The results for this experiment show that salt, while it might be beneficial in extremely small amounts relative to the amounts tested for other variables such as the enzyme and substrate in this experiment, actually slows down the rate of the reaction compared to a reaction without any addition of salt. The reason that this happened is because with the extreme amounts of salt added, the independent variable, especially in trial 2, it blocked the active sites of the enzymes, which is why the substrate, hydrogen peroxide, couldn’t follow the induced fit function and bind with the enzyme, catalase, which is why the reaction rate, the dependent variable, in the bigger picture slowed down. The results make sense in the light of the concept about salt concentrations affecting the binding of substrate to enzymes, and how they can affect the shape of the active site. If too little salt is added, then the side chains on the enzymes will be attracted to each other, which will result in denaturation of the side
The results for this experiment show that salt, while it might be beneficial in extremely small amounts relative to the amounts tested for other variables such as the enzyme and substrate in this experiment, actually slows down the rate of the reaction compared to a reaction without any addition of salt. The reason that this happened is because with the extreme amounts of salt added, the independent variable, especially in trial 2, it blocked the active sites of the enzymes, which is why the substrate, hydrogen peroxide, couldn’t follow the induced fit function and bind with the enzyme, catalase, which is why the reaction rate, the dependent variable, in the bigger picture slowed down. The results make sense in the light of the concept about salt concentrations affecting the binding of substrate to enzymes, and how they can affect the shape of the active site. If too little salt is added, then the side chains on the enzymes will be attracted to each other, which will result in denaturation of the side