Set the following settings on the Simulation. Starch: 2 Amylase: 2 Temp: 35 Maltose: 0 Maltase: 0 pH: 7 Glucose: 0 Amylase Inhibitor: 5 Question 10 During this simulation, write what you observe. Make sure to include the following as they are worth one point each. 1. If amylase is attached to the amylase inhibitor, will it break down starch? 2. What happens to the enzyme/inhibitor complex when it touches starch? 3. How does the presence of the amylase inhibitor affect the rate of the entire reaction? (Faster or Slower) 4. What would happen if you add a couple of maltase molecules?

Answer 1

During the simulation with the specified settings, here are the observations and responses to the questions:

1. If amylase is attached to the amylase inhibitor, will it break down starch?

   • No, if amylase is bound to the amylase inhibitor, it will not be able to break down starch. The inhibitor prevents the enzyme from functioning properly.

2. What happens to the enzyme/inhibitor complex when it touches starch?

   • When the enzyme/inhibitor complex touches starch, the complex remains inactive. The presence of the inhibitor prevents the amylase from interacting with the starch substrate, so no breakdown occurs.

3. How does the presence of the amylase inhibitor affect the rate of the entire reaction? (Faster or Slower)

   • The presence of the amylase inhibitor slows down the rate of the entire reaction. Since amylase is inhibited, it cannot effectively catalyze the breakdown of starch into smaller sugar units.

4. What would happen if you add a couple of maltase molecules?

   • Adding a couple of maltase molecules would not significantly change the outcome in this scenario because maltase specifically catalyzes the hydrolysis of maltose into glucose. Since there is no maltose present in the simulation, the addition of maltase molecules will not lead to any reactions or product formation until maltose is available. Hence, they would remain inactive until maltose is produced from the starch breakdown (which is inhibited in this case).

Answer 2

rewrite as a freshman and shorter

Answer 3

During the simulation with the following settings, here are my observations:

1. If amylase is attached to the amylase inhibitor, will it break down starch?

   • No, amylase cannot break down starch if it's attached to the inhibitor.

2. What happens to the enzyme/inhibitor complex when it touches starch?

   • The complex stays inactive and can't do anything with the starch.

3. How does the presence of the amylase inhibitor affect the rate of the entire reaction? (Faster or Slower)

   • The reaction is slower because the inhibitor stops amylase from working.

4. What would happen if you add a couple of maltase molecules?

   • Adding maltase wouldn’t help since there's no maltose to break down, so it would just remain inactive.

Answer 4

Now, adjust the temperature. What happens when you increase the temperature (1 point)? What happens if you decrease the temperature (1 point)? Do either of the enzymes become denatured with temperature? If so, at what temperatures

Answer 5

When adjusting the temperature in the simulation:

1. What happens when you increase the temperature?

   • When you increase the temperature, the reaction rate generally increases up to a certain point, as the molecules move faster and interact more frequently. However, if the temperature gets too high, the enzymes can become denatured, losing their shape and function.

2. What happens if you decrease the temperature?

   • If you decrease the temperature, the reaction rate slows down because the molecules move less and collide less frequently. Enzyme activity decreases significantly at lower temperatures.

3. Do either of the enzymes become denatured with temperature? If so, at what temperatures?

   • Yes, enzymes can become denatured with extreme temperatures. For most enzymes, denaturation typically occurs at temperatures above 50-60°C (122-140°F). For this simulation, if the temperature is increased beyond this range, the enzymes could lose their activity. Conversely, lowering the temperature too much (often below 0°C) can also inhibit enzyme function, but it typically does not cause denaturation; instead, it may just slow down the reaction.

Answer 6

in one paragraph as a freshmen and shorter

Answer 7

When you increase the temperature, the reaction rate usually speeds up because molecules move faster, but if it gets too hot (above 50-60°C), the enzymes can become denatured and stop working. On the other hand, decreasing the temperature slows down the reaction because molecules move less and collide less often. While low temperatures may not denature enzymes, they can significantly reduce their activity. So, extreme temperatures, either too high or too low, negatively affect how enzymes function.