abstract - increased the maximum velocity of the reaction,...

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This experiment tested the effects of different concentrations of Hydrogen Peroxide, different concentrations of peroxidase, and different temperatures on the performance of the enzyme peroxidase. The reaction was carried out multiple times to test each variable using hydrogen peroxide, peroxidase from turnips, and guiacol, which functions as a hydrogen donor and changes color as it is oxidized. This color change allows for reaction rate to be studied using a spectrophotometer, which measures light absorption over time. These values for absorption were used to calculate the initial velocity of the reaction under all of the different conditions. The results were analyzed using Michaelis-Mentin enzyme kinematics and Lineweaver-Burk plots. Increasing enzyme concentration
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Unformatted text preview: increased the maximum velocity of the reaction, as did increasing substrate concentration. This is because more reactants were available, which allowed the enzyme-substrate complex to be converted to product more quickly. Increasing the temperature of the system increased the maximum velocity to a certain point because it caused an increase in kinetic energy of the system, which increased interaction between the enzyme and substrate. However, temperatures higher than the optimal temperature resulted in a decrease in maximum velocity because the enzyme had begun to denature. At the highest temperature tested (75 Degrees C) the enzyme had completely denatured, and thus the reaction did not proceed....
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This note was uploaded on 10/11/2009 for the course BIOL 205 taught by Professor Chernin during the Fall '09 term at Bucknell.

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