Perhaps everyone has probably heard about casein protein. It is the main element. Unfortunately, such a protein product is not always taken seriously. But in vain! After all, casein is very useful for both athletes and ordinary people. Its main feature is the correct consumption of protein.

Translated from Latin, casein means cheese. By scientific definition, it is interpreted as a complex protein found in milk. This component is part of milk, which is used by almost all mammals on earth. The main part of it in milk is 82%, while whey contains only 18%. When milk sours, all the casein turns into a precipitate, which consists of the formation curd mass. Thus, we can say with confidence that cottage cheese mostly consists of casein.

The peculiarity of this product is that it has a storage function. This unique ability is achieved by its natural origin. Due to the fact that casein protein breaks down several times longer than regular whey protein, the required amount of amino acids enters the human body. These properties of casein allow it to be actively used by people involved in heavy sports, as well as by those who want to get rid of excess body weight.

IN different types sports, it is most often used in the form of micellar casein. This means that the product consists of suspended particles. When the product is mixed with water, the result is a fairly thick consistency. It is very easy to use and you do not feel any discomfort or unpleasant aftertaste. When micellar casein enters the stomach, a person feels a great surge of strength and complete satiety, which will be felt for a long period of time.

This effect is achieved due to the fact that 100% casein contains 88% protein per 100 grams of micellar product, while 1.5% is fat. It is worth noting the fact that casein protein does not contain carbohydrates! Such unique features of the product enable the body to receive all the important amino acids. After taking casein, a person will feel full for approximately 6-8 hours. This time has a positive effect on muscle tissue. After all, they not only noticeably increase in mass, but also do not collapse between breaks in eating.

Casein protein is very effective in burning fat deposits and reducing hunger. If you actively engage in physical exercise and use this product, achieving the desired result will be very simple.

Important to know!

Protein, which would include 100% proteins, does not exist in nature. Maximum only 95%!.

For gaining muscle mass, this kind of protein plays an important role. It has anti-catabolic properties.

It is not recommended to use casein before or after a workout. Thus, you will not achieve results. After all, during periods of physical activity, the body needs proteins that have the ability to be quickly absorbed. It follows from this that this product should be consumed only before bed, in an amount of 40 grams.

To lose weight, take 20-30 grams 2-4 times a day, and the same before bedtime. In this situation, it plays the role of satiating and preserving muscles.

Casein will be best absorbed in a dose of 30-40 grams. In this case, it must be mixed with milk. When the product is combined with liquid, it is best to mix it using a shaker or mixer.

The taste of the drink will be similar to a curd product. If you want to experiment, you can add cocoa, vanillin or sugar to it.

We must not forget that casein is included in the daily calorie intake. So for 100 grams of product, it will contain 360 kcal.

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Introduction

When they say that “life is a form of existence of protein bodies” (F. Engels), they mean not only that the most important components of the human body consist of proteins (muscles, heart, brain and even bones contain a significant amount of protein), but also the participation of protein molecules in all the most important processes of human life. The importance of proteins is determined not only by the variety of their functions, but also by their indispensability for other nutrients. If fats and carbohydrates are interchangeable to one degree or another, then it is impossible to compensate for proteins with anything. Therefore, proteins are considered the most valuable components of food. Dairy proteins are more valuable than meat and fish proteins and are digested faster. In my work I want to consider the properties of one of the proteins - casein.

Basic physical and chemical properties casein

CASEIN (from Latin caseus - cheese), the main protein fraction cow's milk; refers to storage proteins. In cow's milk, the casein content is 2.8-3.5% by weight (of all milk proteins - about 80%), in women's milk it is two times less, and also g-casein (2.5% of the total).

The elemental composition of casein (in%) is as follows: carbon - 53.1, hydrogen - 7.1, oxygen - 22.8, nitrogen - 15.4, sulfur - 0.8, phosphorus - 0.8. It contains several fractions that differ in amino acid composition.

Casein is a phosphoprotein, therefore, casein fractions contain phosphoric acid residues (organic phosphorus) attached to the amino acid serine by a monoester bond (O-P)

In milk, casein is found in the form of specific particles, or micelles, which are complex complexes of casein fractions with colloidal calcium phosphate.

Casein - a complex of 4 fractions: ? s1, ? s2 , ?, ?. The fractions have different amino acid compositions and differ from each other by replacing one or two amino acid residues in the polypeptide chain. ? s - and? - Caseins are most sensitive to calcium ions and in their presence they aggregate and precipitate. ? - Casein is not precipitated by calcium ions and in casein micelles, located on the surface, plays a protective role in relation to sensitive ones. ? s - and? - casein. However? - casein is sensitive to rennet and under its influence breaks down into two parts: hydrophobic para-β-casein and hydrophilic macroprotein.

Polar groups located on the surface and inside casein micelles (NH 2, COOH, OH, etc.) bind a significant amount of water - about 3.7 g per 1 g of protein. The ability of casein to bind water characterizes its hydrophilic properties. The hydrophilic properties of casein depend on the structure, charge of the protein molecule, pH of the environment, salt concentration and other factors. They are of great practical importance. The stability of casein micelles in milk depends on the hydrophilic properties of casein. The hydrophilic properties of casein affect the ability of acidic and acid-rennet curds to retain and release moisture. Changes in the hydrophilic properties of casein must be taken into account when choosing a pasteurization regime during the production of fermented milk products and canned milk. The water-binding and water-holding capacity of the cheese mass during cheese ripening and the consistency of the finished product depend on the hydrophilic properties of casein and its breakdown products.

Casein in milk is contained in the form of a complex complex of calcium caseinate with colloidal calcium phosphate, the so-called caseinate calcium phosphate complex (CCPC). KKFK also includes small quantity citric acid, magnesium, potassium and sodium.

The primary structure of all caseins and their physicochemical properties have been studied. These proteins have a molecular weight of about 20 thousand, an isoelectric point (pI) of approx. 4.7. They contain increased amounts of proline (the polypeptide chain has a b-structure) and are resistant to denaturants. Phosphoric acid residues (usually in the form of a Ca salt) form an ester bond primarily with the hydroxy group of serine residues. Dried casein is a white powder, tasteless and odorless, practically insoluble in water and organic solvents, soluble in aqueous solutions of salts and dilute alkalis, from which it precipitates when acidified. Casein has the ability to curdle. This process is enzymatic in nature. In newborns, the gastric juice contains a special proteinase - rennin, or chymosin, which splits off a glycopeptide from (-casein) to form the so-called steam - casein, which has the ability to polymerize. This process is the first stage of curdling of all casein. In adult animals and humans, the formation of steam - casein occurs as a result of the action of pepsin. In its curdling ability, casein is similar to fibrinogen in blood plasma, which, under the action of thrombin, is converted into easily polymerized fibrin. It is believed that fibrinogen is the evolutionary precursor of casein. The ability to curdle is of great importance for the effective assimilation of milk by newborns. because it ensures its retention in the stomach. Casein is easily accessible to digestive proteinases already in its native state, while all globular proteins acquire this property during denaturation. During partial proteolysis of casein, which occurs during the assimilation of milk by newborns, physiologically active peptides are formed, regulating such important functions as digestive, blood supply to the brain, activity of the central nervous system, etc. To isolate casein, skim milk is acidified to pH 4.7, which causes casein to precipitate. Casein contains all the amino acids necessary for the body (including essential ones), and is the main component of cottage cheese and cottage cheese; serves as a film former in the production of adhesives and adhesive paints, as well as a raw material for plastics and fibers.

Casein, like all proteins, has amphoteric properties - it can exhibit both acidic and alkaline properties.

When the solution reacts alkaline, casein becomes negatively charged, as a result of which it is able to react with acids:

On the contrary, in an acidic solution, casein acquires the ability to react with alkalis, i.e. cations, and it becomes positively charged.

In milk, casein has pronounced acidic properties. Its free carboxyl groups of dicarboxylic amino acids and hydroxyl groups of phosphoric acid easily interact with ions of alkali and alkaline earth metal salts (Na + -, K +, Ca 2+, Mg 2+), forming caseinates.

Free amino groups of casein can interact with aldehydes, such as formaldehyde:

This reaction underlies the determination of protein content in milk using the formol titration method.

Casein, like whey, comes from cow's milk. It accounts for approximately 80 percent of the total milk protein content, the other 20 percent being whey protein. Casein is insoluble and is a whole milk protein.

Casein is often called calcium caseinate, which includes calcium ion in the protein structure.

Benefits of Casein

Advantages casein protein quite a lot, especially for those who maintain an active training regimen. First of all, casein is an animal protein, which puts it above plant proteins such as soy in terms of benefits for muscle hypertrophy after exercise. All major animal milk proteins contribute to muscle protein synthesis, including through activation of the mammalian target of rapamycin (mTOR) and are complete proteins (containing all essential amino acids, including BCAA and glutamine).

Side effects of casein

A number of people are allergic to casein. They may experience side effects such as stomach upset, pain, diarrhea, vomiting, or other problems.

Additionally, taking large amounts of casein can cause some digestive problems even for those who do not have allergies. Taken in large quantities, it can cause bloating and discomfort, especially in those around you.

6. Fractional composition of casein

1). Characteristics of the main fractions.

2). Physicochemical properties of casein.

In freshly milked milk, casein is present in the form of micelles built from casein complexes. The casein complex consists of an agglomerate (cluster) of the main fractions: a, b, Y, H-caseins, which have several genetic variants.

According to recent data, casein can be divided according to the scheme (Fig. 1), based on the revision of the Committee on Protein Nomenclature and Methodology of the Association of American Dairy Scientists (ADSA).

All casein fractions contain phosphorus, unlike whey proteins. The as-casein group has the highest electrophoretic mobility of all casein fractions.

as1-casein is the main fraction of as-caseins. As1-casein molecules consist of a simple nomenclature chain containing 199 amino acid residues. Like b-casein and unlike H-casein, it does not contain cystine. as2-casein - fraction of as-caseins. As2-casein molecules consist of a simple polypeptide chain containing 207 amino acid residues. It has properties in common with both as1-casein and H-casein. Like H-casein and unlike as1-casein, it contains two cysteine ​​residues:

as-casein - fraction of as-caseins. Its content is 10% of the content of as1-casein. It has a structure identical to that of as1-casein, except for the location of the phosphate group.

b-casein, its molecules consist of a simple polypeptide chain and contain 209 amino acid residues. It does not contain cysteine ​​and at a concentration of calcium ions equal to their concentration in milk, it is insoluble at room temperature. This fraction is the most hydrophobic due to its high proline content.

N-casein - has good solubility, calcium ions do not precipitate it. Under the action of rennet and other proteolytic enzymes, H-casein breaks down into pairs - H-casein, which precipitates together with as1, as2 - b-caseins. N-casein is a phosphoglycoprotein: it contains the tricarbohydrate galactose, galactosamine and N-acetyl-neuralinic (sialic) acid.

The group of U-caseins are fragments of b-casein, formed by proteolysis of b-casein by milk enzymes.

Whey proteins are heat labile. They begin to coagulate in milk at a temperature of 69°C. This simple proteins, they are built almost exclusively from amino acids. They contain significant amounts of sulfur-containing amino acids. They do not coagulate under the influence of rennet.

The lactoalbumin fraction is a fraction of thermolabile whey proteins that does not precipitate from whey when it is half-saturated with ammonium sulfate. It is represented by b-lactoglobulin and a-lactoalbumin and serum albumin.

b-lactoglobulin is the main whey protein. Insoluble in water, soluble only in dilute salt solutions. Contains free sulfhydryl groups in the form of cysteine ​​residues, which are involved in the formation of the taste of boiled milk during heat treatment of the latter. a-lactoalbumin is the second major protein in whey. Plays a special role in the synthesis of lactose; it is a component of the enzyme lactose synthetase, which catalyzes the formation of lactose from uridine diphosphate galactose and glucose.

Serum albumin passes into milk from the blood. The content of this fraction in the milk of cows with mastitis is significantly higher than in the milk of healthy cows.

Immunoglobulins are a fraction of thermophilic whey proteins precipitated from whey when it is half-saturated with ammonium sulfate or saturated with magnesium sulfate. It is a glycoprotein. Unites a group of high molecular weight proteins that have common physicochemical properties and contain antibodies. In colostrum, the amount of these proteins is very large and amounts to 50-75% of the total protein content of colostrum.

Immunoglobulins are very sensitive to heat. Immunoglobulin is divided into three classes: Ug. , Ur M (UM) and Ur A (UA), and the Ur class is in turn divided into 2 subclasses: Ur (U1) and Ur 2 (U2). The main fraction of immunoglobins is Ur 1

The proteozo-peptone fraction (20%) refers to thermostable high-molecular peptides that do not precipitate when kept at 95°C for 20 minutes. and subsequent acidification to pH 4.6, but precipitated with 12% trichloroacetic acid. The proteozo-peptone fraction is a mixture of fragments of milk protein molecules. This fraction is intermediate between the protein substances themselves and polypeptides. Electrophoresis in polyacrylamide gel revealed about 15 electrophoretically different zones, the main ones - components 3,5 and 8 - are characterized by a low content of aromatic amino acids and methionine and a relatively high content of glutamic and aspartic amino acids. Contain carbohydrates.

5. Physical properties of milk

1). Density, viscosity, surface tension.

2). Osmotic pressure and freezing point.

3). Specific electrical conductivity.

The density of milk or volumetric mass p at 20°C ranges from 1.027 to 1.032 g/cm2, and is expressed in degrees of lactodensimeter. Density depends on temperature (decreases as it increases), chemical composition(decreases with increasing fat content and increases with increasing amounts of proteins, lactose and salts), as well as the pressure acting on it.

The density of milk, determined immediately after milking, is lower than the density measured after a few hours by 0.8-1.5 kg/m3. This is due to the volatilization of some gases and an increase in the density of fat and proteins. Therefore, the density of prepared milk must be measured no earlier than 2 hours after milking.

The density value depends on the lactation period, animal diseases, breeds, and feed rations. So. Colostrum and milk obtained from different cows have a high density due to the increased content of proteins, lactose, salts and other components.

Density is determined by various methods, technometric, hydrometric and hydrostatic balances (density of ice cream and milk in Germany).

The density of milk is influenced by all its components - their density, which have the following density:

water - 0.9998; protein - 1.4511; fat - 0.931;

lactose - 1.545; salt - 3,000.

The density of milk varies depending on the solids and fat content. dry matter increases density, fat decreases. Density is influenced by protein hydration and the degree of fat hardening. The latter depends on temperature, processing method and partly on mechanical influences. As temperature increases, the density of milk decreases. This is explained primarily by changes in the density of water, the main component of milk. In the temperature range from 5 to 40°C, the density of fresh skim milk in terms of the density of water decreases more strongly with increasing temperature. This deviation is not observed in experiments with a 5% lactose solution.

Therefore, the decrease in milk density can be explained by changes in protein hydration. In the temperature range from 20 to 35°C, a particularly strong drop in cream density can be observed. It is caused by the “solid-liquid” phase transition in milk fat.

Expansion coefficient milk fat significantly higher than water. For this reason the density raw milk with temperature fluctuations it changes more than the density of skim milk. These changes are greater the higher the fat content.

There is a direct relationship between density, fat content and dry fat-free residue. Since the fat content is determined by the traditional method, and the density is measured quickly with a hydrometer, it is possible to quickly and easily calculate the solids content of milk without the laborious and time-consuming determination of dry substances by drying at 105 ° C. Why are conversion formulas used:

C=4.9×F+A + 0.5; SOMO=F+A+ 0.76,

where C is the mass fraction of dry substances, %

SOMO - mass fraction of dry skimmed milk residue, %; F - mass fraction of fat, %; A is the density in hydrometer degrees, (oA); 4.9, 4, 5; 0.5; 0.76 - constant coefficients.

The density of individual dairy products, like the density of milk, depends on the composition. The density of skim milk is higher than that of raw milk and the coefficients are constant.

The density of individual dairy products, like the density of milk, depends on the composition. The density of skim milk is higher than that of raw milk and _________. As fat increases, the density of the cream decreases. Determining the density of solid and pasty dairy products is more difficult than liquid ones. For milk powder, a distinction is made between actual density and bulk density. To control the actual density, special numbers are used. Density butter, like milk powder, depends not only on the amount of moisture and dry fat-free residue, but also on the air content. The latter is determined by the flotation method. This allows you to determine the air content in the oil by its density. This method is approximate, but in practice it is sufficient.

The density of milk changes when adulterated - it decreases when H2O is added, and increases when skimmed or diluted with skim milk. Therefore, the density value indirectly judges the naturalness of milk if falsification is suspected. However, milk that does not meet the requirements of GOST 13264-88 in terms of density, i.e., below 1.027 g/cm3, but whose integrity is confirmed by a stall test, is accepted as varietal.

The viscosity or internal friction of normal milk at 20°C is on average 1.8 × 10-3 Pa.s. It depends mainly on the content of casein and fat, the dispersion of casein micelles and fat globules, the degree of their hydration and aggregation; whey proteins and lactose have little effect on viscosity.

During storage and processing of milk (pumping, homogenization, pasteurization, etc.), the viscosity of milk increases. This is explained by an increase in the degree of fat dispersion, enlargement of protein particles, adsorption of proteins on the surface of fat globules, etc.

Of practical interest is the viscosity of highly structured dairy products - sour cream, yogurt, fermented milk drinks, etc.

Surface tension of milk is lower than the surface tension of H2O (equal to 5×10-3 n/m at t -20°C). The lower value of surface tension compared to H2O is explained by the presence of surfactants in milk - phospholipids, proteins, fatty acids, etc.

The surface tension of milk depends on its temperature, chemical composition, state of proteins, fat, lipase activity, storage duration, technical processing modes, etc.

Thus, surface tension decreases when milk is heated and especially strongly when it is lysed. since as a result of fat hydrolysis they form surfactants - fatty acids, di- and monoglycerides, which reduce the surface energy.

The boiling point of milk is slightly higher than H2O due to the presence of salts and partly sugar in milk. It is equal to 100.2°C.

Specific electrical conductivity. Milk is a poor conductor of heat. It is caused mainly by Cl-, Na+, K+, N ions. Electrically charged casein, whey proteins. It is equal to 46×10-2 Sm-1 depends on the lactation period, breed of animals, etc. Milk obtained from animals with mastitis has an increased electro_______________________

Osmotic pressure and freezing point. The osmotic pressure of milk is close in value to the osmotic pressure of the animal's blood and averages 0.66 mg. It is caused by highly dispersed substances: lactose and chlorides. Protein substances and colloidal salts have little effect on osmotic pressure; fat has virtually no effect.

Osmotic pressure is calculated from the freezing point of milk, which is equal to -0.54 ° C according to the formula according to the laws of Raoult and Van't Hoff

Rosm. = t×2.269/K, where t is the decrease in the freezing temperature of the solution under study; WITH; 2.269 - osmotic pressure of 1 mole of substance in 1 liter of solution, MPa; K is the cryoscopic constant of the solvent; for water it is 1.86.

Therefore: R osm. =0.54×2.269/1.86+0.66 MPa.

The osmotic pressure of milk, like other physiological fluids of animals, is maintained at a constant level. Therefore, when the chloride content in milk increases as a result of a change in the physiological state of the animal, especially before the end of lactation or during illness, there is a simultaneous decrease in the amount of another low-molecular component of milk - lactose.

Freezing point is also a constant physical and chemical property of milk, since it is determined only by the truly soluble components of milk: lactose and salts, the latter being contained in a constant concentration. The freezing temperature varies within a narrow range from -0.51 to -0.59°C. It changes during the lactation period when the animal becomes ill and when milk, water or soda are adulterated. And due to the deviation of lactose increment. At the beginning of lactation, the freezing temperature decreases (-0.564°C) and in the middle it increases (-0.55°C); at the end it decreases (-0.581оС).

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