In the presence of the enzyme alcohol dehydrogenase, the rate of reduction of acetaldehyde to ethanol increases as you increase the concentration of the substrate, acetaldehyde. Eventually the rate of the reaction reaches a maximum, where further increases in the concentration of the substrate has no affect on the reaction rate. This kind of event is common to many enzymatic reactions.
Can you please explain in detail what is happening here, so I can better understand it?© BrainMass Inc. brainmass.com October 24, 2018, 8:54 pm ad1c9bdddf
Pretend you have only 1 molecule of enzyme (alcohol dehydrogenase, ADH) in a tube. You add a little bit of substrate (acetaldehyde). The enzyme will convert the acetaldehyde into ethanol as fast as it can. Now, repeat the experiment with a little bit more acetaldehyde in the tube. The 1 molecule of ADH present will do its best to convert the substrate into product. In so doing, the enzyme is getting more activity. We call this "enzyme activity." ...
Using the scientific method for testing the effects of acidic fluid on enzymatic activity
Design and carry out an experiment in which you will test the effects of acidic fluid on enzymatic activity.
1. What question are you asking? Clearly state your hypothesis. Describe your IV and DV.
2. Design your experiment. Provide a detailed account of the materials and methods used to conduct the experiment. Also include the methods for data collection and analysis.
3. Conduct the experiment and record your results. Make a data table that summarizes your findings. You could include what you observed - "which samples showed bubbling?
4. Use your knowledge about enzymes to interpret your results. It may be necessary for you to refer to your textbook. What effect does the acid have on the enzyme?
5. Was your hypothesis supported? What is your conclusion?