Arş. Gör. Yeliz GÜLDORUM

Dear students,  

Click to access lecture notes and related documents. If you have any questions about course, please send an email to yelize@yildiz.edu.tr

I wish you a successful term.

Dear students,

 Please read the notes I have provided for the Result and Discussion section below very carefully.

Each section will submit their laboratory reports in their own section; otherwise, late reports will not be accepted and will not be evaluated.

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?

• Does a change in the environment have an impact on the outcomes?