Enzymes
...s will take place due to several more particles. The collisions speed up the reaction, resulting in more oxygen produced in the same amount of time, as opposed to a smaller amount of oxygen produced within a smaller amount of substrate. This exhibits a linear relationship, where the amount of oxygen produced by the enzyme increases as the volume of the substrate increases as well. Apparatus/Method: Figure 1.1 Observations: Figure 1.2: Comparing the Amount of Oxygen Produced with various Substrate Volumes Number of enzyme discs used: 3 Time Constant: 7 minutes Mass of each disc: 0.3grams Trial Substrate Volume:H202 (in mL) Oxygen Gas Produced (in mL) 1 1 Such little gas was produced that results were not conclusive. 2 2 N/A 3 3 1.3 4 4 2.1 5 5 2.5 Experimental Uncertainties: Figure 1.4 Manipulated Variable Controlled Variables - The amount of Substrate (hydrogen peroxide) - Time (7 minutes)- Mass and sizes of enzymes (0.9 grams)- # of enzymes (3 discs)- pH levels (in terms of acidic/basic substrates)- temperature- chemicals (salt concentration in the substrate) Conclusion: Since the oxygen gas produced from the enzyme increased as the substrate volume increased, approximately two moles of H202 will produce one mole of 02 when reacted with catalase. In reference to Figure 1.2, 3mL of H2O2 produced 1.3mL of O2 gas, and 4 mL H2O2 produced 2.1 mL of O2 gas, which is correct according to theory of moles. Extension Questions: à Enzymes are proteins that have complicated structures to suit it’s function. à a globular protein, which takes on a tertiary and quaternary structure is designed to keep the enzyme strong and operative due to the stability of the covalent bonds (disulfide bridges), and hydrogen bonds. àThese bonds allow the structure to become hydrophobic, non-polar which prevents the enzymes from being consumed in reactions with water à weak hydrogen bonds also allow the structure of the enzyme to change it’s shape for the substrate to fit in its designated location on the enzyme (the active site) àThe active site is the spot on the enzyme where the substrate attaches to the enzyme. The substrate attaches to the enzyme like a puzzle piece or like how a ‘lock and key’ fit (induced fit model). After the lock and key fitting, (enzyme substrate-complex) the disulfide bonds assist in stabilizing a tight fit for the substrate molecule onto the enzyme. à Collision theory (particles of substrate collide into enzymes) à Successful collisions are what speed up the reaction with the enzymes à Enzymes decrease the potential energy level of the transition state, which allows more collisions to take place so that the reactions can reach the transition state and become products more faster à Endergonic reactions have more energy in the products than the reactants while exergonic reactions have products with less energy than the reactants à Enzymes work to reduce the activation energy. Heat can increase the activation energy, which would be an exergonic reaction, but the enzymes reducing the activation energy makes the reaction endergonic. à 50 minutes à 200 minutes à 25 minutes a) àWhen temperature increases to a comfortable level for the enzymes (reacting with substrate), the particles in the substrate and enzymes collide with more force, which increases the rate and speed of the reaction. However, if the temperature is too high or low, the proteins can unravel, denature, and lose its function. à The amount of substrate also affects the rate of reaction. When more substrate can react with an enzyme, the enzy...