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).
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), 23ºC (approximately room temperature), 32ºC, and 48ºC. The pH levels tested were; pH3, pH5, pH7, and pH9. The competitive inhibitor used was Hydroxylamine. These tests resulted in the ability to determine the optimal temperature: 32ºC because it closest to body temperature. The best pH level was found to be pH5.
An enzyme is a protein that serves as a catalyst, which is a chemical agent that changes the rate of a reaction without being consumed by the reaction. 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 enzyme.
Temperature: If the optimal human body temperature is 36ºC, then the enzyme's optimal temperature should be...
Citations: Dolphin, Warren D. 2005. Biological Investigations. Lab Topic 7 Determining the Properties of an Enzyme, ed. Kent A. Peterson, pp.79-89.
New York, NY: McGraw-Hill
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