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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simpler compounds by the action of enzymes‚ complex organic catalysts‚ which are produced by microorganisms such as molds‚ yeasts‚ or bacteria. Enzymes act by hydrolysis‚ a process of breaking down or predigesting complex organic molecules to form smaller compounds and nutrients. For example‚ the enzyme protease breaks down huge protein molecules first into polypeptides and peptides‚ then into numerous amino acids‚ which are readily assimilated by the body. The enzyme amylase works on carbohydrates‚
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being tested if amylase‚ an enzyme found in saliva‚ would be denatured by being put in an acid or high temperatures. This lab is about denaturing amylase. It is tested by exposing it to pH and temperature changes. It is then mixed with Benedict’s solution‚ is a solution that changes color from blue to reddish brown when maltose is present. Amylase breaks starch into maltose‚ so is the amylase isn’t denatured‚ it should change colors. Amylase is an enzyme. Enzymes are a type of catalyst‚ and
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steeping is a risky process and may result in the degradation of cotton cellulose while rot steeping‚ hot caustic soda treatment and hot washing with detergents are less efficient for the removal of the starch sizes. * Enzymatic desizing : Enzymes are solubilizing bio catalysts‚ mainly proteins‚ thermo labile (readily changed or desized by heat) and highly specific in their action. A
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Enzyme Kinetics and Protein Determination: How Enzyme Catalase Concentration Affects Reaction Rate and Determining the Identity of Unknown Proteins through Absorbance By: Alexander Mak 7238991 Partner: Yasmin Ismail BIO2137 Section A7 Corrector: Chieu Anh Ta September 18‚ 2014 Introduction: The first lab’s primary objective is to observe the different reactions rates amongst the five different catalse concentrations of parsnip. The rate at which the enzyme catalyzes increases 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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hydrogen ion concentration of a substrate. By changing the pH of the catalase‚ the enzyme was denatured. Denaturing is the result of altering the characteristics or properties of an enzyme by temperature‚ pH level‚ or substrate concentrate. As the optimal conditions of the enzyme are changed‚ bonds in the enzyme are broken and the enzyme unfolds at the tertiary and quaternary level. When this happens‚ the structure of the enzyme and active site is changed. With the change in the active site‚ the substrate
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BIOLOGY 22 MODULE 1 – Chemical Basis of Life v2.0 * Levels of Organization – biological functions are ultimately based on the properties of atoms and molecules * Subatomic particles – neutrons‚ electrons‚ protons * Atoms * Compounds * Complexes of compounds * Organelles – bodies within cells that perform specific functions * Cell * Specific combination of organelles * Can metabolize and reproduce * Least elaborate living structure * Significance
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purpose of the first week experiment was to determine the effect of Nitrophenyl phosphate concentration‚ the substrate‚ on the enzyme‚ acid phosphatase‚ reaction. In an enzyme reaction‚ there is substrate that binds to the active site of the enzyme and product is the end result. The enzyme is the catalyst for the reaction which means that it speeds up the process. Without enzymes‚ the majority of reactions would not occur because the activation energy level would be unattainable. With this in mind‚ the
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between other cuvettes‚ for example‚ absorbance differences between cuvette 1s and 2s or 2s and 3s. It is assumed that the relative concentration of enzymes does not catch up that of iron cofactors. In other words‚ even though we put more iron cofactors to interact with enzymes after a certain point‚ it cannot speed the reaction further because no more enzymes can interact with extra iron cofactors. Furthermore‚ we can notice that even though the higher amount of iron cofactors indicates the higher absorbance
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