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TaigaStarch hydrolysis is fastest at an optimal enzyme concentration where substrate and enzyme are present in appropriate proportions for efficient catalysis. Below this concentration, the reaction rate will be slower due to limiting enzyme availability. Above this concentration, the reaction rate may decrease due to substrate saturation or enzyme inhibition.
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What is the independent variable between temperature and enzyme activity?
To find out how enzyme concentration affects the activity of the enzyme you must:vary the concentration of the enzyme, by preparing different concentrations (keeping the volume of solution the same)keep the temperature, substrate concentration and pH constantmeasure the activity of the enzyme at each concentrationHow the enzyme activity is measured will depend on the specific enzyme involved.You need to have plenty of substrate (excess substrate) so it doesn't run out during the experiment.In this type of experiment, the enzyme activity is the dependent variable, the temperature, pH and substrate concentration are control variables and the enzyme concentration is the independent variable.
What are the four factors that effect enzyme activity?
The four factors that affect enzyme activity are temperature, pH, substrate concentration, and the presence of inhibitors or activators. Temperature and pH can alter the enzyme's shape, while substrate concentration determines the rate of reaction. Inhibitors and activators can either decrease or increase enzyme activity, respectively.
What are 3 things that can alter enzyme activity?
1. Temperature. 2. P.H level. 3. Enzyme concentration
How does initial concentration of substrate effect enzyme activity?
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
What would be the likely outcome if you increased the concentration of substrate for an enzyme in the presence of a noncompetitive inhibitor?
Increasing the concentration of substrate will not overcome the effect of a noncompetitive inhibitor. The inhibitor binds to the enzyme at a site other than the active site, causing a conformational change that reduces the enzyme's activity. Therefore, increasing the concentration of substrate will not result in a significant increase in enzyme activity.
