An experiment was run to determine which enzyme (pectinase‚ and cellulase or combinations of the two enzymes) maximizes juice production and would be most cost effective. The proposed hypothesis was if the enzyme‚ pectinase‚ is added to apple juice‚ then the more juice will be extracted than if cellulase were added because pectinase holds the cell wall together and if it is separated apart from each other‚ then the more juice would be able to flow out. The experimental data show that during the ten
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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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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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I. Aim The aim of the three experiments is actually to investigate the effects of different factors such as temperature‚ 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
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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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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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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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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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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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Catalase in Various Concentrations of Hydrogen Peroxide QUESTION: How long does the catalase take to float to the top of a cup filled with different amounts of hydrogen peroxide concentration? PREDICTION: A prediction that can be made for this experiment is that the higher the concentration‚ the faster time it takes the catalase to react with the solution. As the concentration increases from 1% to 100%‚ the average reaction rate of the catalase will decrease‚ as the catalase will speed up the reaction
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