DE2857037A1 - PROCESS FOR OBTAINING FOOD PROTEINS OF VEGETABLE ORIGIN, WITH ELIMINATION OF THE TOXIC AND NON PROTEINACEOUS SUBSTANCES - Google Patents

Description

Process for the production of food proteins

of vegetable origin ----

The invention relates to the treatment of herbal;

Raw materials, in particular for the extraction of the - "

keep food proteins under removal gif «- ^: -" tiger 'non-protein substances.

One is concerned with at the moment to an ever increasing extent

the extraction of vegetable food proteins
Origin. Numerous publications have been issued in this area. Reference is made at-; for example on the work of T.Staron in "La Rivista ι Itäliana Delle Sostanze Grasse", Volume 4, July 1974.
This publication gives a report on a
Meeting of the International Congress on Plant Proteins for Human Nutrition in Mantua on | October 3 and 4, 1973. This work and the one in it

cited literature summarize the state of the art in the field of production of vegetable proteins which are suitable for human and animal nutrition.

The methods known to date do not always meet
needs. For example, great efforts have been made in the treatment of the soybean and plant, but there are other natural ones
Sources of vegetable proteins, the utilization of which has not yet been realized 1. Even in the case of the | Soybean in particular are the extracted proteins

. i

due to their often undesirable taste and also · of side effects not perfectly suitable for human nutrition. They also occur in vegetable proteins often poisonous accompanying substances that are present in the natural substrates, so that the extraction j and extraction processes lead to protein fractions, | which have to be subjected to additional cleaning and detoxification. !

030603/0011

The invention relates to a general method for

Extraction of food proteins of vegetable origin, in particular a process that is based on the

. . various vegetable raw materials in the form of

i; > 5 grains, press cake, tubers or green plants

! '^; which contain proteins is applicable,

■ _t their previous treatments inadequate or poor

■ I to the production and extraction of the food

proteins were adapted. The procedure according to the! 10 invention makes it possible to use vegetable raw materials, ! e.g. soy, to which numerous researches have already been devoted, neutral, i.e. of taste and indigestible ; ; borrowed substances to gain free protein products without side effects. The procedure ensures a simultaneous detoxification of the proteins obtained if there are toxic substances in the treated vegetable raw materials available.

In its general form, the method according to the invention is for the recovery of food proteins of vegetable origin characterized in that one

a) the vegetable raw material containing the proteins with hydrogen peroxide in a reaction medium, which has a pH value in the alkaline range of 8.5 to 11.5, so that the proteins in the reaction

25 tion medium can be made soluble,

b) those insoluble in the liquid medium of step (a) Separates substances and thereby forms a protein solution,

j c) the protein solution at a pH of 6 to 8.5 ! 30 acidifies and thereby the insoluble fraction, the 'other compounds than the desired food

contains intermediate proteins, precipitates,

d) the insoluble substances in the protein solution of the

030603 / Ό011

Step (c) is separated and a clarified protein solution is obtained, ".",

e) the clarified solution adds at least one enzyme of the peroxidase type , which the remaining water ; substance peroxide and the clarified protein solution : capable of destroying any peroxides present, '

f) adding at least one antioxidant to the protein solution obtained in step (e), j

g) in step () solution obtained in a known \ manner of treatment f subjecting through which the

proteins contained therein are separated , and '

the proteins isolated by conventional methods. ',

As already mentioned, the method of the inventions according to j dung generally to the treatment of any vegetable \ Licher substances food proteins contain applicable. For example, the procedure for the \ treatment of the following substrates are used: j

1) seeds (soy, broad beans, peas, lupine, i sunflower, safflower, cereals, corn, oats), i

2) oil cake (soy, sesame, arachidin, sunflower, ι rapeseed, linseed, cotton, safflower, copra, areca palm, jojoba), j

3) tubers (potato) and;

■ ■ ■ ■ ■ ■. ■ '■■■' * '' '' '■■' ■■ '■ ■ ■ ■■ ■ - ■ ■ -: j ι

4) Green plants (alfalfa, spinach, sorghum). ';

. ' -.- ■■ '■■■. ■■■ '■. ■;. ■ .... ■. ■. · ■■ - ■. ·, '■. ■ ..-'. ■■■■ ■ · ■ '. ■ :.' ■ ■ ■ i ■ ', The method of application of the method will of course vary, ' a little with the type of substrate treated. In the case of the various substrates; I.

■. '■■■. ■ ■ ■ ι ι

The means used are described in more detail. j |

030603 / Ό01 1

s' ■ ■. . ■■ ■■ ■ - ■■■■■■■. ■■■

Λ) seed

The seed intended for nutrition or ' from which a fraction (oil) is obtained for nutrition, must be of good quality and very specific Meet criteria that are generally defined.

These criteria in terms of quality, grade and variety include

1) the specific weight,

2) water content, ash content, protein content, oil content,

Cellulose content, foreign and diseased grain content, anti-nutritional factors, mycotoxins, residues of pesticides, broken grain, impurities (spoiled grains, foreign grains, plant residues, Minerals, dead insects, remains of animals);

3) germinated, moist, moldy, gelled, warm and acidic parts that contain living insects and having odors are generally discarded.

The parts intended for the extraction of proteins must meet the requirements established by ordinances that apply to every production.

2) oil cake ν

For the extraction of the oil from the seed, the destruction the natural poisonous substances or bitter substances and to remove the remaining solvents there are numerous different processes in which the solubilities and the nutritional value of the proteins are changed Oil cake often insufficiently de-oiled, contaminated with dust and with fuller's earth and lecithins from refining of the oil mixed.

According to the invention, the proteins intended to supply the seeds for human consumption

030603 / Ό01 1

from which they originate, cleaned and, if possible, peeled. The oil must be extracted by cold pressing and with "---" * food-grade solvents - ~ ^. The temperature of the heat treatment of the oil cakes must not exceed 1O5 ° C and they must not contain "\: more than 2% oil and 8% moisture.;:;

j 3) tubers and roots

The tubers and roots must meet the standards set by the food industry (canning factories, starch factories, etc.). i

4) green plants . ;

Green plants must be harvested when the protein content is highest (generally, before flowering).
Since the greater part of the proteins in the leaves corresponds hold ', it is expedient that part of the plant; to treat. Avoid having too many

I impurities, soil and various remnants and back!

stalls are taken. ;

The proteins must be extracted immediately after harvesting. Intermediate storage favors the

Binding of phenols to the proteins, and this has ^to: consequence that these compounds are insoluble and their ι nutritional value is reduced.

■ "■" "'· ■■■ · ■■■ · .- ■ ·.: - ■ -. -. · J

Before the plant material to be treated in the encryption \

. ■ ■ ■. ■■■. ■■■ .. ■ ■ ι

drive according to the invention is used , J

mechanical preparation, of course, which is necessary for j

serves, the contact with the reaction medium in the j

Stage (a) to make it easier to be subjected. This j happens with known technical means: cleaning,

Peeling, dry grinding followed by sieving or j.

Wet grinding, for example in a colloid mill. It goes without saying that these technical means must match the respective form of the plant material to be treated

030603 / OU11

be adjusted. Examples of this will be given later.

An essential stage of the process according to the invention : manure consists in treating the plant material

5 with hydrogen peroxide in an alkaline medium ¹ in such a way that the proteins contained therein are made soluble. This step is carried out under conditions that ensure intimate contact between the plant material and the liquid reaction medium. It is essential that: the medium is kept at such a pH value by adding any agent with which the pH value can be brought into the alkaline range. These agents are known to those skilled in the art of treating plant materials. Organic and / or inorganic compounds are suitable, e.g. sodium

■ hydroxide. Sodium carbonate, potassium hydroxide, ammonium hydroxide »' and magnesium hydroxide, and organic bases, e.g., alkanolamines such as ethanolamine. Preferred as an alkali

I 20 chemical agent is sodium hydroxide. In general are compounds with divalent cations, e.g.

■ .. Calcium hydroxide or magnesium hydroxide, less favorable for the extraction of proteins, but this one

ί Effect can be caused by the electrolytic effect of the a-25 set hydrogen peroxide are canceled.

¹ The exact pH value can vary depending on the species

: vary a little of the plant material. in the

ι In the case of seeds, the pH is between 8.5 and

. 11.5 held. In the case of tubers and roots as well

30 in the case of green plants, it is sufficient if the pH value is between

i is held around 8 and 9.

ι '. These embodiments will be used in the later • Examples illustrated. The amount of the to be used depending on the type of plant material

030603/0011

alkaline solution is generally about 2 to ¹ "· 10 parts by weight of alkali solution per part by weight of plants» "! material. In the case of seeds, the amount " ^r is about 5 to 10 parts, while for tubers and roots a smaller amount of 2 to 5 parts alkaline solution is sufficient. ". ":,."

The alkaline solution serves as the reaction medium · It can also serve as a grinding medium when the plant material wet grinding:

The solubilization of the proteins is achieved through the interaction of the alkaline medium and the hydrogen peroxide achieved. As far as the applicant is aware, a plant material has never been proposed to treat in an alkaline medium so that the proteins contained therein using the reducing Effect of hydrogen peroxide can be extracted. Hydrogen peroxide is a valuable reagent for the extraction of food proteins as it Due to the fact that it simply decomposes to water and oxygen, no harmful return: stand in the reaction medium leaves behind · i

The amount of hydrogen peroxide j to be used varies with the respective plant material. When using hydrogen peroxide to 33.3 vol .-% ■, that! is currently available in the industry, the | _H2 O2 ^{M € n} g ^{e generally} between 0.2 and 3% by volume, based on the solution formed by the alkaline reaction medium.

The hydrogen peroxide can be added to the medium as such or in the form of at least one precursor compound, preferably a food grade precursor, e.g. sodium peroxide, which forms H.O- in situ in the reaction medium.

030603/0011

-Away-

Step (a) is advantageously carried out at ambient temperature, but moderate heating can also be used to be worked. The contact time of the plant material and the alkaline medium in the presence of hydrogen peroxide must suffice for practically the ! total proteins contained in plant material

are to be made soluble. In general, a contact time of 5 to 20 minutes is sufficient.

: In the second stage (b) of the procedure, the

insoluble substances separated from the protein solution. j This separation can be carried out by any known method, for example by centrifugation. The composition and nature of the insoluble fractions vary with the treated plant material. However, in many cases they can be used as fodder be recycled.

': Another important stage of the procedure according to the

; Invention is stage (c), in the course of which the

Protein solution to a pH that depends on the

i.

Plant material varies between 6 and 8.5, fishing becomes acidic, and which becomes an insoluble fraction

leads, the exact composition of which also _{varies with the:} ι plant material. For example contains

this fraction in the case of seeds heteroproteins, j I 25 polysaccharides (mucus, pectin) and other compounds j fertilize. The acidification takes place by addition at least

• i an acidic substance. Preferably j

a specialist in the treatment of food

ι · ■ · ..... ■ / 'I

known acids, advantageously hydrochloric acid, sulfuric

i j

j 30 acid, phosphoric acid and carbon dioxide or an organic

j '■; acid, e.g. acetic acid, lactic acid or citric acid

ί. . "Nene acid, is used. Strong hydrochloric acid is expedient or food grade sulfuric acid

j I

used. It should be noted that the reducing effect of H ₉ O- is retained at this stage

030603/001 1

Contact of the hydrogen peroxide with that

rial thus takes place in the course of stages (a) and

In step (d) of the process, the protein solution is clarified before it is used in step (e) "- .; in which the remaining hydrogen peroxide and all..; Any traces of peroxide that may be present are destroyed by adding at least one enzyme is added on the type of peroxidase preferred enzyme catalase, derived especially from beef liver \ catalase In the examples hereafter ι figures made using the enzyme to be used as' In the case of catalase beef liver ^vari-:... ated this Amount, for example, between 200 and 400 g per 100 kg of dry protein mass in the solution.

Step (e) must be during one for the destruction of the hydrogen peroxide and the peroxide of the solution be carried out in sufficient time. In general, a treatment time of 5 to 10 minutes is sufficient.

Step (f) of the process consists in adding to the protein solution coming from step (e) at least one antioxidant known for this procedure, for example di-t-butyl-p-cresol, which is abbreviated to BHT, or another analogous compound added ■■ ->'■■' ■■ · ■■ .. is set. '"" ■ ^: γ ·'. '' ■ '■''■■■"■ γ ■"' ■■ "■ '.: ■■ ■

It should be noted that in the process according to the invention the antioxidant is used during an intermediate stage of the process is used and thus at the same time has a protective effect on the proteins. Further it should be noted that in known processes for the production of proteins from plant materials already has been proposed to counteract the proteins by adding reducing agents to the reaction medium Protect from oxidation. Only after the final protein fraction has been separated off and dried is j the antioxidant was added for protection. Against it

030603/0011

-Αί .--

already works in the method according to the invention Strongly reducing reaction medium. The antioxidant is thus used in step (f) of the process and not added after the final separation of the protein fraction.

In step (g) the desired proteins are isolated with the aid of known methods. For example, the protein solution can be adjusted to the isoelectric pH value by adding a food acid of the HCl or HpSO _{4 type, ie to a}

pH 4.7 to 5 can be acidified. It is also possible to make a hot precipitation of the proteins, by coagulating the proteins by blowing steam into the solution. As a variant, the medium can be acidified by cultivating a microorganism therein and, for example, lactic acid fermentation is carried out according to the method described in FR-PS 75 14 676 of the applicant. In this process, the extracted proteins are biologically precipitated. The precipitated proteins will be isolated by centrifugation and optionally subjected to an additional treatment in which the protein sediment is washed and then dried, with food proteins in powder

25 shape can be obtained.

The centrifuge water and wash water separated from the protein sediment in the last stage of the process contains non-protein nitrogen, sugar, mineral salts and various other elements. This water ^! can itself be used for the production of food proteins by using it as a nutrient medium for microorganisms that are involved in the production of proteins. ' of multicellular microorganisms enable * a

j ■ ■ a suitable procedure for this purpose is provided in the

Ϊ 35 French patent application 77 17 449 of the applicant

ι ■ '■■ "'.: ■ ■ ■ ·

030603/001 1

-43-

described. This patent application relates to a process for the production of food proteins from .. ' small mushrooms or from multicellular microorganisms, ■ -'-- a device for carrying out the process and " the proteins produced in this way . This process .: Consists, in short, in that the fungus Tricho- ; derma album is cultivated at a temperature below 28 ⁰ C in a liquid nutrient medium , the pH of which is kept between about 3.7 and 4.8 and a content of dissolved oxygen of about 6 to 10 mg / l.

The invention is described in more detail below under \ reference to the figures, the main stages of the process in his ^presence! Turn to ■ ι

granular seeds (Fig. 1), tubers and roots (Fig. 2) and

Green plants (Fig.3) ""!

represent schematically . In addition, FIG. 4 shows a variant of the method in its application to soybean oil cake, it being possible; . . simultaneously concentrates and isolates of proteins

to win. ^]

In Fig.1 , precise information is given about the application of the process in the case of seeds, t As already mentioned, the washing water and the centrifuge water of the process can be supplemented with nutrients and used as a nutrient medium for thread-like microorganisms for the production of proteins of multicellular microorganisms , which contain 55 to 70% protein nitrogen , according to the FR-PS 77 17

449 are used. 1

2 is a corresponding one of Fig.l schematic representation of j, but in this case, the method!

030603/00 i-1

applied to the treatment of tubers and roots. In this case, too, the procedure can go through a treatment of the centrifuge water and wash water to recover proteins from multicellular ones Organisms are supplemented by the method described in FR-PS 77 17 449.

The same applies to Fig.3, which shows the application of the method to the production of food proteins illustrated from green plants.

The same observation applies to Figure 4, which shows a method for the simultaneous manufacture of concentrates and represents isolates of proteins from heat-treated soy oil cake.

While the method is effective on tubers, roots and green plants in a general manner according to the Schemes in Fig.2 and 3 can be carried out, the application of the one shown in Fig.l varies Procedure with the substrates. These embodiments are described below.

20 soybeans

When applied to soybeans, the process enables the production of isolates or the simultaneous production Production of a concentrate and an isolate.

The isolates can be obtained from raw or cooked press cake, the concentrates from cooked press cake i be won. ;

The H_0 ₂ is used in an amount of 0.3 to 1 vol .-%. The press cakes are finely ground and sieved on a 100 to 150 µm sieve or ground directly in a liquid medium in a colloid mill.

030603/0011

Obtaining isolates

The extraction is carried out at a pH of 10 to 11.5. The pH depends on whether ^dei: Sojapreßkuchen raw or cooked. Clarification by precipitation takes place at a pH value of 7.3 to /

7 7 "■ I"

Simultaneous Production of concentrates and isolates

In this case, cooked soybean press cake, made from peeled soybeans , is used as the starting material; and contains 50% proteins. The extraction is carried out with 5 to 10 parts of 0.03n to 0.05n NaOH (pH 8.5 to 10) containing 0.3 to 1% H ₃ O ₃ . A contact time of 20 minutes is suitable. .

Fig. 4 schematically shows the practical implementation .

Oilseed rape, sunflowers, safflower, broad beans, arekaj palm and copra . '■

; ■ - ■. ■., ■.; ■■■■■. ■ ■ ^: ι

As applied to the press cake encryption allows

drive the extraction of odorless, white or I.

:, ocher colored isolates of good quality. The pro- j

Teins are mixed with 10 parts of O, ln sodium hydroxide

(pH 11.5) containing 2% H ^ extracted. The !

Contact time is 5 to 10 minutes. ί

The press cakes are finely ground beforehand and sieved on a sieve with a mesh size of 150 to 300 μm or, preferably, ground in a liquid medium in a colloid mill, whereby oxidations are limited. Clarification takes place in the case of rapeseed and small broad beans at pH 7, in the case of sunflowers and safflower at pH 8.5 and in the case of the oil palm and copra at pH 6.5.

0 30603/0011

Pea and sesame seeds

The proteins from pea flour and sesame press cake are extracted with 10 parts of 0.05N sodium hydroxide containing 1% ^H ? ° 2. The contact time is 5 to 10 minutes. Clarification is carried out at pH 7 in the case of peas and pH 8 in the case of sesame seeds.

Peanut, cotton, lupine, flaxseed, and jojoba

The press cakes from seeds of this group are rich in poisonous substances (aflatoxins, gossypol, alkaloids, glycosides, cyano compounds, resorcinol derivatives), so that their residence time in the extraction solution must be extended. The extraction is carried out with 10 parts of Ο, ΐη-sodium hydroxide, which contains 2% ΗρΟ_. The extraction time is 20 minutes to 1 hour for the peanut and cottonseed and 1.5 to 2.5 hours for the lupine, linseed and jojoba.

The clarification can in the case of the peanut and in the case of jojoba at pH 7, in the case of cottonseed, lupine and linseed at pH 8 can be made.

Cereals, corn, oats and other cereals

The grain is mixed with 5 to 7 parts of an alkaline solution of pH 9, which contains 0.3 to 0.5% H ₉ O ₅ , extra-

here. The contact time is 5 to 10 minutes. The '_; Clarification is expediently carried out at pH 7.

Determination and test methods

The organic nitrogen is determined quantitatively after mineralization according to the Berthelot method. the Composition of proteins according to amino acids is determined after acid hydrolysis and dissolution in a Technicon TSM certainly.

The bacteriological purity of the fractions obtained is ■ checked on selective media.

030603/0011

The toxins (aflatoxins, thioglycosides and gossypol);. i. and the various metabolites (chlorine-forming acid II; re (acid chlorogenic) are after the extraction by " ^:

Thin layer chromatography determined.

The nutritional value of the isolates and concentrates is given to ma'nnj.i- » Chen Sprague-Dawley SPF rats of 50 g determined. ;

The activity of bovine catalase is determined by quantits ~. ": ■ tive determination of HpO- on the oxygen meter (Oxy-. -" l meter) or by chemical means according to the following

10 method determines:

Reagents; 25 g sodium tungstate, 10 ml phosphoric acid:

·> - 4o ml

D = 1.71; distilled water. They are left for 2 hours:

den, add 4 g of ammonium metavanadate and 50 ml of distilled water. It is allowed to boil _f 2.5 hours 40 ml ι nitric acid (d = 1.38) and 100 ml of distilled water. The mixture is left to boil for 2 hours, 4 g of Reinecke salt and 50 ml of nitric acid (D = 1.38) are added and the mixture is left to boil for 1 hour. This reagent is stable.

Method for determining the catalase activity

20 Place in a test tube with stirring

0.1 ml of solution containing catalase and HpO-,

1.9 ml phosphate buffer of pH 7 and 1.0 ml H ₂ O.

3 ml of 5N sulfuric acid are added and 2 ml of this solution are placed in a second test tube. One sets 0.1 ml of reagent, stirs and reads on the spectrophoto-

meter at X. = 490 nm.

A blank test is carried out with 2 ml of 2.5N sulfuric acid and 0.1 ml of reagent.

^30th Products used for extraction ¹

The sodium hydroxide and acids (HpSO-, HCl) are of food grade. The antioxidants are added in the permitted amounts. The BHT is in

030603 / OU11

an amount of 2 to 7 mg / 1 is used.

The catalase of beef liver is produced as follows:

100 g freshly removed or frozen liver from Healthy cattle are ground in the "Turmix" mixer in 600 to 5,800 ml of isotonic sucrose (25 g / l). the

! ■ Solution is filtered through glass wool to remove the insoluble: borrowed fraction to remove. This preparation must be used immediately in the manner described (200 to 400 g liver / 100 kq

: Product) can be used or can also be frozen

; 10 become.

! The results obtained

■ I The amounts of raw materials treated will be

ι '. depending on the substrates between 10 and 50 kg dry matter varies. The obtained average

¹ 15 results are given in the following eight tables, which are analyzed individually below.

i Table I.

i The solubility of proteins in sodium hydroxide solution

• i and its precipitability at pH 5 vary considerably in: 20 depending on the substrates (the yields on

j isolates vary between 27 and 77%).

■ Of the factors that change the extractability,

j are the quality of the grain, the denaturation of the

..- '. Proteins by those used to extract the oil;

i ■ ■. .- ■ '"· ■' ■.

j 25 processes and the high content of ash, cellulose, i Phenols and fatty acids which, when the:

j. - Fats arise, to name a few.

i In most cases the yields of iso- | vary j laten if the regulations regarding the : 30 substrates between 50% and 80%.

030603/001 1

Table II

In this table, the compositions of ^are: ~ - 'fractions indicated by amino acids. It gives ^SiOH: · that the isolates generally of lysine, threonine and \

Methionine-cystine are depleted, not because the amino-

acids are destroyed, but because they are in the proteins insoluble in the sodium hydroxide or in the washing - j

water and centrifuge water remain · '"■ -}.

In the method according to the invention, nothing occurs
Loss of essential amino acids still requires synthesis
of lysine alanine. In addition, the fractions insoluble in the sodium hydroxide can be used for feeding cattle
be used. The washing water and centrifuge water mainly contain proteins, amino acids,
Sugar, ash and impurities (o-diphenols, aromatic amines, etc.). After adding nutrients ! they can be used for the cultivation of filamentous fungi j (Trichoderma album) for the production of proteins i

serve according to the described in FR-PS 77 17 449 enclosed method.

Table III

This table shows the balance of the simultaneous
Production of soy concentrates and isolates. the
Is the composition of the concentrate excellent? only a small amount of protein is lost. The one from wash water and
The dry matter removed from centrifuge water consists of! Ash, organic acids, acidic and difficult to digest , lent sugars, pigments, saponins, phenols, bitter, peptides and substances that give flavor and too
Cause flatulence.

The concentrates obtained are in the form of an odorless and tasteless white powder that is light
is texturable. The nutritional value of these concentrates is
very high. They are easily incorporated into numerous human foods without them

030603 / -00 M.

unpleasant taste and smell and side effects (Flatulence).

The concentrates prepared in the manner described have better physical and organoleptic properties than the alcoholic and acidic concentrates . ■ i

Tables IV and V

In Tables IV and V, a raw soy press cake is used compared to a heat treated soy press cake. These tables illustrate the impact of technology on the behavior of proteins and their compositions according to amino acids.

Table VI

This table shows the excellent results obtained with peanut, cottonseed and rapeseed thanks to the use from hydrogen peroxide in an alkaline medium. Under the working conditions will be in 20 to 30 minutes the aflatoxins are completely destroyed and the content of gossypol, thioglycosides and isoflavones

20 very much reduced.

The process thus enables very good recycling the oil cake by destroying polluting and natural toxins. Also eliminated and modified there is a large number of organic molecules (phenols, flavones, saponins, complex sugars, pigments etc.) that change the shelf life, intake and nutritional value of food. This effect was confirmed by numerous nutritional experiments.

Table VII

The bacteriological ones made on these isolates Tests show that the quality of these products is excellent. . ■

0 30 60 3 / Ό 01 1

Table VIII: Nutritional value : _

The nutritional value of 16 proteins obtained after the process ^ ; were compared to milk casein supplemented with - 'methionine . The experiment was carried out on young male weaned SPF rats of the -Sprague Dawley breed . The duration of the experiment was 17 days and the protein content in the feed was 10%. Every food has been supplemented with essential amino acids. Each experimental group consisted of 20 animals. '■' ~ _: _

The analysis of Table VIII shows that groups fed milk casein and Trichoderma album differ very clearly from all other groups which received vegetable proteins, the structure and composition of which had the biological value for the rat

15 seem to limit.

The good results with all tested food compositions of the invention proves ^j the improving effect of the proceedings according to. In the case of alfalfa, the large quantities of protein produced per year and hectare (1,800 to 3,000 kg) are remarkable.

Furthermore, the extraction of the dehydrated alfalfa is preceded by a pressing process that produces large amounts of juice. . This appropriately supplemented lucerne juice is an excellent starting material for the production of fungal proteins (Trichoderma album) according to the process described in FR-PS 77 17 449 .

The above results show that the method enables according to the invention the exploitation of many sources of vegetable proteins that are not yet sufficiently out at the time in the world for this purpose uses are. Examples of these are vegetable substances such as rapeseed, sunflowers, peas, broad beans, grain tubers and green plants . In the case of soy bean, the invention enables the recovery of proteins that are beneficial for human nutrition

030603 / '0 0 11

-ZS-

tion are usable.

According to an additional very advantageous feature of the invention, the method also enables a Detoxification of the substrates, especially the peanut and the cottonseed, causing immediate the populations of giving underdeveloped countries access to better, protein-balanced food.

The invention can also be used with the essential aim of detoxifying herbal substances without that the proteins contained therein are destroyed.

In this case, the method according to the invention can be extended to step (a) of the treatment described above the plant materials are limited with hydrogen peroxide in an alkaline medium. For example the invention can be used to treat numerous mycotoxins which the grain and the foodstuffs contain, to remove.

In the method according to the invention, the fact that the treatment is far in the basic range lying pH value begins and the reaction with H-Op Performed at a low pH is of great importance as that with the vegetable proteins associated disruptive molecules here in irreversible structures, which are then removed

25 can be converted.

The invention is very interesting and advantageous for the treatment of cooked soybean oil cakes. In this case the reaction with hydrogen peroxide | at a pH value not exceeding 10; leads · Soy protein concentrates were previously obtained by concentrating them in an acidic or alcoholic ^{: medium.} The invention thus enables the production of concentrates of soy proteins which are perfectly suitable for human consumption,

0 30 603 / Ό0 1 1

13-

as they are free of substances that give the product an undesirable taste and odor and / or are difficult to digest. ■ ■ -

030G03 / 00 M.

Tabel

Protein content of the fractions and distribution of proteins in the protein
salary
the sub
strate
in %
Dry
Dimensions protein
salary
the in
NaOH un
soluble
chen
fraction
in% TM In NaOH
insoluble
Proteins
in the
total
proteins protein
salary
of the Se
diments
the Klä
tion in
% TM Proteins
in the Sedi
ment the
clarification
in the
total
proteins L different factions Receive
tene
Isola
te in
% the
Ges. -
Per
teine protein
salary
from the
water
in %
TM Proteins
in the
Waste
sern in
% the
total
proteins 50 18th 14th - -; protein
salary
the iso
late in
% TM '60 32 ^: 26th Raw soy oil cake 50 35 30th 60 6th .93 58 ,. 14th 6th Heat treated
Soy oil cake. 37 23 42 - - 87 34 "42.; ; 24 Rapeseed oil cake .37; 20th 19th 63 5 82 60 '.'. 30th , 16 Sunflowers-
oil cake 32 12th 17th .- 100 75 . · '18 8th Safflower oil cake 27 8th 18th 43 . 0.5 91 67 23 . 14th Seeds of
small broad bean ■■ ■, ■ 20 15th 60 ■ - - 82 35 9 5 Oil palm - oil cake -. 24 17th 64 .- - 81 27 . · 10 Copra oil cake ■ 27 ^; , 7 14th 60 2 85 64 23 '■' 20- Peeled peas, ^j L; y, ^-55 ;. ; 32. 23 55 .5 96 61 32 - ■ 11. Sesame oil cake - "55; ' 18th 16 5.2 1 97
¹ -. , 77 15th 6th Peanut Oil Cake 92

ο co -J

Table I (cont.)

Protein content of the fractions and distribution of the proteins in the various fractions

O CD O CO

!Protein-
:salary
Ider sub ¹ straete
in %

Dry matter

Protein ■ content .. \ in: INaOH un-;! dissolve ¹
j fraction I in% TM

In NaOH. : unsolvable

Proteins in% of the 'total' iproteins

Protein content; des Se- ', diments of clearing in,% T.M.

Proteins
in the Sedi

Protein content

ment derider iso-

clarification
in

Total proteins j

I late in
the i% TM

Get! ProteinH

tene isolates in% of total proteins

salary of the water .

in.% - V.

T. M.; ■ -,

Proteins in the. ^; Sewage in

of total proteins

Cottonseed j
Oil cake ■ 55 42 ■ . i so; 3 80 40 • · ■ ■ ■ I
21 .. 9: Lupine seeds;
'-' ■ ■. · ...!. ■■■■, - ■■ j 38 11 ; ι ⁵ 30th 1 82 62 26 7'Y 22 '..- .. Flaxseed:;
-Oil cake .; .31 .22 - j .55
I. I ³⁵ 5.. 75. .35 12th , S - ■■ Jo j oba oil cake ■■
j 25th I ⁹ '■ !
j 37.
I. 15th 2 72 , 43 • 17 ■;, / ■ ; -is,;, '
■ Cereal seeds |
■ ":.. ■ ■"-; . ^■■: ■■ '■ ,:' ..- · - ■ ι 12th : ■ ■ .. 3. I 19.5 18th 0.5 88 75 8th Potato- ,
bulbs ^! 7th ! · -: ■■ 2 ! . > ⁹ ' I 20 1 78 75 7th I ⁵ ■ ·· Freshness: ■ · .-. ·. ; -; ■
Alfalfa!
-, 1- ,; 3 U - '.8 ; ..... 20 · · 25th 5 65 55 16 ■ 20

Tabel

II

LYS
HIS
ARG
ASP
THR
SSR
GLU
PER
GLY
ALA

cys + met;

VAL
ILE
tf.U
TYR
. PHlE

soy

Amino acid composition in% per 16 g nitrogen

O:

CD

6.3
2.6
7.2

(10.2
4.0
5.3

16.5
6.1

3.8;

4/1

3.6:

4.8
4.2
6.7
4.6
6.1

* 3
ft 0)

o al

ß
rs

cn

6.1
3.3

7.1
11.5
4.2
4.2
16.5
5.6
4.0
4.9
2.7
6.3
6.0
8.8
3.9
6.0.

ί
3

ft

Chi

cn

Ρ) ι

sins:

PJ: Φ P)

ft; 3 CQ

K rt ω H- ti 3 *

6.4
2.9

7.1

11.2

4.8

4.2

14.5

5.5
2.3
7.1

11.5
3.2
4.3

20.9

5.21 8.1
4.1 '3.7

5.5
1.8
6.7
5.8
9.3
4.4
5.9

3.8
2.2
4.7
5.3
8.1
3.6
5.5

N
fD
3
rt

JHi P) β CQ

CQ Ch Φ

6.1
2.8
7.4

11.2
4.0
4.4

17.6
5.6
4.0

• 4.3
3.5
5.5
5.9
8.3
3, 2
6.0

Rapeseed

O:

(D

5.7
2.9
5.7
7.5

HJ H

H 3
PJ

ft p)

H- O

O ffi

O:

CQ

(D

H CQ O

H PJ rt

4.9
2.7
6.1
9.1

4.8 j 5.8

4.6; 5.2

19.4! 16.4

7.3
5.2
.4.5
4.8
6.1

7.0
5.3
5.2
3.3
6.2

4.6i 5.4
8.5) 8.5
3.0 '3.9
4.4 '5.0

6.5
3.2

7.3
8.7
5.1
4.7

16.5
6.3
5.0
4.8

! 3.7
5.9
5.1
8.3
4.3
4.8

(D PJ

3 cn

rt ο,

H 31

H- 5

Ki PJ

β cn

LQ CQ

(D (D

PJ β

cn 3

M Cb

Ci

3 Ν LQ (DI 3 <

rt Pj:

Μ Co

PJ H

ft H-

iQ

(D

7.4 3.7 6.6 5.5 3.3 3.2 26.7 8.9 4.6 4.0 6.2 4.5 3.8 6.0 1.9 3.5

Sunflower

6.4 3.2 | 6.7 8.2 4.7 4.4 iS, 4 6.0

5.1 4.6 5.1 5.7 5.3 8.0 3.2 4.8

CC
I ι HJ H
UJ * -i Oil cake PJ
^ s
ft P)
H- O
0 K
3
β
3 H*
θ:
cn 1-'
Η
Ω
3 *
Φ 4.0 3.8 2.5 2.5 8.4 7.3 10.1 10.4 3.7 4.3 4.0 4.5 21.9 20.4 5.0 5.1 5.5 6.1 4.0 4.8 4.4 2.9 6.0 6.0 4.5 5.7 7.2 8.6 3.5 2.3 5.1 5.1

CO (D Cb H- 3 (D 3 ft

P ;: hi

3.1 2.6

10.6 7.6 3.9 4.0

20.2 5.2 4.5 4.3 3.5!

6.1! 5.5 7.7 3.3! 6, Oi

cn

Φ PJ

3 CQ

rl- Ω

H, 3 *

H- K

i-h PJ

β cn

lq cn

Φ Φ

PJ β

M.

CQ Qj

Small broad bean

co

pj

PJ

rt ο

H 3

3.5 2.9 9.6

10.1 3.5 3.9

22.3 4.3 4.5 4.2 3.8 6.0 5.3 6.9 3.0 6.0

5.3 2.3

.9.9 8.1 3.3 3.8

24.9 5.2 7.9 3.2 9.6 3.8 4.0 5.0 1.5 1 ,?

7.1 2.9 8.8

11.3 4.0 4.4

19.4 4.7 4.4 3.9 3.7 5.2 4.5 7.5 3.5 4.8

S-

ft PJ

H H

tr

(D

7.0 2.9 8.1 11.4 4.2 4.8

17.3 5.2 4.7 4.4 1.9 5.3 5.1

8, σ

3.2

5.1

H Φ P): Ch M H-

U3 rt

PJ

Cb

5.5

2.6

8.2

12.0

3.7

4.8

19.2

■ 5.5

.4.1

4.2

0.8

5.6.

5.1

8.5

4.3

5.5

CQ O M PJ ft

6.0

2.7

9.8

11.4

3.8

4.3

16.7

.4.9

3.8

4.1

2.1

■ 5.8

.5.6

9.4

4.1

5.3

Tabel

II (cont.)

O CD O CO

oil cake Composition] 3 Insoluble in NaOH
lich parliamentary group lor H
cn
O
D)
rt 1 Centrifuge water Wash water and laugh j Insoluble in NaOH
che faction ■ - 3 H
cn
O
D)
ft I. Viaschwasser and
centrifuge water % per C. ! 9 0! 16 G nitrogen 3 centrifuge water Wash water and Seed grain Peeled E r b S. e I s 0 1 a t , 9 Centrifuge water I. Wash water and | ] 1 3, S a f 3 3.5 Sediment of
clarification 3, 2 2, 4 * Amino acids in 3.8 1 4th 5.0 6th before Group I ρ 3 c a 4th , 0 6th 8th before Group I Insoluble in NaOH Clarification I] Sediment of the | 7th , 7 7th , 5 X 3, 3 3.0 3.0 3, 1 2, 6th ^; : Eruka palm
ί 1.9 16 _r 6 1.1 oil cake 8th 2, Insoluble in NaOH H
tn ι
D.
D)!
rt 1 , 2 2 ,1 6th 4th 8th ,1 2 , 2 2 , 7 LYS 10, O 9.1 3.1 11 4th 13, 1 oil cake 14.4 10 _r 6 Ϊ7.0 4, 8th 2, 8th 2 , 6 14th , 9. 8th r8 2 6th 2 , 6 9 ,8th 18th , 4 HIS 11 3 9.9 10.4 10, 2 8th, 7th 4.1 9.5 4th , 0 .8.7 2, 5 10, 1 1 , 7 9 , 5 12th , 2 8th rl 8th , 4 11 , 4 12th , 0 , ARG 3, 1 3.7 11.6 3, 0 2, 8th 2.3 3.4 4th _r o 2.8 12; 0 9, 6th 14th , 6 3 , 2 4th , 5 12th , 0 11 , 5 3 , 0 3 , 9 iASP 4, 7th 4.1 3.4 4, 2 4, 0 14.9 4.5 Ί8 ,8th 3.8 8th, 0 3, 9 9 , 6 4th , 3 4th , 4 4th , 2 3 , 6 4th , 6 3 , 7 THR 21 0 20.0 4.4 21 4th 28, 2 9.0 21.3 3 ,8th 29.5 3, 7th 4, 7th 3 ,8th 27 , 2 18th , 3 4th , 6 4th , 3 17th ,8th 20th , 6 SER 5, 3 5.6 21.2 4, 6th 5, 2 3.2 4.0 3 , 7 3.8 4, 6th 22nd 4th 4th , 6 4th , 9 4th , 3 18th , 0 17th , 0 4th , 6 3 , 3 GLU 5, 4th 5.6 5.1 4, 5 11 0 4.7 4.8 4th , 9 5.0 20, 8th 4, 4th 20th , 6 4th , 6 4th , 4 4th , 9 4th ,8th 3 , 9 5 , 0 .PER 4, 0 ■ '4.8 4.5 4, 5 3, 5 20.0 4.4 3 , 4 . 4.0 3, 7th 5 3 4th , 0 6th , 3 4th , 2 4th , 5 3 , 9 3 , 7 4th , 6 N) GLY 3, 2 2.3 4.7 3, 0 2, 0 3.9 2.5 6th , 0 4.5 4, 8th 4th 0 4th , 3 4th , 7 2 , 6 4th , 6 4th , 7 1 , 6 3 , 3 OO ALA 6, 5 6.4 1.3 6, 5 4, 3 4.3 6.1 4th , 2 3.2 4, 8th 3 9 4th , 2 4th ,1 5 , 0 1 , 2 0 ,8th 5 , 5 3 , 2 cn CYS + MET 4th 1 5.2 5.9 4, 8th 2, 9 4.3 4.5 7th ,8th 2.5 4, .0 6th , 0 4th , 7 2 , 6 4th , 9 5 , 7 6th , 0 5 , 6 2 , 9 \ / AL 7th 6th 8.0 4.6 6, 7th S ₁ 0 3.6 7.7 3 , 2 4.2 5, , 0 4th , 7 6th , 0 4th , 2 8th , 0 5 , 4 6th , 2 8th , 9 3 , 5 O ILE 2 , 6 3.3 7.0 3, 5 2 0 5.5 2.1 4th ,1 2.5 3 _f 8 7th , 9 4th , 5 2 , 0 3 «9 8th ,1 9 ,1 3 ,8th 2 , 6 CO LEU 4th 5.4 3.9 5, 2 , 2 4.6 4.9 , 5 2.2 7th 1 ,8th 6th ,8th 2 , 3 5 , 4 2 , 9 3 , 2 5 2 , 6 TYR - 5.9 7.2 4th 5 ,8th 3 , 0 6th , 7 5 , 7 PHE 2.6 4th , 5 5 , 2 4.6 ......

Tabel

II (cont.)

c *>

σ> ο co "■>

Ο
H" S. e S. a 2 Add > ar denomination after> E χ - d η u fi 4th φ
3 amino acids building Η ·
H- m in Per 16 g. PI
φ
3 ε
Q) nitrogen M. u ρ ine M. - ■ c
η
■ ZT M.
H- M.
3 2 O: H- H
3 H 6th trif Ο:
ι- · before 3 W. 1 1 e trif black L. CU
QJ M φ cn
O ν ε
Φ QJ ' 3 O
3 "
Φ NaOl 14th φ
3 s:
QJ Tt
C.
η
3 * before NaO cn
O 6th uge ε
CU kuch Fra NaO M. uge SSB. (T η
ZT 2
Φ QJ
O cu: α
η η-
C 3
3 (D tj
Qj 3 cn
rr η
> 1 3 *
H * C CU C. 8th meet cn
η
■ ZT
t Φ
3 Fra X
C. CU 0 3 black Λ C. Mrun cn
O 3 φ TJ ZC
OJ C ιΟ 3
rr Hi QJ
C cn
iCy (β 7 \ 3 3 ugei 0)
V)
V) TT 3 4th SSB ΙΤ 3 Η *
CU Z O TT 3 CU (T Φ Φ Ct 3 3 φ rr M. rt 8th CU φ Η * ι— ■ 0) rf M C. 3 ¹ ^ H- σ: 19th H- θ: 8th cn O 0: rr j cn C. t-J η- θ: cn <· O M. 3 CU 0 cn 7th cn 3 cn ! cn 3 O cn «.
Q) £ 3 I. 4th i cn C. 3 I. 9 Φ C. I. ¹ Φ α 3 3 I. α V) 3 2, 4th ¹ cn 3 4th 5 3 3 , 6 5.3 φ ■ 5.3 cn α
Φ 3, 8th 2 , 2 5 ¹ Φ Q. .3 3, 8th 3, 0 2 α 4.8 2 , 7 , 7 2.4 5.5 6.0 3.1 5.7 LYS 14, 1 2 , 6 5 5, 5 3 , 3 1, 9 1, 2 17th ,1 3 _f 0 10 , 9 6, 3.3 , 3 12.0 3.1 2.2 10.0 3.7 HIS 8th, 2 13th , 0 4th 2, 5 2 , 7 14, 4th 16, 3 12th ,1 12.5 9 , 9 2, 3.3 , 6 10.4 8.2 10.6 11.1 14.0. ARG 3, 1 9 , 3 7th 14, 0 11 , 4 9, 5 10, 2 3 , 4 9.8 4th , 9 11 13.5 , 0 3.3 11.3 11.3 3.5 10.3 ASP 4, 9 3 ,8th 3 10, 0 12th , 7 3, 4th 2, 1 4th ,1 3.7 5 , 2 9, 9.5 , 3 3.9 4.5 4.1 4.4 4.1 THR 19 6th 4th , 7 ■ "5 2, 1 2 , 5 4, 5 4, 5 24 , 3 ■ 4.6 23 / 0 3, 3.2 , 5 24.1 6.2 4.9 20.8 5.2 SER 3, 7th 19th , 5 4, 9 4th , 5 21 3 18 4th , 0 23.9 4th ,1 4, 4.4 ,8th 4.5 19.3 17.6 4.4 25.7 GLU 4, 5 4th , 2 m 24, 5 20th , 3 4, 0 3, 4th , 3 3.7 4th , 6 20, 20.7 , 9 3.3 5.0 4.8 3.8 3.3 PER 4, 4th 5 , 4 M. 2, 7th 4th , 6 4, 8th 3, 3 , 2 4.3 4th , 0 4, 4.3 , 3 3.2 4.1 3.6 3.4 4.5 GLY 6, 4th 5 , 2 cn
O 2, 1 5 , 9 4, 4th 4, 2 , 6 4.4 2 , 3 4, 4.3 , 6 2.0 3.8 3.5 1.5 3.4 ALA 4, 8th 2 , 9 Ql 4, 2 3 , 3 2 5 3, 3 , 3 2.0 4th , 7 4, 3.9 , 9 4.0 1.6 1.4 4.8 3,3- ' CYS + KET ■■ -4, 5 5 , 4 3, 5 2 , 0 6, 1 6, 3 , 7 4.9 3 , 4 1, 2.0 , 5 4.8 5.1 5.1 5.8 3.2 VAL 7, 1 4th , 6 rr 4, 2 5 , 9 4th 5 4, 4th , 9 3.6 6th , 3 5, 5.6 , 4 8.2 5.1 5.5 8.3 3.4 ILE 3, 4th 7th ο 4, 3 3 , 2 7th 7th 7, 2 ,1 6.4 3 , 7 4, 4.2 , 4 4.1 8.7 8.2 5.0 .5,4: LEU - 4, 8th 3 , 7 7, 1 7th , 4 2 1 3, 2 ,8th 2.8 7th ,1 7, 6.9 , 2 4.3 3.7 6.0 4.9 3.0 TYR 7th 5 , 5 3, 5 .4 , 4 4th 9 4, ,1 5.4 , 2 3, 3.2 5 4.7 5, Γ 1.6 -ΓΚΕΤ 5 0 5 , 9 6, 7.6 2 , 2 % 17th , 9 O 10 , 7 M.
Φ 3 , 5 dime 3 , 6 3
rt 27 , 9 QJ 3 , 2 C. 5 ,8th cn 3 , 5 6th , 6 α 1 , 5 φ 1
X , 6 0 2 , 5 7th 2 , 3 3 2 ,8th 5 , 3 7th 2 · 3 2 1 5 7th 9 6th 4th 7th 1

OO

on ■ <] ο

CaJ

Tabel

II (cont.)

Amino acid composition in% per 16 g nitrogen

Le in s a a t

Jo j ο b a

grain

potato

alfalfa

cn ο ω

η H . '. ■ - ^Μ ■ s .. .- O: H· M Γ Qi: W ι ^Ο: 3 * 3 ...;: I ^Ν QJ η 3.1 ■ ^ ro ' 'ro W. I ro cn * r : 3 * C. a: Z '3 η C. ro ζ ι- 3 C. ¹ D QJ O 'rf ZS : η οι uQ 3 η t-I C ' ■■; η £ Ο ro S. OJ X M. Η · O): ro ; - «- J Ι 3 ro TC Η » M ■ 3 CU rf 3 rf c '< 0) C. O) TC c ■ Η · 3 ; ία (I. rf 3 ' CU O rf ro *! , ._ i H t- ¹ . C. ■ 3 θ: 3 ■ ' i ! ■ ο ο: cn CO £ c ■ '; ■ Is 3 cn "· I. Q) 3 '! ... a cn a: ' i ro cn H

ν ε

ro οι

3 cn

rf Π

η ζτ

W- £

Hi Q;

C cn

iQ cn

ro ro

3 £

QJ Q) rf Tf O

cn
O

M. QJ rf

3 O

ro

C 3

Q)
cn
cn a ro

cn

Ql

N S

ro a;

01-

η- η

• -! ■ 3 ·

H- £

H, QJ

c cn

vQ cn

ro ro

Ql

cn
cn a ro

C 3

rf

rt

(Π

ro

Ό 3: N ro

3 rf

CU

rf

ro

N Sr

ro Qj. 3 cn rf Π I 3- ■ Η · ί Hi QJ

C cn

vQ cn ■ ro ro ^;

³ ^

OJ C cn

ro

LYS 4, 8th 3 4th r7 4th r8 4th r7 3 r5 3, 8th 4th 4th , 2 3 , 5 2 6th 7th ,1 3 , ι 7th , 6 7th , 0 4.6 HXS 2, 3 2 2 , 5 1 r7 3 , 0 2 rl 2, 2 2 1 , 9 3 , 0 2 . 1 2 ,1 1 , 6 3 ,1 2 , 7 3.7 ARG 9, 5 .8th 9 , 9 11 r4 8th ,1 8th 8th, 3 7th 6th , 6 5 , 2 4th 4th 5 , 2 6th , 7 6th , 2 6th , 5 4.1 ASP 10, 2 11 9 , Z 7th , 9 9 , 9 9 , 2 10, 1 10 16 , 0 6th , 2 5 21st 12th , 9 28 ,1 11 , 0 10 , 0 28.6 THR 4, O 4th 3 , 9 2 r6 5 f3- 5 , 4 5, 5 5 4th , 3 3 , 3 2 4th 5 , 0 1 , 9 5 , 3 5 , 3 4.8 SER 4, 4th 5 : 4 , 6 3 f2 5 , 3 5 , 6 'S, 2 4th 4th «2 4th , 5 4th 4th '5 ,1 2 , 6 4th , 4 4th , 7 5.1 GLU 22 1 21st 21st , 5 32 ,1 12th , 3 12th , 0 12, 1 12th 17th f4 29 , 6 32 15th 12th , 6 22nd , 5 11 ,8th 11 , 6 12.6 PER 4, 3 4th 4th , 7 3 , 0 5 , 5 6th , 4 5, 4th 5 5 U 10 , 0 11 4th 4th , 2 11 , 5 4th , 4 5 ,1 5.9 GLY 5, 7th 5 , ^Λ 5 , 2 7th , 4 7th , 6 8th , 4 7, 3 7th 9 , 3 3 ,8th 3 3 4th , 9 1 , 3 5 ,1 5 , 5 3.9 ALA 4, 4th 5 4th , 6 3 , 0 : 4 , 5 4th , 9 4, 4th 4th 4th , 3 3 , 5. 3 4th 4th ,8th 1 ,8th 5 , 7 6th , 2 6.5 CYS ^ MET 3, 4th 1 3 Γ ³ 5 , 7 5 , 6 5 / 2 5f 3 5 4th , 4 3 , 9 3 3 3 , 6 1 , 5 3 ,8th 2 , 4 0.5 VAL 5, 5 5 5 '3 3 ,1 5 , 6 5 , 6 ■ 6, 1 6th 5 , 7 4th ,8th 3 5 5 , 9 5 , 2 6th , 7 6th ,8th 5.3 ILE 4, 6th 5 4th Js 3 , 5 4th , 2 5 , 2 4, 8th 5 3 , 4 4th , 0 3 4th 5 , 2 2 , 9 5 , 3 5 , 3 3.6 LEU 7, 1 7th 7th , 2 6th rl 7th , 6 8th ,8th 8th, 4th 8th 5 , 5 6th , 9 6th 6th 10 , 2 2 ,1 9 , 0 9 , 9 5.3 TYR 2 8th 2 2 "8th 1 , 7 5 > o ' 3 , 7 5, 5 5 4th , 0 2 , 6 3 3 5 , 3 2 , 0 4th , 6 4th , 9 2.6 PKE 4th 8th 5 5 , 2 2 , 6 5 ,8th 5 , 7 5 , 4 5 2 , 6 5 , 2 4th 4th 5 , 9 4th , 4 6th , 0 6th , 0 2.9 , 0 , 2 , 3 , 5 , 4 , 3 ,1 ,8th ,8th , 9 ,1 , 9 , " ^A ,1 , 6 , 0 , 6 , 0 , 7 , 3 , 3 , 0 , 6 , 2 , 5 , 2 , 7 ,8th , 6 ,8th , 6 , 6 , 3 , 6 , 4 , 4 , 0 , 2 , 2 _r 6 , 6 ,1 ,1 «2 , 9 / 7 , 9 , .7 ,1 , 2 , 5 ;, 5 , 3 ,8th , 9 ,8th , 3 , 0 , 5 , 3 , 9 , 9 , 7

Tabel

III

Balance of the simultaneous production of soy concentrates and isolates and composition of the fractions according to amino acids in % per 16 g of nitrogen

o co ο ar> ο co

O O

■ , LYS Protein content Get-j In concentration Protein content Receive protein protein Dry I. HIS ' of the concentrate nes con kicked of the isolate tenes salary salary mass in ARG steps in% centrate naltene in % dry Isolate of the Ab of the Ab sewage ASP Dry matter in % Proteins mass and in % water water in % THR and together Dry in the Together the in % in% d. SER settlement after Dimensions total settlement after total Dry total GLU amino acids proteins amino acids prote mass U. proteins PER in% / 16 g N in% / 16 g N ine Together GLY settlement ALA n.Amino CYS-MET acids / VAL in %/ ILE 16 q N LEU 64 70 76 90 20th 12th 4th 16 TYR 6.2 5.4 7.8 PHE 2.6 2.4 3.5 7.5 • 7.7 10.1 11.6 12.4 13.2 4.5 3.3 4.7 5.4 4.4 3.3 18.2 21.7 23.9 5.2 - r. 5.4 4.0 4.0 3.8 4.6 4.5 3.6 4.8 3.7 2.2 2.2 4.7 4.9 3.1 4.9 5.4 3.2 7.7 ■ 7.6 3.9 3.7 3.7 4.3 5.4 6.0 3.4

cn ο

CO

Tabel

IV

Solubility of the soy oil cake at ambient temperature as a function of the pH value

CO O CO O to

O O

pH = 3.0 51.4 protein R oh he ■ S ο 1 a - 0 1 k ] 0 ö s 1 i c u c h e r 0 r a k t: protein
amount in
% the
total
proteins Amount of
Dry
mass in
% the
entire
Dry
Dimensions pH = 5.0 59.4 amount in
% the
total
proteins L. Protein-:
salary
in %
Dry
Dimensions 0 I s ο 1 a : h e F. 0 14.6 32.0 pH = 8.0 35.9 65.9 Dry 93.0 82.8 protein
amount in
% the
total
proteins t 5.0 L ο .n 12.3 .31.0 Insoluble fraction pH = 10.0 28.9 87.7 mass in
% of
entire
Dry
Dimensions 0 92.2 i9.5 lot
the
Dry
mass i.
% the
entire
Dry
Dimensions 12.3 Sewage 17.1 30.4. protein pH = 12.0 18.7 36.6 58.6 90.6 98.4 0 9.4 30.1 protein
salary
in %
Dry
Dimensions 23.3 32.3 salary
in %
Dry
Dimensions 27.9 69.0 91.4 46.3 0 20.7 26.7 39.0 pH = 3.0 66.4 13.3,., 46> 7 93.0 48.8 22.8 19.4 pH = 5.0 64.8 43.5 Heat treated 60.0 23.3 23.7 3.9 pH = 8.0 64.8 96.1 32.0 29.0 32.8 3.2 22.8 pH = 10.0 60.6 96.7 77.2 Soy oil cake 32.3 ³ ' ⁹ 20.7 pH = 12.0 40.6 88.5 79.3 4.7 20.7 74.5 74.3 0 9.2 i 6.; 2, '",
»J; )>ι>
*) J>, 20.1 37.0 67.6 0 8.2 »>; ί 3 ^λ 47.3 7.6 10.2 20.6 12.8 56.8 14.1

ι ι

ro oo

O CO

Table V Raw soy oil cake

Composition of the fractions obtained at different pH values in% per 16 g of N

(O

σ> ο CaJ

O O

Unsolvable i MET 5 , 5 PH = 3 , 4 (Away- 9 pH _ C , 4 7th , 9 PH egg 6th " 8th , 3 Away- I. 4th pH 3 = 10 away I. 2 Jnl ( , 7 12th , 9 away Rougher! 3 liche 2 , 6 Sol Ie , 4 6th U.N- ,8th 3 ,1 -! 5 , 5 9 Salvation 4th whats 3 3H , 2 ,1 What Soy 9 Frac 7th , 3 fraction , 7 3 solving Sol , 4 8th , 4 Unsolvable 8th , 5 5 liche 6th Soluble ser 0 3S- ,8th • Soluble , 4 ser oil 5 tion 11 rl , 6 7th liche ,8th 15th , 9 lich 3 Soluble , 7 ! 1 Frac 2 fraction 7, 9 Liehe , 7 fraction , 5 7.1 ku 4th 3 , 9 ,8th 8th liche frac- ,8th 5 , 2 Frac 4th fraction ,8th wMs-j 7th tion 4th 3, I.
I. 7th Frac ,1 , 3 3.5 9 4th , 5 , 4 5 Fraction , 7 5 , 5 tion I. 1 G ser 9 9 8th, 9 tion , 9 2 8.7 1 13th , 3 , 5 8th tion ,8th 16 , 5 6th ',1 -7 7th 1 12, ., 9 , 2 , ~ 14.1 9 .5 , 3 , 7 3 , 2 5 , 4 4th ,1 2 ^ 4th 5 Iso- 4, 5 , 6 , 0 4.4 chen 5 4th , 2 , 7 jwäs- ^; 2 , 9 4th , 2 2 , 7 8th, 3 5 lat 4, 8th , 3 , 7 5.2 1 LYS 4th , 9 Iso- , 0 ■ ser 3 , 4 4th ,8th 0 , 7 16, 9 4, 9 16, 3 , 0 , 9 21.2 2; KIS .1 , 9 lat ,8th, 5 , 3 1 , 5 ■ 5, 2 , 5 5, 2, 8th 5.7 5, 9 3 , 2 Iso- , 0 6.2 3 ARG :; 5 , 9 , 2 5 2 , 5 4th , 5 2, 6th Iso- , 2 5, 0 6, 7th 2.5 3, 5 2 ,1 lat , 3 4.3 4th ASP 5 , 7 5 , 4 5 7th , 5 5 ,1 6, 0 lat , 7 17, 7th 13, 4th 7.8 4, 3 1 ,8th , 4 3.9 6, 6th DOOR 8th ,8th 2 , 6 6th 11 , 2 6th , 4 11 c O 5, 5 4, 3 12.0 4, 3 13th , 5 5 , 4 0.2 2, 6 ' SER 3 , 9 7th ,8th 8th 3 , 4 0 , 9 4, A. 5 ', 9 4, 4, 3 3.7 4, 8th 3 , 4 2 , 5 3.9 7, 5 . GLU 5 ,8th 12th , 9 4th , 7 4th , 5 5, 9 2 , 7 4, 3 19 3 4.5 4, 5 2 , 2 8th , 6 4.6 12, 4th PER .: 3 19th 17, 7th - 5, 19.7 6, 22nd 12th 6.2 3, GLY .. 4th 5 5, 11 5, 4, 5.3 2, 6th 4th 2.2 4, ALA 19th 3 4, '3 4, 3.8 5, 5 5 4.2 13, CYS + 5 '4 4, 4th 6 ^ O, 4.0 6th 17th 5, VAL 3 2 1, 19th - 5, 2.1 1 5 4, ILS 4th 5 5, '5 4, 5, 5.2 6th 3 4, LEU 2 5 6, 3 8th, 5.4 5 .4 3, TYR 5 8th 8th, 3 3, 8.5 9 1 5, ■ Ρ.ΗΞ 5 3 3, 2 5, 3.8 3 5 5, 7th 5 6, 5 5.9 6th 5 7, .3 9, 5 3 3, 5
i 1, 8th 4th 5 .. 9, 3 6th 15, 4, 5, 21 6, 4, 4, 4, 4, 6, 0, . -

OO cn

CD CO

CD O Ca)

Table V (cont.): Heat-treated soy oil cake Composition of the fractions obtained at different pH values in% / 16 g N

pH = 3

pH. =; 5 ;

■ pH = 8 ■■■ ...:

pH = 10

pH = 12

- Insoluble

Frak-Frak ^ ^ic J ^öliche sol- Fraction Frak-Frak- jFrak-Frak- liehe tion ^ ioft tion: Frak-Iso-

ition lat

LYS. ■
HIS

ARG
AS?
THR
SER
, GLU
PER
GLY
ALA

CYS + MET
VAL

ILS

LEU

TYR

PHE

5.7 7.5 6.3 7.9 6.1 2.5 -3.7 2.6 3.6 2.8 6.9 13.1 7.2 13.9 7.4 11.6 13.3 11.8 12.8 11.2 3.9 4.0 4.0 3.9 4.0 4.6 3.0 4.9 2.9 4.4 20.6 ■ 23.5 19.6 24.7 18.6 6.8 4.1 5.3 3.6 5.6 3.7 4.2 3.9 4.2 4.0 4.4 4.2 4.4 4.5 4.3 2.5 1.5 2.8 1.7 3.2 .5.2 ■ 2.7, 5.0 2.3 5.5 5.1 3.0 5.2 2.5 5.9 7.5 3.9 7.8 3.0 8.3 - 3.6 4.2 3.6 4.9 3.2 5.4 '5.0 5.5
I. 3.6 6.0

5.5 2.5

7.1.

11.7 3.7 4.2

25.8 5.3 3.7 4.4 2.7 5.1 4.1 7.4 3.2 5.6

Insoluble _ dissolve! Fraction ion borrowed

Ab- Frak-Isowastion ilat ser. i

Soluble-soluble heat-resistant fraction S traded! Fra- ι

Ab-; tion was-; ! ser!

Isolate

6.2 5.4 7.8 2.6 2.4 3.5 7.5 7.7 10.1 11.6 12.4 13.2 4.5 3.3 4.7 5.4 4.4 3.3 13.4 21.3 23.9 5.2 5.4 4.0 4.0 3.8 4.6 4.5 3.6 4.8 3.5 2.6 2.2 4.7 4.9 ■ 3.1 4.9 5.4 3.2 7.7 7.6 3.9 , 3.7 3.7 4.3 5, Λ 6.0 3.4

6.1
3.0

6.7
10.9
4.9
4.6
15.8
5.5
4.5
5.5
1.6
6.2
5.3
8.6
4.1
5.9

5.4 2.3

8.1

12.4

3.3

4.1

21.6

5.6

3.8

4.1 1.2 5.0 5.3 7.9 4.0 6.0

Soy ■ ■, ·! Abplkuchen \

water·

8.2 3.6

10.5 12.3 4.8 4.0 22.0 4.1 4.2 4.7 5.1 2.5 2.9 3.8 3.9 3.4

6.5 2.9

7.9 11.8 4.2 4.7 13.7 5.4 3.9 4.1 3.6 5.0 5.0 7.2 3.6 5.3

Table VI Content of toxins, detoxification and distribution of the

remaining toxins (peanut, cottonseed and rapeseed oil cake)

the end
gangs
oil
cake In NaOH
insoluble
che
fraction Isolates Wash water
and centric
fuaenwasser Peanut 570 - Aflatoxins,
Parts / billion 300 0-2 2-25 2-10 Cottonseed Gossypol, ° / oo
free 2 0.03 0.01 0.05 total 14th 0.5 0.3 0.2

ITC + VTO, / oo 6.5

0.1-0.5 0.1-0.5 4-6

Isoflavones,

° / oo 9.5 0.2-1 0.1-0.5 2-3

Table VII Bacteriological properties of the proteins obtained

Bacteriological standards recommended by the PAG

Proteins obtained ■:

Aerobic germs Anaerobic germs Fungal spores Streptococci d.Group Streptococcus aureus

Sulphite-reducing clostridia

Escherichia coli enterobacteria Schigella Salmonella Arizona

<2 χ OK ⁴ / g

<io ⁴ / g

<10 / g

absent / 1 g

<iO ² / g

absent / 10 g
absentä '/ 0, 1 g
abv; esend / 25 g
absent / 25 g
absent / 25 g

1000-7000 / g absent / g 2 to 5 / g ^: absent / g absent / 10 g

absent / g absent / 10 g absent / 1 g absent / 25 g absent / 25 g absent / 25 g

030603 / ^ 001

Table VIII

protein <- * . 0.25 KJ ω X NS t t e r υ η g s ν e r rn 14th 35 '18 xn H ■ 1 tn L. 30th 20th , 15 H 11 20th 20th , 20 H ί 5 ₃ I.
H φ S L 1 C H e H H 14th 85 ) W. O:: !
■ o P. 14th 75 ) H ■ CX) source H- 0 ο H- Composition of the feed ο 51, ). 47, O cn 54, O 8th , 45 tn 54 8th , 45 cn φ ω H- cn cn 51, P. H : Φ H ₁ 51, C. , cn grain
strength [—I 0 H- LJ. rt UJ. 2C .20 O 2 , 10 O 2 , 15 O 3 O I. W. H ^; H O υ 2C 'U H- rt rt 2C cn O
co Sucrose O O QJ N OJ 8th 8th P. M. 3 H ■ P. cn cn 1— ' 8th cn iQ H, O 8th φ \ Peanut oil 3 " I. Φ ι .2 : 1 I. P. Φ 4th OJ 4th OJ C / j " P. O O P. P. 2 I. I. Φ H ₁ 2 rt H ₁ Cellulose 0 ο: CT H rt 3 ■ 0 rt 0 rf j P. rt 50 3 H . M. rt! rt , 15 s; H- Hi 0.25 H, 3 ^ iramin- and OJ H Φ cn 4th , 35 4th O tr 0 0 I. ξ] P. P. .4 ü p: Qj Φ 4th 0 P Φ. cn Φ η 0 , 15 : ° ' 0 0 p. ■■ tr Pj! O rt: rt <j <$ O 3 tD Φ 0 rt ι Φ H ₁ η Ρ 0 , 15 0 ISI G O φ ^: O (D. J-I O O 0 N H ₁ ] I. H- ο 3 OJ 0 0 φ 5 H, , ty η ; H <j <3 3 3 0 Φ H- H H O 3 OJ 3 * Oj rt 3 Φ 3 ! cn O O 3 iQ cn cn 3 Φ Φ rt 3 zn M. Φ 40 P. 3 3 tn rt (I) O O tj P. H ₁ I. P. l-i 05 P. Φ i- $ cn; H , H-" Φ rt P. Hi tr 05 rt td cn P. P. P. 3 ο tr (D rt cn H ₁ QJ cn rf rt rt ; ι co H O Φ 3 Π ti 12th 18th 22nd 11 14th 11 2: 11 13th O 53.75 43.35 44, 75 ⁷⁵ 54.55 1, 54.50 45, 95 54.85 49.70 co 20th 20th 20th 20th 20th 14th 12th 05 20th 2C 20th 20th O
O 8th .: 8th 8th 8th 8th 50, 95 53 8th 8th 8th 8th 2 V 2 1 2 2 20th .20 2 0 2 0 8th 8th Mineral additive3 ⁴ ■ 4th 4th 4th 4th 2. 2 4th 4th 4th 4th DL-methionine 0.15 0, 25th 25th 0.35 O, 0 0 15th 0.35 0.3! L-lysine HCl 0 0 0 O, 4th .4 30th 0.50 0 0.50 0 L-threonine 0 0 0.10 0, 0, 45 O, 45 0 0 0.30 0 0, 45 O, 20th O, 15th 0,

Tabel

VIII (cont.)

O OD O

Middle Ge 9 P. 12.0 KJ cn SC 57 , 2 ■ ■ t e r U η cn 57 1 cn H cn 5 9 1 57 H g s ν e r Ώ ¹ 57 ! 3 i 10, I.
H ' S U C. H H e H 57 H ! » O:; ■ Ώ PJ i rt tr ¹ \ ■ C. r weight of jFood intake ' li O H- FUt Composition ( O 0 cn 0 cn Ies fodder ro cn cn: cn cn PJ 1-" : (D H ₁ . H, C. Rats too | me / day / al ο 5.4 H- LJ. rt , 0 LJ. LJ. O 3 2 O H tr : 3 3, O ' C3 O H O O H- rt ft PJ N Start, g :. G. . O PJ N PJ , 7 PJ 3 1 | —I cn cn M > PJ cn [—I cn U3 H{ O rt ro Middle Ge 4.4 sr I. ro , 2 PJ ro 6th PJ O Φ cn '. ³ ' PJ OJ O PJ I. I. ro Hi H, weight of G MQ. Pj O O: he M. ■ 12 ,8th rt 3 32 rt J-I 115 ι £ j rt. 3 rf H- ¹ ft 118 rt ^ i ^) H- . H ₁ 3 Rats after cn ro cn 0 tr PJ i C PJ O Pj: p. ro ro • 17 days, C E P ro ro p? sr 0 ,1 3 <^ ft ■ tr O <j rt <j 3 CJ ro (_j H- PJ 10 N 1, O 10.6 'O ro H ⁴ 0 0 11 O N I. I. 3 3 0 3 ; 125 PJ Q 5 3 p. ■ sr Μ <j 3 3 ro H- H H 0 PJ Tuesday rt 3 j3 ro 4, (0 3.4 cn O 3, 3 cn cn 3 ro ro I. rt 3 cn ! n ~ ?? PJ 3 ω pd rt ro O O PJ j I 'i 1 3 H ₁ I. 3, PJ ι 3.0 H ¹ PJ ro 3 ' Pj Hi cn (- » I— ' ro OO rt ■ Hi ro rt W. cn * C3 PJ PJ Pj 3 I.
U) cn tr ro ; 4th rt H- H ₁ PJ cn rt rt rt I. -j H, O ¹ Cb 3 CD 3 3 co C. 57 57 57 57 '■■ 5 " 57 57 57 57 1 57 57 1149 125 156 129 126 125 119 I 120 . ■■ 12th i 3 3 116 127 112, 0 12.3 12.0 10 1 ro 9 O 12.5 10, 4th 10.5 3 11 : 4.0 '5.3 4.2 4, 4th 4th 10, 5 12, 0 4.0 6th 3, 7th 3.7 , 3 3.3 4.7 ; 3.5 3 6th 3 3, 5 4, 1 . 3.2 3 3, 5 -3./5 , 0 3, 3, 5 57 117

Claims (18)

Claims 1) Method of Obtaining Food Proteins of vegetable origin with removal of toxic substances and non-protein substances, characterized in that that he a) the vegetable raw material that contains the proteins, / with hydrogen peroxide in a reaction medium that has a pH in the alkaline range from 8.5 to 11.5 has treated and thereby makes the proteins soluble in the reaction medium, b) separating the substances insoluble in the liquid medium of stage (a) from the liquid medium of stage (a) and thereby forms a protein solution, c) the protein solution at a pH of 6 to 8.5 acidifies and thereby the insoluble fraction, the compounds other than the desired food proteins contains, fails, d) the insoluble matter from the protein solution of the Stage (c) separates and here a clarified problem 030603 / 0C11 receives cash redemption, e) adding at least one enzyme of the peroxidase type to the clarified solution, which removes the remaining hydrogen destroy peroxide and any peroxides present in the clarified protein solution able to f) adding at least one antioxidant to the protein solution obtained in step (e) and g) the solution obtained in step (f) is subjected in a known manner to a treatment by which the proteins contained therein are separated off, and the proteins are isolated by conventional methods. 2) Method according to claim 1, characterized in that the vegetable raw materials containing proteins one of the following substrates is used: a) seeds (soy, broad beans, peas, lupine, sunflower, safflower, cereals, corn, oats), b) Oil cake (soy, sesame, peanut, sunflower, rapeseed, Linseed, cottonseed, safflower, copra, palm kernel, jojoba), c) tubers (potatoes) and d) Green plants (alfalfa, spinach, sorghum). 3) Method according to claim i or 2, characterized in that step (a) is carried out under conditions which ensure intimate contact of the vegetable raw material and the liquid reaction medium, the raw material for this purpose previously known treatments of the type are adapted to the plant material used, for example cleaning, peeling, dry grinding with subsequent sieving or wet grinding, for example in a colloid mill. 030603/0011 4) Process according to claim 1 to 3, characterized in that the pH of the reaction medium is Stage (a) by adding an organic and / or ... '' inorganic basic agent, e.g. sodium hydroxide, Sodium carbonate, potassium hydroxide, ammonium "- hydroxide, calcium hydroxide and magnesium hydroxide, or an organic base, such as alkanolamines, ethanolamine, holds in the alkaline range, with as alkaline agent is preferably used sodium hydroxide. : 5) Process according to claim 1 to 4, characterized in that the pH of the reaction medium in the step. (a) in the case of seeds between about 8.5 and 11.5 and in the case of tubers and roots and in the case of j of green plants lasts between about 8 and 9. 6) Method according to claim 1 to 4, characterized in that net that cooked soybean oil cake is stored at a pH value not exceeding 10 in the alkaline range; acts and thereby a soy protein concentrate wins. 7) Method according to claim 1 to 5, characterized ^ that the alkaline solution to be used in step (a) in an amount of about 2 to 10 parts by weight ' used per part by weight of the vegetable raw material; this amount in the case of seeds about 5 to 10 parts by weight and in the case of tubers and roots' 2 to 5 parts by weight. j 8) Process according to claim 2, characterized in that j one serving as the reaction medium in step (a) alkaline solution also used as a medium for grinding the; vegetable raw material used if a previous Wet milling of the starting material is carried out. 9) Process according to claim 1 to 8, characterized in that the hydrogen peroxide as such or in j Form of at least one preliminary stage, preferably a j 030603 / Ό011 -4ο Food grade precursor such as sodium peroxide used. 10) The method according to claim 1 to 9, characterized in that the hydrogen peroxide in an amount of 0.2 to 3 vol .-%, based on the volume of the alkaline solution and calculated as H "0 _? at 33.3% by volume, used. 11) Method according to claim 1 to 10, characterized in that one in step (a) at ambient temperature works and thereby the plant material and the alkaline medium in the presence of hydrogen peroxide during A sufficient amount of time is kept in contact to produce virtually all of the proteins that are in the plant material are included to make them soluble. 12) Method according to claim. 1 to 11, characterized in that in step (c) the protein solution coming from step (b) is brought to a pH between about 6 and 8.5, depending on the plant material, by adding at least one acidic substance, preferably a food grade acid, e.g. hydrochloric acid, sulfuric acid or phosphoric acid, or an organic acid, e.g. Acetic acid, lactic acid or citric acid, with hydrochloric acid and sulfuric acid being preferred. _: 13) Method according to claim 1 to 12, characterized in that that the enzyme in step (e) is an enzyme of the peroxidase type, preferably catalase, in particular Catalase obtained from beef liver is used. 14) Method according to claim 13, characterized in that the catalase in an amount of 200 to 400 g per 100 kg of dry protein mass in the from step (d) coming solution used. 030603/001 1 15) Method according to claim 1 to 14, characterized in that that the antioxidant is di-t-butyl-p-cresol or another antioxidant or a mixture of known antioxidants is used. .. 16) The method according to claim 1 to 15, characterized in that in step (g) the proteins by treating the protein solution coming from step (f) with an edible acid, for example HCl or HpSO., Up to the isoelectric pH value ( 4.7 to 5) or by coagulating the proteins by blowing steam into the solution or by performing a biological ^] precipitation of the proteins by cultivating a micro ι Organism in the solution wins. ' 17) Suitable for human and animal nutrition, produced by the method according to claims 1 to 16 Proteins. , 18) Soy protein concentrate, made according to the process ^! according to claim 6. 030603 / 0C1 1