Abstract
Enzymes are the catalysts that are vital to living organisms because they speed up the rate of reaction to allow metabolism to happen in a productive rate. The purpose of this lab was to examine how temperature, pH level and concentration of enzyme affect enzyme kinetics. In this investigation, catalase, harvested from bovine liver, was used as the enzyme and hydrogen peroxide was the substrate in the reaction. The reaction modelled in the lab can be found in normal metabolism within the liver as it is necessary to decompose excess hydrogen peroxide into water and oxygen. Nine investigations with distinct factor alterations were conducted including high temperature (60°C), low temperature (3°C), room temperature (27°C), acidic pH level (pH 3), basic pH level (pH 11), neutral pH level (pH 7), high concentration (90%), low concentration (<1%), and standard concentration (30%). 3 mL of catalase were placed within each test tube and 2mL of the hydrogen peroxide was added. For temperature, significant results found include the most efficient temperature being 27°C, reacting within 1.2 seconds; a decrease of reaction rate occurs when the temperature increases (7.1 seconds) because enzyme denatured, the reaction rate also decreased (3.4 seconds) with temperature was low because molecules did not have enough energy to move and collide fast enough.. For pH level, the basic (pH11) enzyme worked the fastest (14 seconds) due to mistake in timing. Theoretically, the neutral enzyme is the most efficient because an alteration in pH often denatures the enzyme. For enzyme concentration, high concentration (90%) was suppose to react the fasted because of increase of available active site, in reality though, low concentration catalase solution was the most efficient (2.9 seconds) and high concentration was the least efficient, reacting within 12.4 seconds, possibly because of the limited surface area available for diffusion.
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