The average results are all written down to one decimal place because although the stopwatch gives results to two decimal places it is impossible to get accurate times to two decimal places due to the fact that our reaction times are not fast enough to stop the stopwatch precisely. If you double the concentration of Hydrogen Peroxide then the rate of reaction doubles as well.
Average final volumes of oxygen for each concentration of hydrogen peroxide. Evaluation Overall, I believe my experiment went well and that I gained sufficient results because I repeated each concentration three times and investigated eight concentrations in total. I believe that my results were also relatively reliable because as the concentration decreased the volume of oxygen produced also decreased.
Also, most of the points were on or close to the curve of best fit for each concentration. However, there are some factors that I must take into consideration. Apparatus Limitations Firstly, there were limitations on the apparatus that I used.
Each piece of apparatus has an apparatus error with an upper and lower limit. This obviously affects the amount of catalase present, which means that there could be more or fewer collisions and resulting successful collisions between enzyme and substrate molecules depending on the greater or lower mass of yeast.
For example, if there were more molecules of yeast, the rate of reaction would increase because there would be more collisions between enzyme and substrate molecules.
This would result in a greater probability of successful collisions, and therefore more enzyme-substrate complexes being produced. This means that in my results, the volume of gas produced in the first 5 seconds may have been higher than it should have been if I had used exactly 0.
The same idea applies to the substrate concentration in that the pipettes also had an apparatus error. This means the amount of substrate could have been different for each repeat, even though I used the same concentration. So in cm3, the actual volume could have been either If there were fewer molecules of hydrogen peroxide, there would have been fewer collisions between molecules of enzyme and substrate, resulting in fewer enzyme-substrate complexes being made.
However, I do not believe the substrate concentrations were significantly different because my repeats were mostly concordant, so a similar amount of oxygen was produced which must mean that there was a similar number of substrate molecules in each concentration.
Choice of Method I tried to select the method I considered would be most accurate. I decided on the gas syringe method because, as I explained in my section on preliminary work, it measured the volume of gas directly and minimised the volume of oxygen which could potentially dissolve in water.
However, some oxygen was displaced in the gas syringe and I had to solve this by subtracting this small amount from the volumes produced in each of the reactions. Also, I noticed if the barrel was wet, the syringe often got stuck for a short time before it recorded the volumes of gas. To prevent this I had to dry out the barrel and syringe before commencing the procedure.
It was very hard to insert the small 5cm3 beaker into the conical flask, and when it came to tipping it over, some of the substrate was still trapped inside the beaker.
I solved this by swirling the conical flask constantly throughout the reactions, which seemed to solve the problem, although this meant that the amount of swirling had to be the same in order to ensure a fair test.
I tried to keep this constant by making sure I swirled the conical flask evenly. The accuracy of the results showed that this factor did not distort the results too much, and so a similar amount of substrate molecules were present in each reaction.
Another factor which was hard to measure was the volume of gas produced, because some of the higher concentration reactions were very fast, so it was hard to read the correct values every time.
I tried to make this as accurate as possible by keeping my eyes level with the gas syringe. Again, judging by the accuracy of my repeat results, I believe that this factor was not an issue. Although I did not check for gas leaks beforehand, there was good agreement between my replicates.
If my replicates had not been so close I would have had to change the tube.The Effect Of Substrate Concentration On The Activity Of The Enzyme Catalase A Level Biology Project Aims This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase.
The Effect of Substrate Concentration on the Activity of the Enzyme Catalase Words | 8 Pages. The Effect Of Substrate Concentration On The Activity Of The Enzyme Catalase A Level Biology Project Aims This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase.
(A) At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration. The catalytic site of the enzyme is empty, waiting for substrate to bind, for much of the time, and the rate at which product can be formed is limited by .
Investigating the effect of enzyme concentration on the rate of an enzyme-catalysed reaction. James Moore Conclusion: For the conclusion we see that in fact the hypothesis is correct. When independent variable increases so does the dependent variable.
As the amount of enzyme concentration increases so will the rate of the enzyme catalysed reaction. What Effects of Concentrations of An enzyme is described as a biological catalyst that speeds up the rate of a chemical reaction.
In order for an enzyme to perform its given job, it needs what is known as a substrate to bind to the active site of the enzyme so that the enzyme can speed up . Apr 30, · Investigate the effect of substrate concentration on the rate of activity of the enzyme catalase. Hypothesis I believe that as the concentration of the hydrogen peroxide (substrate) decreases, the rate of reaction will decrease as timberdesignmag.coms: 5.