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ph effects on enzyme activity
introduction to effects on temperature on enzyme activity
introduction to effects on temperature on enzyme activity
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What pH the Enzyme Named Peroxidase Works Best At The aim of my investigation is to find out what pH the enzyme named peroxidase works best at. We can find the enzyme peroxidase if we grind up celery, or most other animal and plants. A chemical reaction in plants and animals produce hydrogen peroxide, this can poison them if it is allowed to accumulate. The enzyme peroxidase acts as a catalyst for decomposing hydrogen peroxide, it is broken down into water and oxygen. The reaction is: 2H20 = 2H20 + O2 (Aq) (L) (G) I plan to measure the amount of oxygen given off by the celery at different pHs and whichever pH helps the enzyme produce the most oxygen. Before I do this I must do a preliminary plan to see what my other variables should be so that I can get the best results. I predict that the optimum pH will be around 7 because if it goes any lower or higher than this it could change the enzymes shape and/or charge properties of the substrate so that either the substrate cannot bind to the active site or it cannot undergo catalysis. Different enzymes have different optimum pHs and it is hard to say what it will be because some enzymes work best at low temperatures and others at high temperature. As you can see from the graph the two different enzymes, represented by red and green lines, have a different optimum pH. When the pH is altered is will become denatured or it may be optimum it depends on what is the best pH that the enzyme responds to. I believe it will be 7 because this is in the middle, 7 isn’t too high or too low but it could be wrong depending on the enzyme. I think it is pH7 because this is ... ... middle of paper ... ...yme more. I would also try and get the celery to be the same age because my experiments over two days with two different celeries, which could have had an effect and gave odd results. The odd results could of came from anything though, we could of measured slightly wrong, measured the solutions wrong, or when we did measure the solutions there could have been leftover acid in the syringes. I was able to get sensible results in the end after redoing the tests that had odd results. But overall I successfully carried out my investigation fairly and accurately. My experiment was good because I have measured all my solutions accurate, added the solutions together in the same order, timed my experiment to the best of my ability, I have kept the temperature the same and I have produced an experiment that is fair and accurate.
For example, incubating the samples at different temperatures would create more data points to establish an optimal temperature. From the results in the experiment in this study, it is known as temperature increases, enzymatic activity increase, and vise versa. However, what can not be observed is at what point does the increase in temperature begin to denature the enzyme, above 60°C. Furthermore, assays can be preformed to determine optimal pH, as well. From Dutta’s, and his partners, experiment it shows that there is a range where the Heliodiaptomus viduus’s lactase shows the most activity, which is between 5.0 and 6.0
a fair test, the free enzyme must be diluted to the same extent as the
The purpose of conducting an experiment using various temperatures, pH levels, and enzyme concentrations was to observe the effects these factors had on the rate of horseradish peroxidase activity. Furthermore, testing how peroxidase reacts to different set ambient conditions and finding the conditions that allow for maximum rates. Enzymes are used in this experiment to demonstrate the importance of certain environmental conditions since they affect the speed of an enzymatic reaction in order to carry out life. An extract from horseradish is used as the enzyme since it contains peroxidase which has a highly accessible active site. The experiment was administered by using a spectrometer as a tool to measure oxygen production using an indicator called guaiacol which would allow the rate of horseradish peroxidase activity to be seen. Environmental circumstances, such as enzyme concentration, temperature, and pH, are tested by using guaiacol as an indicator of oxygen production and H2O2 as an oxygen producing agent. The ending results conclude that higher enzyme concentration can increase the speed of the rate of enzyme activity. The results also conclude
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
The Effect of Temperature on the Action of Peroxidase Enzyme Aim To find the effect of temperature on an enzyme in this case peroxidase, by studying it decomposing hydrogen peroxide. Planning I am measuring the amount of gas given off in the reaction. By collecting this figure I can determine the rate of reaction. If I know the rate of reaction I can find out what temperature peroxidase works best at. Equipment · Trough · Clamp · 100ml measuring cylinder · Stop clock · 10ml measuring cylinder · Delivery tubes · Bung · Conical flask Variables Change
My results did not completely support my hypothesis, while I was correct about pH, temperature, enzyme concentration and inhibitors I was incorrect about substrate concentration. I originally believed that increasing substrate concentration
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
In this experiment, in the first part, the best concentration of enzyme was determined by recording the absorption over time. In the second part, the best concentration was selected from the previous experiment which was C and the optimum pH was determined.
The Effect of a Catalase on the Breakdown of Hydrogen Peroxide Aim To follow the progress of a catalysed reaction by measuring the volume of gas produced as the reaction proceeds. Using the initial rates of a series of experiments I will be able to find the orders of the reaction with respect to enzyme and substrate. Also to find out if concentration has an effect on the reaction when an enzyme is used to accelerate the breakdown of hydrogen peroxide.
2) A small amount is required as the enzyme is used again and again as
Moreover, the class average curve shows a similar trend, as the curve flattens, at 70% but with an enzyme activity of 5.3 x10-3 seconds. This indicates that even though the saturation point is the same it was considerably lower than our results, which could indicate sources of systematic error in the design of the practical.
I must use the same amount of enzyme each time I do an experiment so I
From looking at the results I can conclude that when the pH was 3 and
The pH of the solution would alter the rate of the reaction if it was