FSQ 2204 - Experiment 1 parviz
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Apr 3, 2024
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EXPERIMENT 1A and 1B PROTEIN DENATURATION Objective: To experiment with different methods of denaturing the protein present in milk (Casein) Materials required: Distilled white vinegar (acetic acid), 5% acidity Hot plate/ Bunsen burner Pasteurized whole milk Beakers Rennet tablets (Junket) Balance Epsom salt (magnesium sulfate) Thermometer Cheesecloth Foil Rubber bands Hammer Stirring rod/ wood Popsicle Sticks Eyedroppers Heatproof gloves Heatproof pads Weigh boats Graduated cylinder Background Denaturation occurs when the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure, there are four types of bonding interactions between "side chains" including hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions, which may be disrupted because of different conditions and reagents. The most common observation in the denaturation process is the precipitation or coagulation of the protein. Procedure –
PART A1 Precipitation of casein from milk with an acid (vinegar) 1. Weight the empty beaker and record the weight. Weigh and record the weight of 50 milliliters of milk in the beaker. Record the weight of the milk in the data table (weight of beaker with milk –
the weight of beaker = weight of milk). 2. Place the beaker with the milk on a hot plate. Heat the milk to 21°C (70°F). Turn off the hot plate and remove the beaker.
3. Add 6 milliliters of vinegar to warm the milk and stir for 2 minutes, then allow the milk to sit for 5 minutes. The casein will precipitate into heavy white curds. 4. Cut out a piece (2-3 layers) of cheesecloth large enough to cover the top and 2 inches down the sides of a beaker. Use the rubber band; fasten the cheesecloth over the top of the beaker. Pour the curdled milk into the beaker, collecting the curds (casein) in the cheesecloth and allowing the vinegar and whey to drain off into the bottom of the beaker. 5. Gather up the cheesecloth with the casein and rinse in cool water by dipping into another beaker containing water. 6. Squeeze the casein until almost dry, then spread out the cheesecloth to let the casein dry for 5 minutes. 7. Weigh the precipitate (Do not weigh the cheesecloth with the precipitate). Record your results. PART –
A2: Enzymatic coagulation of the casein from milk with rennet
1. Place 1/4 of a crushed rennet tablet into a beaker. 2. Weigh the empty beaker and record the weight. Weigh and record the weight of 50 milliliters of milk in the beaker. Record the weight of the milk in the data table (weight of beaker with milk - weight of beaker = weight of milk). 3. Place the beaker with the milk on a hot plate. Heat the milk to 43°C (11 0°F). Pour the hot milk over the rennet tablet, stir for 2 minutes, and allow the milk to sit on the lab bench for 5 minutes. 4. Collect the curds by pouring the curds and liquid into a beaker covered with Cheesecloth (2-
3 layers) (see step 4 in Part 1). Gather up the cheesecloth and squeeze out the liquid whey from the curds. Spread out the cheesecloth to allow the curds to dry for 5 minutes. 5. Weigh the curds. (Do not weigh the cheesecloth with the curd). Record your results. DATA TABLE- MILK CURDS (2 points) Weight of milk/soymilk Weight of curd Describe the curd (color, texture) Milk + acid Milk + rennet Weight of beaker with milk –
weight of beaker = Weight of milk
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Related Questions
PROCEDURES
1. Search at least five food products at home.
2. Determine the major fat component (Saturated or Unsaturated)
RESULTS
FOOD PRODUCTS
French Fries fried using
vegetable oil
French Fries fried using
Types of Fats
Unsaturated
Advantages/Disadvantages
It has health benefits/It is costlier
Saturated
It is much cheaper/ Not healthy – fats
will be deposited in veins
derived from animal oil
--
CONCLUSIONS
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✪
H₂N.
✪
H₂N
H₂N
H₂N
✪
H₂N
✪
H₂N
NH₂
0
H₂N
0
NH₂
ht
Biglie
O
✪
H₂N
NH₂
NH₂
·00
H₂N.
H₂N
NH₂
A
OH
CO₂H
V8 Protease
(cat)
H,O, pH 7
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Question: Why are we using this materials in the experiment is there any reason why we using it?
Quantification of Total Protein in Serum Experiment;
Materials:
Fatty acid free beef albuminl solution: 100 g / L
Reagent Ⅰ
Sodium potassium tartrate 9g / LSodium hydroxide 0.2 mol / L Potassium iodide 5 g / L
Reagent Ⅱ
Serum from blood
Copper sulphate solution: 150 g / L
Working solution: 5 ml of reagent copper sulphate solution is prepared by mixing into 1 L of reagent Ⅱ. This reagent is stable for 6 months at 2-8 ° C
Procedure:
*Three test tubes are taken. These are marked as blank, standard and sample tubes.*Only 5 ml of working solution is put into the blank tube.*0.1 ml reagent I and 5 ml working solution are put into the standard tube.*0.1 ml of serum and 5 ml of working solution are put into the sample tube.*After mixing each tube separately, it is waited for 30 minutes at room temperature and measured at 545 nm in the spectrophotometer.*Color permanence is…
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serum protein electrophoresis
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A)
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B)
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C)
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b. 137 mL
c. 163 mL
d. 263 mL
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Temperature
4 °C
21 °C
30 °C
37 °C
90 °C
Absorbance at zero min
1.300
0.952
0.876
0.914
0.903
Absorbance after 10 min of incubation
1.160
0.743
0.042
0.016
0.758
Aomin – A10min
0.140
0.209
0.834
0.898
0.145
Enzyme activity in 10 min (umoles)
Enzyme activity (umoles pyruvate/min)
CALCULATIONS: show calculations
Where extinction coefficient is 6.22 x 103
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Test/ samples
Glucose
Starch
Molisch’s test
Purple ring
Fehling’s test
Red precipitate
Red precipitate
No precipitate
No precipitate
Barfoed’s test
No precipitate
No precipitate
Iodine test
No colour
No colour
Blue colour
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Answered
proteln structure 1
Which is an example of primary protein structure?
Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer
a.
Multiple folded protein chains create an overall shape of a protein complex,
b Amino acids form a particular sequence of residues
A protein contains many alpha helices.
A protein folds around itselrto exposehydrophilic groups on its surface
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731375SSO
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O Dinitrogen Trioxide vapor: N203
OAmmonium Chloride: NH4CI
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Compound W
FAST ACTING
GEL
PETt
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True
False
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Molecule
Test
Positive Result
Negative Result
Protein
Biuret reagent
Pink or purple
Blue
Simple sugars
Benedict's reagent
Green, Orange or Red
Blue
Starch
Iodine
Orange, Blue or Purple
Yellow
Lipids
Brown paper
Oily Stain
No stain
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A. The solution contains carbohydrates.
B. The solution contains lipids.
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D. The solution contains starch.
E. The solution contains protein.
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627.271 627.604
100 -
627.938
628.271
628.604
628.938
627.0
628.0
629.0
mass/charge (m/z)
628.271
626.271
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O 1884.813
% Abundance
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all answers are correct
icterus
lipemia
hemolysis
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/evo/index.html?deploymentld=D55750828934189288909969212&elSBN=9781305657571&snapshotld=2199898&id%3D1..
O To *
MINDTAP
Q Search this ca
Use the References to access important values if needed for this question.
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moles
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c) form a crystal or solid
d) change the pH toward 14
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Ceresin Wax
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Hydroxypropyl Methylcellulose
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need only the relationship discussed in the pdf posted and the numbers posted below.
The next 6 questions will ask for the numbers you calculated for each of the letters below.
pH when
Average charge of group
Group
Ka
pKa
[A]/[HA] = 1
when pH = pK
alpha-COOH
~10-2
A
C
alpha-NH3*
~10-9
В
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Protein sequence is always read (blank) terminal to (blank) terminal.
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