205 Lab W/8:00 Enzyme II Write-Up Methods: My partner and I ran two experiments to measure the activity of the enzyme horseradish peroxidase under varied conditions. The first of which measured the effects of altered pH levels‚ while the goal of the second was to examine the effects of varied temperatures. To test the effects of pH on horseradish peroxidase‚ we began by zeroing a Spec 20 with 5.0mL of substrate (25mM guiacol) at pH 6.5. Once the Spec 20 was accurately zeroed‚ we added 100μL
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Four environmental factors of enzymes were tested in lab. The changing of pH‚ substrate concentrations‚ temperature‚ and an inhibitor (NaCl) and the effects it hade on the enzyme turnip peroxidase. Enzymes are biological catalysts which increase reaction rates by lowering the activation energies of substrates. A substrate is a reactant that interacts with the enzyme. The enzyme and substrate can be viewed as the recently discovered "induced fit model"‚ which suggests enzymes are flexible and dynamic
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Japan)‚ while puerarin (≥98%) and glycitin (≥99%) were obtained from Tokyo Chemical Industry Co. (Tokyo‚ Japan) and LC Laboratories (MA‚ USA)‚ respectively. Ovalbumin (OVA‚ ≥98%) was purchased from Sigma-Aldrich (Steinheim‚ Germany). Horseradish peroxidase (HRP)-conjugated goat IgG to mouse IgG Fc and HRP-conjugated mouse IgG against T7-Tag were individually purchased from Organon Teknika Cappel Products (PA‚ USA) and Novagen (MA‚ USA)‚ respectively. Toyopearl CM-650M cation exchange resin was
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Temperature on Peroxidase Ability to Break Down H2O2 By: Rodneika Crutcher Abstract Temperature affects the ability of peroxidase to break down hydrogen peroxide. In this experiment our professor extracted peroxidase from potato tissue. In order to determine how temperature affects peroxidase we created solutions and measured their absorbance levels after water bath treatments. The more absorbent the solution was the less hydrogen peroxide there was in the solution. This means the peroxidase was able to
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Factors that Affect the Rate of Reaction of Peroxidase Purpose: To determine the effect of various factors on the rate of reaction between an enzyme and its substrate‚ and also to determine the optimal ranges under which the enzyme activity is maximized. Also to determine whether saline and alcohol are inhibitors or activators Hypothesis: PH factor prediction: I predict that as the pH increases so the activity of the enzyme will increase until it reaches optimum pH range (pH 7) because the
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have no effect on the reaction whatsoever.I predict alcohol is an inhibitor of Peroxidase because alcohol when alcohol bind to theallosteric site it changes the active site shape of the enzymes thus deactivating enzymaticactivitiesI predict salt is an activator of Peroxidase because salt contains Na ions which attaches tothe allosteric site changing the shape of the enzyme to fit a substrate. Materials: • Peroxidase (enzyme in potato) • Hydrogen peroxide‚ 3% • A strong acid‚ pH3 (lemon juice
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Abstract: Enzyme-catalyzed hydrolysis reaction occurs when an enzyme cleaves glycosidic linkage where a substrate binds to active site forming an enzyme-substrate complex. By adding water to the enzyme-substrate complex‚ products are release. One of the main factor that effect enzyme-catalyzed reactions is temperature. After an enzyme reaches an optimal temperature‚ the enzyme will result in irreversible denaturation. The irreversible denaturation causes the protein to loose its function making
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Finding the Optimal pH of the Enzyme Peroxidase with the Aid of a Spectrophotometer ABSTRACT The peroxidase enzyme was partially purified‚ and the enzyme activity was calculated with the use of a spectrophotometer‚ demonstrating the effect of pH on peroxidase activity. The objective of this exercise was to determine the ideal pH for peroxidase activity. The data concluded that the optimum pH for peroxidase activity is 5‚ and the “standardized” enzyme volume is 2.8mL
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How Enzymes Work In Different Environments By Sarah Smith Biology1111 October 20‚ 2011 Lab Partner: Nellie Greer ABSTRACT Peroxidase is an enzyme found in potatoes that catalyzes the breakdown of hydrogen peroxide‚ H2O2‚ into O2 gas and water. We examined the different pH environments that can affect the enzyme activity during the breakdown of H2O2. In order to do this‚ we added different levels of pH‚ low‚ medium‚ and high‚ into different test tubes with the enzyme and H2O2‚
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Title of Lab: Preparation and Assay of Phenolase and Peroxidase from Sweet and Irish Potato Hypothesis: Polyphenol Oxidase enzyme activity can be detected by change in colour of solution‚ Inhibitors prevent the reaction of the enzymes with substrates‚ the enzyme is relatively specific. Aim: To design and conduct an experiment to demonstrate enzyme activity of Polyphenol Oxidase and Peroxidase when mixed with catechol‚ caffeic acid‚ pyrogallad‚ tyrosine‚ guacol‚ and water‚ to test the effect of
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