Description: A peroxidase enzyme‚ which was extracted from a brassica compestris (turnip)‚ is tested under various conditions in temperature‚ pH level‚ and competitive inhibitor (hydroxylamine). ABSTRACT: In order to determine the properties of an enzyme‚ a peroxidase enzyme was extracted from a brassica compestris (turnip) and tested under various temperatures‚ pH levels‚ and by a competitive inhibitor (hydroxylamine). The enzyme activity was measured in various ways depending on the activity
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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 are important components of life‚ facilitating reactions that are necessary for an organism to live. Enzymes can be very specific to what environment they function best in1. Numerous environmental impacts were tested for the enzyme peroxidase which catalyzes the decomposition of hydrogen peroxide. The basic decomposition reaction was carried out first without any environmental alterations. The hypothesis for this reaction was supported. The enzyme caused the amount of absorbance increase
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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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different from the hypothesis because while the enzyme appeared to not work as well‚ I expected a more significant change. Most of the time‚ there was only a millimeter of difference of the foam between the two samples while I expected a greater difference such as 10 millimeters. Enzymes speed up chemical reactions and at the active site‚ a substrate can be broken down or two substrates can form a larger molecule. Hydrogen peroxide is broken down by peroxidase into water and oxygen which is released in
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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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The Affects of pH on Peroxidase Enzyme Claire Bell Biology 1130 Jazmen Myers Section 36 Abstract Peroxidase is a turnip enzyme; it is used in the oxidation of hydrogen peroxide to lower activation energy‚ speeding up the reaction. The activity of peroxidase is highly dependent on its environment and most importantly the pH level. Peroxidase has been the focus of many recent studies and is believed to possibly reduce swelling among other things. We conducted an experiment testing
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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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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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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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