DE1767800A1 - Process for the production of loosening proteins which form foam by whipping - Google Patents

Description

Applicant. "GÜNTHER PRODUCTS, INC., 701 West Sixth Street,
Galesburg, 111., V.St.A.

Process for the production of loosening, by
Beat foaming proteins

In the food industry, proteins such as egg white, hydrolyzed milk albumin and soy protein have been used as
Loosening agents used. These are capable of trapping air in an aqueous mixture, for example a basic sugar syrup used in confectioneries or flour-sugar mixtures used in bakeries. A good loosening agent must of course be able to envelop an optimal amount of air in the shortest possible time, ie it must be able to be whipped very quickly and very frothy. It is also desirable that the corresponding loosening is achieved with a minimum amount of foaming agent
will. ■

Leave egg white, hydrolyzed milk white and soy protein
use as a loosening agent for certain mixtures.

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However, in order to be able to be whipped sufficiently foamy, they must be taken in relatively large concentrations.

The same applies to those from the USA patents 2 381 407 and 2 302 029 known loosening agents. In the The products described in the former patent are made using papain as a ferment, but are bad foaming agents and when they are beaten have a relatively high density. The products according to the USA patent 2,502,029 are comparable to ordinary soy protein. In these known methods, the starting protein extracted or separated, but not hydrolyzed. The substances obtained leave in terms of their foamability and iLrss taste left a lot to be desired.

Task as *. · The invention is to create a process for the production of an egg visg product that can be beaten very well and easily *; \ mä after whipping results in loose products, is more soluble in water than the known substances and has a milder and more pleasant taste than these.

The products produced according to the invention are vegetable Proteins. An oil-free vegetable protein, preferably soy

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BATH ORIGINAL

Protein, which has conveniently been extracted in an aqueous alkali solution, is either in a basic or acidic aqueous medium hydrolyzed. The degradation takes place to a certain degree, which is determined by viscosity measurements of the aqueous solution of the hydrolyzed protein is determined. It is then modified with pepsin. The pepsin-modified hydrolyzed protein obtained in this way can be in the presence Beat the water and sugar very quickly to a light foam.

To achieve optimal results, the hydrolysed protein at its isoelectric, point in water is insoluble, but should also be sufficiently hydrolyzed such that the viscosity of a 10 vcn #igen aqueous solution at a pH 9.3 and 48 ° C not more than 100 cP, preferably 5-20 cP.

It has been found to be a hydrolyzed vegetable protein pepsin enzyme hydrolysis gives a completely different product * than the enzyme hydrolysis of unmodified protein. The otherness relates to its loosening properties, because it can be whipped into foam at least twice as well as the known and usual means and also one tastes better than this.

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«Ο

According to an exemplary embodiment of the invention, a protein-containing material, such as oil-free soya flour or flakes, with an aqueous alkali solution, for example sodium carbonate or sodium hydroxide, preferably at a pH between 7 # 5 and 10.0 and a temperature of j50 - 50 ° C extra-

Φ here. The insoluble components can be extracted from the extract solution separated either by filtration or centrifugation. The clear extraction liquid becomes quite a bit Subjected to weak alkaline hydrolysis, taking about 1-2 hours at a temperature of 50 - 85 ° C is treated with a lye, e.g. sodium or potassium hydroxide »The amount of alkali compound used is between about 5-10 percent by weight based on the protein content of the extraction liquid, of course, temperature, loading

The duration of the action and the amount of alkali depend on the desired degree of hydrolysis. It is very important to stop hydrolysis before the protein has broken down to the point where it is soluble at its normally insoluble isoelectric pH. Subsequent to the hydrolysis, the pH value is adjusted to the isoelectric pH value of the paw protein, pH 4.1-4.5 #, and the precipitated cheesy precipitate is decanted from soluble carbohydrates, minerals and the like. washed free ·.

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ORIGINAL IHSPSCTED

During the enzymatic conversion, the purified, alkaline-modified professional clot is first treated with a suitable acidifying agent, such as sulfuric or hydrochloric acid, and brought to a pH of 1.2-2.5 and a temperature of about 25-10 ° C. The pepsin (l 10,000 strength) is then usually added in an amount of 0.05-0.5 percent by weight based on the protein content of the solution. £

The enzyme conversion continues for 18-24 hours. Afterward the solution can be heated up to 6o - 70 ° C. In order to interrupt the enzyme action, the pH value is increased with Lye adjusted to 5.0 - 5.5 and the insoluble components separated by filtration or centrifugation. The clear aqueous solution containing the insoluble components is then dried by spraying to produce a very lightly colored, to form free flowing product.

Two products manufactured according to the invention, for the sake of simplicity designated as E-500, were made with soy protein, a hydrolyzed milk protein and egg white in an icebox gauze mixer and in a standard corn syrup sugar mixer to determine their sole properties.

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V.

.0 X i_ .v. -._

Table A. Blow
volume
κ / 1 Chocolate decorated 42 80/20 60 cake 38 59 136 81 (Chocolate Chiffon Pie)
% Loosening cream
medium density
used (l) g / l 138 E-500,!, Sample Grain syrup / sugar 80 4.4 66 E-5'DO, 2nd sample % Curl
funds
used (l) 74 4.4 Soy protein . 1 4.4 Egg white 1 4.4 hydrolyzed tea
Milk protein 1 4.4 1 1

(1) Percent of loosening agent based on the total dry weight,

The possible uses of a loosening agent aiit the impact strength and the relatively mild and pleasant taste _; 3 of the above-described E-500s according to the invention are diverse and versatile. One of the special properties of the S- »500 loosening proteins is their ability to loosen up mixtures of whole eggs and whip them until foamy. Egg white, soy protein and hydrolysed milk proteins do not have this effect. For example, 260 g of fresh whole eggs and 5 g of E-500 protein can be used in 2 minutes in an ¹¹ Mixmaster "whipper to a specific gravity of 0.19

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BATH ORIGINAL

be beaten. This is a stiff, firm foam that can be drawn into a battered dough and the like.

The same amount of fresh whole egg was shown with 10-15 g of egg white (or with soy protein or hydrolyzed milk protein) too , no foam formation after 10 - 15 minutes of whipping.

Accordingly, the protein products according to the invention can be used particularly well for the production of a sponge-like mixed cake when using the whole egg, add it to the dry batter mixture and whisk it into a light, frothy batter

■ will.

The E-. 5QG protein is because of its low taste and Because of its good loosening effect, it is also suitable for other products (or jacketed) biscuit products are used. When packed Baby cake or cookie dough mixes are made with the loosening agents according to the invention the impact ability as well as the volume of the albumen largely improved »

The E-500 proteins can also be used in dry batter mixes (chiffon pie mixes) that are easy to use Adding hot water in minutes to a light, flat > Let the foam beat up. This whipped foam is then placed in a cake or baking pan and cooled with it

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BATH ORIGINAL

the filling settles. For this use, the usual foaming agent should be beaten three to four times in order to achieve the same loosening and foaming.

In general, it can be said that the E-500 proteins Because of their extremely good foam-forming effect together with the low taste, especially for dry, packaged food mixtures are suitable where a quick loosening is desired. Splash cake, baby cake or cookie dough mixes, Ice cream powder and the like are only a few of the foods in which the novel protein products are used can be.

In the general manufacturing procedure described above of the proteins, the hydrolysis was carried out on the extraction liquid after the insoluble components were removed, but before the glycinin was separated from sugars, salts and the like. According to another embodiment of the According to the method according to the invention, the alkaline hydrolysis can also be carried out directly on the soya flour or the soya flakes, or it can be applied to the purified, separated glycinin precipitate (glycinin curd).

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An alkali metal or alkaline earth metal hydroxide is preferably used for the hydrolysis and it has been found that sodium hydroxide alone or together with calcium oxide is particularly effective. The hydrolysis temperature is very variable and depends on the particular prevailing conditions. However, the protein conversion (hydrolysis) is usually carried out at temperatures of 40 - 80 ° C. The enzyme conversion of the partially hydrolyzed protein takes place at a pH value of 1.2 2.5 and temperatures of 20 - 50 ° C. The concentration of 1: 10,000 pepsin (strength pepsin) is generally 0.05 - 0, 7 % of the amount of protein used. Larger amounts of pepsin can also be used, but this is not economical.

After the enzyme conversion, the pH of the reaction mass becomes prior to the separation of the soluble from the insoluble constituents usually set at 3.0-5.5. The mass can Can also be heated to 40-100 ° C to produce heat-coagulable protein to precipitate and to facilitate filtering. However, this is not absolutely necessary, it depends on the desired product. Heating can be either before or after Adjustment to the stated pH.

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ORIGINAL INSPECTED

The various conditions of alkaline hydrolysis, such as Temperature, time, concentration of the alkali solution, pH, etc. can be varied widely without affecting the properties of the end product can be significantly influenced. However, it must be noted that the individual factors are simultaneous and changed accordingly. So in general there will be a temperature decrease with a stronger lye or a longer hydrolysis egg t balanced

The invention is based on the following exemplary embodiments explained in more detail, Unless otherwise stated, the amounts are expressed in parts by weight.

example 1

50 kg oil-free Soyaflocker were slurried in water at a 1 5OO TemperatüP of 3O ⁰ C for 10 minutes. Hlerza was added 750 g of caustic soda in 2 liters of water and the Hasse was washed continuously for 1 hour. The insoluble flocculant residue was separated from the soluble components by centrifugation. The extr action liquid obtained in this way was heated to 80.degree. C. and 500 g of 55% water peroxide were added to the subsequently stirred Lüstüag inolaen. After 10 minutes, 2 kg of 50% caustic soda solution were added and the solution was gently agitated at 80 ° C. for 30 minutes. This was followed by 10 pilgrim sulfuric acid

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BATH

the adjustment to a pH value of 4.4 * around the partially modified To precipitate glycinin. This was then separated and added twice by decanting with 600 l of water Washed at room temperature,

The (at 30 ° C), washed clot was then adjusted with 20 #iger hydrochloric acid to a pH of 1.5, (in this stage was dissolved the clot up to about 90 $). A solution of 57 g of pepsin (1! 10,000) in 500 ml of water was added and the mixture was stirred for 4 hours. Mach 2 hours and after 4 hours the pH of the solution was brought back to Ij3 with 20% hydrochloric acid. The total enzyme Uiawandluriga time was 20 hours. After the conversion, the solution was warmed to γο ° ö and the pH was adjusted to % Q with a 15% caustic soda solution. To make filling easier, g kg of kieselguhr were added and the soluble and insoluble constituents were then separated by filtration. The resulting liquid was spray dried and gave a very pale, mild product corresponding to the E-5QQ listed in Table A,

Example 2

50 kg of oil-free soya oil was slurried in 1000 l of water at 50 ° C. and mixed for 5 minutes (until it was completely moistened). 15 % caustic soda solution was added and at the same time

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the pH adjusted to 8.5. This was held at 8.0-8.5 for one hour with continuous stirring. After centrifugation and separating the soluble from the insoluble constituents, the pH of the extraction liquid (at 50 ° C) adjusted to 4.4 - 4.6 with 5 # sulfuric acid at 50 ° C and allowed the precipitated glycine oil clot to settle. The liquid above was decanted and the glycinin precipitate was washed once more by decanting with 1000 water at 50 ° C. 750 g caustic soda in 2 liters of water and 750 g of lime (calcium hydroxide) in 2 l of water were added and move the solution slowly for 2 1/2 hours. Then its pH was adjusted to 4.4-4.6 with 15 # sulfuric acid and the precipitated Separated clots by decanting.

The enzyme conversion of the partially hydrolyzed precipitate was carried out as in Example 1.

Example 3

50 kg of oil-free Soyaflocken were slurried in 1,250 1 of water at 50 ⁰ C and mixed for 15 minutes. A solution of 1 kg of caustic soda in 2.5 1 of water at 50 ^° C. and a solution of 1 kg of lime in 2.5 1 of water at 50 ^° C. were added and the slurry was slowly ^{moved at 50 °} C. for 2 1/2 hours . The pH of the solution was then adjusted to 4.4-4.5 with 10% hydrochloric acid.

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The precipitation together with the residue of the flakes was carried out Separated decanting and twice with 1250 liters of water at 50 ° C washed. ·

To the washed clot and the flake residue, 20% hydrochloric acid was added to adjust the pH to 1.5 at 28 ° C. 100 g of pepsin (1; 10,000) in 400 ml of water were then added to the acid mixture. The slurry was stirred continuously for 5 hours and then left to stand for a further 17 hours. The total duration of the enzyme treatment was accordingly 22 hours. After 1, 3 and 5 hours, the pH was readjusted to 1.5. After the conversion, the mixture was slowly heated to 65 ° C. over a period of 30 minutes, the pH was adjusted to 5.1-5 _a 2 with a 15 # solution of caustic soda and the soluble and insoluble constituents were separated off by filtration. Diatomaceous earth served as a filter aid. The sparkling clear liquid obtained in this way was dried by spray drying and gave a slightly colored, mild, free-flowing product which corresponded to the E-500 mentioned.

Example 4

75 kg of oil-free soy flakes were in 1000 1 of water at one temperature slurried at 35 ° C for 5 minutes. 1? 50 g of caustic soda dissolved in 2.5 l of water were added and the slurry was

1 09 8 4 0/04 8 2

Stirred nuently for 1 1/2 hours. The soluble components were separated from the insoluble components by centrifugation and the extraction liquid is heated to 70 ° C. 4 kg 50 # caustic soda solution were added and the solution held at 70 ° C for 45 minutes. Then the pH of the solution was 10% Hydrochloric acid adjusted to 4.5 and the precipitated glycinin clot separated and washed twice by decanting with 1000 l of water at 30 ° G.

The precipitate washed in this way was then treated with 25 # hydrochloric acid and adjusted to pH 1.6. 27 g of pepsin (1: 10,000 starch) dissolved in 200 g of water were added and the mixture was slowly stirred for 3 hours. After this time the pH was readjusted to 1.6 with hydrochloric acid and the mixture was left to stand for 18 hours. 15 #ige Ktznatronlösung controlled the pH to 4.3 * 10 kg of diatomaceous earth facilitated the filter and separating the soluble from the insoluble components * The clear filtrate was added a solution of caustic soda _£ until the pH value to 5.1 * increased by evaporation was concentrated to a pesticide content of about 30 % and the liquid was then spray dried «

The degree of alkaline hydrolysis of a partially degraded protein was determined by measuring the viscosity of a 10% solution

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BATH ORIGINAL

source viscosity
CP -H- customary 6200 customary 3000 Example . 11 Example 2 7th

of the protein at 48 ° G using a Brookfield viscometer certainly. Some results of these measurements are in Table B. summarized,

Table B.
10 % protein solution -

(- Sodium Hydroxide
pH value 9a5)

(1) isolated soy protein
(not dismantled)

(2) isolated soy protein
(not dismantled)

(>) 4 · experimental protein

(partially dismantled)

(4) + experimental protein

(partially dismantled)

<¥ Viscosity tests were carried out on the protein after the alkali conversion and before the enzyme conversion »

++ Brookfield viscometer; Temperature 48 ° C.

The preparation of the enzyme-modified loosening agents from the unmodified and the modified proteins given in the table showed that the E-500 foam-forming protein could only be formed from the low-viscosity proteins (3 and 4) and not from the high-viscosity proteins (1 and 2). The latter two produced a loosening agent similar to soy protein during enzyme hydrolysis.

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BAD OBiGlNAU

A typical example of an E-500 protein has the following composition:

Protein (N χ 6.25) 81.00 %

Moisture 4.00 %

Ashes 14.00 %

Carbohydrate (various) 1.00 yes

100.00 %

Example 5

Acid hydrolysis of protein 50 kg of oil-free soy flakes were slurried in 500 l of water at JO ⁰ C for 10 minutes. To adjust the pH to 8.7, a 15% caustic soda solution was added to the agitated slurry, which was stirred for 1 hour. The insoluble flake residue was separated by centrifugation of the soluble constituents and washed once with 250 1 water at 30 ⁰ C. The combined solutions were then treated with sulfuric acid and the pH adjusted to 4.3 to precipitate the glycinin clot. This was separated and washed twice with 600 1 water at 30 ⁰ C.

The washed glycinin precipitate (glycinin curd) (which contained about 12 weight percent solids) was dissolved in 100 liters of water Slurried and concentrated with vigorous stirring 15 kg

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(98 %) sulfuric acid was added to make an acid concentration of 10 % . This acidic solution was then heated to 80 ° C and held at that temperature with agitation for 1 hour.

After 1 hour, the solution was diluted with 1500 liters of cold water and the pH value is adjusted to 4.4 with 20% caustic solution, to precipitate the partially modified glycinin clot. It was separated and twice by decanting with 1500 liters of water washed at room temperature.

This washed precipitate was then enzyme modified with pepsin and treated further according to the process steps described in Example 1, impure, very weakly colored, relatively "mild" To form protein product.

A 10 $ solution of the acid hydrolyzed protein from which the pepsin-modified product made had a viscosity of 7.5 cP (pH 9.5 / 48 ° C).

The end product was the "Standard Chocolate Chiffon Whip Test "lightly beat to a minimum density of 0.310 g / ml and it took 2 minutes and 50 seconds to achieve a density of." To achieve 0.44 g / ml.

Example 6

To 62.5 l of water at 30 ° C and in a 113.5 l Kettle was 5 kg of solvent-extracted soy flakes

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admitted. A 15 # solution of caustic soda was added to to set a pH value of 8.5. The flake slurry was then agitated for 1 hour, during which time the pH was adjusted kept at 8.5 by adding caustic soda solution. The agitation was stopped and the slurry settled for 2 hours calmly. The clear overhead liquid (which was approximately 1/2 the original volume of the slurry) was removed and filtered through a mesh sieve to remove small amounts to separate very finely divided flake particles.

To the remaining slurry in the kettle, an equivalent volume of 30 ° C water was added and the slurry for 30 minutes stirred for a long time, the pH being 8.5. The suspension was again left to stand for 2 hours to settle settled and the clear liquid above was removed as described.

The two clear solutions were combined and then heated to 80 ° C. for alkali hydrolysis. A 40 # caustic soda solution was added to adjust the pH to 11.8 and the solution agitated gently for 25 minutes. With 20 # hydrochloric acid the pH was adjusted to 4.4. To settle the felled Protein, the slurry was left to stand for 4 hours the clear liquid floating above is removed by decanting »The protein clot was once with cold well water washed using an amount equivalent to the original volume of the solution,

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A sample of the washed precipitate was separated and further concentrated to 20 # pesticide content. After dissolving at a pH of 9.5 and heating to 48 ° C for 1 hour a viscosity determination was carried out. It resulted in 155 oP.

The contaminants in the washed precipitate in the kettle were adjusted to 6-7% by adding water and the pH was brought to 1.5 with 20% hydrochloric acid. After the slurry had been heated to 30.degree. C., 0.4 % of 1 ι 10,000 pepsin (based on the weight of the dry solids) were added. The mixture was stirred for 5 hours during which time the pH was adjusted to 1.5 twice. The reaction mixture was then left to stand at 50 ° C. for 17 hours, so that the total time for enzyme conversion was 22 hours.

After this period the solution was heated to 70 ° C and their pH value raised to 5 * 1 with caustic soda solution. After adding The soluble components were filtered off from the insoluble components using filter aid.

The clear liquid from the filter press was in one stream spray-dried in hot air and gave a lightly colored, free-measuring powder.

In the "Chocolate Chiffon Whip Test" a minimum density of the whipped product of 0.05 g / ml was determined. To a density

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of 0.44 g / ml required 1 minute and 45 seconds. A pepsin-modified soy protein made by a similar process but without protein hydrolysis showed a minimum density of 0.409 g / ml in the same test and a whipping time of 3 minutes and 50 seconds was required, to get a density of 0.44 g / ml.

The aforementioned "Chocolate Chiffon Whip Test" is as follows 154 g chocolate cream base ingredients (a mixture from cane sugar, non-fat milk powder, cocoa, starch and gelatine) and 9 g of the foam-forming loosening agent dry mixed in a small bowl of a Mixmaster impact device. 240 ml (1 cup) boiling water is added and Beaten at top speed (No. 12) for 4 minutes. The density of the whipped mixture is determined by weighing determined from a sample in a calibration cup.

The foam-forming loosening agent produced according to the invention can also be used with slightly moist grain syrup »2 kg of grain syrup were placed in an impact device and 50 g of loosening agent mixed with 0.2 l of water were added. the The mass was beaten slowly until it was well mixed and then very quickly until the optimum volume was reached. By cooking a mixture of 2 kg of corn syrup, 2 kg of cane sugar and

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With 0.25 l of water at II5 -ρ, a boiled syrup was made, which was added hot to the cold corn syrup containing the loosening agent in the impact device. During the addition, mixing was carried out at a low speed of the device. The resulting mixture was then whipped at high speed for 2 minutes. The amount of the foamy product was measured in g / l. About 1 % loosening agent (500 g per 50 kg, syrup consisting of 60 % grain syrup and 40 % cane sugar) is required to get 491-524 g per liter of whipped product. Of the products according to US Pat. No. 2,502,029, at least 2 % or twice as much loosening agent are required in order to achieve the same amount of foam. Of the products according to the USA patent 2 J58l 407, even 6-8 times the amount is needed for this result.

In addition to these advantages mentioned, there is also the fact that the inventive Process gives high yields. The products have a mild taste and taste better than the products, which are obtained without hydrolysis, and they are at the isoelectric Point of hydrolyzing protein completely soluble in water. They are also soluble over the entire pH range.

In addition to soy protein, other vegetable proteins, for example the proteins of cottonseed, peanut, sesame seeds and the like can be used.

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For the acidic hydrolysis of the protein can be any non-toxic hydrolyzing acid, e.g. sulfuric acid, hydrochloric acid and phosphoric acid, be used. Mineral acids are preferred.

The purification of the protein first by alkaline extraction followed by precipitation and washing are optimal process steps. The precipitation and separation carried out after the extraction of the protein from the mother liquor is not mandatory, but can be carried out as desired. But when the protein does not precipitate at its isoelectric pH and the clear liquid above is not removed, a significant amount of salts is included in the protein which is to be "enzyme modified. This creates an end product that is which has a higher sodium chloride content than is desirable. The cleaning after the enzyme conversion is similar not mandatory, but it is useful.

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Claims (8)

Claims 1. Method of making loosening, by whipping foam-forming proteins, characterized in that oil-free vegetable protein up to a predetermined degradation product determined by viscosity measurements in an aqueous solution hydrolyzed and then the hydrolyzed protein is modified with pepsin,. 2. The method according to claim Ij, characterized in that the Vegetable protein is extracted with an alkaline aqueous solution and the insoluble residue is separated * the The pH of the remaining solution was adjusted to the isoelectric point, the precipitate formed was separated off and then is slurried again in water before hydrolysis » j5. Method according to claim 1, characterized in that the (| vegetable protein is hydrolyzed under alkaline conditions, 4. The method according to claim 1, characterized in that the vegetable protein hydrolyzed under acidic conditions will. . Ί09840 / 0482 5. The method according to claim 1, characterized in that the protein is hydrolyzed or degraded to such an extent that it is at its isoelectric point is insoluble in water, but that its viscosity in a 10% by weight solution in water at pH 9.5 and 48 ° C does not exceed 100 cP. 6. The method according to claim 3, characterized in that the Protein is hydrolyzed to such an extent that it is 20 percent by weight Solution in water at a pH of 9.5 and a temperature of 48 ° C is 100 - 1000 cP. 7. The method according to claim 1, characterized in that the protein is hydrolyzed to such an extent that it is isoelectric Point is insoluble in water, but the viscosity of a 10 weight percent solution in water at pH of 9.5 and a temperature of 48 ° C about 5 - 20 cP amounts to. 8. The method according to one or more of claims 1 to 7 * characterized in that soya is used as the vegetable protein. 109840/0482