Peroxidase Enzyme Lab
Description: A peroxidase enzyme, which was extracted from a brassica compestris (turnip), is tested under various conditions in temperature, pH level, and competitive inhibitor (hydroxylamine).
ABSTRACT:
In order to determine the properties of an enzyme, a peroxidase enzyme was extracted from a brassica compestris (turnip) and tested under various temperatures, pH levels, and by a competitive inhibitor (hydroxylamine). The enzyme activity was measured in various ways depending on the activity. Temperature effects showed the amount of activity and determined the optimal pH level. The spectrometer showed the absorbance units at 500nm and determined the optimal temperature. The temperatures tested where 4ºC (approximately refrigerator temperature), …show more content…
The enzyme dramatically speeds up reactions by lowering the activation energy barrier. Every enzyme has a unique shape because the substrates that bond to it are all different shapes. It fits like a lock and key. Once the substrate enters the active site, the enzyme slightly changes shape in order to lock in the substrate and holds it in place. Enzymes allow organisms to live by increasing the rate of a chemical reaction. The peroxidase enzyme catalyzes the reaction of the formation of oxygen. Various temperatures and pH levels will be tested in order to determine the optimal environment for the peroxidase …show more content…
The optimal temperature is not exactly the same to the human body however it is relatively close (four degrees difference).
The hypothesis for the effect of various pHs on the activity of the peroxidase enzyme was not clear enough and did not predict any results. Based on the experiment, the best pH for the peroxidase enzyme is pH 5.
Meanwhile, the hypothesis for the effect of boiling the extract was correct. The results obtained in the experiment supported the original hypothesis that when proteins (which an enzyme is) are heated to a temperature above 70ºC, the enzyme will be dead when it is boiled.
Based on the effects of the hydroxylamine treated extract, the original hypothesis is again accepted. Because the inhibitor, hydroxylamine, blocked the substrate of hydrogen peroxide from entering the active site, the absorbance units decreased compared to the normal extract absorbance units.
Further work that would be needed to test explanations would include a more variety of temperatures as well as other enzymes and compare the results between various enzymes.
ABSTRACT:
In order to determine the properties of an enzyme, a peroxidase enzyme was extracted from a brassica compestris (turnip) and tested under various temperatures, pH levels, and by a competitive inhibitor (hydroxylamine). The enzyme activity was measured in various ways depending on the activity. Temperature effects showed the amount of activity and determined the optimal pH level. The spectrometer showed the absorbance units at 500nm and determined the optimal temperature. The temperatures tested where 4ºC (approximately refrigerator temperature), …show more content…
The enzyme dramatically speeds up reactions by lowering the activation energy barrier. Every enzyme has a unique shape because the substrates that bond to it are all different shapes. It fits like a lock and key. Once the substrate enters the active site, the enzyme slightly changes shape in order to lock in the substrate and holds it in place. Enzymes allow organisms to live by increasing the rate of a chemical reaction. The peroxidase enzyme catalyzes the reaction of the formation of oxygen. Various temperatures and pH levels will be tested in order to determine the optimal environment for the peroxidase …show more content…
The optimal temperature is not exactly the same to the human body however it is relatively close (four degrees difference).
The hypothesis for the effect of various pHs on the activity of the peroxidase enzyme was not clear enough and did not predict any results. Based on the experiment, the best pH for the peroxidase enzyme is pH 5.
Meanwhile, the hypothesis for the effect of boiling the extract was correct. The results obtained in the experiment supported the original hypothesis that when proteins (which an enzyme is) are heated to a temperature above 70ºC, the enzyme will be dead when it is boiled.
Based on the effects of the hydroxylamine treated extract, the original hypothesis is again accepted. Because the inhibitor, hydroxylamine, blocked the substrate of hydrogen peroxide from entering the active site, the absorbance units decreased compared to the normal extract absorbance units.
Further work that would be needed to test explanations would include a more variety of temperatures as well as other enzymes and compare the results between various enzymes.