These rates are actually the slopes of the lines that were graphed during each reaction. The trend of data showed that the enzyme-catcalled reaction rates gradually decreased as the amount of substrate decreased. MATERIALS AND METHODS Materials: 2- 10 ml Graduated cylinders 1 pipette 5 to 10 medium sized test tubes 10 drops of cold Chicken liver (Enzyme Catalyst (Peroxides)) 25 ml of buffer (H2O) 25 ml of substrate (H2O) Cold bath Labor Equipment Changing Concentration Methods: Set-up Labor equipment. Place the chicken liver enzyme into a cold bath to maintain a cold temperature.
In separate graduated cylinders, measure out ml of substrate and mi of buffer and pour both into a test tube. Add 2 drops of catalyst. Cap immediately with Labor stopper, and start the computer measurement program. Stop recording once the stopper pops off. Using the software, find the slope of the line, which will represent the reaction rate. Print the graph for your records. Repeat steps 3 and 4, increasing the substrate by 1 ml and decreasing the buffer by 1 ml, keeping the total volume at ml. Do this until you reach ml of substrate and Mol of buffer. See data table) Compare reaction rates using the different slopes from the varying concentrations. RESULTS DATA TABLE Substrate (H2O) Buffer Enzyme Catalyst (Peroxides) Reaction Rate (Slope) ml Mol 2 drops 0. 663 kappa/s ml Mil 0. 545 kappa/s mm I ml 0. 429 kappa/s ml 0. 295 kappa/s 0. 208 kappa/s The table above shows the results of our experiment where we investigated what would happen to the rate of an enzyme-catcalled reaction if we varied the amount of substrate. Our table shows the 5 different amounts of substrate that e used in combination with the buffer and the amount of enzyme used.
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The volume of the combination always totaled 6 ml. The results of our experiment can be found by comparing the reaction rates for each trial. These rates are actually the slopes of the lines that were graphed during each reaction (See graphs). As is shown in the table, the rates gradually decreased as the amount of DISCUSSION Our research question evolved into, Los there a relationship between the amount of substrate and the rate of an enzyme-catcalled Since the results showed a decrease in rate as the amount if substrate decreased we can include that there is a relationship between the two.
In other words, a higher concentration of substrate will yield an increase in the rate of the reaction. Since this reaction was between an enzyme, peroxides, and a substrate some generalizations can be made. When an enzyme catalysts a reaction a definite effect can be noted. The catalyst increases the rate of the reaction. In this case the catalyst was the chicken liver, which contained the enzyme peroxides. Since an enzyme is involved, the reaction rate is increased. Every reaction has an activation energy, which is the amount of energy needed to make the reaction happen.
Molecules with higher kinetic energy can match the activation energy and actually proceed with the reaction, but not all molecules have enough energy to do this. The enzyme lowers the activation energy required for the reaction by allowing the molecules to take its path as an alternate because it has a lower activation energy. If the reaction has a lower activation energy then more molecules will be able to have enough kinetic energy to proceed with the reaction. What happened during our experiment is that we kept the mount or concentration of catalyst constant and varied the concentration of the substrate.
Our results showed that the reaction rate and concentration of substrate are proportional. Why this happens is interesting. A reaction is the change of the substrate into a new and different thing, called the product. The collision theory states that reactions happen as molecules collide, but they must collide at the correct orientation so that the activation sites on the molecules will match up. If you can increase the number of molecules in a reaction, you will also increase the chances of having the molecules collide.
When we increased the concentration of substrate we increased the number of molecules, and thereby increasing the chances of the molecules colliding. So increasing the concentration of the substrate increased the rate of the reaction. Our results are based on theory, as stated above, and experimental evidence. Our evidence was not without flaws. [email protected] Plan was to take four trials of every different concentration of substrate (see table). We had a difficult time manipulating the equipment and knew so when we kept getting drastically efferent data for the same concentration.
We disregarded this data, realizing that the temperature of the enzyme had to be stabilized. Once we regulated this and got a handle on the equipment our data began to make more sense. Unfortunately, the amount of time we spent working out these problems was time away from our data collection. We were not able to take multiple samples like we planned. This always makes the data less reliable because we only have one trial for each concentration on which to base our conclusions. Graphs provide us with proof that there was some error in our data collection ethos.