Part B: Practical Report The Effect of Temperature on Enzyme Activity Aim: To investigate how temperature effects the enzyme catalase. Hypothesis: If the temperature of water is increased then the enzyme will react quicker to form oxygen and water‚ when compared to cold water. Purpose: To design and conduct a plan of a practical about the effects of temperature on enzymatic activity with a partner. Introduction: An enzyme is a protein‚ which speeds up a specific chemical reaction without altering
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4 minutes‚ 6 minutes‚ and 8 minutes. After these enzyme samples were collected‚ we used a clean pipet tip to remove 500 microliters of the solution from the "Control" reaction tube and added it to the "End" cuvette. For the second portion of the lab‚ we labeled five cuvettes S1-S5 filled with 0‚ 12.5‚ 25‚ 50‚ and 100 nmol of p-Nitrophenol respectively. Then we used a calibrated spectrometer to record the absorbance of each of these cuvettes‚ the E1-E5 cuvettes from the first part of the experiment
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produced as a bi-product of some metabolic reactions. Hydrogen peroxide is a highly active chemical used in household products for bleaches and cleansing wounds. In a cell its build up would be highly toxic. However‚ liver cells contain an enzyme‚ catalase‚ which immediately breaks down hydrogen peroxide. It is a peroxidase and breaks up the toxic hydrogen peroxide to water and oxygen which are both nontoxic. The reaction is exothermic‚ meaning that energy is released in the form of heat. It is the
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Sang Kim Enzyme Catalyst Purpose/Problem: There are four parts to the Enzyme Catalyst lab - Activity A‚ B‚ C‚ and D. In activity A‚ the characteristics of enzyme actions will be observed. The main purposes are to determine the rate of an enzyme catalyzed reaction‚ to study the characteristics of an enzyme mediated reaction‚ and to observe the effect of heat on enzyme activity. The purpose of activity B is to use the Titration Protocol to determine the initial amount of H 2O2 present
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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 the hydrogen peroxide. We also tested another enzyme reaction for pH. In this test we learned that high pH equal high reaction rate. The 4 items tested were acetic acid (vinegar)‚ sodium
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200cm³ Liver Catalase Solution 100cm³ of following Buffer Solution – pH5 pH7 pH9 pH11 Method: The materials were collected. The test tube rack one with 4 test tubes had been labelled A to D. The 2cm³ of each buffer solution had been inserted to test tubes A to D. 3cm³ of hydrogen peroxided was introduced to the tubes then a few drops of detergent had been included to the tubes A to D. We then used test tube rack two with 4 test tubes and labelled them 1 to 4. The 2cm³ of catalase solution
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were; 4 °C‚ room temperature which was 22°C‚ body temperature which is 37°C‚ and 77°C. The total time of each trial was 2 and a half minute‚ 1 minute for the H2O2 to acclimatize to the temperature‚ 1 and a half minutes for the reaction to occur. Catalase causes Hydrogen Peroxide to break down into water and oxygen. Therefore the difference of enzyme rate reaction was determined by putting liver into hydrogen peroxide mixed with detergent and the oxygen. The detergent will capture this oxygen visualizing
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Date: Wednesday‚ November 16‚ 2011 Holly Lawson - white Title: API 20E Introduction: The general principle of the experiment is to use a battery of biochemical tests for identification of enteric bacteria. This testing system consists of a strip containing 20 chambers‚ each consisting of a microtube and a cupule to allow testing of 20 different tests nearly simultaneously. Materials: inoculating loop‚ test tube containing 5 ml of sterile saline‚ wash bottle of water‚ plastic API
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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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Effects of Temperature‚ pH‚ Boiling‚ 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
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