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What is the effect of mercury chloride on salivary amylase activity?
Mercury chloride is known to inhibit salivary amylase activity by binding to the enzyme and disrupting its function. This inhibition can lead to a reduction in the ability of the enzyme to break down starch into sugars in the mouth, affecting the initial stages of carbohydrate digestion.
What effect does EDTA have when added to a lactase meditated reaction?
EDTA removes the ions that lactase needs to function as an enzyme. If enough EDTA is added, lactase will no longer have any of it's ion cofactors to aid in the break down of lactose.
What is a question that can be answered using scientific method?
"What effect does temperature have on the rate of enzyme activity?"
Why does denaturing by temperature or pH make an enzyme non-functional?
Active site of an enzyme is fixed for particular substrate, or you can understand it better via lock-key theory, in which substrate acts as a lock and active side of the enzyme as a key, and you know well that each lock has a specific key to make it unlock. So if active site of an enzyme is altered due to any reason, it can not be fixed into the its particular substrate, and functioning of an enzyme obliviously requires a substrate.
How do you make urease solution?
To make a urease solution, simply dissolve urease enzyme powder in an appropriate buffer solution of your choice, such as phosphate buffer at the desired pH. The concentration of urease in the solution will depend on the specific experiment or assay you are conducting, so adjust the concentration as needed. Remember to keep the solution cold and handle the enzyme with care to maintain its activity.
What is the purpose of the extracellular enzyme experiment?
Extracellular enzyme is an enzyme that performs its role or function outside a cell. The purpose of experimenting extracellular enzyme is to know how can it affect our body when the bacteria secretes.
What switchs on enzyme activity while what can switch off or reduce enzyme activity?
Enzyme activators like cofactors or substrates can switch on enzyme activity by binding to the enzyme and promoting its function. Conversely, inhibitors can switch off or reduce enzyme activity by binding to the enzyme and preventing its normal function.
Which variable is the student's experiment described in the Prelab Activity designed to test?
The student's experiment in the Prelab Activity is designed to test the effect of changing the concentration of hydrogen peroxide on the rate of enzyme activity in the enzyme catalase. This involves manipulating the independent variable (concentration of hydrogen peroxide) to observe its impact on the dependent variable (rate of enzyme activity).
What are three that ways to control enzymes?
Temperature: Enzyme activity can be controlled by adjusting the temperature, as most enzymes have an optimal temperature at which they function best. pH: Enzyme activity is also influenced by the pH of the environment, and maintaining an appropriate pH level can help regulate enzyme function. Inhibitors: Enzyme activity can be inhibited by specific molecules that bind to the enzyme and prevent it from carrying out its catalytic function. This can be used as a way to control enzyme activity in biological systems.
Would lowering the pH of the enzyme solution affect the enzyme?
Yes, lowering the pH of the enzyme solution can affect the enzyme's activity. Enzymes have an optimal pH at which they function best, so altering the pH can disrupt the enzyme's structure and function, potentially leading to decreased activity or denaturation.
In a paper on the catalytic activity of an enzyme, in which section would you find detailed information on how the enzyme was prepared and handled in the experiment?
materials and methods
How does a noncompetitive enzyme inhibitor function to inhibit enzyme activity?
A noncompetitive enzyme inhibitor works by binding to the enzyme at a site other than the active site, causing a change in the enzyme's shape. This change makes it harder for the substrate to bind to the enzyme, reducing its activity.
In an experiment of Pepsin and BAPNA is pepsin the substrate?
No, pepsin is not the substrate in the experiment with BAPNA. BAPNA is the synthetic substrate used in this experiment to test the activity of the enzyme pepsin by measuring the rate of substrate cleavage. Pepsin acts on BAPNA as the enzyme, not the substrate.
How does an allosteric inhibitor function to regulate enzyme activity?
An allosteric inhibitor regulates enzyme activity by binding to a site on the enzyme that is different from the active site. This binding changes the enzyme's shape, making it less effective at catalyzing reactions.
What does copper(II) sulfate do to the enzyme activity?
Copper(II) sulfate is an inhibitor of enzyme activity. It can denature proteins by disrupting the secondary and tertiary structures of enzymes, leading to a loss of their function. Additionally, it can inhibit enzyme activity by interfering with the binding of substrates to the active site of the enzyme.
What is an example of a sentence using the word 'enzyme'?
"During this experiment, we will be looking to see the effects of heat on enxyme activity" "This stain remover contains an enzyme"
How does temperature change the action of enzymes?
Temperature can affect enzyme activity because enzymes work best within specific temperature ranges. At low temperatures, enzyme activity decreases as the molecules move more slowly, decreasing the likelihood of enzyme-substrate collisions. At high temperatures, enzyme activity can be disrupted because the enzyme structure can become denatured, leading to a loss of function. Optimal temperature for enzyme activity varies depending on the specific enzyme.
