(Reference the images below from the lab to answer the following questions) QUES
ID: 50330 • Letter: #
Question
(Reference the images below from the lab to answer the following questions)
QUESTION 1
In experiment 1 what color did the negative control turn when tested with IKI?
dark purple
blue/black
it did not change
pale pink
10 points
QUESTION 2
In a test tube, I added 1ml of starch and 20ml of amylase solution. After two hours, I added IKI. What happened?
the solution turned dark purple when IKI was added
the solution turned blue/black when IKI was added
the solution stayed the same color as the IKI dye when it was added
the solution turned pale pink when the IKI was added
10 points
QUESTION 3
Which of these molecules is LEAST likely to be an enzyme?
catalase
amylase
lactase
glycogen
10 points
QUESTION 4
Based on your data from experiment 2, which balloon had the largest diameter?
cold
room temperature
hot
all were the same
10 points
QUESTION 5
When I was a child, a common treatment for small cuts was to pour hydrogen peroxide on the cut, which would kill any bacteria (and hurt like crazy!). However, I noticed that the solution always bubbled when it was added to the cut, what was causing this?
the bacteria were dying and releasing oxygen
there were yeast in the cut releasing catalase in gaseous form
the hydrogen peroxide was breaking down into water and oxygen gas
the blood from the cut was boiling
10 points
QUESTION 6
A student in this course was interested in expanding her results from experiment 2 and she added a test tube in boiling water. She found that the balloon did not inflate at all. Why was this the case?
the enzyme is denatured by the high temperatures
the boiling of the water removed oxygen from the balloon
the boiling water reduced the atmospheric pressure around the balloon
hydrogen peroxide is boiled into a gas at high temperatures
10 points
QUESTION 7
Which of the following does not directly influence rate of a reaction?
pH
temperature
toxicity of the product
substrate concentration
10 points
QUESTION 8
A researcher decides to speed up the rate of his enzyme-catalayzed reaction so he adds more and more substrate. He sets up a series of test tubes and first adds 2ml of enzyme to each one. He then adds substrate as follows: He has one tube with 5ml of substrate, one with 10ml, one with 20 ml, one with 40ml and one with 80 ml. His results show that the product is formed more quickly from 5-10-20ml of substrate, but does not go any faster with 40 or 80ml than it did at 20ml. What is happening?
He needs to add more substrate to see a faster response
He needs to be more accurate in checking his product, as his results are clearly an error
He has reached the limit of how fast that amount of enzyme can act, regardless of how much more substrate is added
He forgot to add the product to each tube
10 points
QUESTION 9
The active sites of enzymes bind which of the following?
coenzymes
cofactors
substrates
regulators
10 points
QUESTION 10
I have found a digestive enzyme whose optimum pH is 2. Where in the body is this enyzme most likely to function?
stomach
mouth
small intestine
pancreas
dark purple
blue/black
it did not change
pale pink
Lab 9: Enzymes Concepts to explore: Enzymes -Selectivity . Activators Inhibitors Catalysts . Activation energy .Activation site -Reaction rates Enzymes are specialized proteins that serve as biological catalysts to decrease the activation enerB normally needed for a reaction to occur. This means the reaction rate is up to millions of times faster than it would be without the enzyme. Most biochemical reactions require enzymes for them to occur at fast enough rates to be useful. Typical nomenclature for enzymes follows the pattern using the name of the substrate or the chemical reaction it catalyzes, and ends with ase", eg. catalase, amyl ase. (In other words, any time you see a word end in "ase you know it is an enzyme). Products Enzyme Enzyme Enzyme a.)Suhtrate entering b)Enxyme/suhestrate c) Prodocts leaving active site of enayme active site of enzyme Figure 1: The speciticity of enzymes is controlled by their lock and key fit with a spe- dfic substrate. Enzymes are extremely selective, and are often described as havinga "lock and key" fit (Figure 1). Their shape determines which substrates they bind and interact with. The activation site Lab 9: Enzymes is the pocket where the substrate attaches and where the reaction occurs. After the enzyme/substrate complex forms and catalysils occurs, the "new substrate is released from the active site, and the en zyme can repeat the process. Enzymes levels are not reduced or altered during the reaction. This means they are efficient and can be used repeatedly. Enzymes determine the rate at which the reaction oc rs (not how it occurs). Their activity is affected by temperature, pH, enzyme and substrate concentration, and other chemicals that may be present (such as salts, which can change the protein structure). Variations in temperature and alkalinity can change the shape of the proteins, such as enzymes, which makes them inactive (they can no longer bind to their substrate). The pH can alter charge of the proExplanation / Answer
1. It did not change
Since the color for negative control is asked therefore, the answer will be no change because negative control does not give any response when the experiment is carried out and will remain unchanged.
2. The solution stayed same color.
The solution's color remained unaffected by the addition of dye.
3. Glycogen
From the given information glycogen is most likely not an enzyme. Moreover, enzymes generally end with an "ase" in their name.
4. Hot air
Based on the experiment the balloon with hot air will have the largest diameter because hot air occupies more volume than cold air.
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