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If amylase is attached to the amylase inhibitor, it will not break down starch. The inhibitor binds to the amylase enzyme, preventing it from catalyzing the hydrolysis of starch into simpler sugars.
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When the enzyme/inhibitor complex touches starch, there is no reaction that occurs between the complex and the starch. The amylase remains inhibited and cannot interact with the starch substrate to initiate breakdown.
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The presence of the amylase inhibitor affects the rate of the entire reaction by making it slower. The inhibitor reduces the availability of active amylase molecules, which decreases the overall rate of starch breakdown.
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If a couple of maltase molecules are added, they will not directly affect the reaction involving the starch and the amylase inhibitor, as maltase specifically acts on maltose (a disaccharide) rather than starch (which is a polysaccharide). Therefore, the presence of maltase would likely have no impact on the reaction's rate involving the amylase and starch. However, if the starch were to be broken down into maltose first (when amylase is functional), maltase could then help further break down maltose into glucose.
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)
1 answer