Gelatinized bean protein

Abstract

The present invention relates to a soy protein composition having improved gel strength at neutral pH, and a method for producing the same.

Description

Technical Field

[0001] The present invention relates to the field of plant proteins, in particular to bean protein isolates, and more particularly to pea protein isolates. Background Art

[0002] Humans need 12% to 20% of their daily protein intake from food, which is provided by animal products (meat, fish, eggs, dairy products) and plant products (cereals, legumes, algae).

[0003] In industrialized countries, people primarily consume animal protein, but numerous studies have linked excessive animal protein consumption, rather than plant protein, to increased rates of cancer and cardiovascular disease.

[0004] Furthermore, animal protein presents numerous drawbacks, both in terms of allergenicity (particularly proteins found in milk or eggs) and environmental protection (associated with the harmful effects of intensive farming).

[0005] Therefore, there is an increasing demand in industry for plant-derived compounds that have superior nutritional value and functional properties, unlike animal-derived compounds that have various disadvantages.

[0006] Soybeans have been and continue to be the most important plant-based alternative to animal protein. However, using soy has certain drawbacks. Soybean seeds are often genetically modified and require solvent de-oiling to obtain their protein.

[0007] Since the 1870s, seed plants, particularly peas, have been actively cultivated in Europe (primarily in France) as an alternative protein source to animal protein for animal and human food. Peas contain approximately 27% protein by weight. The term "pea," in its broadest sense, specifically includes all wild varieties of "smooth peas," as well as all mutant varieties of "round peas" and "wrinkled peas," for various uses (human food, animal feed, and / or other applications). These seeds are non-GMO and do not require solvent de-oiling.

[0008] Pea protein, mainly vicilin, has been industrially extracted and processed for many years. Patent EP1400537 can be cited as an example of a pea protein extraction process. In this process, the seeds are ground without water (the so-called "dry grinding" process) to obtain soy flour. This soy flour is then suspended in water to extract the protein. Other processes for extracting soy protein are also described in documents US4060203 A, FR2889416 A1 and WO 2011 / 124862 A1. Document JP55-131351A describes a process for producing soy protein isolate: fine-grained soy flour is placed in an aqueous solution and the protein portion is precipitated by bringing the aqueous solution to an acidic pH. The precipitated protein solution is then neutralized and heat-treated (or atomized) to form soy protein isolate.

[0009] However, legume proteins, particularly pea proteins, have much lower gelling properties than soy proteins. As mentioned in "Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques" (Bastistaa et al., International Journal of Biological Macromolecules, Vol. 36 (2005), pp. 135-143, 2005), pea and lupin proteins have lower gelling abilities than soy proteins.

[0010] Therefore, it is valuable to obtain soy proteins, especially soy protein isolates, and even more particularly pea protein isolates, with improved gelling power or gel strength. These soy proteins can be added to food or pharmaceutical products. The pH of these products varies greatly, ranging between 4 and 9. In many applications, such as meat or fish substitutes, the proteins are "neutral pH," that is, around pH 6 to 8. In the case of these meat and fish substitutes, for example, the proteins help to bind other textured proteins together after gelation. Therefore, it is particularly advantageous to provide new and improved soy proteins with a gel strength greater than that at neutral pH.

[0011] Attempts have been made to reduce the particle size of protein isolate and concentrate, and to study the functional properties of the resulting composition. For example, Sun et al.'s paper (Reduction of particle size based on superfinegrinding:Effects on structure, rheological and gelling properties of wheyprotein concentrate, Journal of Food Engineering, Phase 186, 2016, 69-76 pages) describes the use of nano-bead mills to grind whey protein concentrate. They have studied the different properties of protein, including particle size, gel strength, dyeing and infrared structure under different pH values. In terms of gel strength, compared with the protein before grinding, the protein composition after grinding has higher gel strength at acidic pH (4.5), and has lower gel strength at neutral pH (6.5) and alkaline pH (8.5).

[0012] The paper by Hayakawa et al. (Microparticulation by Jet Mill Griding of Protein Powders and Effects on Hydrophobicity, Journal of Food Science, Vol. 58, No. 5, 1993, pp. 1026-1029) describes the use of an air jet mill to microgranulate casein and egg white-type proteins, as well as soy fiber. This document does not describe soy proteins. Nor does it describe increasing protein gel strength.

[0013] Liu et al.'s paper (Ball-milling changed the physicochemical properties ofSPI and its cold-set gels, Journal of Food Engineering, No. 195, 2017, pp. 158-165) describes grinding soy protein isolate using planet BM and Mixer Mill MM400 ball mills to slightly reduce its particle size (average size of 80 microns). However, although the gel strength of this isolate under acidic conditions (when glucose-δ-lactone is present) can be increased using Mixer Mill MM400 grinding mills, it is still very weak (the maximum increase is about 30%). In addition, grinding with plant BM type grinding mills does not result in any difference in observed gel strength. Similarly, the document does not study the protein gel strength at neutral pH. Summary of the Invention

[0014] According to a first aspect of the present invention, a soy protein composition is provided, the soy being particularly selected from peas, lupins and broad beans, characterized in that the gel strength of the protein composition according to test A is greater than 200 Pa, preferably greater than 250 Pa, more preferably greater than 300 Pa, and most preferably greater than 350 Pa. The soy protein composition is preferably selected from soy protein isolates, more preferably from pea protein isolates.

[0015] According to another aspect of the present invention, a method for producing a protein composition is provided, characterized in that the method comprises the following steps:

[0016] 1) Processing leguminous plant seeds, preferably selected from peas, lupines and beans;

[0017] 2) Grinding the seeds to make a water suspension;

[0018] 3) Separate the water-insoluble fraction using centrifugal force;

[0019] 4) At 55°C + / - 2℃ and 65℃ + / - 2℃, preferably 60℃ + / - coagulation of the protein by heating to an isoelectric pH at 2°C for between 3.5 minutes and 4.5 minutes, preferably 4 minutes;

[0020] 5) recovering the coagulated protein flocs by centrifugation;

[0021] 6) Adjust pH to 6 + / - 0.5 and 9 + / - between 0.5;

[0022] 7) As an option, heat treatment can be performed;

[0023] 8) drying the coagulated protein flocs;

[0024] 9) Grinding the coagulated protein flocs with an air jet grinder and drying to obtain particles with a particle size D90 of less than 20 microns, preferably less than 15 microns, more preferably less than 10 microns.

[0025] According to a final aspect of the present invention, a legume protein composition, preferably a legume protein isolate selected from pea, lupin and bean, more preferably a pea protein isolate according to the present invention, is proposed for industrial use in food or pharmaceuticals, in particular in animal and human food.

[0026] The present invention can be better understood from the following detailed description. Summary of the Invention

[0028] According to a first aspect of the present invention, a soy protein composition is provided, the soy protein being in particular selected from peas, lupins, and broad beans, characterized in that the gel strength of the protein composition according to Test A is greater than 200 Pa, preferably greater than 250 Pa, more preferably greater than 300 Pa, and most preferably greater than 350 Pa. The soy protein composition is most preferably peas. For example, the gel strength of the protein composition according to Test A may be less than 450 Pa, for example less than 400 Pa. The soy protein composition is preferably selected from soy protein isolates, more preferably from pea protein isolates.

[0029] The term "protein composition" as used herein refers to a composition obtained by extraction and purification, comprising proteins, macromolecules composed of one or more polypeptide chains consisting of a plurality of amino acid residues linked to each other by peptide bonds. In the specific context of pea proteins, the present invention particularly relates to globulins (which comprise approximately 50-60% of pea proteins). Vicilins are primarily divided into three subfamilies: legumin, tardigrades, and tardigrades.

[0030] The term "legume" as used herein refers to the order Vicia, a dicotyledonous plant. This plant family is one of the most important flowering plant families, second only to the orchids and the Asteraceae in terms of species diversity. It encompasses approximately 765 genera and over 19,500 species. Many legumes are important cultivated plants, including soybeans, beans, peas, chickpeas, broad beans, peanuts, lentils, alfalfa, various clover varieties, broad beans, carob, liquorice, and lupine.

[0031] "Gelling power" refers to the functional property of a protein composition's ability to form a gel or network, while increasing viscosity and producing a state of matter intermediate between a liquid and a solid. The term "gel strength" may also be used. To quantify this gelling power, it is necessary to generate such a network and assess its strength. To perform this quantification, Test A is used in the present invention and is described as follows:

[0032] 1) At 60°C + / - At 2°C, the protein composition to be tested contains 15% + / - Solubilization was carried out in water with 2% dry matter at a pH of 7;

[0033] 2) At 60°C + / - Oscillate at 2°C for 5 minutes;

[0034] 3) Cool to 20℃ + / - 2°C, stirred at 350 rpm for 24 h;

[0035] 4) preparing the suspension in an applied stress rheometer equipped with concentric columns;

[0036] 5) Measure the elastic modulus G' and the viscous modulus G" by applying the following temperature profile:

[0037] a. Stage 1: at 20°C + / - After stabilization at 2°C, the + / - 2℃ heated to 80℃ + / - 2°C temperature, measurement parameter G'1;

[0038] b. Stage 2: at 80°C + / - 2℃ for 110 minutes; c. Stage 3: from 80℃ within 30 minutes + / - 2℃ temperature cooling to 20℃ + / - 2℃ temperature at 20℃ + / - G'2 was measured after stabilization at a temperature of 2°C;

[0039] 6) Calculate the gel strength equal to G'2-G'1.

[0040] Preferred are applied stress rheometers with concentric columns, such as the DHR 2 (TA, Instruments) and MCR 301 (Anton Paar). These have a Peltier temperature control system. To avoid evaporation problems at high temperatures, paraffin oil is added to the sample.

[0041] A "rheometer" in the sense of this invention is a laboratory instrument capable of measuring the rheological properties of fluids or gels. It applies forces to the sample. Generally, its characteristic dimensions are very small (the mechanical inertia of the rotor is very low), allowing for fundamental investigations of the mechanical properties of liquids, gels, suspensions, pastes, etc., under applied forces.

[0042] The so-called "applied stress" mode allows the determination of intrinsic viscoelastic quantities of a material, which depend, inter alia, on time (or angular velocity ω) and temperature, by applying a sinusoidal stress (oscillatory mode). In particular, this type of rheometer allows the determination of the complex modulus G*, which in turn allows the determination of the modulus G' or elastic part and G" or viscous part.

[0043] The first three steps involve resuspending the protein in water under precise conditions to maximize subsequent measurements.

[0044] The water is preferably selected from permeate water, but drinking water can also be used.

[0045] Its temperature is 60℃ when it is initially resuspended + / - 2°C (first and second steps), then 20°C after dissolving for 24 hours and cooling before measurement + / - 2°C (third step). In general, unless otherwise stated, the temperatures given in this description always include + / - A change of 2°C, for example 20°C + / - 2℃ or 80℃ + / - 2℃.

[0046] Add the required amount of protein to the water to obtain 15% + / - A suspension with a 2% dry matter content is prepared. For this purpose, equipment familiar to the skilled person is used, such as a beaker or a magnetic rod. A volume of 50 mL is shaken at 350 rpm for at least 10 hours at room temperature. In general, the dry matter content given in this specification always includes the dry matter content, unless otherwise stated. + / - 2% change, for example 15% + / - 2%. Use a pH meter and acid-base reagent to adjust the pH to 7 + / - 0.5, which is well known in the prior art.

[0047] The fourth step is to introduce the sample into the rheometer, covered with a thin layer of oil to limit evaporation.

[0048] In the fifth step, the following temperature schedule was used: a. Phase 1: from 20°C to + / - 2℃ heated to 80℃ + / - 2℃ temperature; b. Stage 2: at 80℃ + / - 2℃ for 110 minutes; c. Stage 3: from 80℃ within 30 minutes + / - 2℃ temperature cooling to 20℃ + / - 2℃ temperature.

[0049] The parameter G' is continuously measured and recorded during this timeframe.

[0050] The sixth and final step of Test A is to operate on the records. Two values ​​are to be extracted: G'1 = the value of the temperature at 20°C at the beginning of phase 1. + / - G' value after stabilization at 2°C, G'2 = G' value at 20°C at the end of stage 3 + / - G' value after stabilization at 2°C.

[0051] The gelling force is equal to G'2-G'1.

[0052] Preferably, the protein richness of the pulse protein composition according to the invention is more than 80%, preferably more than 85%, more preferably more than 90% by weight relative to the total weight of dry matter.

[0053] Protein abundance is measured by any technique known to those skilled in the art. Preferably, the total nitrogen content (calculated as a percentage of the total dry weight of the composition) is measured and the result is multiplied by a factor of 6.25. This method is well known in the field of plant proteins and is based on the fact that proteins contain an average of 16% nitrogen. Any dry matter determination method known to those skilled in the art may also be used.

[0054] The particle size D90 of the protein composition is preferably less than 20 microns, more preferably less than 15 microns, most preferably less than 10 microns.

[0055] "D90" in the present invention refers to the particle size in micrometers, which is divided into two groups in terms of quantity, accounting for 90% and 10% of the total particles in the protein composition, respectively.

[0056] For D90 measurement, a laser particle size analyzer is preferably used, more preferably a Malvern Mastersizer 2000. The following parameters are used: use in liquid form, dispersed in ethanol; refractive index: 1.52; absorption index: 0.1; no ultrasound is used.

[0057] Preferably, the protein composition according to the present invention has a high solubility at neutral pH. In order to quantify the solubility of the protein composition, according to the present invention, test B is used. This test comprises the following steps:

[0058] Add 150 g of distilled water at 20°C + / - 2°C to a 400 mL beaker while stirring with a magnetic bar and accurately add 5 g of the soy protein sample to be tested. If necessary, adjust the pH to 7 with 0.1 N NaOH or 0.1 N HCl. Make up to 200 g with water. Mix at 1000 rpm for 30 minutes and then centrifuge at 3000 g for 15 minutes. Collect 25 g of the supernatant and place it in a crystallizing dish that has been dried and tared in advance. Place the crystallizing dish in a thermostat at 103°C + / - 2°C for 1 hour. Then place it in a desiccator (with a dehydrating agent) to cool to room temperature and weigh it.

[0059] Solubility corresponds to the content of soluble dry matter, expressed as a percentage of its weight to the weight of the sample. The solubility is calculated as follows:

[0060] [Math.1]

[0061]

[0062] in:

[0063] P = sample weight (unit: g) = 5 g

[0064] m1 = weight of the crystallization dish after drying (unit: g)

[0065] m2 = weight of the empty crystallizing dish (unit: g)

[0066] P1 = collected sample weight (unit: g) = 25 g

[0067] Advantageously, according to Test B, the solubility of the protein composition of the invention is between 30% and 65%, such as between 33% and 62%, in particular between 38% and 60%.

[0068] Another advantage of the present invention is that it improves the gelling properties of pea protein while maintaining its solubility. However, these properties appear difficult to reconcile: for example, increasing the solubility of a protein through proteolysis is coupled with a loss of its gelling properties. Without being bound by any theory, this can be explained by the fact that, in general, once proteins aggregate, they must form a network to form a protein gel. Gelatinized proteins are larger, remain so even when returned to solution, and therefore generally have lower solubility. However, the present invention reconciles these two properties.

[0069] According to another aspect of the present invention, a method for producing a bean protein composition is provided, wherein the method comprises the following steps:

[0070] 1) Processing leguminous plant seeds, preferably selected from peas, lupines and beans;

[0071] 2) Grinding the seeds to make a water suspension;

[0072] 3) Separate the water-insoluble fraction using centrifugal force;

[0073] 4) At 55°C + / - 2℃ and 65℃ + / - 2℃, preferably 60℃ + / - coagulation of the protein by heating to an isoelectric pH at 2°C for between 3.5 minutes and 4.5 minutes, preferably 4 minutes;

[0074] 5) recovering the coagulated protein flocs by centrifugation;

[0075] 6) Adjust pH to 6 + / - 0.5 and 9 + / - between 0.5;

[0076] 7) As an option, heat treatment can be performed;

[0077] 8) drying the coagulated protein flocs;

[0078] 9) Grinding the coagulated protein flocs with an air jet grinder to obtain particles with a D90 particle size of less than 20 microns, preferably less than 15 microns, more preferably less than 10 microns.

[0079] The process begins with step 1) processing leguminous plant seeds, preferably selected from peas, lupins and beans.

[0080] When the legumes selected are peas, the peas processed in step 1) may have previously undergone steps well known to those skilled in the art, such as cleaning (to remove unwanted particles, such as stones, dead insects, soil residues, etc.) or by a well-known "shelling" step to remove the outer fibers (outer cellulose coating) of the peas.

[0081] It may also have undergone treatments designed to improve its organoleptic properties, such as dry heating (or roasting) or wet blanching. When blanching, the temperature is preferably between 70°C. + / - 2℃ and 90℃ + / - 2℃, adjust pH to 8 + / - 0.5 and 10 + / - 0.5, preferably 9 + / - These conditions are maintained for 2 to 4 minutes, preferably for 3 minutes.

[0082] The process according to the invention comprises step 2): grinding the seeds and preparing a water suspension. If the seeds are already watered, the water is retained, but it can also be replaced and the seeds ground directly. If the grains are dry, a flour is first prepared and then suspended in water.

[0083] Milling is performed by any suitable technique known to the skilled person, such as a ball mill, a cone mill, a spiral mill, an air jet mill or a rotor / rotor system.

[0084] During the grinding process, water can be added continuously or discontinuously at the beginning, during or at the end of the grinding so as to obtain, at the end of this stage, an aqueous suspension of ground peas having a dry matter (DM) weight of between 15% and 25%, preferably 20% by weight relative to the weight of the suspension.

[0085] At the end of grinding, the pH value can be checked. Preferably, at the end of step 2, the pH value of the aqueous suspension of ground peas is adjusted to between 5.5 and 6. + / - 0.5 and 10 + / - 0.5, for example, the pH is adjusted to 6 + / - 0.5 to 9 + / - 0.5. Optionally, adjust the pH to 8 + / - 0.5 and 10 + / -0.5, for example, to adjust the pH to 9. The pH can be adjusted by adding an acid and / or a base, such as sodium hydroxide or hydrochloric acid.

[0086] Then, according to the process of the present invention, step 3) is carried out: the water-insoluble fraction is separated by centrifugal force. This mainly consists of starch and polysaccharides called "internal fiber". The soluble proteins in the supernatant are concentrated.

[0087] According to the process of the present invention, step 4) is carried out: at 55°C + / - 2℃ and 65℃ + / - 2℃, preferably 60℃ + / - The protein is coagulated by heating to an isoelectric pH at 2°C for between 3.5 and 4.5 minutes, preferably 4 minutes. This is to separate the desired pea protein from the other components of the supernatant in step 3). For example, the applicant's patent EP1400537 describes an example process from paragraphs 127 to 143. Good control of the time / temperature schedule is crucial: as will be illustrated below, these parameters are crucial for obtaining a gelled protein composition according to the present invention.

[0088] The next step 5) involves recovering the coagulated protein flocs by centrifugation and separating the solid portion of the protein concentrate from the liquid portion of the sugar and salt concentrate.

[0089] In step 6), the flocculent material is resuspended in water and its pH is adjusted to between 6 + / - 0.5 and 9 + / - The dry matter content of the suspension is adjusted to between 10% and 20%, preferably 15%, by weight. The pH value is adjusted using any acidic or alkaline agent. Ascorbic acid, citric acid, and potassium salts or sodium hydroxide are preferred.

[0090] As an option, step 7) can be performed: a heat treatment aimed at ensuring the microbiological quality of the protein. This heat treatment can also be used to functionalize the protein component. Preferably, the heat treatment is carried out at 100°C. + / - 2℃ to 160℃ + / - A typical ratio of 2°C is heating for 0.01 to 3 seconds, preferably 1 to 2 seconds, followed by immediate cooling.

[0091] In step 8), the coagulated protein flocs are dried to a dry matter weight ratio of at least 80%, preferably at least 90%, relative to the dry matter weight. For this purpose, any technique known to those skilled in the art, such as freeze drying or atomization, may be employed. Atomization is a preferred technique, particularly multi-effect atomization.

[0092] The dry matter content is determined by any method known to those skilled in the art, preferably using the so-called "drying" method. This involves heating a known amount of a sample of known mass to determine the amount of evaporated water: initially, the sample is weighed and its mass m1 is measured in grams. The sample is then placed in a heating chamber to evaporate the water until its mass stabilizes and the water is completely evaporated (preferably at 105°C at atmospheric pressure). Finally, the sample is weighed and its mass m2 is measured in grams. The dry matter content is calculated as follows: (m2 / m1)*100.

[0093] The final step 9), like the aforementioned step 4), is crucial for obtaining the protein composition according to the present invention. It involves grinding the coagulated protein floccules and drying them to obtain particles with a D90 particle size of less than 20 microns, preferably less than 15 microns, and more preferably less than 10 microns. An air jet mill is used in this step of the process. An opposed air jet mill is preferably used, and more preferably a Netzsch CGS10. This type of mill reduces size by generating collisions: particles accelerated by high-speed gas jets fragment upon impact.

[0094] In an advantageous method according to the invention, the gel strength of the protein composition according to test A is at least 150%, advantageously at least 200%, for example at least 300% of the gel strength of the protein flocculent dried in step 8. The gel strength of the protein composition according to test A can, for example, be at most 600% of the gel strength of the protein flocculent dried in step 8.

[0095] As mentioned above, one advantage of the present invention is that protein solubility can be maintained during the grinding step. Advantageously, the solubility of the protein composition according to Test B is at least 75% of the solubility of the dried protein flocculent in step 8, advantageously at least 90%.

[0096] One advantage of the present invention is that the protein composition of the present invention can exhibit a high gel strength at different pH values, in particular at a neutral pH value, such as the conditions of Test A. The protein composition according to the present invention is advantageously used in any type of food and pharmaceutical product: the pH value of the food or pharmaceutical product may be between 4 and 9, for example between 5 and 8.5, in particular between 6 and 8, or even about 7.

[0097] According to a final aspect of the present invention, a legume protein composition, preferably a legume protein isolate selected from pea, lupin and bean, more preferably a pea protein isolate according to the present invention, is proposed for industrial use, in particular for animal and human food.

[0098] Due to their improved gelling power, the protein composition according to the present invention is particularly suitable for food applications, such as plant-based yogurts or meat-analogs. It can be used in particular for meat or fish substitutes. It can be used, in particular, as a binding agent, for example, in the production of meat or fish substitutes. Therefore, another aspect of the present invention is a method for producing a meat or fish substitute comprising the protein composition according to the present invention.

[0099] The present invention will be better understood with reference to the following non-limiting examples. Example

[0100] Example 1: Production of a bean protein composition according to the present invention

[0101] After the outer fibers are shelled in a hammer mill, the pea seeds are ground into flour. They are then soaked in water to a final concentration of 25% dry matter relative to the weight of the suspension and a pH of 6.5 for 30 minutes at room temperature. The flour suspension with a dry matter weight percentage of 25% is then added to a hydrocyclone to separate a light phase consisting of a mixture of protein, internal fibers (pulp) and dissolved substances and a heavy phase containing starch. The light phase leaving the hydrocyclone is then raised to a dry matter weight percentage of 10.7% relative to the weight of the suspension. The internal fibers are separated by a WESTFALIA type centrifugal decanter. The light phase at the outlet of the centrifugal decanter contains a mixture of protein and dissolved substances, while the heavy phase contains pea fibers.

[0102] The protein is coagulated at its isoelectric point by adjusting the pH value of the light phase at the outlet of the centrifugal decanter to 4.6 and heating the solution at 60°C for 4 minutes. After the protein has coagulated, the protein flocs can be recovered. The protein flocs are resuspended in drinking water to form a suspension, and the dry matter mass accounts for 15.1% relative to the mass of the suspension. The pH value of the suspension is adjusted to 7 with caustic potash. Finally, it is heat-treated at 130°C for 0.4 seconds and then flash-cooled. The suspension is then atomized on a NIRO MSD multi-effect atomizer with an inlet temperature of 180°C and an outlet temperature of 80°C. The mass of the powder obtained is 92.3% relative to the total weight of the dry matter, of which 85.5% is protein. This powder is called the "base material of the composition according to the invention."

[0103] The powder was then milled using a Netzsch CGS10 opposed air jet mill to give a powder with a D90 particle size of 7.3 microns.

[0104] The resulting powdered protein composition is referred to as a "micronized protein composition according to the present invention."

[0105] Example 2: Comparative Example to Demonstrate the Effect of a Heating Table on the Coagulation of a Protein Composition

[0106] The purpose of this example is to demonstrate the influence of the coagulation table on the functionality of the protein composition according to the invention.

[0107] After the outer fibers are shelled in a hammer mill, the pea seeds are ground into flour. They are then soaked in water to a final concentration of 25.1% dry matter relative to the weight of the suspension and a pH of 6.5 for 30 minutes at room temperature. The flour suspension with a dry matter weight of 25% is then added to a hydrocyclone to separate a light phase consisting of a mixture of protein, internal fibers (pulp) and dissolved substances and a heavy phase containing starch. The light phase leaving the hydrocyclone is then raised to a dry matter weight of 11.2% relative to the weight of the suspension. The internal fibers are separated by a WESTFALIA type centrifugal decanter. The light phase at the outlet of the centrifugal decanter contains a mixture of protein and dissolved substances, while the heavy phase contains pea fibers.

[0108] The protein was coagulated at its isoelectric point by adjusting the pH value of the light phase at the outlet of the centrifugal decanter to 4.6 and heating the solution at 70°C for 4 minutes. After the protein coagulation, the protein flocs were recovered. The protein flocs were resuspended in drinking water to prepare a suspension, and the dry matter mass relative to the mass of the suspension was 14.9%. The pH value of the suspension was adjusted to 7 with caustic potash. Finally, it was heat treated at 130°C for 0.4 seconds and then flash cooled. The suspension was then atomized on a NIRO MSD multi-effect atomizer with an inlet temperature of 180°C and an outlet temperature of 80°C. The mass of the powder obtained was 91.9% relative to the total weight of the dry matter, of which 84.9% was protein. This powder was called "base material for comparative protein composition No. 1".

[0109] The powder was then milled using a Netzsch CGS10 opposed air jet mill to obtain a powder with a D90 particle size of 8.2 microns.

[0110] The resulting powdered protein composition was designated "Micronized Comparative Protein Composition No. 1."

[0111] Example 3: Comparison of different protein components obtained in Example 1 and Example 2

[0112] To compare protein composition, the aforementioned experiment A was used, as well as dry matter and protein abundance.

[0113] [Table 1]

[0114]

[0115] Table 1 above clearly demonstrates the importance of the synergistic effect of the coagulation temperature and particle size reduction to a particle D90 of less than 10 μm in maximizing gelling power. The gelling power of the micronized protein composition according to the present invention is approximately four times greater than that of the base protein composition according to the present invention, the base of comparative protein composition No. 1, and comparative micronized protein composition No. 1.

[0116] Example 4: Production of the soy protein composition according to the invention

[0117] After the outer fibers are shelled in a hammer mill, the pea seeds are ground into flour. They are then soaked in water to a final concentration of 25% dry matter relative to the weight of the suspension and a pH of 6.5 for 30 minutes at room temperature. The flour suspension with a dry matter weight percentage of 25% is then added to a hydrocyclone to separate a light phase consisting of a mixture of protein, internal fibers (pulp) and dissolved substances and a heavy phase containing starch. The light phase leaving the hydrocyclone is then raised to a dry matter weight percentage of 10% relative to the weight of the suspension. The internal fibers are separated by a WESTFALIA type centrifugal decanter. The light phase at the outlet of the centrifugal decanter contains a mixture of protein and dissolved substances, while the heavy phase contains pea fibers.

[0118] The protein is coagulated at its isoelectric point by adjusting the pH value of the light phase at the outlet of the centrifugal decanter to 5.0 and heating the solution at 60°C for 4 minutes. After the protein has coagulated, the protein flocs can be recovered. The protein flocs are resuspended in drinking water to form a suspension, and the dry matter mass accounts for 18% of the mass of the suspension. The pH value of the suspension is adjusted to 7 using sodium hydroxide. Finally, it is heat-treated at 130°C for 0.4 seconds and then flash-cooled. The suspension is then atomized on a NIRO MSD multi-effect atomizer with an inlet temperature of 180°C and an outlet temperature of 80°C. The mass of the powder obtained is 93.2% relative to the total weight of the dry matter, of which 80.7% is protein. This powder is called "base 2 of the protein composition according to the present invention"

[0119] This powder was then milled twice using a Netzsch CGS10 opposed air jet mill, yielding a first powder with a D90 particle size of 16.9 μm and a second powder with a D90 particle size of 7.9 μm. The resulting powdered protein compositions were designated "Micronized Protein Composition 2 According to the Invention" and "Micronized Protein Composition 3 According to the Invention," respectively.

[0120] To compare protein composition, the aforementioned experiments A and B were used, as well as dry matter and protein abundance.

[0121] [Table 2]

[0122]

[0123] Table 2 above further demonstrates that it is possible to maximize the gelling power. The gelling power of the micronized protein composition according to the present invention is more than doubled. In addition, protein solubility can be maintained.

Claims

1. A bean protein composition, wherein the bean is pea, characterized in that: The protein composition according to Test A has a gel strength greater than 200 Pa, and the soy protein composition has a D90 particle size less than 20 μm, wherein the gel strength according to Test A is achieved by: 1) solubilizing the test protein composition in water containing 15% + / - 2% dry matter at a pH of 7 at 60°C + / - 2°C; 2) Oscillate at 60°C + / - 2°C for 5 minutes; 3) Cool to 20°C + / - 2°C and stir at 350 rpm for 24 hours; 4) preparing the suspension in an applied stress rheometer equipped with concentric columns; 5) Measure the elastic modulus G' by applying the following temperature profile: a. After stabilization at 20°C + / - 2°C, heat from 20°C + / - 2°C to 80°C + / - 2°C within 10 minutes and measure parameter G'1; b. Stabilize at 80°C + / - 2°C for 110 minutes; c. Cool from 80°C + / - 2°C to 20°C + / - 2°C within 30 minutes, and measure G'2 after stabilization at 20°C + / - 2°C; 6) Calculate the gel strength equal to G'2-G'1; The bean protein composition is obtained by a production method comprising the following steps: 1) Processing legume seeds, wherein the legume seeds are peas; 2) Grinding the seeds to make a water suspension; 3) Separate the water-insoluble fraction using centrifugal force; 4) heating at a temperature between 55°C + / - 2°C and 65°C + / - 2°C at the isoelectric pH to coagulate the protein for a time between 3.5 minutes and 4.5 minutes; 5) recovering the coagulated protein flocs by centrifugation; 6) Adjust the pH to between 6+ / -0.5 and 9+ / -0.5; 7) As an option, heat treatment can be performed; 8) drying the coagulated protein flocs; 9) Grinding the coagulated protein flocs with an air jet grinder and drying to obtain particles with a D90 particle size of less than 20 microns.

2. The soy protein composition of claim 1, wherein the soy protein composition is a soy protein isolate.

3. The bean protein composition according to claim 1 or 2, characterized in that The protein abundance of the legume protein composition relative to the total weight of dry matter is greater than 80%.

4. The bean protein composition according to claim 1 or 2, characterized in that The soy protein composition has a D90 particle size of less than 15 microns.

5. The bean protein composition according to claim 1 or 2, characterized in that The soy protein composition has a solubility of 30% to 65% according to Test B, which is defined as follows: Add 150g of distilled water at 20℃+ / -2℃ into a 400mL beaker, stir with a magnetic bar, and accurately add 5g of the soy protein sample to be tested; Adjust the pH to 7 with 0.1N NaOH or 0.1N HCl; Add water to 200g; Mix at 1000 rpm for 30 min and then centrifuge at 3000 g for 15 min; Collect 25 g of the supernatant and place it in a pre-dried and tared crystallizing dish; Place the crystallization dish in a thermostat at 103°C + / - 2°C for 1 hour, then cool it to room temperature in a desiccator and weigh it; Solubility corresponds to the content of soluble dry matter, expressed as a percentage of its weight to the weight of the sample. The solubility is calculated as follows: Where: P is the sample weight, unit: g, m1 is the weight of the crystallization dish after drying, unit: g, m2 is the weight of the empty crystallization dish, unit: g, P1 is the collected sample weight, unit: g.

6. The method for producing a bean protein composition according to any one of claims 1 to 5, characterized in that: The production method comprises the following steps: 1) Processing legume seeds, wherein the legume seeds are peas; 2) Grinding the seeds to make a water suspension; 3) Separate the water-insoluble fraction using centrifugal force; 4) heating at a temperature between 55°C + / - 2°C and 65°C + / - 2°C at the isoelectric pH to coagulate the protein for a time between 3.5 minutes and 4.5 minutes; 5) recovering the coagulated protein flocs by centrifugation; 6) Adjust the pH to between 6+ / -0.5 and 9+ / -0.5; 7) As an option, heat treatment can be performed; 8) drying the coagulated protein flocs; 9) Grinding the coagulated protein flocs with an air jet grinder and drying to obtain particles with a D90 particle size of less than 20 microns.

7. The method according to claim 6, characterized in that The heat treatment in step 7 includes heating in the range of 100° C.+ / −2° C. to 160° C.+ / −2° C. for 0.01 seconds to 3 seconds, followed by immediate cooling.

8. The method according to claim 6 or 7, characterized in that The drying in step 8 is accomplished by atomization.

9. The method according to claim 6 or 7, characterized in that The grinding in step 9 is accomplished with the aid of an opposed air jet grinder.

10. The method according to claim 6 or 7, characterized in that The gel strength of the protein composition according to Test A is at least 150% of the gel strength of the dried protein flocculent in step 8.

11. Use of the composition according to any one of claims 1 to 5 in food or medicine.

12. The use according to claim 11, wherein the pH of the food or drug is between 4 and 9.

13. Use according to claim 11 or 12, wherein the food product is a meat or fish substitute.

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