Does Too Much Salt Affect The Reaction Rate
The hypothesis proposed that if a small amount of salt was added to the reaction, then it cause the rate of the reaction to speed up, but if too much salt was added, then it will instead decrease the rate of the reaction. The data revealed that no additional amount of salt was the reaction that had the highest rate. As shown previously in the data table, the first trial’s average reaction rate of 4.5 mL/min was higher than the other two reaction rates where salt was added for trial 2 and trial3, 2.125 mL/min and 3.5 mL/min, respectively. There was some support for the prediction. Our prediction included the point that if too much salt was added, then the reaction rate would slow down, which is what is demonstrated by the second trial, with 5 mL of salt water. The data revealed that the average rate of reaction for
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the second trial, or the one that had the additional 5 mL of salt, was 2.125 mL/min, while the average rate of reaction for the third trial, or the one that had the additional 2.5 mL of salt, was 3.5 mL/min. These data findings are significant because it demonstrates how if too little or too little salt was added, then the reaction rate would slow down.
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
chains. If too much salt is added, there will be too much concentration of it, which will result in the blockage of the active site on many of the enzymes present in the reaction. The confounding variable about the accuracy of the quantity of substrate, salt, or enzyme put into the glass tube could have affected the reaction rate and the results of the reaction. If too much or too little, essentially not the exact quantity noted down, was placed into the glass tube, due to some residue remaining in within the beakers used to contain these materials, then the reaction could have been affected by that, either slowing or increasing the reaction rate. In addition, another confounding variable such as air bubbles escaping from the dropper into the bin of water could have resulted in some oxygen being lost to the surroundings, and not going directly into the graduated cylinder, which would have messed up the results about the amounts of oxygen displaced or produced. The concept of the factors that can affect an enzymatic reaction is demonstrated when producing vaccinations or producing new treatments for medical conditions or diseases. This concept of enzymes being affected by various factors is important because it helps scientists and doctors all around the world imitate bodily conditions in labs in order to test out new drugs in other ethical methods instead of the testing them on subjects, or human experimental units, in order to advance research in a particular disease or condition. Additional research questions such as how much quantity of salt is the perfect amount to have the highest rate of reaction for this particular experiment may synthesize a mathematical or generalized formula that can relate to other enzymatic reactions, in order to learn more about enzymes and how they react with substrates in specific microenvironments.
the second trial, or the one that had the additional 5 mL of salt, was 2.125 mL/min, while the average rate of reaction for the third trial, or the one that had the additional 2.5 mL of salt, was 3.5 mL/min. These data findings are significant because it demonstrates how if too little or too little salt was added, then the reaction rate would slow down.
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
chains. If too much salt is added, there will be too much concentration of it, which will result in the blockage of the active site on many of the enzymes present in the reaction. The confounding variable about the accuracy of the quantity of substrate, salt, or enzyme put into the glass tube could have affected the reaction rate and the results of the reaction. If too much or too little, essentially not the exact quantity noted down, was placed into the glass tube, due to some residue remaining in within the beakers used to contain these materials, then the reaction could have been affected by that, either slowing or increasing the reaction rate. In addition, another confounding variable such as air bubbles escaping from the dropper into the bin of water could have resulted in some oxygen being lost to the surroundings, and not going directly into the graduated cylinder, which would have messed up the results about the amounts of oxygen displaced or produced. The concept of the factors that can affect an enzymatic reaction is demonstrated when producing vaccinations or producing new treatments for medical conditions or diseases. This concept of enzymes being affected by various factors is important because it helps scientists and doctors all around the world imitate bodily conditions in labs in order to test out new drugs in other ethical methods instead of the testing them on subjects, or human experimental units, in order to advance research in a particular disease or condition. Additional research questions such as how much quantity of salt is the perfect amount to have the highest rate of reaction for this particular experiment may synthesize a mathematical or generalized formula that can relate to other enzymatic reactions, in order to learn more about enzymes and how they react with substrates in specific microenvironments.