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Enzyme lab report
Amber King
11/09/23
Biology 1406
Abstract:
In living cells, enzymes function as catalysts to quicken chemical reactions. The
objective of this experiment is to identify the ideal temperature for enzyme activity by
examining how temperature affects a catalase reaction. Multiple temperature ranges
were tested in the experiment. Each experiment used five milliliters (mL) of 3%
hydrogen peroxide solution and five milliliters (mL) of water, with bath temperatures
ranging from 10, 21.5, 40, 60, and 80 °C. Upon the administration of 1 mL of catalase
solution, the total amount of oxygen gas produced over a fifteen-second interval was
measured. Setting the bath temperature to 40°C produced the most oxygen gas
generation since it is the closest to an enzyme's ideal temperature of 37 . The result of
̊
this lab indicates that the enzymes cannot function if the temperature is not at their
optimum temperature as a low temperature would slow the enzyme reaction and a high
temperature would denature the enzyme entirely. Furthermore, the more substrate
concentration an enzyme has the more it will have an increased chemical reaction. The
interesting part about this is that enzymes play an important role in every human body's
function. In fact, without enzymes, the human body would be unable to function
because the chemical reactions essential to maintaining the body would fail to occur
fast enough.
Introduction
The vast majority of enzymes are proteins; thousands of enzymes are found inside
every cell and serve the body in many ways. Knowing more about enzymes can help
you understand how the human body reacts.
Chemical reactions are aided by enzymes
and are accelerated by them
(Newman, 2022). Enzymes assist in the body's functioning
in numerous essential functions. The body uses enzymes to reduce larger, more
complicated molecules into smaller ones. Toxins in the body are broken down by the
liver, and enzymes aid in the destruction of the toxins. Enzyme specificity depends on
the protein folding patterns that are determined by the amino acid sequence. The
protein structure may lose its structural stability and its capacity to function as an
enzyme if the enzyme is subjected to changes such as changes in temperature or pH
(
Enzyme | Definition, Mechanisms, & Nomenclature
, 1998). An enzyme's distinct shape
is significant because it affects the way an active site can bind to substrates. This lab
will use hydrogen peroxide, water, and catalase solutions to illustrate how essential
temperature, PH, and substrate are to catalase. This experimental setup will allow
monitoring of catalase activity at different degrees of temperature. The hypothesis is
that the catalase enzyme will accelerate the reaction when it is at its ideal temperature.
A specific enzyme found in virtually all living things is catalase. One of its key roles is to
catalyze the breakdown of hydrogen peroxide into water and oxygen.
Materials and Methods:
Constant temperature bath
Five small test tubes
3% Hydrogen Peroxide
Water
Thermometer
Five Gas syringes
Catalase Solution
Lab clock
Waste Bin
Sink
Gloves
Lab Coat
Googles
The constant temperature bath, which was set to 10 degrees Celsius, was taken off the
instrument shelf and placed on the workbench. From the container shelf, a small test
tube was retrieved and placed in the constant-temperature bath. 3 % Hydrogen
peroxide was measured and inserted into the test tube after being retrieved from the
material shelf. The water bottle had been taken from the material shelf, and 5 ML of
water was placed in the test tube. One gas syringe from the instrument shelf was
removed and placed on the workstation, once the temperature was stabilized and
reached the same temperature as the bath, 1 ML of catalase solution from the material
shelf was placed it in the test tube. A gas syringe was retrieved and inserted into the test
tube immediately after adding the catalase solution; the black stopper automatically
sealed the flask. Pause the experiment, double-click on the gas syringe to get the gas
volume, record the time, and then press play to resume the lab. Pause the lab for fifteen
seconds, then record the final volume in the gas syringe. Place the test tube in the sink
after emptying it into the waste bin. This experiment will be repeated four times more,
but the constant temperature bath will be reset to 21.5, 40, 60, and 80 degrees Celsius
each time. After completing the lab four times more, pour the test tubes into the waste
bin and place them in the sink, then place the constant-temperature bath back on the
instrument shelf. The workbench should be clean.
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Related Questions
ENZYME CATALYSIS LAB
EFFECT OF TEMPERATURE
What chemical reaction is being catalyzed in this experiment? Label the substrate(s), enzyme and product(s).
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ENZYME CATALYSIS lab
Construct a hypothesis addressing the effect concentration will have on rate of reaction.
What chemical reaction is being catalyzed in the experiment? Label the substrate(s), enzyme and product(s).
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9:34 AM
You sent
Help me with this one
Select true if the statement is CORRECT and false if OTHERWISE
1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change.
2. Catalysis is defined as the acceleration of a chemical reaction
3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease.
4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it
5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity.
6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature.
8. Enzymes can be classified by the kind of chemical…
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Result nad Discussion
Lead Acetate Reaction:
Samples: lysine, cysteine, methionine
Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2
-To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
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Only section 6-31
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Pls explain in detail
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43
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[One - Biomolecules]
INSTRUCTIONS
— Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer.
— Answer properly
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Select true if the statement is CORRECT and false if OTHERWISE
1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change.
2. Catalysis is defined as the acceleration of a chemical reaction
3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease.
4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it
5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity.
6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature.
8. Enzymes can be classified by the kind of chemical reaction catalyzed.
9. The living cell is the site of tremendous…
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Using this information solve for enzyme activity over time 1 unit - 1 umole per minute.Total reaction volume is 1ml Note: reaction was run for 15 minutes (use relavent formulas) please show full working out. The first part of this question is done 1:5 concentration = 144.7uM and 1:10 concentration 142.4uM. (Use this to solve for enzyme activity) refer to image for all other details and show all working out. Thanks
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Biochemistry question:
Which of the following statements seen in the attached image about enzyme kinetics is FALSE?
Please help with this question. The answer choices are in the attachment.
Thank you
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Enzyme Concentration
8.
Why doesn't it matter if enzymes keep getting
added to graph E? What would it take to increase the rate of enzyme activity?
Then answer the following questions:
1. Transfer of Energy and Matter: Is an enzyme used up in a chemical reaction?
Explain.
2. Transfer of Energy and Matter:
How would your diagram be different if the enzyme activity was anabolic
instead of catabolic? (E.g., an enzyme to build muscle proteins).
a.
Rate of Reaction
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100
increasing
enzyme
ativity
optimum
pH
5 6
9 10 11
7
8
pH
20
40°
60°C
Temperature
1. How do pH and temperature affect enzyme activity?
2. What do the graphs suggest about the activity of the enzyme?
3. Draw a graph that represents the role of enzymes in metabolism. (Rubrics on
next page.)
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8
eBook
Select all of the following that could apply to the brown curve.
Enzyme concentration is
higher.
Temperature for an enzyme
is too high.
Temperature for an enzyme is
optimal.
Activation energy is lower.
Enzyme concentration is
lower.
Activation energy is higher.
Reactants
Progress of reaction,
Products
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Part 1: Assess the following partial results section below by editing it for brevity by omitting
any unnecessary parts (1 point), explain why you decided to remove certain sections (1
point):
To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule
were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for
the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of
inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was
incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the
substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes.
Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the
molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further
diluted to find the minimal…
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Temperature and enzymatic activity
Grade 9 students posed the following question: "What is the convenient temperature for the activity
of an enzyme?"
For this reason, they realized the experiment described below:
-They put the same quantity of cooked starch in each of the two test tubes A and B.
-They added a small quantity of fresh saliva to each of the two tubes.
-Then, they placed both tubes for a convenient duration at different temperatures:
•Tube A in ice where the temperature is 0°C
Tube B in a water bath where the temperature is 37°C.
N.B.: Saliva contains an enzyme: amylase.
•The chemical medium is neutral in both tubes A and B.
By using an appropriate technique, these
students obtained the results shown in the
opposite document.
1- Represent, in the same table, the
variation of the quantities of cooked starch
in the tubes A and B in function of time.
2- Pick out the posed problem by grade 9
students.
3- Analyze the obtained results.
What do you conclude?
Quantity of cooked…
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Chemical Biology, halpp
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Sample pH vs Initial Velocity (AA450/60
seconds)
a bo16
0.0014
0.0012
o.001
0.0008
0.0006
0.0004
0 0002
pH Sample
what does it mean? Does it agree with what we know about enzyme
kinetics and why or why nol? If there were anomalies, what were they and what are some possible reasons for this
occurring? Was an optimal pH identifiable? Why or why not?
Initial Velocity (AA450/60seconds)
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Course Code: BIO121
Course Name: Principles of Biology I
Read the question carefully first
Answer the question-3(b) given chemical reaction according to the question (i) (ii) (iii) with step
by step clear explanation.
Enzyme X
3
(b)
Given a chemical reaction: A + B-
(i)
(ii)
(iii)
Enzyme X can be used to catalyze the reaction above. Enzyme X binds to molecule A and B, and
converts these molecules into product C. Using the lock and key model, explain how enzyme X is
specific to its action.
Predict what would happen to the rate of enzyme activity if the concentrations of molecule A and B
are increased.
Suggest ONE (1) way of how the activity of enzyme X can be controlled.
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Give typed full explanation
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Need help with number 3
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Experiment #1:
The Effect of
Concentration on
Reaction Rate
Number of
Drops of
Enzyme
2
4
6
Reaction Rate
(kPa/min)
sgorbyt lov
0.27
0.73
1.29
Experiment #2:
The Effect of pH on
Reaction Rate
pH of
Solution
4
7
10
Reaction Rate
(kPa/min)
0.36
0.97
0.89
Experiment #3:
The Effect of
Temperature on
Reaction Rate
Temperature
10°C
35°C
55°C
Reaction Rate
18. Predict what would happen if you added 20 drops of enzyme to the test tube.
(kPa/min)
0.58
1.43
0.36
17. What type of relationship exists between substrate concentration and reaction rate? Could
you explain why you think this relationship exists?
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Deepika_Biology
From a kinetics experiment, Kcat was determined to be 55sec^-1. For the kinetic assay, 0.05mL of a 0.05mg/mL solution of the enzyme was used, and the enzyme has a molecular weight of 30,000g/mole. Assume a reaction volume of 3mL. Calculate Vmax (um*min^-1) for the enzyme and catalytic efficiency (in M^-1sec^-1) for the enzyme. The Km for the enzyme was determined to be 8.3*10^-2M.
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3)
Catalase Experiment
Food
Rate of fizzing (1-10)
Boiled potato
Raw potato
Cooked liver
1
Raw liver
10
Students conducted an experiment to check the rate of enzyme action on different types of food. The table
shows the results of an experiment in which students placed hydrogen peroxide on several food samples and
recorded the relative amount of fizz that each produced. The fizz was produced by oxygen bubbles released by
the action of the enzyme catalase, which is found in almost every living cell.
The students conducted a second experiment, using the raw chicken liver from the previous experiment. They
modified the chicken liver and used: one whole piece, one piece cut into two, a piece that they pulverized in a blender.
ALl the Livers were the same mass. The liver was placed in test tubes and hydrogen peroxide was then added to each.
Here are the results:
Chicken Liver and Enzyme Action
Liver Condition Rate of fizzing
whole
9
two pieces
11
pulverized
14
Based on the students'…
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Enzyme Investigation An enzyme was isolated from digestive juices taken from the small intestine. An experiment was set up to test the ability of the enzyme to break down protein. Two test tubes, labeled A and B, were placed in a hot water bath at 37°C, human body temperature. Test tube A contained only protein and test tube B contained protein and the enzyme. The chart below shows the set-up. After two hours, the contents of both test tubes were analyzed. Test tube A showed only the presence of protein. Test tube B showed the presence of the end products of protein digestion, indicating the enzyme had successfully broken down the protein. Identify the end products of protein digestion that made up the contents of test tube B after the two hours.
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This is for question #15.
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Answer for the number 3 question, Thank you.
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A 45 year-old male presents with fever and cough. He is found to have bacterial pneumonia. He is administered a drug that inhibits bacterial enzyme that catalyzes bacterial DNA synthesis. The drug cited above produced the kinetic data shown below. The mechanism of action of the drug is non-competitive inhibition of enzyme; drug binds to active site. Please explain.
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EXPERIMENT 3: Why do enzymes react differently?
DATA SHEET
Given the following standards and the corresponding standard curve table, what is the
amount of substrate consumed given that 1.6 mM of substrate is prepared with an
enzyme gave an absorbance of 0.345?
0.4
0.8
1.2
1.6
Substrate with enzyme
Concentration (mM)
Standard curve table:
Varying Absorbance Absorbance Absorbance
Final
Initial
AcP
Component
Change
Depleted
umol
mM
540 nm
540nm
0.1
0.037
0.088
0.029
0.0784
0.2
0.074
0.022
0.052
0.1406
0.4
0.074
0.074
0.086
0.148
0.2000
0.6
0.222
0.136
0.2325
0.8
0.296
0.204
0.092
0.2487
1.2
0.444
0.345
0.099
0.2676
0.104
0.106
1.6
0.592
0.740
0.488
0.2811
2.0
0.634
0.2865
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