Conclusion in the experiment casein was successfully

Conclusion In the experiment casein was isolated from milk magic skim milk by isoelectric focusing method. When the isolated casein was subjected to acid hydrolysis and alkaline hydrolysis, the appearance of the isolate before and after autoclaving was compared, and a significant change occurred. The protein suspension gave positive results for the biuret test and the Hopkins call test and therefore based on these results the protein suspension components were determined to be peptide bound nitrogen and tryptophan. Alternatively, the alkaline hydrolyzate provides only positive results

Xanthoproteic test, ninhydrin test and Hopkins Cole test; therefore, it consists of amino acids, free amino groups and tryptophan. In the protein assay by the Bradford method, the calculated concentration of unknown protein solution was 138 μg / mL. This is calculated using the equation y = mx + b. Experiment 0 Material separation and hydrolysis of casein from milk  Powder skim milk (5 g) • 10% acetic acid • Protein isolate • 8 N H 2 SO 4 • 16 N H 2 SO 4 • solid Ba (OH) 2 • saturated Ba (OH ) 2 solution • Aluminum foil • 50 mL Erlenmeyer flask • Cotton • pH paper • Litmus paper • pH meter • Autoclave color reaction of intact protein and hydrolyzate • 5 M NaOH • 0.01 M CuSO 4 solution • 10% NaOH • 0.02 % Naphthol solution • NaOBr (fresh formulation) • Mortar and mortar • 0.1% ninhydrin solution • Concentration HNO 3 • Concentration. NaOH • Hopkins call reagent • Concentration H 2 SO 4 0 0 Protein determination by Bradford method • Unknown protein solution • Bradford reagent • BSA standard (bovine serum albumin, 0.2 mg / mL in water solution) • Large test tube • Serum Petting tube (1 mL and 5 or 10 mL)

Procedure 0 In a 100 mL beaker, 5 g of milk magic milk was dissolved in 20 mL of hot distilled water. The solution was heated to 55 ° C. on a hot plate and the temperature monitored using a thermometer. One minute after reaching the desired temperature, the solution was removed from the hot plate and the initial pH of the milk solution was recorded. With continuous stirring, 10% acetic acid was added dropwise to the solution until the pH reached 6 and the volume of acid used was recorded. The solution was allowed to stand until a large amorphous material was formed and was filtered off by gravity filtration. The filtered precipitate was dried between filter papers and divided into two portions. One is used for acid / base hydrolysis, the other is wrapped in aluminum foil and stored in a refrigerator. A portion of the protein isolate was cut into very small pieces and placed in a 50 mL Erlenmeyer flask. For acid hydrolysis, 4 mL of H 2 SO 4 was added with alkaline hydrolysis and 5 mL of boiling water containing 0 g of Ba (OH) 2 was added.

Casein casein accounts for 80% of protein in cow's milk. Casein is a slowly digesting protein that is separated from milk. It contains 92% protein and is very "tough". Therefore, it is a very popular protein with weight gain agents. Casein has a lower BV value than whey, but it is more effective for building muscle. Casein supplements encourage the body to gain energy using carbohydrates and stored fat, since casein is used by the body to make muscle and small amounts are used as energy source. Casein is also expensive with supplemental glutamine that also carries bodybuilding

Conclusion In the experiment casein was isolated from milk magic skim milk by isoelectric focusing method. When the isolated casein was subjected to acid hydrolysis and alkaline hydrolysis, the appearance of the isolate before and after autoclaving was compared, and a significant change occurred. The protein suspension gave positive results for the biuret test and the Hopkins call test and therefore based on these results the protein suspension components were determined to be peptide bound nitrogen and tryptophan. Alternatively, the alkaline hydrolyzate only gives positive results

Since casein is present in micelles in cow's milk, it is a protein source of cheese which forms curd during processing. As a dietary supplement, casein is made from chymosin casein or caseinate; it is usually in the form of an acid combined with sodium, calcium or potassium. Low pH conditions in the stomach cause the casein to clot, form lumps or coagulate and retard gastric emptying. Unlike whey protein that continues to melt in the stomach, they quickly become empty, casein is converted into a solid mass and slowly empties from the stomach. These differences in digestive properties can contribute to different AA concentration patterns observed after ingesting whey or casein. Therefore casein is called "late" and whey is called "fast" protein.