RU2529707C2 - Method of producing whey protein hydrolysate with high degree of hydrolysis and low residual antigenicity - Google Patents

Abstract

FIELD: chemistry.

SUBSTANCE: invention relates to biotechnology and provides a method of producing a whey protein hydrolysate with a high degree of hydrolysis and low residual antigenicity. The method includes preparing an aqueous mixture of whey proteins from a dry concentrate of native whey proteins or from a protein mass obtained from denatured whey proteins and water, containing 8.0-10% dry substances, including 6.6-8.5% protein, establishing active acidity at 6.5-7.0 pH units, heating to 45-48°C, adding an enzyme composition of 1.5-2.0% pancreatin enzymatic preparation with activity of 45 units/g or 15-20% minced bovine pancreatic gland with activity of 4.5 units/g, 0.5-1.0% Protamex enzymatic preparation and 2.0-2.5% Flavourzyme 1000 L enzymatic preparation, performing enzymatic hydrolysis at 45-48°C in the presence of 0.30-0.33 vol% chloroform, for 18-24 hours until achieving content of amine nitrogen in the mixture of 500-600 mg%. The obtained hydrolysate is heated to 87-90°C in order to inactivate enzymes, cooled, filtered, vacuum concentrated and spray-dried.

EFFECT: invention enables to obtain protein hydrolysates with high degree of hydrolysis and low residual antigenicity and increases biological and nutritional value thereof, improves organoleptic properties and storage stability.

4 cl, 5 dwg, 1 tbl, 6 ex

Description

The invention relates to the dairy industry, in particular to the production of purified whey protein hydrolysates with a high degree of hydrolysis and low residual antigenicity, used in the manufacture of a wide range of dietary (therapeutic and prophylactic) food products, including for children and adults suffering from food allergies.

The method includes preparing an aqueous mixture of whey proteins from a dry concentrate of native whey proteins or from a protein mass from denatured whey proteins and water containing from 8.0% to 10.0% solids, including from 6.6 to 8.5% protein, the establishment of active acidity at the level of 6.5-7.0 units. pH, heating to 45-48 ° C, application of the enzyme composition from 1.5-2.0% pancreatin enzyme preparation with an activity of 45 units / g or 15-20% of minced cattle pancreas with an activity of 4.5 units. / g, 0.5-1.0% of the enzyme preparation Protamex and 2.0-2.5% of the enzyme preparation Flavourzyme 1000 L, enzymatic hydrolysis at a temperature of 45-48 ° C in the presence of 0.30-0.33 vol. % chloroform, for 18-24 hours until the amine nitrogen content in the mixture is 500-600 mg%. The resulting hydrolyzate is heated to 87-90 ° C to inactivate the enzymes, cooled, filtered, concentrated in vacuo and dried by spraying.

The invention allows to obtain a protein hydrolyzate with a high degree of hydrolysis, having a balanced amino acid composition close to the ideal protein, good taste and low residual antigenicity.

The obtained hydrolyzate is characterized in that when it is obtained from a whey protein concentrate it contains less than 7% lactose, and when it is obtained from denatured whey protein from a protein mass, it is low-lactose with a lactose content of not more than 0.5%, and more than 80% of the protein material is concentrated in the low molecular weight fraction peptides and free amino acids in the range of molecular weights of less than 2.0 kDa. The invention improves the biological, nutritional value, organoleptic properties and quality of the obtained hydrolyzate with the possibility of its use in hypoallergenic mixtures and other functional products.

Known methods for producing milk protein hydrolysates with reduced antigenicity (including whey) using proteases of microbial and animal origin.

Closest to the technical solution to the claimed hydrolyzate is the method (patent for invention No. 2407399, IPC A23J 3/30, A23J 3/34. A method for producing partial protein hydrolysates and milk formulas containing them. - Application. March 16, 2006, publ. December 27, 2010), which provides for the preparation of a hydrolyzate from a mixture of whey protein and casein, while the ratio of whey protein: casein is approximately 60:40. Hydrolysis of the protein mixture is carried out using the Amano N protease (supplied by Amano Enzyme U.S. A. Co., Ltd., Elgin, IL) isolated from the Bacillus subtilis strain, introduced in an amount of 0.5-1.0% of the mass fraction of protein in the mixture. During hydrolysis, the temperature of the mixture is maintained at a level of 50-60 ° C, and its active acidity is at a level of from 6.5 to 8 units. pH, by automatically titrating the mixture with a solution of sodium hydroxide or potassium. The hydrolysis process is completed when the protein mixture reaches a degree of hydrolysis of 4-10%. The invention allows to obtain a protein hydrolyzate with a pleasant taste and emulsifying properties that does not cause an immune response in the form of IgG antibodies to serum proteins of cow's milk. At the same time, peptides with a mass of less than 2.0 kDa comprise at least 70% of the weight of the hydrolyzate.

The disadvantage of this method, an analog of the claimed process, is the limited degree of hydrolysis (4-10%). In the hydrolyzate with this level of hydrolysis, high molecular weight protein structures may remain that retain the antigenic properties of the original protein.

The objective of the invention is to develop a method for the production of whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity, with high biological value at low cost, for the manufacture of which does not require complex and expensive equipment and materials.

The technical result of the claimed invention on a method for the production of a whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity consists in increasing the biological, nutritional value, improving the organoleptic properties and storage stability of the obtained hydrolyzate with a high degree of hydrolysis with the possibility of its use in hypoallergenic mixtures and other functional products destination.

The technical result is achieved by the fact that in the method for the production of a whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity, which involves preparing an aqueous mixture of whey proteins, establishing the optimal active acidity, heating the mixture, introducing the enzyme composition, carrying out enzymatic hydrolysis, heating to inactivate the enzymes, cooling , filtration, concentration and drying, according to the invention:

1. To prepare an aqueous mixture of whey proteins using

- a dry concentrate of native whey proteins obtained by ultrafiltration and diafiltration with spray drying, with a protein content of at least 80%, or

- a protein mass of denatured whey proteins obtained by thermo-acid coagulation and precipitation of a solution of native whey protein concentrate from the solution, additionally subjected to freeze, soak, freeze, thaw and rinse with water to remove lactose, salts and acid.

2. Before hydrolysis, an aqueous mixture of whey proteins is prepared containing 8.0-10.0% solids, including 6.4-8.5% proteins.

3. Set the active acidity of the aqueous whey protein mixture at the level of 6.5-7.0 units. pH, heated to 45-48 ° C and make the composition of the enzymes in percent by weight of protein in the mixture:

- 1.5-2.0% pancreatin enzyme preparation with an activity of 45 units / g, 0.5-1.0% Protamex enzyme preparation and 2.0-2.5% Flavourzyme 1000 L enzyme preparation, or

- 15-20% minced cattle pancreas with an activity of 4.5 units / g, 0.5-1.0% of the enzyme preparation Protamex and 2.0-2.5% of the enzyme preparation Flavourzyme 1000L.

4. Hydrolysis is carried out at a temperature of 45-48 ° C and the active acidity of the mixture is 6.5-7.0 units. The pH, which is maintained by adding a solution of sodium hydroxide, in the presence of 0.30-0.33 vol.% chloroform for 18-24 hours to a content of amine nitrogen in a mixture of 500-600 mg%.

5. The resulting hydrolyzate is heated to 87-90 ° C, incubated for 8-10 minutes, cooled to 65-70 ° C and filtered to obtain a clear filtrate free of insoluble residue.

6. The resulting filtrate is concentrated on a vacuum evaporator to a mass fraction of solids of 35-37% and dried on a spray dryer at an inlet temperature of 130-140 ° C and an output of 80-85 ° C.

The claimed technical result is achieved by combining the following factors:

1. To obtain the hydrolyzate, whey protein is used. It is known that milk whey proteins are more complete in their amino acid composition than casein, in particular because of the higher content of branched chain amino acids and sulfur-containing amino acids than casein (Food chemistry / Nechaev A.P., Traubenberg S. E., Kochetkova A.A. et al. Edited by A.P. Nechaev, 2nd edition, revised and revised - St. Petersburg: GIORD, 2003). Also, recent studies by foreign scientists have established that whey protein hydrolysates contain peptides with biological activity (Ile-Val, Leu-Val, Val-Leu, Ile-Ile, Leu-Ile, Ile-Leu), formed during the hydrolysis of whey proteins and containing its composition of branched chain amino acids. These peptides significantly enhance the absorption of glucose in the muscles, facilitating the processes of building skeletal muscle tissue (Morifuji M, Koga J, Kawanaka K, Higuchi M: Branched-chain ammo acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles). The results of other studies showed that only the use of whey protein hydrolyzate stimulated the accelerated accumulation of glycogen level in skeletal muscle, which was not observed when taking casein hydrolysates and branched chain free amino acid preparations (Morifuji M, Kanda A, Koga J, Kawanaka K, Higuchi M: Post-exercise carbohydrate plus whey protein hydrolysates supplementation increases skeletal muscle glycogen level in rats).

To implement the technology of protein hydrolyzate with low residual antigenicity described in this invention, as a source of whey protein using:

- a concentrate of native whey proteins with a protein content of 80%, characterized by the presence of lactose, salts and acids;

- protein mass from denatured whey proteins obtained by thermo-acid precipitation from a solution of native whey proteins and washing with water.

The use of protein mass from denatured whey proteins is due to the fact that upon receipt of the indicated hydrolyzate from the concentrate of native whey proteins, a certain amount of native whey proteins that are not affected by hydrolysis, which can cause an allergic reaction, remains in the fermentation mixture. The conversion of native whey protein into an insoluble form by thermal coagulation allows us to solve the problem of the presence of undigested proteins in the hydrolyzate. In addition, the whey protein concentrate contains lactose, salts and a residual amount of acids, which are completely converted into the hydrolyzate and limit its use in case of contraindications to the absorption of lactose and high salt content.

Protein mass from denatured whey proteins is obtained by thermoacid deposition from an aqueous solution of a concentrate of native whey proteins with a mass fraction of solids of 6.0-7.0%, dehydration of the protein precipitate by self-pressing, freezing, aging, thawing, washing with water and pressing. The protein mass contains 30-32% solids, 82-85% protein in solids and only trace amounts of native whey proteins are present. Washing the protein mass also helps to remove lactose from it and lower the content of salts and acid.

As a result of freezing, the structure of the protein mass changes. The protein mass obtained by thermoacid deposition, after self-pressing, has a finely dispersed structure and has a significant water-holding ability (figure 1). Moisture separation is difficult, as small particles of protein quickly clog the pores of the filter material. After freezing, holding and thawing, the structure of the protein mass becomes coarsely dispersed, it takes the form of loose grains, easily giving off moisture, washed in water without the formation of protein dust and quickly separated from the wash water on the filter material (figure 2).

Washing is carried out by a twofold volume of partially demineralized water. The effectiveness of the washing process is controlled by the active acidity of the protein mass. Rinsing, with a complete replacement of the wash water, is repeated 3 times.

Indicators showing the effect of washing the protein mass are shown in table 1.

Table 1 The comparative content of ballast substances in the protein mass before and after washing with water Indicator Before rinsing After rinsing The lactose content,% 3.5-4.0 0.1-0.2 The salt content,% (in terms of Na lactate) 2.0-2.5 1.5-1.75 The acid content,% (in terms of lactic acid) 0.7-0.9 0.4-0.5 Active acidity, units pH 5.4-5.5 6.4-6.6

Washing the protein mass with water removes residual amounts of water-soluble proteins, lactose, salts and acids from it. Moreover, after removal of acids from the protein mass, significant amounts of alkali are not required to maintain the pH at the optimum level for enzymes, that is, the final product contains significantly less salts than in the prototype, which improves the organoleptic properties and the quality of the resulting hydrolyzate. As a result, the amount of technically harmful salts — lactates — is reduced in the hydrolyzate, which, due to its high hygroscopicity, impedes the drying process of the hydrolyzate, causing it to stick to the walls of the dryer and clump the dried product. The formation of adverse unwanted impurities caused by the reactions of free amino acids in the product with residual amounts of lactose, salts and acids, including Maillard compounds, melanoidins, and caramelization products, is also reduced. These impurities give the product an undesirable color, degrade its taste and reduce its biological value.

2. Enzymatic hydrolysis is carried out by a composition of enzymes under optimal conditions.

The hydrolysis of the protein substrate is carried out by a specially selected enzyme composition, which includes: a complex of proteolytic enzymes of the pancreas of cattle, a complex of proteases isolated from bacteria of the genus Bacillus introduced in the enzyme preparation Protamex, and a proteinase-peptidase complex isolated from microscopic Aspergillus Oryzae fungi as part of the enzyme preparation Flavourzyme. The use of a complex of proteinases and peptidases of various specificities allows us to achieve the necessary specificity and depth of hydrolysis of the substrate and to obtain a product with high yield and good organoleptic characteristics.

The used composition of enzyme preparations forms a complex of proteinases and peptidases with different specificity and high activity, which allows for deep hydrolysis of the protein in one stage and to obtain a relatively small amount of bitter hydrophobic peptides and free aromatic amino acids forming them in the product. As a result, good taste qualities of the finished product are achieved.

3. Concentration and drying of the hydrolyzate are carried out subject to standard optimal conditions for similar products.

The advantage of the proposed method in comparison with the prototype is:

- the complete exclusion from the composition of the nitrogen fraction of the hydrolyzate of native high molecular weight proteins by coagulation of the protein substrate and converting its protein complex into a completely insoluble form. Further, in the process of enzymatic hydrolysis, the enzymatic cleavage of the precipitated protein complex occurs with the release of peptides and free amino acids into the aqueous phase. As a result, the nitrogenous fraction of the hydrolyzate is represented only by protein hydrolysis products and does not contain native proteins that can cause allergenic reactions;

- due to washing the denatured protein, leaching of some salts and acids from it is achieved. As a result of the decrease in the acidity of the protein substrate, a substantial addition of alkali to the reaction mixture is not required to maintain its active acidity at an optimal level, and the final product contains significantly less salts than in the prototype, which improves the organoleptic properties and quality of the resulting hydrolyzate and favors its use in infant formula ;

- the inventive hydrolyzate obtained from the washed denatured protein contains a low amount of lactose (not more than 0.5% of the mass fraction of solids) and can be used in infant formula and other functional products for patients with lactose intolerance;

- the composition of enzymes from cattle pancreas, Protamex enzyme preparation and Flavourzyme enzyme preparation used for hydrolysis of an aqueous mixture of whey proteins has a high complex endoproteinase and exopeptidase activity, which allows for deep hydrolysis of the protein in one stage. The specificity of the complex of enzyme preparations used in the claimed method is such that when it acts on the substrate, a relatively smaller amount of free aromatic amino acids and short peptides with a bitter taste are formed. As a result, the palatability of the resulting product improves;

- in the inventive enzymatic hydrolyzate of more than 80% of the protein material is concentrated in the fraction of low molecular weight peptides in the range of molecular weights of less than 2.0 kDa (Fig.3), which allows to achieve low residual antigenicity not exceeding 1 · 10 ^-5 antigenicity of the original whey protein. Due to this, the inventive hydrolyzate can be used as a protein component for the preparation of products of therapeutic and preventive nutrition of children and adults with food allergies;

- the inventive method is implemented using widespread in the food industry capacitive equipment (tanks and baths with mixers) and does not require significant capital costs for implementation in production, thereby reducing the cost of the hydrolyzate.

The claimed combination of features allows to obtain a high quality whey protein hydrolyzate: with a high degree of hydrolysis and low residual antigenicity, with a low content of unsplit proteins, which is comparable to or exceeds the prototype.

Deviation from the claimed features to a greater or lesser extent leads to a decrease in the nutritional and biological value of the resulting hydrolyzate, deterioration in its quality and organoleptic properties.

The technical result of the claimed invention on a whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity, obtained by the claimed method, also lies in the possibility of its use as a preventive and therapeutic nutrition for persons with lactose intolerance.

The technical result is achieved by the fact that in the inventive hydrolyzate with a high degree of hydrolysis, more than 80% of the protein material is concentrated in the fraction of low molecular weight peptides in the molecular weight range of less than 2.0 kDa, the content of peptides with a molecular weight range of 2.0-6.0 kDa does not exceed 20 %, the content of peptides with a molecular weight of more than 6.0 kDa does not exceed 1%. The inventive hydrolyzate obtained by the claimed method.

All of the above proves in comparison with the prototype increased biological and nutritional value, organoleptic properties, the quality of the claimed hydrolyzate.

Brief Description of the Drawings

The figure 1 presents a micropreparation of the precipitate of denatured whey proteins after precipitation of the protein (finely dispersed structure of protein particles, firmly retaining moisture).

PA figure 2 presents a micropreparation of the precipitate of denatured whey proteins after freezing-thawing (protein aggregates in the aqueous phase).

The figure 3 presents the molecular weight distribution of nitrogen fractions in the protein hydrolyzate obtained by the claimed method.

The figure 4 presents the molecular weight distribution of the nitrogenous fractions of the protein hydrolyzate obtained by enzymatic hydrolysis of native whey proteins.

The figure 5 presents the molecular weight distribution of the nitrogenous fractions of the protein hydrolyzate obtained by enzymatic hydrolysis of denatured whey proteins.

A method for the production of whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity is as follows.

A dry concentrate of native whey proteins containing 95% solids and at least 80% proteins is mixed with water in a mass ratio of 1: 8.5-1: 11.0 to obtain a mixture with a mass fraction of solids of 8.0-10.0 % (proteins 6.7-8.4%). Set the active acidity of the mixture at the level of 6.5-7.0 units. pH by adding 20% sodium hydroxide solution and heated to 45-48 ° C. A composition of enzymes is added to the mixture prepared for hydrolysis (in% of the mass of proteins in the mixture): 1.5-2.0% pancreatin enzyme preparation with an activity of 45 units / g or 15-20% cattle pancreas with activity 4.5 units / g, 0.5-1.0% of the enzyme preparation Protamex with an activity of 1.5 AU / g and 2.0-2.5% of the enzyme preparation Flavourzyme 1000 L with an activity of 1000 LAPU / g. Dry pancreatin enzyme preparation is preliminarily diluted in pasteurized drinking water with a temperature of 28-30 ° C. Hydrolysis is carried out at a temperature of 45-48 ° C and the active acidity of the mixture is 6.5-7.0 units. The pH, which is maintained by adding a solution of sodium hydroxide, in the presence of 0.30-0.33 vol.% chloroform for 18-24 hours to an amine nitrogen content in the mixture of 500-600 mg%. The hydrolyzate is heated to 87-90 ° C, kept for 8-10 minutes to inactivate the enzymes, cooled to 65-70 ° C and filtered on a frame filter press using filter material with a pore diameter of 0.2 μm, the transparent filtrate is concentrated on vacuum evaporator at a temperature of 46-48 ° C and a dilution of 0.92-0.94 ati to a mass fraction of solids of 35-37%, the concentrate is dried on a spray dryer at an inlet temperature of (130-140) ° C and the outlet is (80-85) ° C.

In the case of the preparation of an aqueous mixture with a protein mass of denatured whey proteins, a protein mass of denatured whey proteins is first obtained. For this, an aqueous solution of whey proteins with a mass fraction of solids of 6.0-7.0% is prepared from a dry concentrate of native whey proteins containing at least 80% of proteins. The resulting solution is heated to a temperature of 85-90 ° C and acidified to a pH of 5.4-5.5 with hydrochloric acid, resulting in coagulation of whey proteins, accompanied by the formation of a precipitate. The upper clarified layer is removed, the remaining protein precipitate is poured into a self-pressing bath using a lavsan filter cloth. Moisture is separated until the suspension takes the form of a protein mass, characterized by a non-fluid, granular structure. The result is a protein mass with a mass fraction of solids of 16-18%. Protein mass is frozen to a temperature of minus 18 to minus 24 ° C and kept at this temperature for 5-7 days. The frozen protein mass is thawed at a temperature of 18-22 ° C, the separated moisture is removed by self-pressing, the dehydrated protein mass is washed with a double volume of partially demineralized water three times, and the washing water is removed by self-pressing. The dehydrated protein mass is pressed at a pressure of 4.5-5.0 ati for 1.5-2.0 hours to obtain a pressed protein mass with a mass fraction of solids of 30-32%, protein substances in a dry residue of 82-85%. The washed pressed protein mass in the claimed invention is called the protein mass of denatured whey proteins.

The protein mass of denatured whey proteins is mixed with water in a mass ratio of 1: 2.0 - 1: 3.0 to obtain a mixture with a mass fraction of solids of 8.0-10.0% (proteins 6.6-8.5%) . Next, the process is carried out similarly to the method described above.

Example 1

22.4 kg of dry concentrate of native whey proteins of milk containing at least 80% of proteins (KSB-80) are mixed with 246.4 kg of water. The mixture is stirred until the dry protein concentrate is completely dissolved. A 20% sodium hydroxide solution in an amount of 400 ml was added to the protein suspension to establish a pH of 7.0 and heated to a temperature of 48 ° C. Pancreatin with an activity of 45 units / g in an amount of 0.27 kg is dissolved in 1 liter of water until a homogeneous consistency is obtained. A suspension of pancreatin, 0.1 kg of the enzyme preparation Protamex with an activity of 1.5 AU / g and 0.36 kg of the enzyme preparation Flavourzyme 1000 L with an activity of 1000 LAPU / g is added to the heated protein suspension. Add 810 ml of chloroform. The active acidity of the reaction mixture is adjusted to pH 7.0 by adding 600 ml of 20% NaOH. Enzymatic hydrolysis is carried out at a temperature of 48 ° C for 18 h until the accumulation of amine nitrogen 500 mg%. In the process of hydrolysis, the active acidity of the mixture is controlled by keeping it at a pH of 6.5 with 20% NaOH in an amount of 300 ml. The hydrolyzate is heated to a temperature of 87 ° C, incubated for 10 minutes, cooled to a temperature of 65 ° C. The heated hydrolyzate is filtered on a frame filter press using filter paper and a belting-type filter cloth under a pressure of 0.02 MPa as a filter baffle. Get 230 l of a transparent filtrate. After filtration is completed, the filter press is washed with 70 L of water to remove residual hydrolyzate. The filtrate and washing water are concentrated on a vacuum evaporator at a temperature of 48 ° C and a vacuum of 0.92 atm to a mass fraction of solids of 37%. 51.1 kg of concentrate are obtained. The concentrate is dried on a spray dryer at an inlet temperature of 140 ° C and an outlet of 85 ° C. The mass of dry powder is 18.5 kg.

The resulting product is characterized by the following indicators:

Indicator Moisture content, % 5.5 Mass fraction of total nitrogen,% 11.5 Mass fraction of amine nitrogen,% 6.2 Mass fraction of lactose,% 6.8 Mass fraction of ash residue,% 5.8 Active acidity (ppm solids 2%), units pH 6.5 Residual antigenicity Less than 1 · 10 ^-5

The distribution of nitrogenous fractions by molecular weight in the hydrolyzate obtained in this embodiment of the invention is shown in figure 4.

Example 2

Prepare a protein mixture for hydrolysis analogously to example 1. Instead of pancreatin, minced cattle pancreas in the amount of 2.7 kg. Enzymatic hydrolysis, heating, cooling, filtration, concentration and drying are carried out analogously to example 1. The mass of dry powder is 18.9 kg

Example 3

28.0 kg of dry concentrate of native whey proteins of milk containing at least 80% of proteins (KSB-80) are mixed with 238.0 kg of water. The mixture is stirred until complete dissolution of the dry protein concentrate (10%). A 500% sodium hydroxide solution in an amount of 500 ml was added to the protein suspension to establish a pH of 7.0 and heated to a temperature of 45 ° C. Pancreatin with an activity of 45 units / g in an amount of 0.45 kg is dissolved in 1.5 l of water until a homogeneous consistency is obtained. A suspension of pancreatin, 0.22 kg of the Protamex enzyme preparation with an activity of 1.5 AU / g and 0.56 kg of Flavourzyme 1000 L enzyme preparation with an activity of 1000 LAPU / g are added to the heated protein suspension. Add 880 ml of chloroform. The active acidity of the reaction mixture is adjusted to pH 7.0 by adding 750 ml of 20% NaOH. Enzymatic hydrolysis is carried out at a temperature of 45 ° C for 24 hours before the accumulation of amine nitrogen 600 mg%. The hydrolyzate is heated to a temperature of 90 ° C, incubated for 8 minutes, cooled to 70 ° C. The heated hydrolyzate is filtered on a frame filter press as in Example 1. The clear filtrate is concentrated to a mass fraction of solids of 35% and dried as in Example 1. The dry powder mass is 22.1 kg.

Example 4

Prepare a protein mixture for hydrolysis analogously to example 3. Instead of pancreatin, minced cattle pancreas in the amount of 4.5 kg is introduced. Enzymatic hydrolysis, heating, cooling, filtration, concentration and drying are carried out analogously to example 1. The mass of dry powder is 22.6 kg

Example 5

26 kg of dry whey protein concentrate are dissolved in 386 l of softened water, the resulting solution is heated to a temperature of 90 ° C, acidified with a 10% solution of hydrochloric acid in an amount of 2.3 l to pH 5.4 and left without stirring to precipitate coagulated proteins in within 2 hours. The upper clarified layer is removed by siphoning, the protein precipitate is poured into a self-pressing bath lined with lavsan filter cloth. Water is separated until the suspension takes the form of a protein mass, characterized by a non-fluid structure. The result is a protein mass with a mass fraction of solids of 18%. The amount of protein mass is 131.6 kg. The protein mass is frozen to a temperature of minus 18 ° C and maintained at this temperature for 7 days. Frozen protein mass is thawed at a temperature of 18 ° C, the separated moisture is removed by self-pressing, the dehydrated protein mass in the amount of 84.8 kg is poured into 170 l of partially demineralized water at a temperature of 20 ° C, the suspension is kept with periodic stirring for 1 hour. The washing water is removed by self-pressing of protein mass until a non-flowing consistency is obtained. The washing of the protein mass is repeated two times. After the third washing, the dehydrated protein mass is transferred to cheese compression molds and pressed at a pressure of 4.5-5.0 bar for 2.0 hours. The pressed protein mass is obtained in an amount of 66.3 kg with a mass fraction of solids of 32%, protein substances in the dry residue of 85%. The pressed protein mass is mixed with 198.9 kg of water. Further, the process is carried out analogously to example 1. The mass of dry powder 17.6 kg

The resulting product is characterized by the following indicators:

Indicator Moisture content, % 5.5 Mass fraction of total nitrogen,% 12.3 Mass fraction of amine nitrogen,% 6.4 Mass fraction of lactose,% 0.5 Mass fraction of ash residue,% 3.8 Active acidity (ppm solids 2%), units pH 6.5 Residual antigenicity Less than 1 · 10 ^-5

The distribution of nitrogenous fractions by molecular weight in the hydrolyzate obtained in this embodiment of the invention is shown in figure 5.

Example 6

33 kg of a dry whey protein concentrate are dissolved in 415 l of softened water, the resulting solution is heated to a temperature of 85 ° C, acidified with a 10% solution of hydrochloric acid in an amount of 2.1 l to a pH of 5.5 and left without stirring to precipitate coagulated proteins in within 2 hours. The upper clarified layer is removed by siphoning, the protein precipitate is poured into a self-pressing bath lined with lavsan filter cloth. Water is separated until the suspension takes the form of a protein mass characterized by a curd structure. The result is a protein mass with a mass fraction of solids of 16%. The amount of protein mass is 188.2 kg. The protein mass is frozen to a temperature of minus 24 ° C and maintained at this temperature for 5 days. The frozen protein mass is thawed at a temperature of 22 ° C, the separated moisture is removed by self-pressing, the dehydrated protein mass in the amount of 108.9 kg is poured into 204 l of partially demineralized water at a temperature of 20 ° C, the suspension is kept with periodic stirring for 1 hour. The washing water is removed by self-pressing of the protein masses to obtain a curd texture. The washing of the protein mass is repeated three times. After the third washing, the dehydrated protein mass is transferred to cheese pressing molds and pressed at a pressure of 4.5-5.0 bar for 1.5 hours. The pressed protein mass is obtained in an amount of 91.2 kg with a mass fraction of solids of 30%, protein substances in the dry residue of 82%. The pressed protein mass is mixed with 182.0 l of water. Further, the process is carried out analogously to example 3. The mass of dry powder is 21.5 kg.

Claims (4)

1. A method of producing a whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity, comprising preparing an aqueous mixture of whey proteins, enzymatic hydrolysis, heating the hydrolyzate to inactivate enzymes, cooling, filtering, concentrating and drying, characterized in that preparing an aqueous mixture of whey proteins from dry concentrate of native whey proteins or from protein mass from denatured whey proteins and water, containing from 8.0 to 10.0% solids, while m number from 6.6 to 8.5% protein, the active acidity of the mixture is set at 6.5-7.0 units. pH, the mixture is heated to 45-48 ° C, a composition of enzymes from 1.5-2.0% pancreatin enzyme preparation with an activity of 45 units / g or 15-20% of minced cattle pancreas with an activity of 4.5 units / g, 0.5-1.0% of the enzyme preparation Protamex and 2.0-2.5% of the enzyme preparation Flavourzyme 1000 L and carry out enzymatic hydrolysis at a temperature of 45-48 ° C in the presence of 0.30-0.33 vol.% chloroform, for 18-24 hours until the amine nitrogen content in the mixture is 500-600 mg%, the resulting hydrolyzate is heated to 87-90 ° C to inactivate the enzymes, cooled, filtered, concentrated in vacuo and ysushivayut sputtering method. 2. A method for the production of whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity according to claim 1, characterized in that a dry concentrate of native whey proteins with a protein mass fraction of at least 80% is used to prepare an aqueous mixture of whey proteins. 3. A method for the production of whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity according to claim 1, characterized in that for the preparation of an aqueous mixture of whey proteins using a protein mass of denatured whey proteins with a solids content of 30-32% and a protein content of dry residue 82-85%. 4. A method of producing a whey protein hydrolyzate with a high degree of hydrolysis and low residual antigenicity according to claim 3, characterized in that the protein mass from denatured whey proteins is prepared by preparing from a dry concentrate of native whey proteins with a protein mass fraction of at least 80% aqueous whey protein solution with a mass fraction of solids of 6-7%, heating to a temperature of 85-90 ° C, acidification with hydrochloric acid to a pH of 5.4-5.5, precipitation of coagulated proteins, self-compression of precipitated proteins to mass the solids content (16-18)%, by freezing to a temperature of minus 18 ° C to minus 24 ° C, holding for 5-7 days, thawing at a temperature of 18-22 ° C, washing twice with a volume of partially demineralized water three times and pressing at a pressure of 4.5-5.0 Ati for 1.5-2.0 hours

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