Drag the molecules to the correct place on the graphic. (Hint: Use the Key on the simulation)(1 point)

Question

Drop target 1
Drop target 2
Drop target 3
Question 2
Identify the following in the reaction shown above:(1 point)
Substrate Starch
Product
Enzyme


Question 3
Identify the following in the reaction shown above:(1 point)
Substrate
Product
Enzyme Maltase


Set the following settings on the Simulation.
Starch: 3

Amylase: 0

Temp: 35

Maltose: 0

Maltase: 3

pH: 7

Glucose: 0

Amylase Inhibitor: 0

Question 4
What did you observe?(1 point)
Responses

Starch was denatured
Starch was denatured

Starch was not broken down by the maltose enzyme
Starch was not broken down by the maltose enzyme

Glucose was present
Glucose was present

Starch was broken down by the maltose enzyme
Starch was broken down by the maltose enzyme
Hit the reset button and then set the following settings on the Simulation.
Starch: 3

Amylase: 2

Temp: 35

Maltose: 0

Maltase: 0

pH: 7

Glucose: 0

Amylase Inhibitor: 0

Question 5
Which of the following did you observe?(1 point)
Responses

Amylase did not have a reaction with starch.
Amylase did not have a reaction with starch.

Amylase reacted with starch to create glucose molecules
Amylase reacted with starch to create glucose molecules

Amylase reacted with starch to create maltose molecules
Amylase reacted with starch to create maltose molecules
Question 6
After those two simulations, what is a logical conclusion you can reach?(1 point)
Responses

Any enzyme will break down any molecule
Any enzyme will break down any molecule

Some enzymes can break down more than one substrate
Some enzymes can break down more than one substrate

Enzymes are specific to a substrate
Enzymes are specific to a substrate
Question 7
What did you observe when amylase and starch touched during the simulation? (You may need to run it a few times to catch it)(1 point)
Responses

Nothing, starch remained the same.
Nothing, starch remained the same.

Starch was broken down to glucose
Starch was broken down to glucose

Starch was broken down to maltose
Starch was broken down to maltose

Starch was broken down to glucose then, maltose.

Answer 1

Here are the suggested answers to your questions based on the simulation and biological principles:

Question 1: (Drag molecules to the graphic) Since you have not provided the graphic, I'm unable to specify which molecules to drag to which spaces. However, typically you would drag the substrate (starch), the product (maltose or glucose), and the enzyme (amylase or maltase) to the corresponding places according to the simulation's key.

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Question 2: Identify the following in the reaction shown above:

• Substrate: Starch
• Product: Maltose (assuming maltose is the product formed from starch breakdown)
• Enzyme: Amylase (if amylase is the enzyme acting on starch)

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Question 3: Identify the following in the reaction shown above:

• Substrate: Maltose
• Product: Glucose (as maltase breaks down maltose into glucose)
• Enzyme: Maltase

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Question 4: What did you observe?

• Starch was not broken down by the maltose enzyme This is correct since maltase specifically breaks down maltose, not starch.

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Question 5: Which of the following did you observe?

• Amylase reacted with starch to create glucose molecules If the simulation showed that amylase converts starch into glucose, then this is accurate.

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Question 6: After those two simulations, what is a logical conclusion you can reach?

• Enzymes are specific to a substrate This is a key concept in biochemistry where enzymes generally work on specific substrates.

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Question 7: What did you observe when amylase and starch touched during the simulation?

• Starch was broken down to glucose then, maltose. If amylase acted on starch, the logical pathway would then yield glucose molecules following the breakdown process.

Feel free to adjust based on specific details from your simulation if needed!

Answer 2

Hit the reset button and then set the following settings on the Simulation.
Starch: 3

Amylase: 2

Temp: 35

Maltose: 0

Maltase: 2

pH: 7

Glucose: 0

Amylase Inhibitor: 0

Question 8
After letting the simulation run for about a minute, answer whether something true or falsethat happened during this simulation. (1 point)
True False
All starch was converted into maltose and then glucose.

When maltose touched amylase it was turned back into starch.

The end result was enzymes bouncing around with only maltose molecules.

Only glucose and enzymes were present at the end.

Hit the reset button and then set the following settings on the Simulation.
Starch: 0

Amylase: 5

Temp: 35

Maltose: 0

Maltase: 0

pH: 7

Glucose: 0

Amylase Inhibitor: 0

Question 9
For this question, you will need to adjust the pH until all of the enzymes are denatured. At what pH does all of the amylase become denatured? You must reset the simulation many times as you adjust the pH only. Make the solution more basic and more acidic until all of the enzymes are denatured. (1 point)
Responses

6.0 and 7.5
6.0 and 7.5

5.5 and 7.5
5.5 and 7.5

5.5 and 8.5
5.5 and 8.5

6.5 and 7.5

Answer 3

Here are the suggested answers for Questions 8 and 9 based on your simulation setup and general knowledge about enzyme behavior:

Question 8

After letting the simulation run for about a minute, answer whether the following statements are true or false:

1. All starch was converted into maltose and then glucose.

   • True (If there was sufficient amylase for starch breakdown)

2. When maltose touched amylase it was turned back into starch.

   • False (Amylase does not convert maltose back into starch; it only breaks down starch)

3. The end result was enzymes bouncing around with only maltose molecules.

   • False (If amylase is working, you would expect to see glucose as well as maltose)

4. Only glucose and enzymes were present at the end.

   • False (If starch is not fully converted, and maltose might be present as a product along with glucose)

Question 9

For this question, to determine the pH at which all of the amylase becomes denatured, you would typically need to know the optimal pH range for amylase activity, which is generally around 6.7 to 7.0 for salivary amylase. Based on common specific values:

• 6.0 and 7.5 - Likely not correct since these may not completely denature the enzyme.
• 5.5 and 7.5 - This is a feasible choice; pH levels below 6 can start denaturing amylase.
• 5.5 and 8.5 - Unlikely, since 8.5 is basic and would typically not denature unless it's highly extreme.
• 6.5 and 7.5 - This is also plausible because while 6.5 is still near optimal, moving towards 7.5 can begin to affect enzyme activity.

From typical biological concepts, the best guesses would be 5.5 and 7.5, as they are more likely ranges for denaturation of amylase enzymes based on pH.

If you find after testing that denaturation occurs below pH 6.0, that would confirm this as the correct selection. Please do the simulation to confirm your hypothesis based on this guidance.

Answer 4

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?

(4 points)
0 / 10000 Word Limit
Question 11
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 (1 point)? (3 points)

Answer 5

Here are suggested observations and responses for Questions 10 and 11 based on your simulation settings:

Question 10 Observations

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 be inhibited from breaking down starch. The inhibitor effectively prevents the enzyme from catalyzing the reaction.

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

   • The enzyme/inhibitor complex cannot catalyze the breakdown of starch. Instead, the inhibitor remains bound to the enzyme, preventing it from interacting with the starch substrate. The starch remains unchanged.

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 causes the reaction to proceed slower or may completely halt it because it prevents the enzyme from functioning properly.

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

   • Adding maltase molecules would not affect the breakdown of starch since maltase specifically catalyzes the conversion of maltose into glucose. Starch would still remain unchanged because maltase does not act on starch directly. However, if some maltose were produced before the inhibitor was introduced, maltase could break it down into glucose.

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Question 11: Temperature Adjustments

• What happens when you increase the temperature?

  • When you increase the temperature, the reaction initially may speed up due to increased kinetic energy, which can enhance enzyme activity. However, if the temperature is raised beyond the enzyme's optimal range, it can lead to denaturation, where the enzyme loses its functional shape and activity.

• What happens if you decrease the temperature?

  • When you decrease the temperature, the reaction rate typically slows down because the kinetic energy of the molecules is reduced. This means that molecular collisions are less frequent, and enzyme activity may significantly decrease.

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

  • Yes, enzymes can become denatured with temperature changes. Most enzymes, including amylase, begin to denature at temperatures above approximately 40-50°C (104-122°F). Similarly, if the temperature decreases significantly (below approximately 0°C or freezer temperatures), the enzyme activity can be drastically reduced or cease, but it does not typically denature in the same way as a high temperature would.

These observations and conclusions should comprehensively answer the questions based on your simulation setup. Adjust them as needed based on specific details from your experiment!

Answer 6

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?

(4 points)

Answer 7

Certainly! Here’s a detailed response for Question 10 based on the simulation settings you provided:

Question 10 Observations

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

   • No, the amylase will not break down starch if it is attached to the amylase inhibitor. The inhibitor binds to the amylase enzyme and prevents it from interacting with starch, thus inhibiting its catalytic activity.

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

   • When the enzyme/inhibitor complex touches starch, nothing happens to the starch. The complex remains intact with the inhibitor bound to the amylase, and starch is unable to be broken down because the enzyme is inactive in its inhibited state.

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 causes the rate of the reaction to be slower. Since the inhibitor prevents amylase from catalyzing the breakdown of starch, the reaction halts or proceeds at a significantly reduced rate compared to an environment without the inhibitor.

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

   • Adding a couple of maltase molecules would not directly affect the breakdown of starch, as maltase specifically catalyzes the conversion of maltose into glucose. Since there is no maltose present (as starch is not being broken down due to amylase inhibition), the maltase will remain unused. However, if maltose were generated through a previous reaction, maltase could then act on it to produce glucose.

These observations capture the relationships between the substrates, enzymes, and inhibitors in your simulation and clearly address the required points. Adjust any details as necessary based on your specific observations during the simulation!

Answer 8

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 (1 point)? (3 points)

Answer 9

Here are the observations and answers for the effects of temperature adjustments in your simulation:

Temperature Adjustments

1. What happens when you increase the temperature?

   • When you increase the temperature, the reaction rate initially tends to increase due to higher kinetic energy, which causes more frequent collisions between the enzyme (amylase) and substrate (starch). However, if the temperature exceeds the optimal range for amylase (approximately 35-40°C), the enzyme may begin to denature, leading to a loss of its functional shape and activity.

2. What happens if you decrease the temperature?

   • When you decrease the temperature, the reaction rate slows down significantly. The reduced kinetic energy means that molecular collisions are less frequent, leading to lower enzyme activity. At very low temperatures, enzyme activity may become negligible, and the reaction may come to a halt.

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

   • Yes, amylase can become denatured with temperature. Generally, enzymes like amylase begin to denature at temperatures above approximately 50°C (122°F). At this point, the enzyme's structure is altered enough that it may no longer catalyze reactions effectively. Conversely, extremely low temperatures (below approximately 0°C) do not cause denaturation in the same way; rather, they lead to decreased activity.

Summary:

• Increasing Temperature: Initially faster reaction rates, but can lead to denaturation above 50°C.
• Decreasing Temperature: Slower reaction rates and potentially negligible activity at very low temperatures.
• Denaturation Temperature: Amylase begins to denature above approximately 50°C.

Feel free to adapt these observations based on the specific behavior you noticed in your simulation!