzyme stopped working. When the enzyme was treated with …show more content…
Introduction
MerriamWebster defines an enzyme as “a chemical substance in animals and plants that helps to cause natural processes.” Enzymes act a catalyst to lower the activation energy of a reaction, the amount of energy needed to undergo a specific reaction. This will make the reaction happen much quicker because less energy is needed. Different enzymes have different threedimensional shapes with an active site, a cleft or depression. Substrates will bind to the active site of an enzyme if it is the correct shape. This makes it easier for the molecules to react. However, there are inhibitors that will prevent the substrates from binding to the active site. Inhibitors do this by either binding to active site, or changing the shape of the active site by binding to some other place on the enzyme. The threedimensional shape of an enzyme can also be changed by high temperatures and different pH levels. The enzyme peroxidase catalyzes the breakdown of peroxide (Dolphin and Vleck, 2014).
The purpose of this study was to test the effects of temperature, pH, boiling, and hydroxylamine on the enzyme peroxidase, which speeds up the conversion of
Peroxidase Extracted From Brassica rapa
Abstract
In this experiment the enzyme peroxidase was extracted from from a turnip,
Brassica rapa, and tested under different conditions. The effects of temperature, boiling, pH, and a competitive inhibitor were tested. The enzyme was tested at temperatures of 4°C, 24°C, 32°C, and 48°C. As the temperature increased, so did the activity of the enzyme. The enzyme was tested at pH levels of 3, 5, 7, and 9. The optimal pH for peroxidase is 5. If the pH was higher or lower than pH 5 the enzyme activity was significantly decreased. When the enzyme was boiled, the enzyme stopped working. When the enzyme was treated with …show more content…
Introduction
MerriamWebster defines an enzyme as “a chemical substance in animals and plants that helps to cause natural processes.” Enzymes act a catalyst to lower the activation energy of a reaction, the amount of energy needed to undergo a specific reaction. This will make the reaction happen much quicker because less energy is needed. Different enzymes have different threedimensional shapes with an active site, a cleft or depression. Substrates will bind to the active site of an enzyme if it is the correct shape. This makes it easier for the molecules to react. However, there are inhibitors that will prevent the substrates from binding to the active site. Inhibitors do this by either binding to active site, or changing the shape of the active site by binding to some other place on the enzyme. The threedimensional shape of an enzyme can also be changed by high temperatures and different pH levels. The enzyme peroxidase catalyzes the breakdown of peroxide (Dolphin and Vleck, 2014).
The purpose of this study was to test the effects of temperature, pH, boiling, and hydroxylamine on the enzyme peroxidase, which speeds up the conversion of