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Complete
report of biochemistry with title “Milk”. Created by:
Name
:
Class/Group
:
Reg.
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After
checked and corrected by assistant and coordinator assistant. So, this report
is accepted.
Makassar, january 2012
Coordinator
assistant Assistant
-------------------------- --------------
Known by,
Responsibility Lecturer
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I.
The title of experiment
Milk
II.
The aims of experiment
1. To
test the freshing of milk
2. To
separating the cassein from milk
3. To
know the reaction of color casein
4. To
know protein coagulated
III.
Preview of literature
Milk is a white liquid produced by the mammary glands
of mammals.
It is the primary source of nutrition for young mammals before they are able to digest
other types of food. Early-lactation milk contains colostrum,
which carries the mother's antibodies to the baby and can reduce the risk of many
diseases in the baby.Milk derived from cattle species is an important food. It
has many nutrients. The precise nutrient composition of raw milk
vary by species and by a number of other factors, but it contains significant
amounts of saturated fat, protein
and calcium
as well as vitamin C.
Cow's milk has a pH
ranging from 6.4 to 6.8, making it slightly acidic. Milk is an emulsion
or colloid
of butterfat
globules
within a water-based fluid that contains dissolved carbohydrates. Because it is
produced as a food source for a neonate, all of its contents provide benefits
to the growing young. The principle requirements of the neonate are energy
(lipids, lactose, and protein), biosynthesis of non-essential amino acids
supplied by proteins (essential amino acids and amino groups), essential fatty
acids, vitamins and inorganic elements, and water.
(Anonyma.2012).
Peptides, polypeptides, and
protein are the universal constituente of the biosphere. They are responsible
for the structural and functional integrity of cells. They form the chemical
basic of cellular functions that are based on highly specific molecular
recognition and binding, and are involved as key participant in cellular
process. A peptide or a protein is a copolymeterIn general, the gross
composition of cow's milk in the U.S. is 87.7% water, 4.9% lactose
(carbohydrate), 3.4% fat, 3.3% protein, and 0.7% minerals (referred to as ash).
Milk composition varies depending on the species (cow, goat, sheep), breed
(Holstein, Jersey), the animal's feed, and the stage of lactation. Although
there are minor variations in milk composition, the milk from different cows is
stored together in bulk tanks and provides a relatively consistent composition
of milk year round in the U.S. thermodynamic control (Folthin,Ransom.2003).
Colic, for instance, is far
more common in the U.S. than in many other places around the world. Two chief
causes for its rise are the stress suffered by babies being regularly separated
from their mothers, and the common difficulties babies have tolerating the
large cow's milk proteins in infant formulas and breastfeeding mothers' diets.
Cow's milk is a foreign substance that has pervaded every corner of our
diets—starting with artificial infant feeds, but finding its way into mother's
breastmilk through the foods she eats as well. As it turns out, health problems
such as childhood diabetes, obesity, bowel disease, osteoporosis, heart
disease, cataracts, colic, ear infections, hyperactivity, and cancer, on the
rise in both children and adults, are strongly linked to infant feeding
choices. While there are literally thousands of research studies, each
revealing at least one of milk's hazards, the dairy industry goes to great
lengths to stifle any damaging rumors. Blanket statements, such as, "There
is simply no scientific research to back up these claims," are easily made.
With a long and successful history of dairy promotion, these are readily
accepted by the public. More
people need to go to the real research and learn the truth for themselves.
They should be very suspicious of these foreign foods being pushed on their
children. They should question motives as well as possible outcomes. Although
some of the dangers of cow's milk consumption relate more to adults than to
children, parents' actions form the basis for lifelong dairy-consuming habits
in their children (anonymb.2011).
Almost every day another
health research finding is made about whole grains, soy, a serving of
vegetables, two fruits per day, cashews, legumes, fish, or some other food, other than milk that is, and
their connection to a reduced risk of heart disease, breast cancer, stroke,
diabetes, or other disease. This is because cow's milk and its derivatives
today make up one-third of the adult diet, and half to two-thirds of caloric
intake in children, thus replacing so much other important, nutritious food
needed in the diet. This leads to insufficient intake of important vitamins,
several minerals, and healthy fiber and vegetable oils. Cancer-preventing
antioxidants in foods are missing in this milk diet as well. While one form of
antioxidant vitamin A is added to milk (but not all dairy products), it is
likely counteracted by the pesticide and drug residues. The full complement of
vitamin A and associated enzymes, found in vegetables and other foods, are required
for cancer prevention. Many, many more kinds of antioxidants are found in
vegetables, legumes, fruits, and grains. If there remains a desire to provide
milk to a child who has no diarrhea, rashes, or other intolerance reactions,
organic (organic—not raw)
non-fat milk would be the best choice. In raw (unpasteurized) milk there can be
many potentially dangerous microorganisms, in addition to the leukemia virus.
In organic milk there are fewer antibiotic residues, no added hormones, and cows are given better feeds. Non-fat means
less chemical residue and no artery-damaging saturated fat. Children can obtain
fat in the form of non-hydrogenated (especially monosaturated) vegetable oils,
be it in potato chips or cashews. Goat's milk is considered by many to be
superior in many ways, and today low-fat versions are available. Much less
documented information is available about goat's milk, but it appears that the
proteins are less problematic for digestion, although allergic intolerance to
these can also occur. Lactose and hormones would remain an issue although, to
date, goats apparently are not injected with extra growth hormone (TVA.2005).
When it was first used,
pasteurization was thought to make raw milk from any source safer to consume.
More recently, farm sanitation has greatly improved and effective testing has
been developed for bovine tuberculosis and other diseases, making other
approaches to ensuring safety of milk more feasible; however, pasteurization
continues to be widely used to prevent infected milk from entering the food
supply. The recognition of many potentially deadly pathogens, such as E.
coli O157:H7, Listeria, and Salmonella, and their presence in milk products
has led to the continuation of pasteurization. The Department of Health and Human
Services, Center for Disease Control and Prevention, and other health agencies
of the United States strongly recommend that the public do not consume raw milk
or raw milk products. Young children, the elderly, people with weakened immune
systems, and pregnant women are particularly susceptible to infections
originating in raw milk (anonymc.2011).
Some folks claim it's
positively deadly. Others liken it to manna from heaven. The truth had to be
out there somewhere, and it was, buried under thick layers of half-truths and
deliberate misinformation. So that's where this site comes in. My goal with
raw-milk-facts.com is to help dispel the myths that have sprung up around one
of Nature's most perfect foods. My body has been my laboratory over the years,
but we're all unique biochemically, so please use what you learn here
carefully- what works for one may not necessarily work for another. As a
Nutrition Consultant, even with three decades of independent nutritional
research and a degree in Biology, I'm not qualified to give out medical advice.
And though I quote highly credentialed medical and scientific professionals,
please consider anything you read on raw-milk-facts.com to be information only.
Click the link above for full details
(Schmid.2004).
IV.
The tool and the
materials
A. The
tools
1.
Small tubes of
15 pieces and 5
pieces
2. Rack tube 2 pieces
3. Measuring cup 10 ml and 25 ml @ 2 pieces
4. pipette drops
5. Stir bar 1 piece
6. Beaker 2 pieces 250 and 1000 ml 1buah
7. Thermometer 2 pieces
8. Excellent 1 coring fruit
9. Spray bottle 1 pc
10. Leg three, asbestos gauze and rubbing alcohol burner
11. stopwatch
12. tube clamp
2. Rack tube 2 pieces
3. Measuring cup 10 ml and 25 ml @ 2 pieces
4. pipette drops
5. Stir bar 1 piece
6. Beaker 2 pieces 250 and 1000 ml 1buah
7. Thermometer 2 pieces
8. Excellent 1 coring fruit
9. Spray bottle 1 pc
10. Leg three, asbestos gauze and rubbing alcohol burner
11. stopwatch
12. tube clamp
B. The
materials
1. Milk
2. Schardinger
reacter
3. Ethanol
4. Ether
5. Acetat
glacial acid
6. Millon
reacter
7. Sodium
hydroxide solution
8. Biuret
reacter
9. Aquadest
10. Tissue
11. Matches
12. Universal
indicator
13. Filter
paper
14. Spiritus
15. Watchman
filter paper
V.
Work procedure
a. Test
freshing milk
1.
Enter 5 ml of saliva
into a test tube
2. Insert 2 drops of 0.1 M CH3COOH
3. Separating the precipitate by filtering
4. Test the filtrate with reagent Millon, Benedict and Molisch and use water as a control
5. Observing the changes that occur
2. Insert 2 drops of 0.1 M CH3COOH
3. Separating the precipitate by filtering
4. Test the filtrate with reagent Millon, Benedict and Molisch and use water as a control
5. Observing the changes that occur
b. Separating
cassein
1.
Entering each 5 ml
of 1% starch solution into four
test tubes
2. I put the tube in ice water, the tube II at room temperature, the tube III in a water bath with a temperature of 38 ° C and the tube ditambahan 2 drops of watery saliva that has been heated in a boiling water bath for 5 minutes yan.
3. Each tube was added I-III watery saliva
4. Add 2 drops of 0.01 N I2 solution into each tube every interval of 5 minutes
5. Observing the speed of the starch solution in each tube.
2. I put the tube in ice water, the tube II at room temperature, the tube III in a water bath with a temperature of 38 ° C and the tube ditambahan 2 drops of watery saliva that has been heated in a boiling water bath for 5 minutes yan.
3. Each tube was added I-III watery saliva
4. Add 2 drops of 0.01 N I2 solution into each tube every interval of 5 minutes
5. Observing the speed of the starch solution in each tube.
c. Tes
color of casein
1. Make a suspension of yeast bread,
yeast tape, and yeast by dissolving 1 / 10 of a teaspoon of each into a 25 mL
aquades.
2. Filling the hole plate 10 drops, each drop of 1% starch solution, lau renumber 1-10.
3. Add 3 drops of each suspension of baker's yeast in holes 2,3,4. Adding yeast tape on holes 5,6,7 and add yeast tempeh in hole 8,9,10. While the number 1 add aquades hole (as controls).
2. Filling the hole plate 10 drops, each drop of 1% starch solution, lau renumber 1-10.
3. Add 3 drops of each suspension of baker's yeast in holes 2,3,4. Adding yeast tape on holes 5,6,7 and add yeast tempeh in hole 8,9,10. While the number 1 add aquades hole (as controls).
d. Coagulation
of protein
1. Adding sucrose into a test tube containing 3 mL of bile
diluted (1:5).
2. Add 3 mL of concentrated H2SO4 slowly.
3. Tilt the tube so that the acid contained in the bottom.
4. Rotate the tube slowly. Observing.
2. Add 3 mL of concentrated H2SO4 slowly.
3. Tilt the tube so that the acid contained in the bottom.
4. Rotate the tube slowly. Observing.
VI.
Observation result
VII.
Comments
Test the Freshness of Milk Test
Freshness of the milk may be marked with the still active enzymes that are found in it, among amylase, lipase, peroxidase, catalase, and so on. To test the freshness of the milk used schardinger reagent (1 ml methylene blue 0.7 ml + 1 ml formaldehyde) is added to the milk cow with care not to shake because of the positive test in a solution of blue color will disappear and if rocking or blue scramble will reappear as leuko-methylene blue is auto-oxidation. In the experiment the blue solution obtained should be blue color disappears. Hi This is due to the milk used is not fresh due to cow milk was taken out of sorts. Function of which is to hydrate xantin penambahahan and hipoxantin. Where the immediate release of H atoms bonded by oxygen or other akseptor as methylene blue water forming leuko methylene blue or colorless.
At pH testing using universal indicator, derived pH 6 where the milk is the optimum pH is 6.5 to 6.8 milk. Results obtained indicate that slightly sour milk.
Casein Separation Test
Fresh cow's milk in the beaker is heated at a temperature of 40. Used a temperature of 40 for optimum temperature on milk for casein clot is 40. Then a drop of acetic acid menambahkann dei drops to 1 ml. Its function is to precipitate the casein in the milk and the casein coagulate. Then sieve to separate the filtrate with casein. A lump of casein obtained with 95% ethanol disuspensikan kemudisn kemb ali screening. Once the lump casein back disuspensikan with ether-ethanol (1: 1). Functions, which is to bind residual ethanol. Casein formed filtered with Buchner funnel and washed with ether to taste. From the obtained experimental blobs of white casein. Filtrate and casein clots will be used for further experiments. Casein structure:
Color reaction Casein
In this experiment, a test that is done some testing Millon, biuret test, and Hopkins-cole test. Millon test principles namely mercury salt formation from tyrosine that ternitrasi. Tyrosine is an amino acid with phenol molecules in its R group which will form the mercury salt with Millon reagent. From experiment looks casein if Millon reagent is added and heated, the solution produced red brick. This memandakan that casein containing tyrosine as one of the constituent amino acids, which in turn means that the structure of casein containing phenol group. Yang terbentuk red color are the salt of mercury from the ternitrasi tyrosine. As for the reaction is
In the biuret test, blobs casein supplemented with biuret reagent a violet ring is formed. It is caused by the reaction of peptides and proteins. Where this reaction, marked with purple color, due to the complex compounds that occur nrantai polypeptide. As for the reaction is
At Hopkins-cole test, blobs added to Hopkins-cole reagent and concentrated sulfuric acid produces purple ring. This occurs because the reagents used glioksilat containing acid, or can be replaced with formaldehyde by the addition of concentrated sulfuric acid. Because triptopan berkondensasi with aldehydes in the atmosphere sulfuric acid and form a purple complex. As for the reaction is
Protein Terkoagulasi
Filtrate from back neutralized casein from precipitation by the addition of 1% NaOH. Once neutral acetic acid added back that serves to form sediment casein. Then memananskannya to boil and form a sediment back. Then concentrated to ½ initial volume. Casein sediment formed is filtered to separate the filtrate with casein and split second to do test Millon and Hopkins-cole.
In Millon test, casein supplemented with Millon reagent is then heated brick red sediment formed, indicating a salt of mercury from the ternitrasi tyrosine in casein.
At Hopkins-cole test, casein supplemented with Hopkins-cole reagent and concentrated sulfuric acid and obtained the purple rings indicate the krypton on casein.
Freshness of the milk may be marked with the still active enzymes that are found in it, among amylase, lipase, peroxidase, catalase, and so on. To test the freshness of the milk used schardinger reagent (1 ml methylene blue 0.7 ml + 1 ml formaldehyde) is added to the milk cow with care not to shake because of the positive test in a solution of blue color will disappear and if rocking or blue scramble will reappear as leuko-methylene blue is auto-oxidation. In the experiment the blue solution obtained should be blue color disappears. Hi This is due to the milk used is not fresh due to cow milk was taken out of sorts. Function of which is to hydrate xantin penambahahan and hipoxantin. Where the immediate release of H atoms bonded by oxygen or other akseptor as methylene blue water forming leuko methylene blue or colorless.
At pH testing using universal indicator, derived pH 6 where the milk is the optimum pH is 6.5 to 6.8 milk. Results obtained indicate that slightly sour milk.
Casein Separation Test
Fresh cow's milk in the beaker is heated at a temperature of 40. Used a temperature of 40 for optimum temperature on milk for casein clot is 40. Then a drop of acetic acid menambahkann dei drops to 1 ml. Its function is to precipitate the casein in the milk and the casein coagulate. Then sieve to separate the filtrate with casein. A lump of casein obtained with 95% ethanol disuspensikan kemudisn kemb ali screening. Once the lump casein back disuspensikan with ether-ethanol (1: 1). Functions, which is to bind residual ethanol. Casein formed filtered with Buchner funnel and washed with ether to taste. From the obtained experimental blobs of white casein. Filtrate and casein clots will be used for further experiments. Casein structure:
Color reaction Casein
In this experiment, a test that is done some testing Millon, biuret test, and Hopkins-cole test. Millon test principles namely mercury salt formation from tyrosine that ternitrasi. Tyrosine is an amino acid with phenol molecules in its R group which will form the mercury salt with Millon reagent. From experiment looks casein if Millon reagent is added and heated, the solution produced red brick. This memandakan that casein containing tyrosine as one of the constituent amino acids, which in turn means that the structure of casein containing phenol group. Yang terbentuk red color are the salt of mercury from the ternitrasi tyrosine. As for the reaction is
In the biuret test, blobs casein supplemented with biuret reagent a violet ring is formed. It is caused by the reaction of peptides and proteins. Where this reaction, marked with purple color, due to the complex compounds that occur nrantai polypeptide. As for the reaction is
At Hopkins-cole test, blobs added to Hopkins-cole reagent and concentrated sulfuric acid produces purple ring. This occurs because the reagents used glioksilat containing acid, or can be replaced with formaldehyde by the addition of concentrated sulfuric acid. Because triptopan berkondensasi with aldehydes in the atmosphere sulfuric acid and form a purple complex. As for the reaction is
Protein Terkoagulasi
Filtrate from back neutralized casein from precipitation by the addition of 1% NaOH. Once neutral acetic acid added back that serves to form sediment casein. Then memananskannya to boil and form a sediment back. Then concentrated to ½ initial volume. Casein sediment formed is filtered to separate the filtrate with casein and split second to do test Millon and Hopkins-cole.
In Millon test, casein supplemented with Millon reagent is then heated brick red sediment formed, indicating a salt of mercury from the ternitrasi tyrosine in casein.
At Hopkins-cole test, casein supplemented with Hopkins-cole reagent and concentrated sulfuric acid and obtained the purple rings indicate the krypton on casein.
VIII. Conclussion
and suggestion
A. Conclussion
1. The milk which used have pH-6 its meaning this
milk is fresh.
2. Cassein
which got have tyrosin amino acd that shown by red brick color when precipitate
is added millon reacter.
3. Cassein
which got have peptide bond because the color become purple when added biurette
reacter.
4. Filtrat
which got from separating casein was contain protein is shown by form
coagulated when boiling.
B. Suggestion
Hope next practicume, practican more
higients and the milk which used should fresh and savetyfrom dirty air.
BIBLIOGRAPHY
Fothin,ransom.2003.Harpers Illustrated Biochemistry.
McGraw-Hill
Schmid.2004.The Secred History of Milk. AGRES: A Voice
for ECO Agriculture USA
TVA.2005.Cow’s Milk. 17 Baldw in St. Second Floor
Toronto.
