Enzyme Kinetics Experiment
Deney Föyü
19.11.2024
Dear students,
Please read the notes I have provided for the Result and Discussion section below very carefully.
For the Result Part
- Show all of your calculations (serial dilutions for 1 mM, 0.5 mM and 0.1 mM) with units in the result section (photos or handwritten are not permitted!).
- Plot the Product Concentration/Time Graph by choosing one of the substrate concentrations 0.1 mM, 1 mM or 0.5 mM to obtain the initial velocity. (I suggest you choose the absorbance value that will give the most meaningful result.) Also, you need to show how you got to the product concentration in this section. (Remember Beert Lamber Law as a hint.)
- II've attached the file you'll need for your report. You should use each concentration values to draw a
Lineweaver Burke plot. The Km and Vmax values from the equation you will get
should be determined, and you should add them to your report with their
respective units.
- When plotting a graph, remember to include the names of the axes, units, and graph.
For Discussion Part
- Discuss the data you obtained from the experiment.
- Explain why yellow color was observed after adding enzyme to substrate concentrations prepared in different amounts.
- Absorbance results were given to different groups at different concentration values. Explain why the absorbances values shown differences.
- Would you expect that the initial velocity for 0.1 mM would be higher or lower than the concentration value of 0.5 mM?
- If the substrate concentration is kept constant and different amounts of enzyme are added, will the initial velocity be the same?
- If an enzyme has a unit, explain what it is.
Does a change in the environment have an impact on the outcomes?
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