Concentration on Peroxidase ABSTRACT The purpose of this experiment was to inspect the effect of environmental conditions on hydrogen peroxidase. The three conditions tested were the effect of peroxidase concentration on the rate of the experiment‚ the effect of pH of the rate of peroxidase activity‚ and the effect of temperature on the rate of peroxidase activity. During the lab‚ the lab group tested 7 test tubes‚ including 1 blank‚ with different amounts of pH 5 buffer‚ H2O2‚ Peroxidase‚ and Guaiacol
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Over a two week period of time in the laboratory‚ we experimented and tested the reaction rate of a peroxidase enzyme and the factors that affected it‚ both positively and negatively. The purpose of these experiments was to probe and manipulate the activity of the enzyme peroxidase by varying temperature‚ pH‚ the amount of enzyme compared to the substrate and the effect of hydroxylamine. Peroxidase activity is expressed when the potato extract is subjected to stresses such as low temperature (El-hilali
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and Hydroxylamine on the Enzyme Peroxidase Extracted From Brassica rapa Abstract In this experiment the enzyme peroxidase was extracted from from a turnip‚ Brassica rapa‚ and tested under different conditions. The effects of temperature‚ boiling‚ pH‚ and a competitive inhibitor were tested. The enzyme was tested at temperatures of 4°C‚ 24°C‚ 32°C‚ and 48°C. As the temperature increased‚ so did the activity of the enzyme. The enzyme was tested at pH levels of 3
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Abstract The enzyme peroxidase has been shown to break down H2O2. Enzymes are known to increase the rate at which a chemical reaction occurs. We looked at factors that affected the breakdown of hydrogen peroxide. These effects are the different temperatures and pH levels the enzymes were placed in. We found that the optimum‚ or best condition‚ temperature for the enzymes tested was about 22 degrees Celsius. The optimum pH level for the enzyme was 7. Introduction Enzymes are biochemical that catalyze
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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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the Catalytic Properties of the Enzyme Peroxidase Extracted from a Turnip Under the Conditions of Temperature‚ pH‚ Boiling and Competitive Inhibitors By Robin Caserta BIO 101 September 30‚ 2013 ABSTRACT The enzyme‚ peroxidase‚ extracted from a turnip was tested for its efficiency in binding to its substrate and its stability under several conditions. To do this‚ we tested effects on peroxidase activity‚ first‚ with different amounts of the enzyme‚ next at temperatures of 4oC‚ Room
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Horseradish Peroxidase Abstract There are several factors that can affect the rate of reaction of peroxidase such as temperature‚ pH‚ concentration of peroxidase present and whether or not it has been boiled. Our experimental data demonstrated that peroxidase activity peaked between 23 degrees Celsius and 32 degrees Celsius. We found the pH to be 7 for optimal activity. As far as the concentration is concerned our results showed that as the concentration of horseradish peroxidase doubled so
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NaCl Effects on Peroxidase Activity My experiment was to see if adding NaCl to solution would have any effects on peroxidase activity. The materials that were used in this experiment were pH 7 buffer(DI water)‚ peroxidase‚ NaCl‚ guaiacol and hydrogen peroxide; added in that order. Blanks were created for each NaCl concentration‚ 0%‚ 5%‚ 7.5% and 10%. Each cuvette had .5ml of pH 7 buffer‚ 1ml of peroxidase‚ .02ml guaiacol for the experimental cuvettes and 0ml of guaiacol for the blank cuvettes‚
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results that higher concentration of iron cofactors shows the higher absorbance. The importance of the existence of iron in this reaction is that the peroxidases in plant cells respond to environmental stress by‚ in this case‚ catalyzing the conversion of toxic metabolic wastes‚ H2O2‚ into the harmless products‚ H2O and O2‚ faster. Therefore‚ as peroxidases help minimize and eliminate harmful chemicals‚ the iron cofactors that help peroxidase’s activity raise the possibility of plants’ survival in harsh
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Enzymes are proteins which serve to reduce the activation energy required for biological reactions (Russell and others 2010). This allows biologically important chemical reactions to occur rapidly enough to allow cells to carry out their life processes (Russell and others 2010). Enzymes are made of one or more polypeptide strands‚ which individually or as an associated complex take on a three-dimensional shape. When properly associated‚ these shapes form the active site and other supporting structures
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