Effect of pH on Enzyme Activity A piece of Solanum tuberosum (potato) was removed and mixed with distilled water in a blender. The resulting solution was filtered through multiple layers of cheese cloth to filter out the liquid by eliminating any large pieces in the solution. The solution created was catechol. Five different solutions were prepared as blanks with each test tube containing 6.0mL of a different pH (pH 4‚ pH6‚ pH7‚ pH8‚ pH10) of phosphate buffer‚ 1.0mL of the enzyme and 1.0mL of water
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Abstract The main goal of the enzyme kinetics experiment was to see how the phosphatase-catalyzed hydrolysis of p-nitrophenyl produced p-nitrophenol in the presence of phosphate and fluoride ion inhibitors of various concentrations. The calculated Km constant was found to be 0.22 for all reactions. The Vmax values for each inhibition ion were 0.00986 for the phosphate ion and 0.00436 for the fluoride ion. The inhibitor constant‚ Ki‚ was determined to be 0.0967 for the phosphate ion. The inhibitor
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In this lab the peroxidase enzyme is tested in a dormant avocado seed as well as an avocado seed undergoing the process of germination. A gas pressure will be used to test the seeds and see if the peroxidase enzyme is present in either of the seeds. A catalyst is very similar to track spikes. Spikes increase a runner’s speed‚ as a catalyst speeds up the chemical reaction time in a plant. Neither the catalyst nor shoes are changed in these actions. Enzymes are macromolecules that act like catalysts
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Enzymes Reactions to Changes in Substrate and Inhibitors Benjamin J. Mora Coronado University of Texas Rio Grande Valley at Edinburgh Abstract Purpose for the experiments was to test the enzymes in various scenarios and see how changing this would affect the rate of reaction. The enzyme source used in the experiments was Turnip Extract. Concentrations of Turnip extract for activity 1 where o.5ml‚ 1.0ml‚ and 2.0 ml as for the rest of the activities 2 Through 4 stayed at a consistent concentration
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The objectives of this experiment were to investigate the activity of enzymes‚ components that influence the enzyme’s activity‚ identify an unknown phosphatase‚ influence of inhibitors‚ and determine if inhibition is competitive or noncompetitive. A spectrophotometer evaluated the measurement of color change over a period time due to product being formed. Determining unknown phosphatase and effects from different inhibitors were determined by varying the pH and substrate concentrations. The unknown
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Activity of the Enzyme Catalase in breaking down Hydrogen Peroxide and the effect of various factors on Enzyme Activity Introduction The enzyme catalase is present in cells in order to speed the breakdown of hydrogen peroxide (H2O2)‚ which is a toxic chemical to the human body. When hydrogen peroxide is broken down‚ the end products are Water (H2O) and Oxygen (O2). In this report‚ the reaction of catalase to hydrogen peroxide is being tested. Furthermore‚ the effects of temperature‚ concentration
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pH‚ and concentration of substrate‚ on the activity of the enzymes. By conducting these three separate experiments also‚ three graphs are able to be obtained where the trend of each factor affecting on the enzyme activity is shown and described clearly. II. Hypothesis Experiment 1 (Effect of Temperature): As the temperature increases‚ the height of the bubble will increase too‚ indicating a faster rate of reaction. Experiment 2 (Effect of pH): Enzymes are affected by changes in pH. Extremely
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Chemistry 512 Enzyme Catalysis Lab Report Pre-lab Questions: 1. Write a balanced chemical equation with state symbols for the reaction catalyzed by peroxidase. 2H2O2 2H2O + O2 (4H1 4O) (4H + 2O + 2O) 2. What is the substrate(s) of this reaction? What is the catalyst? Substrate = H2O2 hydrogen peroxide Catalyst = peroxide 3. At what approximate temperature do enzymes normally operate in the body of a warm-blooded animal? Would your answer change if the enzyme came from a plant or yeast? Enzymes normally
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correlation between catalase concentration and the rate of reaction. This occurs because as the enzyme concentration increases‚ there are more enzymes available to catalyze substrates. More enzymes means more reactions can take place at a time‚ thus a faster rate of reaction. Overall‚ based on the results of table 2.0 and graph 2.0‚ it is prevalent that there is a positive correlation between the concentration of enzymes and the rate of
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Abstract: Enzymes‚ molecules that speed up chemical reactions‚ are specific to one substrate. In this experiment the substrate hydrogen peroxide and the enzyme catalase will be used. The higher the concentration of potato extract‚ or catalase‚ the faster the reaction and the more substrate present will result in a decrease in the time of the reaction. The amount of concentrations of enzymes and substrates are changed to determine if the reaction is further catalyzed by a greater concentration of
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