Theory: The number of hydroxyl groups in alcohol can be estimated by acetylation with acetic anhydride.A known weight of the alcohol is acetylated with acetic anhydride in presence of dry pyridine. The amount of acetic anhydride is used in the excess is hydrolysed by water to acetic acid at the end of reaction. Acetic acid so produced is titrated against standard alkali solution to determine the amount of the unreacted acetic anhydride.
Reaction: (CHsCO)2 + H2O → 2CH3COOH
Reagents: Distilled acetic anhydride, 0.5 N sodium hydroxide, dry pyridine,
Acetic anhydride in pyridine: Mix one volume of acetic anhydride (AR grade ) and three volumes of pure dry pyridine
Procedure: In 250 ml conical flask attached with water condenser, weigh accurately
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Casein has isoelectric pH of about 4.7 and can be easily separated around this isoelectric pH. It readily dissolves in dilute acids and alkalies. Casein is present in milk as calcium caseinate in the form of micelles. These micelles have negative charge and on adding acid to milk the negative charges are neutralized.
Reagents: Beakers (250 ml), Filter-paper, Glass rod, Weight box, Filtration flas, Buchner funnel, Test tubes, Porcelain dish, a sample of milk, 1 % acetic acid solution, Ammonium sulphate solution.
Procedure:
Take a 20 ml of cow’s milk in a beaker & add 20 ml of saturated ammonium sulphate solution slowly and with stirring. The precipitate of fat along with casein is formed. Filter the solution and transfer the precipitates in another beaker. Add about 30 ml of water to the precipitate. Only casein dissolves in water forming milky solution leaving fat undissolved. Heat the milky solution to about 40oC and add 1% acetic acid solution drop-wise, till casein gets
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Result: Weight of casein present in 20 ml of cow’s milk is -------- g.
Experiment No.11
Isolation of lactose from milk (purity of sugar should be checked by TLC and PC and Rf value reported)
Theory: The β-D-Galactopyranosyl-1,4- β-D-glucopyranose is known as lactose (also as milk sugar)os a component of milk. Milk contains generally 2-8 % of lactose by weight. Procedure: Dissolve 10 g dry milk powder in distilled 50 mL water in beaker and place it over a water bath at 50 º C. Add 10 mL ,10 % v/v acetic acid solution and stir the mixture to coagulate . Filter the precipitate (casein) by pressing through a funnel containing cotton; collect the filtrate in a beaker. Add about 1g anhydrous calcium carbonate to the filtrate. Boil the filtrate with stirring for about 10
Poured a small amount of milk over the enzyme beads, then allow the treated milk to run into a small beaker.
Set up: Measure and pour 650ml of water into a beaker and mix it with sodium hydrogen carbonate using a stirring rod until all the sodium hydrogen carbonate has dissolved into the water.
It contains the mineral calcium, which build bones and keep them healthy. Osteoporosis is a condition where your bones are pourous and break or fracture very easily. Drinking milk and obtaining calcium helps prevent this in a major way. Protein is also found in milk, and is also extremely important.. Protein is used by your body to repair and make tissue, such as your hair and nails, and is also used to make enzymes, such as lactase, to speed up chemical reactions in your body. One last thing found in protein is potassium. Potassium helps maintain mineral and water throughout your body, can help control muscle growth and plays a big role in nerve function. Regular drinking milk is broken into four main types, with countless products branching off. These four types are whole milk, 1% milk, 2% milk, and skim milk. The types are divided by their fat contents (whole being the highest in fat, skim being the lowest). The brand of milk that will be used in this experiment is Horizon. This brand is part of the National Organic Program, so the cows producing the milk will not be genetically modified. This means the cows will not be given any hormones or preservatives, which could potentially effect the milk, and how the lactase responds to
Wash (swirl and shake) the organic layer with one 10-mL portion of water and again drain the lower aqueous layer. Transfer the organic layer to a small, dry Erlenmeyer flask by pouring it from the top of the separatory funnel. Dry the crude t-pentyl chloride over 1.01 g of anhydrous calcium chloride until it is clear (see Technique 12, Section 12.9). Swirl the alkyl halide with the drying agent to aid the drying.
Dissolve 40g povidone in 120g water. Blend 200g lactose, 4g Blue#1, 0.8g Yellow #10. Screen rough blend for clumps and blend to uniform color. Add povidone solution to povidone and 515.2g lactose to granulate. Add water to appropriate consistency, then dry product to specification. Sift material to correct fleck size (wet granulation of coating). Blend 450g of sodium glycolate to 20g silicon dioxide. Screen material. Blend 2700g starch, 7980g MC, 50g Mg stearate, 800g of blue granulation (above) (press coating). For the core, blend 2675g cyclophosphamide monohydrate to 5g silicon dioxide, blend with 1150g starch, 150g starch glycolate, and 20g magnesium stearate. Compress core, then surround core with coating by second direct compression. Hardness
Dissolve 2.34 g of cobalt chloride hexahydrate (CoCl2.6H2O) in 100 ml of water in an Erlenmeyer flask. While stirring the oxalic acid solution constantly, add the cobalt chloride solution drop by drop. Let the mixture cool in an ice bath. A precipitate will form slowly.
2) Rinse the solid with about 30 mL of distilled water and decant the liquid from the solid. It is critical that as little solid as possible is lost during this process. Repeat the rinsing two or three times.
Fill granulated cylinder with water by submerging and make sure no bubbles at the top.
The goal of separating the components of milk was desirable because their differences in properties required different techniques to separate them. The casein, Vitamins A, D, and E, and fats were all nonpolar and therefore dissolved in nonpolar solutions.1 Whey, lactose, calcium, phosphate, vitamin B, vitamin C, and water were all polar and therefore dissolved in polar solutions.1
Only one-third of the human population is capable of digesting lactose, which is the sugar found in milk. This is most likely because only certain societies amongst the globe domesticated cows for a food and income source around ten thousand years ago. People who had ancestors that were apart of these communities are more likely to be lactase persistent than those who do not. Communities such as these were often seen in places such as Europe and Africa, which can likely be an explanation for why lactase persistence is often found in those with European and African ancestry, while those with Asian backgrounds are often lactase intolerant.
The Jianqin et al., 2015 study involved forty-five Chinese participants who were randomized and put in a 2 × 2 crossover trial. These participants were given milk in which one had both β-casein types while the other contained only A2 β-casein. The period of treatment for each of the trials was 14 days and a 14-day washout period at baseline and between treatment periods. The results to be looked out for included post-diary digestive discomfort (PD3), and the gastrointestinal function. According to findings of the study, when the participants consumed milk containing both β-casein types, they experienced much stronger PD3 symptoms, had longer gastrointestinal transit times and also had lower levels of short-chain fatty
Once the characteristics of the milk were noted we began to prepare the agar plates for the different milk samples. For cold milk, one agar plate was labeled undiluted, and one plate was labeled “10-1”. 0.5 ml of milk was pipette onto the plate labeled undiluted. 0.1 ml of milk was then pipette onto the plate labeled “10-1”, and the pipette was discarded. Using an alcohol and flame sterilized bent rod, the milk was distributed across the agar plates. The lid was never removed completely, just lifted up enough to allow the rod to thoroughly spread the milk.
After all of the crystals are dissolved add 20 mL of warm water cover the beaker with a watch glass and allow the solution to cool slowly
Milk is very important to all societies, the different varieties in milk gives the opportunity for others to have the ability to gain drink milk. But, scientist now want to try and figure out why some humans can’t digest milk while others can. The scientific research that has been done in order to explain the biological basis of human lactase is archaeological and genetics. Archaeologist examined pottery shards in order to grasp what the animals where actually consuming indicating where the proteins came from. Other scientists did field work with both Africans and Europeans that either had experiences raising a cattle or did not have experiences with cattle in order to show that human lactase is genetic. In order to show and or to further explain the biological basis of human lactase I will first discuss who can actually drink milk, the history of both Europeans and Africans. Next, I will discuss the values of both plant domestication and animal domestication. I will then talk about where cattle’s get their vitamins from and lastly I will discuss the value of milk, as well as how it benefited other people.
There are two types of protein in milk. These proteins in milk consist of 80% casein and 20% whey protein. In cheese-making using milk, the protein in milk that is of most interest is casein. This casein has four major types of molecules. The interactions of each type of casein molecule contribute to the structure and state of casein micelles in milk. Milk is negatively charged in its natural state. This is attributed to the hairy layer of k-casein that is responsible in allowing the dispersion of casein in milk and preventing casein micelles from aggregating. The aim in cheese-making is to make those casein micelles coagulate that will eventually result to a solid mass often called curd. There are different casein coagulation processes that can be done depending on the product that you are aiming to make. First, as for making cottage cheese, one can simply use acid addition directly to milk or by employing starter culture such as streptococci or lactobacilli. Other casein coagulation can be done through enzymatic action using chymosin or rennin. One prominent example of type of cheese done in this way is cheddar. Lastly, casein coagulation can also be produced by acid and heat coagulation. In this process, acid and heat are used to clot milk. Ricotta is a good example of cheese done in this way.