College General Biology I Enzymes‚ test for effect of pH on catalase activity Purpose The main purpose of this experiment was to learn about enzymes and how to test for the effect of pH on catalase activity and to be able to tell if a reaction is an exergonic or endergonic process. Introduction Enzymes are made from amino acids‚ which are made from proteins. In order to make an enzyme‚ hundreds of amino acids are strung together in a very specific and unique order and eventually is folded
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Enzyme Lab Report Introduction The objective of this experiment was to determine if changes in pH or temperature affected the activity of enzymes‚ specifically the enzyme sucrase. Enzymes are protein molecules that act as biological catalysts to increase the speed of the reaction or to lower the activation energy of that reaction. However‚ the activity of an enzyme can be affected by physical factors such as pH and temperature because these factors alter the structure of the enzyme (Freeman‚ 2011)
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Catalase Lab Introduction: Catalase is an enzyme normally found in many plant and animal tissues. Its purpose is to destroy toxic substances which may be introduced into cells. Also‚ some cells use catalase to destroy cellular debris or worn out organelles. In this lab‚ we will use a catalase solution from potatoes and determine the effect of temperature and pH on the action of this enzyme. The substrate of the enzyme will be 3% hydrogen peroxide (H2O2). Catalase works by the following mechanism:
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An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide. Plan Aim: To investigate the rate of the effect of Catalase on hydrogen peroxide. Introduction This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide. Enzymes are biological catalysts‚ which speed up the rate of reaction without being used up during the reaction‚ which take place in living organisms. They do this by
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and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm‚ a wavelength which is best for recording the absorbance values for the experiment. From the results‚ 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also‚ 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the
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the outcome of enzyme activity Introduction In this project I will monitor the rate of activity of Catalase. Catalase is an Enzyme which in the right conditions catalyses the decomposition of Hydrogen Peroxide into water and oxygen; 2H2O2 + Catalase >>> 2H2O + O2 Catalase is found in all cells and protects them from Hydrogen Peroxide which is a dangerous waste product that needs to be eliminated. Without Catalase living things could not survive. What are Enzymes? Enzymes are found in the
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The environmental factors that effected the rate of enzyme reactions were the enzyme concentration‚ pH‚ and temperature. These environmental factors help enzymes break down the poisonous chemicals into harmless substance. When we tested the liver with 2ml of hydrogen peroxide for a normal reaction it showed that it was exothermic. We added more hydrogen peroxide and the reaction rate of the liver was 3. We learned that the catalase is reusable because the liver reacted both times when we put in
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amylose coil.The amount of blue complex that starch gives with iodine can be measured by using a spectrophotometer. α-amylases are found in saliva‚ pancreatic juice‚ human breast milk‚ serum and certain tissues such as the liver. This enzyme catalyzes the hydrolysis of α (1-4) linkages in starch by breaking it down to maltose and some glucose. As the starch is broken down‚ the coiled structure of α-amylase is unfolded. Therefore‚ iodine will no longer be able to form the blue complex with the α-amylase
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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 phosphatase analyzed showed
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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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