The purpose of this lab report was to test and measure the rate of substrate destruction by an enzyme, we tested the destruction of hydrogen peroxide by the enzyme catalase. Hydrogen peroxide is a poisonous by product of metabolism that can damage cells if it is not removed. Catalase is an enzyme that speeds up the breakdown of hydrogen peroxide into water and oxygen gas. H2O2 + catalase → H2O + O2
A catalyst is a substance that lowers the activation energy required for a chemical reaction, and therefore increases the rate of the reaction without being used up in the process. Catalase is an enzyme, a biological catalyst. Hydrogen peroxide is the substrate for catalase. Notes: 1.) One unit of pure catalase decomposes 1 ɥmole H2O2 per minute at 25°C at pH7. 2.) Assume that 1 mL of KMnO4 reacts with 1 mL of H2O2.
When the time is increased I believe that the amount of KMnO4 used will increase.
Part A: A visible change will occur when the catalase solution is added, another change will occur when it is boiled, then cooled and added to the solution. Part B: I predict that the amount of KMnO4 used will be approximately 5 mL, or less. Part C: I predict that for each time interval, it will use slightly more KMnO4, and therefore slightly less H2O2 Materials and Methods
The materials and methods we used were supplied by the teacher. Results
Part A: As the 1 mL of fresh catalase solution was added to the 10 mL of the 1.5% H2O2 solution bubbles formed. When we transferred the 1 mL of boiled and then cooled catalase extract to 10 mL of 1.5% H2O2 it became cloudy. Part B: It took 4.5 mL of KMnO4 to titrate the H2O2 in the solution. The readings for the amount of KMnO4 used in titration in are found in Table 1 Part C: Readings for the digestions and titrations for the samples at 10, 30, 60, 120, 180, and 360 seconds from are displayed in Table 1. The amount of peroxide used against time is displayed in...