The Purpose To test and analyze the effect of pH and temperature on the reaction rate of the enzyme catalase. HYPOTHESIS The more base you add to the liver the reaction will be faster The more heated the liver is the longer it will take the reaction to take place than if the liver is cold or at room temperature, MATERIALS 8 test tubes Safety goggles Test tube rack Water Ice Bunsen burner Liver Hydrogen Peroxide (H2O2) Hydrochloric acid (HCL) Sodium Hydroxide (NaOH) Liver(cut into small pieces) Test tube holder 2 beakers Pipette Stirring rods Paper Towels Beaker stand Method Gather all the material and put on the safety goggles. Place a 1 piece of liver in 6 test tubes. Add water to all the 4 test tubes. Then take 1 beaker and fill it with water, and then place it over it over the bunsen burner on the beaker stand. …show more content…
Label the test tubes with hot Using a test tube holder put the test tubes into the beakers. Place 2 test tubes with the hot label in the hot water and the other 2 with the cold label in the ice. Let the test tubes be in the beaker for 5 minutes. Take all the test tubes out of the beaker and drain the water. Then add 3 ml of hydrogen peroxide using a pipette to all the 4 test tubes. Rate the reaction from 1-5 after adding the H2O2 in the test tubes. Take 2 new test tubes and put 3 ml of H2O2 in them using a pipette. Then add 10 drops of HCL into the 2 test tubes and put the liver piece in RESULTS Trial 1 Trial
Catalase Activity on Substrate Based On Gas Pressure Production Rate Name of the Class Author’s Name Date Enzymes are organic compounds which act as catalysts and speed up biological reactions in biological organisms. They are not destroyed or changed during the reaction but rather they are used over and over again to catalyze many more reactions. Their activity may be affected and altered by factors such as temperature, substrate concentration, enzyme concentration and Ph.
After record your data and determine the absolute rate of the enzyme-catalyzed reaction. Based on the data and observations the hypothesis was accepted. It was accepted because when pH were changed to a variety of levels the transmittance began to get higher reaction rates. The increased absorbance means greater amount of product and a higher reaction rate will be produced.
Utilize a test tube brace to put the test tube containing the obscure strong in the bubbling water shower. Warmth until the greater part of the strong melts. Pour 140-160 mL of faucet water into a 250-mL graduated barrel. Record the volume to the closest 1 mL. Place a buret clasp on a help stand. Gather a calorimeter.
The addition of the extra catechol was supposed to have sped up the reaction with the enzyme and force the inhibitor out of the enzymes active site. If there was more time allowed to observe any possible color changes the results would have been more conclusive and our results more accurate. In other
Screw the liquid onto both test tubes to make sure that they are sealed. You now have to wait for approximately two days, in order to obtain satisfying results. Light the candle/put it on fire. Fill the third test tube with approximately two millimeters of Ethanol.
Lastly, the third graduated cylinder was labeled ‘V’ since it contained 440g of ascorbic acid also known as vitamin C. All three graduated cylinders were put in the 70℃ water bath after adding their own catalase alongside three test tubes of H2O2 for 30 seconds. After the specified period of time, the graduated cylinders were taken out of the bath and the H2O2 was added to each of them and that is when the timer started. The recordings were taken every 30 seconds for 90
1 “substrate” and another “ enzyme.” Instead of using the distilled water, this time you are going to use different pH buffer in the enzyme test tube. In the substrate tube, add 7 mL of distilled water, 0.3 mL of hydrogen peroxide, and 0.2 mL of guaiacol for a total volume of 7.5 mL. For the enzyme tube, instead of distilled water add the pH solution (3) and 1.5 mL of peroxidase which equals a total volume of 7.5 mL. Use the dH2O syringe for our pH solution. To clean the syringe, flush it by drawing 6 mL of distilled water.
Starch solution is then placed into the test tube at a quantity of 5 mL. 5 drops of Lugol’s Iodine solution is added to the test tube. If the color changes, then it is known that starches are present in the solution. Proteins are next tested. In order to do this, 5 mL of gelatin solution is added to the test tube. 10 drops of Biuret’s reagent are added to test for protein.
Move 10 ml of the fourth well to the fifth well. FIll the fifth well with 90 ml of dh20 to reach 100ml. Start with 1% solution for Fluoride 100 ml and move 10ml of the first well into the next. Fill the well with 90ml dh20 to reach 100ml. move 10 ml of the second well to the third well.
OEI: Method: 1. A beaker 100ml tripod 2. Thermometer inside water via retort stand 3.
Claim This lab was conducted to test the effect of adding hydrochloric acid (HCl) to the reaction between hydrogen peroxide (H2O2) and the enzyme catalase, which is and enzyme found in liver (NOAA Office of Response and Restoration). Our group first hypothesized that if 2 milliliters (mL) of hydrochloric acid was added to a mixture of 2 mL of liver extract and 2 mL of hydrogen peroxide, then the acid would intensify the reaction between the hydrogen peroxide and the catalase and cause increased bubbling. Hydrochloric acid is strong and highly acidic (Merriam-Webster), leading our group to believe that it would create more bubbling. However, since the evidence collected did not support this research, adding hydrochloric acid to the liver extract
Enzymes are catalysts in biological systems, that lower the activation energy, so that molecules can begin reacting with each other. Since enzymes have a very selective active site, if the enzyme shape is changed or denatured, it won’t allow the enzyme to bind. Catalytic enzymes break down the toxic hydrogen peroxide into water and oxygen gas. (Bryer) (Baker) The purpose of these labs were to see how different concentrations of pH, and hydrogen peroxide would affect the enzymes, catalase and
Do the same for the other test tubes. Let the test tubes not be disturbed for about 3- 4 mins. Then add the Amylase solution to the Starch solution and start the stopwatch (immediately). After every 1 min take one drop from the test tubes and place then in the test plate that were
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas