JPH0239221B2 - NETSUGERUKASEITANPAKUSHITSUTANRIBUTSU - Google Patents

Description

[Detailed description of the invention]

The present invention relates to novel heat-gelling protein isolates suitable for use as egg white substitutes or bulking agents. Egg whites have certain functional properties that make them useful in a variety of food compositions. One of these properties is the ability of the aqueous solution to heat set into a gel. Such gels are quite rigid and typically have about 35-40 textrometer units (TU) as measured by a GF textrometer. The G.F. Textrometer and its operation were described in the paper developed by H.E.T. Friedman in the Journal of Food Science, 1963, Vol. It is described in detail in "Gigi Yuament". Attempts have been made to provide heat-set vegetable proteins to gels with hardness values similar to or higher than egg whites, but none have been successful until recently their application became known. Conventional isoelectrically produced soybean isolates produce gels that are significantly softer than egg whites; this bean isolate produces gels that are significantly softer than egg whites; such gels have hardness values of less than about 20 T.U. have. It is now surprising that a dispersion of heat-gelable vegetable protein having a hardness value of about 35 T.U. or more and preferably at least about 40 T.U. is an aqueous dispersion of a substantially undenatured vegetable protein isolate. It was discovered that by adjusting and manipulating the PH and ionic strength values of Accordingly, the present invention combines the heat-gelling properties of a substantially undenatured vegetable protein into a food-grade protein of sufficient food grade to provide a dispersion ionic strength of at least about 0.2 molar in its heat-gelling dispersion. of the dispersion and sufficient food grade acidifying agent to give the dispersion pH of up to about 6.0. The present invention also provides a thermogelatable gel comprising a substantially undenatured vegetable protein isolate dispersed in an aqueous phase having an ionic strength of at least about 0.2 molar and a pH value of up to about 6.0. Includes suitable aqueous protein dispersions. Also included within the scope of the present invention are plant protein isolates, food grade salts and food grade acidifying agents in specified proportions, whereby the compositions are Aqueous dispersions of the above type can be produced that can heat gel to gels of at least equal hardness to gels produced from egg whites at the same protein concentration and under the same gelling conditions. The present invention is based on the mixed effects of manipulating the PH and ionic strength conditions of a substantially native plant protein isolate, as measured by differential scanning calorimetry. Assigned U.S. Patent No.
No. 4,169,090 and No. 4,208,323 (the disclosures of which are hereby incorporated by reference) contact protein source materials with sodium chloride under conditions of critical PH and ionic strength to solubilize, precipitate, and eliminate proteins. Description of a method for isolating proteins from protein source materials by diluting protein solutions with water to low ionic strength resulting in the formation of protein micelles in the aqueous phase that are collected as shaped protein micellar material (sometimes abbreviated as "PPM") There is. Protein solutions can be subjected to ultrafiltration. Sedimentation by centrifugation can also be performed prior to the dilution step. The protein micellar material produced by this method is a novel protein isolate, a vegetable protein isolate that produces a thermogelatable dispersion.
The novel protein isolate is described in detail in copending U.S. patent application Ser. No. 081,484 filed October 3, 1979, assigned to the assignee of the present application
The disclosure thereof is intended to be incorporated herein. As described in more detail herein, the novel protein isolate contains at least 90% by weight of vegetable protein as 6.25 times nitrogen as determined by the Kjeldahl method and is a protein micelle consisting of a homogeneous amphoteric protein component. A substantially native protein isolation product in the form of a protein micellar material produced by precipitation of a solid phase from an aqueous dispersion and produced from at least one vegetable protein source material. The protein isolation product is substantially free of lipids, substantially free of lysinoalanine,
Contains substantially the same lysine as the storage proteins in the source material. The isolated product is provided in a dry state by drying the amorphous protein material. The aqueous dispersion of protein micelles from which the isolate is precipitated is prepared by the method of U.S. Pat. can be produced by dissolving the protein in the vegetable protein source material using a protein solution and diluting the protein solution to an ionic strength of 0.1 molar or less for the production of a dispersion. Aqueous dispersions of protein micelles can also be prepared by the method of U.S. Pat.
- Use a food grade salt solution with a pH of approximately 6.8 PH to increase the protein concentration of the protein solution while maintaining a substantially constant ionic strength and to form a concentrated protein solution at approximately 6.8 PH.
Produced by dilution to an ionic strength of 0.2 molar or less. In the latter method, the food grade salt solution is about 0.2 - about 0.8
and a pH of about 5.3 to about 6.2. Further, the protein concentration step is preferably carried out by membrane technology with a volume reduction factor defined as the ratio of the volume of the protein solution to the volume of the concentrated protein solution, from about 1.1 to about 6.0. Further dilution of the concentrated protein solution is carried out by passing the concentrated protein solution through water having a temperature below about 25° C. and a volume sufficient to reduce the ionic strength of the concentrated protein solution to a value of about 0.06 to about 0.12 molar. is preferred. In one embodiment of the latter method, the food grade salt solution has a PH of about 5 to about 5.5 and the phosphorus content of the protein solution is reduced before the dilution step. The food grade salt used in the dissolution process described above is usually sodium chloride, although other salts such as potassium chloride or calcium chloride can also be used. In accordance with the present invention, the thermal gelling properties of the dispersion of protein isolate in water are at least 1 mol sufficient to provide a dispersion ionic strength of at least about 0.2 molar.
of seed food grade salt and a dispersion of at least about 6.0 or less
This is improved by incorporating into such dispersions sufficient at least one food grade acidifying agent to provide the PH. The ionic strength of the protein provided by the at least one food grade salt typically varies from the lower limit of about 0.2 molar up to about 1.5 molar, and within the range of about 0.3 to about 0.75 molar for reasons discussed in detail below. It is preferable that the Although such ionic strength values indicate a relatively high salt concentration for the thermogelling dispersion, the total salt concentration in the food composition in which the thermogelling dispersion is mixed is necessarily very low. Constant within acceptable levels. The PH of the protein dispersion varies from an upper limit of about 6.0 or less to about 3.5, but is preferably in the range of about 4.5 to about 5.5 for reasons discussed in detail below. The incorporation of food grade salt and food grade acidifying agent into the protein dispersion can be accomplished in a number of ways. One method of mixing is to dissolve the food grade salt and food grade acidifying agent directly into the aqueous dispersion of the vegetable protein isolate. Alternatively, after separating the required proportions of food-grade salt and food-grade acidifying agent from the residual aqueous layer, the solid phase precipitated from the isolation process is uniformly mixed and the mixture is dried to form a protein dispersion. Produced from a dry mixture. Such dry mixtures can also be produced by dry blending food grade salts, food grade acidifiers and dry isolates. The mixed dry composition obtained from the latter operation and capable of being dispersed in water to produce a heat-gelling dispersion constitutes an aspect of the invention. The relative proportions of protein, food grade salt and food grade acidifying agent in such a mixed dry composition will depend on the intended protein concentration in the heat gelling dispersion, the form of the acidifying agent and the food grade depends on a number of factors, including the source of the salt. For example, a food grade acidifier can be made to provide a portion of the food grade salt. Also, a full concentration of food grade salts can be supported as part of the food system in which the protein dispersion is used. Generally, about 0.5 to about 4.0 parts by weight of food grade acidifying agent and 0 to about 2.5 parts by weight of food grade acidifying agent are mixed for each 100 parts by weight of dried vegetable protein isolate.
Such compositions include isolates dispersed in an aqueous phase in which the dispersion in water has an ionic strength of at least about 0.2 molar and a pH of up to about 6.0.
Dispersions with protein concentrations of % W/W can be produced. The food grade salt used in this invention to provide the necessary ionic strength is usually sodium chloride, although other food grade salts such as potassium chloride or calcium chloride can be used. The food grade acidifying agent used in this invention to provide the required PH value is any food grade acid, usually hydrochloric acid, but phosphoric acid, citric acid, malic acid and tartaric acid can also be used. Food grade acidifying agents may be of a nature that provides some of the ionic strength to the dispersion, such as sodium tartrate or sodium citrate. It has been discovered that increasing the ionic strength of a protein dispersion by more than about 0.2 molar increases the hardness of the heat-set gel formed from the dispersion at a given pH up to about 6.0 to a maximum value before decreasing once again. It was observed that as the PH further decreased, the gel hardness increased to a maximum value at the same ionic strength values above about 0.2 molar, and that the gel strength decreased with further decreases in the PH value. As the ionic strength of the dispersion increases, a maximum in gel hardness occurs at low PH values. There is a wide range of ionic strengths and PH values where the gel strength does not vary significantly, and over this range the gel strength values are usually greater than 35 T.U., preferably greater than about 40 T.U., and therefore at least egg white (35-40 T.U.). As good as U). For example, soybeans without added sodium chloride
At PH4.5-7.5 for PMM, the gel is generally soft with a hardness value of 4-8 T.U. and the hardest gel (21T.U.).
U) was produced at PH6.5. These values are comparable to the hardness values of egg white (35-40 T.U.). As the concentration of added sodium chloride increases, the gel hardness obtained increases and reaches a maximum value exceeding 48 T.U. of egg white at PH5.0NaCl0.5M. Increasing the concentration of sodium chloride in the range 0.75-1.0 molar over that PH value range slightly decreases the hardness of the gel from this maximum value. Wide range of high gel hardness
Observed at sodium chloride levels above 0.3 molar;
Gels with hardness values above 40 T.U. were obtained at PH4.5-5.5. As sodium chloride increases, maximum gel hardness occurs from PH6.5 to 0.5 at 0 molar NaCl.
The pH decreased to 5.0 at molar sodium chloride and became 4.5 at 1.0 molar sodium chloride. The presence of added salt substantially increases the dispersibility of the protein. At low ionic strengths of 0-0.1 molar, dispersibility ranges from 10-30% and the gels produced under these conditions are extremely soft. 0.2
At molar NaCl and above, the dispersibility is markedly
70% and is relatively insensitive to changes in NaCl concentration and PH. However, heat-set gel hardness is independent of dispersibility above about 30%, and hard and soft gels have poor protein dispersibility.
Can be achieved under conditions of over 70%. The presence of food grade salt influences the final properties of the gel produced by thermal gelation of the dispersion. Gels with similar hardness values have completely different visual appearances. Gel “sliceability” is an important factor in product application
can be measured by the Warner-Bratzler method. This method is used in the Journal of Textile Studies
It is described in detail in the article "Modification of Texture Instruments" by P. d'Avrill Boissey, Vol. 2, pp. 129-195, 1971.
As the ionic strength of the dispersion increases, the slicability of the gel, as measured by the Warner-Bratzler method, increases until it drops again rapidly. For example, the sliceability of soybean PMM gel is relatively independent of pH, but is very sensitive to changes in sodium chloride concentration. The highest value is 0.3−0.5 mol NaCl
This value is obtained in the range of higher or lower
It decreases rapidly at NaCl levels. The sliceability values are inferior to those of egg whites but superior to those of gels from conventional vegetable protein isolates. By manipulating protein dispersions formed from protein isolates by adding sodium chloride and adjusting the pH, heat-set gels can be formed that have the same good or superior hardness as egg white. These results indicate that dispersions or dry mixtures of isolates, food-grade salts, and food-grade acidifiers may be used more effectively than unmodified isolates due to their gelling properties in various food systems. It can be used as an egg white substitute or bulking agent. Food systems in which the compositions of the present invention are specifically utilized include U.S. Pat.
Used in a variety of meat analogs, including bacon analogs as described in No. 3,840,677. The wide range of PH and salt concentration values resulting in high values of gel hardness provides flexibility from a processing point of view. Egg whites are versatile under a wide range of conditions and are often used in meat analogues due to both their gelling and dispersing properties. However, for PMM isolates, the conditions that give the optimal gelling properties as described here are not necessarily the conditions that give emulsifying properties, and the composition of the present invention can be directly substituted for a preparation that is optimized for the multifunctionality of egg white. It shows multifunctionality and is quite sensitive to the environment. The protein source material from which the protein isolate is produced is any of the conventional salt extractable protein sources, usually oilseeds, preferably soybeans or legumes, preferably fababeans and field peas. The responses of isolates from different protein sources are similar, and any differences in gelling behavior result from differences in individual properties such as amino acid composition between the protein sources. Example 1 This example is a specific example of the effect of ionic strength and PH on the gelling properties of a soybean PMM dispersion. Protein isolate was produced from soybeans according to the method of US Pat. No. 4,208,322. 34.1Kg of soybean concentrate (approximately 50% protein by weight) with 50 gallons (228) of 0.35M sodium chloride solution and 15% at 25°C
Mixed at W/V concentration. The mixture has a pH of about 6.3 and about 30
Stir for a minute. The aqueous protein extract was separated from the residual solids. The extracts were concentrated by ultrafiltration on "Romicon" type XM50 and Comicon type PM50 cartridges for a time sufficient to obtain a 4x volume reduction factor. Romicon ultrafiltration cartridges are manufactured by Rohm and Haas and are designated as "50" for a cutoff with a molecular weight of 50,000 Daltons. The concentrate was diluted in cold water at a temperature of 7°C to an ionic strength of 0.13 molar which produced a white cloud of protein isolate in the diluted system. The protein dispersion was allowed to settle to the bottom of the dilution vessel as a highly viscous amorphous gelatinous precipitate. 4.2 Kg of wet PMM containing 72.7% water by weight was separated from the distilled water phase and lyophilized to 95.5% by weight substantially unmodified (as determined by differential scanning calorimetry).
of protein (nitrogen measured by Kiedal method ×
6.25) protein isolate was 1275Kg. A sample of the dried isolate produced by the above method was 20
% by weight aqueous dispersion. Adjust the ionic strength of this dispersion by adding 6N HCl or 6N NaOH for major changes or for minor adjustments.
Changed to 4.5-7.5 by adding 0.1NHCl or 0.1NNaOH. The samples were dispersed at external temperature (20°-25°C) for 30 minutes. The protein dispersion was prepared in a stainless steel gel tube (2 1/2 inch i.d. ×
3/4 inch) (6.3 cm x 1.9 cm). Gel tubes are heated in a boiling water bath for 45 minutes, then heated to 20℃
Cool for a minimum of 20 minutes. The gel was transferred from the tube immediately prior to testing to minimize water loss from the surface. Each gel is sliced into three 3/4 inch (1.9 cm) long cylinders with a diameter of 2 inches (5 cm).
The hardness was tested using a G.F. textilometer using a disk plunger. Each sample was compressed twice and the peak height was measured. The hardness was calculated by the following formula according to the method of Friedman et al. (mentioned above). Hardness (TU) = height of first peak x millivolt/2/voltage The hardness values obtained for various gels are referred to as PH.
It was plotted graphically against NaCl concentration. The results obtained are reproduced in FIG. As seen in Figure 1, the gel hardness increased rapidly for ionic strengths above 0.3 and pH values of about 4.5. As the ionic strength increases, the pH at which the maximum gel hardness is reached shifts downward, reaching a maximum of 48 T.U. at PH 5.0 and NaCl 0.5 mol. Further increasing the concentration of NaCl is accompanied by a slight decrease in gel hardness values, but with a shift towards an optimal PH. PH migration and gel hardness increase from 3.5TU to PH range 4.5−5.5 and ionic strength range of 0.3−0.75M NaCl
High hardness exceeding As a control, gels produced from egg white at various salt concentrations and PH values were relatively insensitive to PH and salt concentrations, and gel hardness values in the range of 35-40 T.U were observed. Example 2 This example illustrates the effects of PH and NaCl on the sliceability of gels produced from soybean PMM dispersions. Soybean PMM was prepared according to Example 1, and gels were produced from a dispersion of dried soybean PMM at each PH and sodium chloride concentration as described in Example 1.
Gel slicability was evaluated using a Warner-Bratzler (WB) apparatus (details described above). The apparatus consists of an electrically powered press and force transmission device to provide the force generated by the deformation of the sample. The signal of the force transmitter is amplified and converted into a hardware recorder (a model with 200 parallel disc registers).
7100B). 3 pieces of 0.04 inch (0.1cm)
blades are attached to the force transmission device, each having a diameter of 1
It has a triangular hole that draws an inch circle. 3 samples
It is placed through the hole in the blade and pulled up through the three 0.045 inch (0.11 cm) slots. 12
Using a crosshead speed of cm/sec, the instrument was calibrated to a 2.5 Kg full scale reading with 5% sensitivity;
The millivolt input to the recorder was varied to keep the sample peak on the scale. The chart speed of the recorder used was 0.1 inch/minute (0.25 cm/minute). The area of the generated peak was measured using a mechanical integrator and recorded in counts. The value obtained is PH
The NaCl concentration was plotted on a chart and the results are shown in Figure 2. The higher the area value, the greater the gel's slicability. As can be seen in Figure 2, the WB area is relatively independent of pH and most sensitive to sodium chloride concentration, with the area being highest between 0.2 and 0.5 molar NaCl and rapidly increasing at higher and lower levels. was found to decrease. Example 3 This example is a specific example of the effects of PH and NaCl on protein dispersibility. Soybean PMM was prepared and a dispersion was produced therefrom according to the method of Example 1. Dispersions used to generate protein gels at various PH and NaCl concentrations were centrifuged at 3000xg for 10 minutes. A sample of the supernatant was taken and the amount of nitrogen was determined by Kiedal analysis. % dispersity of protein was expressed as % of expected total protein (20% by weight). The results obtained are plotted in a diagram against PH and NaCl,
The results are shown in Figure 3. As can be seen in Figure 3, NaCl concentrations above 0.3M consistently resulted in high protein dispersion throughout the entire PH range. Example 4 This example is a specific example of applying adjustment of pH and ionic strength to other protein source materials. (a) PMM isolates were prepared from faba beans and wild peas generally according to Example 1, and gels were prepared using PH and
Hardness values were measured by preparing samples with different NaCl concentration conditions. The response to PH and NaCl concentration was observed similar to that for soybean. For faba beans, the hardest gels were produced under conditions of high NaCl (0.5-1.0 mol) and pH (4.0-5.5). For wild peas, the corresponding conditions were NaCl 0.5-1.0 M and PH 4.0-5.5. The conditions for maximum hardness varied depending on the protein source, with the stiffest gels observed for soybean PMM. (b) Promin D (a commercially available soybean isolate produced by isoelectric precipitation, commercially available from Central Soy) was added to various
20 containing sodium chloride with varying concentrations depending on pH
A gel was formed from the weight percent dispersion according to the method outlined in Example 1. Measure the hardness of the gel,
It was discovered that soybean PMM gels with and without NaCl were significantly stiffer, and the gel hardness was higher in the case of 0.2 molar NaCl than in the case of 0 molar NaCl. Promine D with low pH (4.0-5.0) containing high concentration of NaCl (0.5-1.0 mol)
was extremely soft (4.TU). These results showed that this commercially available isolate had a gelling effect that was quite different from that of soybean PMM. Example 5 This example is illustrative of the use of a composition of the invention to replace a portion of egg whites in a bacon analogue. In accordance with the method outlined in U.S. Pat. No. 3,840,677, the publication of which is incorporated herein by reference, the red and white hues of bacon analogues were prepared using the ingredients and amounts outlined in Tables 1 and 2 of the patent. It was prepared using A series of substitution levels of soybean PMM replacing egg white ("albumen") were tested for white hue at varying PH and NaCl concentrations. The results are shown in Table 1 below.

Table: 55% substitution of egg white at PH 4.5, 0.75 M NaCl (in the aqueous phase) produced an acceptable tissue product, whereas other levels of substitution at higher PH and NaCl concentrations resulted in tissue production. This resulted in a significantly unsatisfactory decline. For red color, 100% replacement of egg white is soybean
Conventional products containing egg white and conventional soy isolate when soy PMM was also used to replace conventional soy isolate in the red phase did not produce an acceptable product in the case of PMM. A product with a texture comparable to the one obtained was obtained. To summarize the present disclosure, the present invention provides novel thermogelatable protein isolates that are produced by manipulation of the PH and ionic strength of dispersions of protein micellar materials and that produce gels of comparable or superior hardness to egg whites. I will provide a. Modifications are possible within the scope of the invention.

[Brief explanation of drawings]

FIG. 1 is a diagram showing the effect of PH and sodium chloride concentration on the hardness of gels produced from substantially undenatured soy protein isolate. FIG. 2 is a diagram showing the effect of PH and sodium chloride concentration on the texture of gels produced from soy protein isolates. FIG. 3 is a chart showing the effect of PH and sodium chloride concentration on the dispersibility of soy protein isolate.

Claims (1)

[Scope of Claims] 1 (a) 100 parts by weight of a substantially undenatured vegetable protein isolate containing at least 90% by weight of vegetable protein (x6.25 nitrogen as determined by the Kjeldahl method); (b) at least A kind of food grade acidifying agent about 0.5 to approx.
4.0 parts by weight, and (c) from 0 to about 2.5 parts by weight of at least one food-grade salt, the composition comprising: 4.0 parts by weight of at least one food-grade salt; It has a protein concentration of about 10 to about 30% (W/
W) A vegetable protein composition capable of producing a protein dispersion. 2. The composition according to claim 1, wherein the food grade salt is sodium chloride. 3. The composition according to claim 1, wherein the food grade acidifying agent is hydrochloric acid. 4. The plant protein isolate is derived from soybean.
Compositions as described in Section. 5 At least 90% by weight of vegetable protein (as nitrogen x 6.25 determined by Kjeldahl method)
1. A method of producing a plant protein composition comprising a substantially undenatured plant protein isolate having improved heat gelling properties comprising:
a food grade salt sufficient to provide the dispersion with an ionic strength of at least about 0.2 molar in the thermogelable dispersion of the protein isolate; a food grade acid sufficient to provide the dispersion with a PH value of up to about 6.0; A method characterized by blending with a curing agent. 6. The method of claim 5, wherein said ionic strength is about 0.2 to about 1.5 molar. 7. The method of claim 5, wherein said ionic strength is from about 0.3 to about 0.75 molar. 8. The method according to claim 5, 6 or 7, wherein the food grade salt is sodium chloride. 9. The method according to claim 5, wherein the PH value is about 3.5 to about 6.0. 10. The method of claim 9, wherein the PH value is about 4.5 to about 5.5. 11. The method of claim 5, 9 or 10, wherein the food grade acidifying agent is selected from the group consisting of hydrochloric acid, phosphoric acid, citric acid, malic acid and tartaric acid. 12 The ionic strength is about 0.3 to about 0.75 molar, the pH value is about 4.5 to about 5.5, the food grade salt is sodium chloride, and the food grade acid is hydrochloric acid. The method described in scope item 5. 13. An amorphous protein material, wherein the protein isolate is formed by precipitation of a solid phase from an aqueous dispersion of protein micelles consisting of an amphoteric protein component and formed from at least one vegetable protein source material. claim 5, wherein the product is substantially free of lipids, substantially free of lysinoalanine and has a lysine content identical to the storage protein in the source material.
The method described in section. 14. The aqueous dispersion of protein micelles from which the isolate precipitates has a concentration of at least 0.2 molar ionic strength and 5.5
dissolving the protein in the at least one vegetable protein source material using a food grade salt solution having a pH of ~6.3 at a temperature of about 15°C to 35°C;
14. The method of claim 13, wherein the dispersion is formed by diluting a protein solution to an ionic strength of 0.1 molar or less. 15. The aqueous dispersion of protein micelles from which the isolate is to be precipitated is prepared using a food grade salt solution having an ionic strength of at least 0.2 molar and a pH of about 5 to about 6.8. The protein in the protein source material is heated to about 15°C to about 35°C.
C. to form a protein solution, increasing the protein concentration of the protein solution while maintaining the ionic strength substantially constant, and diluting the concentrated protein solution to an ionic strength of about 0.2 molar or less. 14. The method of claim 13, wherein the dispersion is produced by: 16 The food grade salt solution has an ionic strength of about 0.2 to about 0.8 molar and a pH of about 5.3 to about 6.2, and the protein concentration step is performed by membrane technology to reduce the volume of the protein solution and the volume of the concentrated protein solution. The volume reduction factor as determined by the ratio of approximately 1.1
~6.0°C, and dilution of the protein concentrate solution is carried out at a temperature below about 25°C and an ionic strength of the protein concentrate solution of about
16. The method of claim 15, wherein the method is carried out by passing through water having a volume sufficient to reduce the volume from 0.06 to about 0.12 molar. 17. Mixing the food grade salt and the food grade acidifying agent homogeneously with the precipitated solid phase after separation from the remaining aqueous phase, drying the homogeneous mixture thus formed, Claims 14, 15 or 16, wherein the food grade salt and the food grade acidifying agent are mixed in the dispersion by forming the dispersion from the method of. 18 Drying said precipitated solid phase after separation from the remaining aqueous phase and homogeneously mixing said food grade salt and said food grade acidifying agent with the resulting dry isolate; Claim 14: mixing said food grade salt and said food grade acidifying agent in said dispersion by forming said dispersion from
15 or 16. 19 Dissolving the food-grade salt and the food-grade acidifying agent in the aqueous dispersion of the precipitated solid phase, so that the food-grade salt and the food-grade acidifying agent are dissolved in the dispersion. Claim 14 mixing
15 or 16. 20 Aqueous protein micelles containing at least about 90% by weight of vegetable protein (6.25 x nitrogen as determined by the Kjeldahl method), consisting of a homogeneous amphoteric protein component, and produced from at least one vegetable protein source material consisting of a substantially undenatured vegetable protein isolate which is an amorphous protein mass by precipitation of a solid phase from a dispersion, said product being substantially free of lipids and containing substantially lysinoalanine; the isolate has an ionic strength of at least about 0.2 and a lysine content substantially the same as the storage protein of the source material;
An aqueous protein dispersion suitable for thermal gelation into a gel, characterized in that it is dispersed in an aqueous phase having a pH value of up to 21. The dispersion according to claim 20, wherein the vegetable protein source material is selected from the group consisting of soybean, fabarbin and wild pea. 22. Claim 20, wherein said isolate is present in said dispersion at a concentration of about 10 to about 30% W/W.
Dispersion liquid as described in Section. 23. The dispersion of claim 20, wherein said ionic strength is from about 0.3 to about 0.75 molar. 24. The dispersion according to claim 20, claim 21, or claim 23, wherein the pH value is about 4.5 to about 5.5.