Hey guys!
I did an experiment the other day and we had catalase in multiple test tube. We then proceeded to change the temperatures of each test tube. One was 0 degree, 20 degrease, 40 degrease, 60 degrease, 80 degrease and 100 degrease. After this we inserted hydrogen peroxide into each test tube and observed how much oxygen was produced.
I have some questions about this experiment:
1. Was the control the beaker that was heated to the enzymes optimum temperature?
2. Is denaturing is caused by the breaking of hydrogen bonds in terms of heat.
3. What are some limitations of this experiment?
4. Was anything besides heat effecting enzyme function?
5. Was the bubbles caused by oxygen being produced?
Thanks guys
