Method for extracting protein from peas
Patent Information
- Authority / Receiving Office
- ES · ES
- Patent Type
- Patents
- Current Assignee / Owner
- COSUCRA GRP WARCOING
- Filing Date
- 2014-11-18
- Publication Date
- 2026-07-13
AI Technical Summary
Existing methods for extracting pea proteins face challenges in achieving high-quality protein isolates with specific desired properties, as they are often cumbersome and costly, affecting protein composition, purity, and functional properties such as solubility, viscosity, and flavor.
A method involving the extraction of pea proteins through an aqueous composition with pH adjustment to 4.0 to 5.8, followed by heat treatment at varying temperatures and times, including isoelectric precipitation and heat treatment, to obtain pea protein compositions with low ash content, high density, and improved flowability and wettability.
The method results in pea protein compositions with lower solubility, viscosity, and gel strength, making them suitable for use in food and feed products, particularly in bakery and confectionery, and effective in clarifying beverages like wine and fruit juices.
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Abstract
Description
Method for extracting protein from peas Field of invention The present invention relates to methods for extracting and purifying proteins. In particular, the present invention relates to the extraction of pea protein. The invention further relates to pea proteins obtainable by the above methods, as well as to foods or food products containing such pea proteins. The invention also relates to the use of such pea proteins in the food or feed industry. Background of the invention Plant-based protein isolates represent a valuable alternative or supplement to animal proteins in food and feed. For example, in food, in addition to plant proteins, they can effectively replace animal proteins, often at a lower cost. Furthermore, many products that traditionally contain animal proteins, particularly dairy products, can be a significant cause of food allergies. Legumes are remarkable because most of them have symbiotic nitrogen-fixing bacteria in structures called root nodules. This arrangement means that the root nodules are sources of nitrogen for legumes, making them relatively rich in plant protein. All proteins contain nitrogenous amino acids. Therefore, nitrogen is a necessary ingredient in protein production. Thus, legumes are among the best sources of plant protein. Because legumes, such as peas (Pisum sativum), are not only high in protein but also readily available and have a particularly well-balanced amino acid profile, they represent a valuable alternative to animal protein. The main challenges in providing plant-based proteins revolve around protein composition and purity, and include aspects related to extraction, fractionation, and pre- and post-isolation treatments. By the time plant protein is isolated and available in a more or less pure form, all the prior manipulations have a significant impact on the quality of the isolated protein. For example, the type and quantity of impurities in protein isolates or extracts determine their final value. Such impurities include, for example, carbohydrates. While carbohydrates are generally undesirable impurities in the final protein isolate, some other impurities, such as vitamins or minerals, may, by definition, not be undesirable, or may even be beneficial to the nutritional and / or physicochemical aspects of the protein isolate.In addition to affecting the final composition of protein isolates or extracts, the extraction and / or purification process can drastically affect the physicochemical or functional properties of the protein isolate. In particular, protein solubility, viscosity, emulsifying capacity, color, taste, and aroma are strongly influenced by the techniques used. As can be seen from the above, obtaining a high-quality protein isolate with specific desired properties can be cumbersome and often involves multiple costly and / or time-consuming manipulations. In light of this, there is still a need to improve protein isolation from plants, particularly legumes such as peas. Document FR2889416A1 refers to pea protein compositions characterized by a particular molecular weight distribution profile and water solubility, as well as methods for obtaining them. Document FR2889417A1 relates to a granulated pea protein composition characterized by an average particle diameter and compressibility value, as well as methods for producing them. Document WO 2010 / 022702 refers to a process for obtaining fat-containing legume protein. Document US 2013 / 0017310 refers to a process for manufacturing soluble and functional vegetable proteins. Khattab RY et al (Nutritional quality of legume seed as affected by some physical treatments, Part 1: Protein quality evaluation; Food Science and Technology, vol. 42, No. 6, 2009, p1107-1112;) describes the effects of different processing methods on the nutritional quality of cowpea, pea and bean seeds, such as the content of antinutritional factors, including tannins, phytic acid, trypsin inhibitors and oligosaccharides. Camacho L et al (Nutritional improvement of commonly consumed legumes fermented by lactobacillus grain cultures; Foods, vol 16, 1991, p5-11) describes the effects of lactic acid fermentation on the oligosaccharide and phytate content in lentil, chickpea and pea flour. Deshpande SS (chapter 4: Fermentation of grain legumes, seeds and nuts in Latin America and the Caribbean, Fermented grain legumes, seeds and nuts: A global perspective (book series: FAO agricultural services bulletin), Food and Agriculture organization of the United Nations, vol. 142, 2000, p99-105, 107) describes fermented foods derived from cereal grains and tubers. Schindler Sabrina et al (Improvement of the Aroma of Pea (Pisum sativum) Protein Extracts by Lactic Acid Fermentation; Food Biotechnology, vol. 26, 2012, No. 1) describes the formation of an unpleasant green or toasted flavor during the storage of legume protein extracts, which limits their application in food. Pea protein extracts were subjected to lactic acid fermentation to improve the flavor by reducing the formation of off-flavors or masking undesirable green notes. Therefore, one of the objects of the present invention is to overcome or improve at least one of the disadvantages of the prior art, or to provide a useful alternative. Summary of the invention According to a first aspect of the present invention, a method for extracting pea protein is provided. The method for extracting pea protein comprises the steps of: (a) provide an aqueous composition comprising pea proteins; (b) isolating said pea proteins from said aqueous composition comprising pea proteins; (c) obtaining said isolated pea proteins as an aqueous suspension having a pH in the range of 4.0 to 5.8; (d) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature in the range of 75 °C to 210 °C, wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5; wherein step (d) comprises subjecting said precipitated pea proteins to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s ± 1 s. According to one embodiment of this method, pea protein extraction involves providing pea proteins that are subjected to isoelectric precipitation followed by heat treatment of the protein precipitate. According to a second aspect of the present invention, pea protein extracts are provided that can be obtained or are obtained by the method according to the first aspect of the invention. According to a third aspect of the present invention, a pea protein composition is provided, comprising at least 60% by weight of protein based on the total dry matter of the composition, wherein said pea protein composition has a nitrogen solubility index at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition. It is also described in this document that an edible composition, preferably a food or feed product, is provided comprising pea proteins according to the second aspect of the invention, or the pea protein composition according to the third aspect of the invention, or pea proteins obtained by the method according to the first aspect of the invention. In a fourth aspect, the present invention provides for the use of pea protein extracts according to the second aspect of the invention, or pea protein composition according to the third aspect of the invention, or pea protein extracts obtained by the method according to the first aspect of the invention in food or feed products, preferably in bakery and confectionery food products. In a fifth aspect, the present invention provides for the use of pea proteins according to the second aspect of the invention, or pea protein composition according to the third aspect of the invention, or pea proteins obtained by the method according to the first aspect of the invention for clarifying brews or drinks, preferably wine or fruit juices. The present inventors have surprisingly discovered that pea proteins have particular functional, physicochemical, and organoleptic characteristics when an aqueous composition comprising pea proteins is subjected to isolation steps such as protein precipitation, after which the isolated proteins are subjected to heat treatment. In particular, it has been unexpectedly discovered that the methods according to the invention as described herein make it possible to obtain pea protein compositions, or pea protein extracts or concentrates that have, among other things, a lower ash content, higher density (both apparent and after settling), better flowability, better wettability, low solubility, lower viscosity, and lower gel strength, compared to pea protein extracts not obtained according to the methods of the invention as described herein. The pea protein compositions of the invention have low affinity for water, which is interesting in applications with low water availability. The specific characteristics of pea protein extracts and pea protein compositions according to the invention as described herein in particular make such pea protein extracts and pea protein compositions particularly suitable for use in the food or feed industry, in particular in bakery or confectionery food products such as biscuits, breads, waffles, cakes, fudge, extruded cereals and bars, etc.Surprisingly, it has been discovered that pea protein extracts and pea protein compositions according to the invention as described herein can be used in the aforementioned bakery and confectionery products, allowing less water to be added during their preparation while maintaining or even improving their quality (such as texture or flavor) or shelf life, and without compromising the workability of, for example, the dough used to prepare the bakery products. Another advantage of using less water in the preparation of bakery products, in particular, is that it facilitates water evaporation during baking, which is not only more cost-effective but also has a beneficial effect on the overall quality of the baked goods.The shelf life of food products containing pea protein extracts and pea protein compositions according to the invention described herein can also be extended. Pea protein extracts and pea protein compositions as described herein are also particularly suitable for replacing, for example, animal proteins such as milk proteins in food products, as well as other vegetable proteins, particularly allergenic vegetable proteins such as wheat protein, in food products.For example, pea protein extracts and pea protein compositions according to the invention as described herein can be used to partially or completely replace milk proteins in confectionery products, such as dulce de leche, or in dulce de leche bars, for which it has been surprisingly observed that a smoother texture can be obtained with the proteins according to the invention. Furthermore, it has been unexpectedly discovered that pea protein extracts and pea protein compositions according to the invention as described herein are particularly suitable for use in rinsing or clarifying liquids, for example, beverages such as wine, beer, or fruit juices. Without wishing to be bound by any theory, it is hypothesized that the particularly low solubility of pea protein extracts and pea protein compositions according to the invention as described herein may be responsible for the rinsing or clarifying ability of the proteins, particularly in relation to reducing the turbidity of the liquids. The independent and dependent claims set forth particular and preferred features of the invention. The features of the dependent claims may be combined with the features of the independent or other dependent claims as appropriate. Appended claims are also explicitly included by reference in the description. Brief description of the figures Figure 1 schematically represents an extraction process according to an embodiment of the invention. Figure 2 represents a graph that represents the gel strength at pH 6 of each extract (A) to (D). Figure 3 represents a graph that shows the nitrogen solubility index profile as a function of pH for each extract (A) to (D). Figure 4 represents a graph that shows the viscosity profile expressed as a function of pH for each extract (A) to (D). Figure 5 represents a graph that shows the nitrogen solubility index profile expressed as a function of pH for each extract E to G. Figure 6 represents a graph depicting the turbidity of different solutions comprising tannins after incubation for 96 h at 4 °C. Figure 7 represents a graph that shows the turbidity of different solutions comprising tannins as a function of incubation time at 4 °C. Figure 8 represents a graph depicting the turbidity of different solutions comprising SiO2 after incubation for 96 h at 4 °C. Figure 9 represents a graph that shows the turbidity of different solutions comprising SiO2 as a function of incubation time at 4 °C. Figure 10 represents a graph showing the turbidity of different solutions after incubation for 96 h at 4 °C. Figure 11 represents a graph depicting the turbidity of different pea protein solutions after incubation for 96 h at 4 °C. Figure 12 represents a graph that shows the fermentation index of different doughs prepared with pea protein extracts. Figure 13 represents a graph that represents the volume of bread prepared in example 5. Figure 14 represents a graph that represents the crumb hardness of the bread prepared in example 5. Figure 15 represents a graph that represents the hardness of the bars as a function of the shelf life of the bars prepared in example 5. Figure 16 represents a graph that shows the nitrogen solubility index profile as a function of pH for each extract H and I. Figure 17 represents a graph representing the sugar / dry matter concentration in % as a function of fermentation time of peas fermented with Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus Crispatus LMG 12005 or Lactobacillus Acidophilus LMG 8151. La Figura 18 representa un gráfico que representa el pH de los guisantes desvainados (7A) fermentados con Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus Crispatus LMG 12005 o Lactobacillus Acidophilus LMG 8151 y el pH de la solución acuosa (zumo) (7B) en función del tiempo de fermentación. La Figura 19 representa un gráfico que representa la acidez de los guisantes desvainados (8A) fermentados con Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus Crispatus LMG 12005 o Lactobacillus Acidophilus LMG 8151 y la acidez de la solución acuosa (zumo) (8B) en función del tiempo de fermentación. Figure 20 represents a graph depicting lactic acid bacteria (Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus Crispatus LMG 12005 or Lactobacillus Acidophilus LMG 8151) concentration of the aqueous solution (juice) as a function of fermentation time. Detailed description of the invention Before describing the present method of the invention, it should be understood that the present invention is not limited to the particular methods, components, products, or combinations described, as such methods, components, products, and combinations may, of course, vary. It should also be understood that the terminology used herein is not intended to be limiting, as the scope of the present invention is limited only by the appended claims. As used herein, the singular forms "a / an", "an" and "the" include singular and plural references unless the context clearly indicates otherwise. The terms "comprising," "comprises," and "made up of" as used herein are synonymous with "including," "containing," or "containing," and are inclusive or open-ended and do not exclude additional, unmentioned members, elements, or steps of the method. It will be appreciated that the terms "comprising," "comprises," and "comprised of" as used herein encompass the terms "consisting of," "consisting of," and "consisting of," as well as the terms "essentially consisting of," "essentially consisting of," and "essentially consisting of." The enumeration of numerical intervals by extreme values includes all numbers and fractions encompassed within the respective intervals, as well as the enumerated extreme values. The term "about" or "approximately," as used herein, refers to a measurable value such as a parameter, quantity, duration, and the like, encompassing variations of + / - 20% or less, preferably + / - 10% or less, more preferably + / - 5% or less, and even more preferably + / - 1% or less from and away from the specified value, to the extent that such variations are appropriate for carrying out the disclosed invention. It is understood that the value to which the modifier "about" or "approximately" refers is also specifically and preferably disclosed. While the terms "one or more" or "at least one", such as one or more or at least one or more members of a group of members, are clear per se, by means of further examples, the term encompasses, among other things, a reference to any one of said members, or to two or more of said members, such as, for example, any of >3, >4, >5, >6 or >7 etc. of said members, and up to all of said members. Unless otherwise defined, all terms used to disclose the invention, including technical and scientific terms, have the meaning commonly understood by a person skilled in the art to which the present invention pertains. Definitions of terms are included in a separate guide to further understand the teaching of the present invention. In the following passages, different aspects of the invention are defined in more detail. Each aspect thus defined may be combined with any other aspect or aspects unless clearly stated otherwise. In particular, any feature stated as preferred or advantageous may be combined with any other feature or features stated as preferred or advantageous. References throughout this specification to "an embodiment" or "embodiment" mean that a particular feature, structure, or characteristic described in conjunction with the embodiment is included in at least one embodiment of the present invention. Therefore, occurrences of the phrases "in an embodiment" or "in the embodiment" in various places throughout this specification do not all necessarily refer to the same embodiment, but may. Furthermore, the particular features, structures, or characteristics may be combined in any suitable manner, as would be apparent to a person skilled in the art from this disclosure, in one or more embodiments.Furthermore, while some embodiments described herein include some but not others features included in other embodiments, combinations of features from different embodiments are intended to be within the scope of the invention and constitute distinct embodiments, as will be understood by those skilled in the art. For example, in the appended claims, any of the claimed embodiments may be used in any combination. In the following detailed description of the invention, reference is made to the accompanying drawings, which form part of it and which illustrate, by way of example only, specific embodiments in which the invention can be implemented. The scope of the present invention is defined by the appended claims. Statements numbered 1 through 68 are also described in this document. 1. A method for extracting protein from peas, comprising the steps of: (a) provide an aqueous composition comprising pea proteins; (b) isolating said pea proteins from said aqueous composition comprising pea proteins, preferably using precipitation, flocculation, filtration and / or chromatography; (c) obtaining said isolated pea proteins as an aqueous suspension having a pH in the range of 4.0 to 5.8; (d) subject said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C. Preferably, the aqueous suspension comprising pea proteins in step (c) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment the dry matter content can be adjusted to this extent by dilution with water. 2. The method according to statement 1, wherein step (d) comprises subjecting said aqueous suspension to heat treatment at a temperature in the range of 75 °C to 210 °C, preferably in the range of 85 °C to 160 °C, for example, from 90 °C to 150 °C. 3. The method according to statement 1 or 2, wherein step (d) comprises subjecting said aqueous suspension to a heat treatment for at least 0.01 seconds, preferably for a time in the range of 0.01 seconds to 20 minutes, preferably in the range of 10 seconds to 10 minutes. 4. The method according to any of claims 1 to 3, wherein step (d) comprises subjecting said aqueous suspension to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s 1 s. 5. The method according to any of statements 1 to 4, wherein the time of subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C in step (d) decreases when the temperature increases. 6. The method in accordance with any of statements 1 to 5, wherein said step (b) comprises concentrating said pea proteins. 7. The method in accordance with any of statements 1 to 6, wherein said step (b) comprises at least one step of precipitation, flocculation, filtration and / or chromatography. 8. The method in accordance with any of statements 1 to 7, wherein step (b) comprises isoelectric precipitation. 9. The method according to any of statements 1 to 8, wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5. 10. The method in accordance with any of statements 1 to 9, wherein step (c) comprises adjusting or maintaining the pH of the aqueous suspension to vary from 4.0 to 5.8. 11. The method according to any of statements 1 to 10, wherein said aqueous composition comprising pea proteins in step (a) has a pH of at least 6.0, preferably in the range of 6.0 to 9.0, preferably in the range of 6.5 to 8.5. 12. The method according to any of statements 1 to 11, wherein the pH of said aqueous composition comprising pea proteins in step (a) is adjusted to at least 6.0, preferably in the range of 6.0 to 9.0, preferably in the range of 6.5 to 8.5. 13. The method according to any of statements 1 to 12, wherein prior to step (a) an aqueous composition comprising peas, preferably shelled peas, is subjected to fermentation, preferably in the presence of lactic acid bacteria. 14. The method in accordance with statement 13, wherein said fermentation is carried out in the presence of one or more Lactobacillus sp. 15. The method according to any of statements 1 to 14, wherein before or during step (b) said aqueous composition comprising pea proteins, or said pea proteins are subjected to heat treatment, preferably to a temperature of at least 30 °C, for example at least 40 °C, for example at most 80 °C, for example at least 50 °C and at most 80 °C, for example at least 53 °C and at most 78 °C, for example at least 54 °C and at most 75 °C. 16. The method according to any of statements 1 to 15, wherein before or during step (b) said aqueous composition comprising pea proteins, or said pea proteins are subjected to pasteurization. 17. The method according to any of claims 1 to 16, further comprising the step of drying said aqueous suspension after step (d), preferably by spray drying, preferably obtaining a pea protein composition having a pH in the range of 4.0 to 5.8, as measured at room temperature on 10 g of pea protein composition suspended in 90 g of water 18. Pea proteins that can be obtained by the method in accordance with any of statements 1 to 17. 19. Pea protein composition comprising at least 60% by weight of protein based on the total dry matter of the composition, wherein said pea protein composition has a nitrogen solubility index (NSI) at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition, and preferably an NSI of at most 11%, preferably at most 10%, preferably at most 9%, preferably at most 8%. Preferably, the pea protein composition has a dry matter content of at least 90% based on the total weight of the composition. The nitrogen content (atomic weight percent) of selected samples was determined using a LECO analyzer. The technique used was the classic Dumas method, which employs thermal conductivity detection (DCT): Weighed samples are burned in oxygen at 1200 °C. The combustion products (including N₂ and NOx) are swept with a helium carrier gas through combustion catalysts, scrubbers, and through a reduced copper-filled tube. The copper removes excess oxygen and reduces the NOx to N₂. The N₂ is then measured using DCT. 20. Pea protein composition according to statement 19, wherein said composition has a pH in the range of 4.0 to 5.8, as measured at room temperature in 10 g of pea protein composition suspended in 90 g of water. 21. An edible composition, preferably a food product or feed, comprising pea proteins according to claim 18, or pea protein compositions according to any one of claims 19 or 20. 22. Use of pea proteins in accordance with claim 18, or pea protein compositions in accordance with any one of claims 19 or 20, in food products or feed, preferably in bakery food products and confectionery food products such as biscuits, breads, waffles, cakes, fudge, extruded cereals and bars, etc. 23. Use of pea proteins in accordance with claim 18, or pea protein compositions in accordance with any one of claims 19 or 20, to clarify beverages and / or concoctions, preferably wine, fruit juice, beer. 24. The method according to statement 13 or 14, where after said fermentation, the peas are ground. 25. The method in accordance with any of statements 1 to 17 and 24, wherein prior to step (a) said method comprises the steps of: - provide peas, preferably shelled peas, - optionally grind said peas; and - hydrate said peas, or optionally ground said peas; 26. The method in accordance with any of statements 1 to 17, 24 and 25, wherein prior to step (a) said method comprises the steps of: (a1) subjecting an aqueous composition comprising peas to fermentation, preferably in the presence of one or more lactic acid bacteria; (b1) grinding said peas; thus obtaining ground peas; (c1) fractionating said ground peas to obtain at least one fraction comprising proteins, also called aqueous composition comprising pea proteins. 27. The method according to any of claims 13, 14, 24 or 26, wherein said peas in step (a1) are fermented until the pH in said peas is at most 5.5, preferably at most 5.0, more preferably in the range of pH 3.5 to pH 5.0, as measured at room temperature on 1 g of said peas that have been ground and then suspended in 9 g of water. 28. The method according to any of claims 13, 14, 24 or 26 and 27, wherein said peas in step (a1) are subjected to fermentation until the pH in said peas is reduced by at least 1 pH unit, preferably by at least 1.5 pH units, as measured at room temperature in 1 g of said peas that have been ground and then suspended in 9 g of water. 29. The method according to any one of statements 13, 14, 24 or 26 to 28, wherein step (a1) comprises adding dried peas and / or shelled peas to an aqueous solution, preferably adding dried peas having a dry matter content in the range of 80% to 95% based on the total weight of the dried peas. 30. The method in accordance with any one of statements 13, 14, 24 or 26 to 29, wherein said peas after step (a1) and before step (b1) have a dry matter content in the range of 35% to 60% based on the total weight of the peas. 31. The method according to any one of statements 13, 14, 24 or 26 to 30, wherein step (a1) comprises fermenting said peas until they have a dry matter content in the range of 35% to 60% based on the total weight of the peas. 32. The method according to any one of statements 13, 14, 24 or 26 to 31, wherein said peas in step (a1) are subjected to fermentation for at least 3 h, preferably for at least 3 h and at most 24 h. 33. The method according to any one of statements 13, 14, 24 or 26 to 32, wherein said peas in step (a1) are subjected to fermentation at a temperature in the range of 30 °C to 50 °C, preferably in the range of 35 °C to 45 °C. 34. The method according to any one of statements 13, 14, 24 or 26 to 33, wherein step (a1) comprises fermenting said peas in the presence of lactic acid bacteria, preferably in the presence of one or more Lactobacillus sp. 35. The method according to any one of claims 13, 14, 24 or 26 to 34, wherein said peas in step (a1) are subjected to fermentation in the presence of at least 102 CFU to at most 1010 CFU of lactic acid bacteria per ml of said aqueous composition comprising peas. 36. The method according to any one of statements 13, 14, 24 or 26 to 35, wherein fractionating said ground peas in step (c1) comprises separating at least part of the proteins contained in the peas from the remainder of the pea, preferably into a fraction comprising at least 50% by weight of protein based on the total dry matter of said fraction. 37. The method according to any of claims 26 to 36, wherein fractionating said ground peas in step (c1) comprises adjusting the pH of the ground peas to a pH of at least 6, preferably at least 7, more preferably a pH of at least 8 and at most 9. This pH adjustment can be carried out using any suitable base, such as sodium hydroxide, potassium hydroxide, or calcium hydroxide. Preferably, this pH adjustment is carried out in an aqueous composition comprising ground peas having a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, or preferably at most 25%. In one embodiment, the dry matter content of the ground peas is adjusted to the aforementioned dry matter content by adding water accordingly. 38. The method according to any of statements 26 to 37, wherein fractionating said ground peas in step (c1) comprises subjecting said ground peas to one or more separation steps, preferably one or more decantation steps, preferably one or more centrifugal decantation steps. 39. The method according to any one of statements 13, 14, 24 or 26 to 38, wherein step (a1) comprises contacting shelled peas with an aqueous solution. 40. The method according to any one of statements 13, 14, 24 or 26 to 39, wherein step (a1) comprises contacting dried shelled peas with an aqueous solution, preferably dried shelled peas having a dry matter content in the range of 80% to 95% based on the total weight of the dried shelled pea. 41. The method according to any one of statements 13, 14, 24 or 26 to 40, wherein step (a1) comprises fermenting said peas until they have a dry matter content in the range of 40% to 60% based on the total weight of the peas. 42. The method according to any one of statements 13, 14, 24 or 26 to 41, wherein said peas after step (a1) and before step (b1) have a dry matter content in the range of 40% to 50% based on the total weight of the peas. 43. The method according to any one of claims 13, 14, 24 or 26 to 42, wherein before, during and / or after the milling stage (b1) an aqueous solution, preferably water, is added, preferably such as to obtain an aqueous composition comprising the ground peas, said composition comprising 15% to 35% dry matter based on the total weight of the composition, preferably comprising 15% to 35%, preferably 18% to 33%, for example 20% to 30%, such as at least 20%, for example at least 21%, for example at least 22%, for example at least 23%, for example at least 24%, for example at least 25%, 26%, 27%, 28%, 29%, for example, at most 30%, for example, at most 35%. 44. The method according to any one of statements 13, 14, 24 or 26 to 43, wherein said peas in step (a1) are subjected to fermentation for a maximum of 24 h, for example, for a maximum of 20 h, for example, for a maximum of 18 h, for example, for a maximum of 12 h, for example, for a maximum of 10 h. 45. The method in accordance with any one of statements 13, 14, 24 or 26 to 44, wherein at the end of step (a1) said peas have an acidity in the range of 25 to 250 mEq OH- per g of peas. 46. The method according to any one of statements 13, 14, 24, or 26 to 45, wherein fractionating said ground peas in step (c1) comprises adjusting the pH of the aqueous composition comprising the ground peas to a pH of at least 6, preferably at least 7, preferably at least 8, more preferably a pH of at least 7.5 and at most 9, preferably a pH of at least 7.5 and at most 8.5, and separating a protein comprising a fraction of said ground peas. Preferably, this pH adjustment is carried out on the aqueous composition comprising ground peas having a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%.In one embodiment, the dry matter content of the ground peas is adjusted to the dry matter content quoted above by adding water accordingly. 47. The method according to statement 46, wherein said at least one fraction comprising protein is subjected to a temperature of at least 30 °C, for example at least 40 °C, for example at least 50 °C, for example at least 55 °C, for example at most 80 °C, for example at least 50 °C and at most 80 °C, for example at least 53 °C and at most 78 °C, for example at least 54 °C and at most 75 °C. 48. The method according to any one of statements 13, 14, 24 or 26 to 47, wherein said aqueous composition comprising peas in step (a1), comprises an aqueous solution, preferably water. 49. The method according to any one of statements 13, 14, 24 or 26 to 48, wherein the amount of peas in said aqueous composition comprising peas in step (a) preferably ranges from 150 to 500 kg of peas per m3 of aqueous composition comprising the peas. 50. The method according to any one of claims 13, 14, 24 or 26 to 49, wherein said aqueous composition comprising peas before or at the beginning of fermentation of step (a1) has a pH of at least 6, for example, at least 6.2, for example, at least 6.4, as measured in the aqueous composition comprising the peas, after said composition has been ground. 51. The method according to any of claims 1 to 17, or 24 to 50, wherein prior to step (b) said aqueous composition comprising pea protein is subjected to a temperature of at least 30 °C, for example at least 55 °C, for example at most 80 °C, for example at least 50 °C and at most 80 °C, for example at least 55 °C and at most 78 °C. 52. The method according to any one of statements 13, 14, 24 or 26 to 51, wherein said lactic acid bacteria are selected from the group comprising Lactobacillus, Leuconostoc, Pediococcus, Streptococcus, Aerococcus, Carnobacterium, Enterococcus, Oenococcus, Sporolactobacillus, Tetragenococcus, Vagococcus and Weisella and combinations thereof. 53. The method according to any one of claims 13, 14, 24 or 26 to 52, wherein the lactic acid bacteria are Lactobacillus sp, more preferably selected from the group comprising Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosae, Lactobacillus pontis, Lactobacillus acidophilus, Lactobacillus plantarum, Lactobacillus helveticus, Lactobacillus buchneri, Lactobacillus delbrueckii and Lactobacillus casei and mixtures thereof. 54. The method according to any one of statements 13, 14, 24 or 26 to 53, wherein the lactic acid bacteria are selected from the group comprising Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosae, Lactobacillus pontis and mixtures thereof. 55. The method according to any one of statements 13, 14, 24 or 26 to 54, wherein the lactic acid bacteria are selected from the group comprising Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosae, Lactobacillus pontis and mixtures thereof. 56. The method in accordance with any one of statements 13, 14, 24 or 26 to 55, wherein said lactic acid bacteria is Lactobacillus fermentum, or Lactobacillus crispatus. 57. The method in accordance with any one of statements 13, 14, 24 or 26 to 53, wherein said lactic acid bacteria is Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus acidophilus, or Lactobacillus plantarum. 58. The method in accordance with any one of statements 13, 14, 24 or 26 to 53, wherein said lactic acid bacteria is Lactobacillus fermentum, Lactobacillus crispatus, or Lactobacillus acidophilus. 59. The method according to any one of claims 13, 14, 24 or 26 to 58, wherein the dried peas before the start of step (a1) have a pH of at least 6.0, preferably a pH in the range of 6.0 to 7.0 (i.e., before fermentation), such as, for example, at least 6.0, for example, at least 6.1, for example, at least 6.2, for example, at least 6.3, for example, at most 6.9, for example, at most 7.0, preferably in the range of 6.25 to 6.75, as measured at room temperature on 5 g of dried peas that have been ground with 95 g of water. 60. The method in accordance with any one of statements 13, 14, 24 or 26 to 59, wherein said fermentation is anaerobic fermentation. 61. The method according to any of statements 1 to 17, or 24 to 60, comprising the steps of: (i1) subjecting an aqueous composition comprising peas to fermentation, preferably in the presence of one or more lactic acid bacteria; (ii1) grinding said peas in the presence of water; thereby obtaining an aqueous composition comprising ground peas; (iii1) fractionating said aqueous composition comprising ground peas to obtain at least one aqueous composition comprising pea proteins, preferably adjusting the pH of said aqueous composition to a pH of at least 6. This pH adjustment can be made using any suitable base, such as sodium hydroxide, potassium hydroxide, or calcium hydroxide. Preferably, this pH adjustment is made in an aqueous composition comprising ground peas having a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, or preferably at most 25%. In one embodiment, the dry matter content of the ground peas is adjusted to the aforementioned dry matter content by adding water accordingly. 62. The method according to any of statements 1 to 17, or 24 to 61, comprising the steps of: (i) grinding said peas; preferably dried peas; (ii) fractionating said ground peas in the presence of an aqueous solution to obtain at least one aqueous composition comprising pea proteins; (iii) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins; (iv) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; and (v) subject said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C. Preferably, the aqueous suspension comprising pea proteins in step (iv) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment the dry matter content can be adjusted to this extent by dilution with water. 63. The method according to any of statements 1 to 17, or 24 to 62, comprising the steps of: (i) subjecting an aqueous composition comprising peas to fermentation, preferably in the presence of one or more lactic acid bacteria; (ii) grind said peas; (iii) fractionating said ground peas in the presence of an aqueous solution to obtain at least one aqueous composition comprising pea proteins; (iv) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins; (v) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; and (vi) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C. Preferably, the aqueous suspension comprising pea proteins in step (v) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment the dry matter content can be adjusted to this extent by dilution with water. 64. The method in accordance with any of statements 26 to 63, wherein said fractionation step comprises fractionating said ground peas into a fraction comprising at least 50% by weight of protein based on the total dry matter of said fraction. 65. The method according to any of statements 26 to 64, wherein said fractionation step comprises separating at least part of the proteins contained in the peas from the remainder of the pea, preferably into a fraction comprising at least 50% by weight of protein based on the total dry matter of said fraction. 66. The method according to any one of claims 61 to 65, wherein obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8 comprises adjusting or maintaining the pH of the aqueous suspension to vary from 4.0 to 5.8. 67. Pea protein composition obtainable by the method according to any of claims 1 to 17, or 24 to 66, comprising at least 60% by weight of protein based on the total dry matter of the composition, wherein said pea protein composition has a nitrogen solubility index at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition, and preferably said pea protein composition has an NSI of at most 11%, preferably at most 10%, preferably at most 9%, preferably at most 8%. 68. Pea protein composition according to any one of claims 19, 20 and 67, wherein said composition has a pH in the range of 4.0 to 5.8, as measured at room temperature in 10 g of pea protein composition suspended in 90 g of water. In one aspect, the invention relates to a method for extracting pea protein, comprising the steps of: (a) provide an aqueous composition comprising pea proteins; (b) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins preferably using precipitation, flocculation, filtration and / or chromatography; (c) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; (d) subject said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C. Preferably, the aqueous suspension comprising pea proteins in step (c) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment can be adjusted to this extent by dilution with water. According to the invention, steps (a) to (d) of the method according to the invention or as specified above may be carried out, and preferably are carried out, in the following order, i.e., step (a) precedes step (b), which in turn precedes step (c), which in turn precedes step (d). However, it should be understood that the heat treatment in step (d) is in any case carried out after the isolation of the precipitated proteins in step (c). As used herein, the term "pea" refers to the round seeds contained in the pod of Pisum sativum and its subspecies, varieties, or cultivars. Preferably, the peas are yellow peas, preferably dried yellow peas, i.e., yellow peas that have been harvested in a dry state. Therefore, "pea protein" as used herein refers to the proteins contained in pea seeds. As used herein, "pea protein extraction" refers to the release and separation of pea proteins from other pea constituents. Pea protein extraction according to certain embodiments of the invention may encompass the isolation or purification of pea proteins. Those skilled in the art will understand that pea protein extracts do not consist entirely of protein, and that a certain amount of additional components (impurities) may be present in pea protein extracts, such as lipids, carbohydrates, minerals, etc. In some embodiments of the invention, pea proteins, pea protein compositions, and pea protein extracts comprise, on a dry matter basis, at least 50% by weight of protein (i.e., 50 g of protein per 100 g of total dry matter), preferably at least 75% by weight of protein. In some embodiments, pea protein extracts comprise, on a dry matter basis, at least 50% by weight to a maximum of 95% or 99% by weight of protein, such as at least 75% by weight to a maximum of 99% by weight of protein. Crude extracts typically comprise a lower protein fraction than refined or purified extracts. As used herein, the term "aqueous composition comprising pea proteins" or "aqueous solution comprising pea proteins" refers to a composition or solution comprising water and pea proteins. In some embodiments, such a solution may comprise additional constituents. In one embodiment, the aqueous composition comprising pea proteins in step (a) of the method according to the invention or as described above comprises at least 1.0% dry matter based on the total weight of the composition, preferably at least 2.0% dry matter, more preferably at least 3.0% dry matter, such as, for example, at least 4.0% dry matter, such as, for example, at least 5.0% dry matter. In another embodiment, the aqueous composition comprising pea proteins in step (a) of the method according to the invention, or as described above, comprises from 1.0% to 40% dry matter, preferably from 2.0% to 30% dry matter, more preferably from 3.0% to 20% dry matter, more preferably from 3.0% to 15% dry matter, such as from 3.0% to 10%. In one embodiment, the dry matter of the fraction comprising the protein comprises at least 50% by weight of pea protein, preferably at least 60% by weight of pea protein, more preferably at least 65% by weight of pea protein, such as, for example, at least 70% by weight, such as at least 55% by weight and at most 80% by weight, for example, from 60% by weight to 80% by weight, for example, from 60% by weight to 78% by weight. In one embodiment, the pH of the aqueous composition comprising pea proteins is at least 6.0, preferably in the range of 6.0 to 8.5, preferably in the range of 7.0 to 8.5, preferably from pH 7.3 to 8.0, such as, for example, at least pH 7.2, for example, at least 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0. For this purpose, for example, sodium hydroxide or any suitable base can be used to adjust the pH to the desired level. In some embodiments, the aqueous composition comprising pea proteins in step (a) of the method according to the invention or as described above is an aqueous composition comprising ground peas. As used herein, the term "milling" has its usual meaning in the field. For further guidance, milling, as used herein, may refer to the process of grinding solid materials, i.e., peas, under exposure to mechanical forces that penetrate the structure by overcoming internal bonding forces. Milling may disintegrate the natural structure of the peas. In a preferred embodiment, the milled particle size of a ground pea comprising at least 25% by weight of dry matter has a D50 of at most 300 pm, preferably at most 250 pm, e.g., at most 200 pm, with D50 defined as the particle size for which fifty percent by volume of the particles are smaller than D50; and D50 measured by laser diffraction analysis on a Malvern-type analyzer. For example, D50 can be measured by sieving or laser diffraction analysis. Malvern Instruments laser diffraction systems can be used advantageously for this purpose. Particle size can be measured by laser diffraction analysis on a Malvern-type analyzer. Particle size can be measured by laser diffraction analysis on a Malvern-type analyzer after the peas have been ground and are in a water suspension with 25% dry matter. Suitable Malvern systems include the Malvern 2000, Malvern MasterSizer 2000 (such as Mastersizer S), the Malvern 2600 series, and the Malvern 3600 series. Such equipment, along with its operating manual, meets or exceeds the requirements set out in ISO 13320.The Malvern MasterSizer (like the Mastersizer S) can also be useful, as it can more accurately measure the D50 towards the lower end of the range, for example, for average particle sizes of less than 8 |jm, applying Mie theory, using appropriate optical means. In certain embodiments, ground peas are ground shelled peas, i.e., peas removed from the pod. Shelled peas are peas from which the outer covering of the seeds has been removed. Removal from the pod can be carried out using techniques known in the field, such as mechanically with shelling machines. It should be understood that when reference is made herein to shelled peas, in some embodiments, not all, but the vast majority of individual peas are shelled, preferably more than 90% of the peas are shelled. In one embodiment, before, during or after grinding the peas, an aqueous solution, preferably water, such as tap water or treated well water, preferably potable water, i.e. water suitable for human consumption, is added to the peas. In a further embodiment, an amount of aqueous solution is added to the peas, such that said composition comprises from 15% to 35% dry matter based on the total weight of the composition, preferably comprising from 15% to 35%, preferably from 20% to 30%, such as at least 19%, such as at least 20%, such as at least 21%, such as at least 22%, for example at least 23%, for example at least 24%, for example at least 25%, for example at least 26%, for example at least 27%, for example at least 28%, for example at least 29%, for example at most 30%, for example at most 35% dry matter based on the total weight of the composition.In a preferred embodiment, the milling process is a wet milling process, such that an aqueous solution is added to the peas before or during milling. The person skilled in the art will understand that if the aqueous composition comprising pea proteins is an aqueous composition comprising ground peas, then all, or substantially all, of the constituents of the pea are included in the aqueous composition. In a preferred embodiment, the aqueous composition comprising pea proteins in step (a) of the method according to the invention as described herein refers to a fraction comprising pea proteins, preferably obtained after grinding the peas, and more preferably obtained after fractionating said ground peas. In one embodiment, step (c1) of the method according to the invention, as described above, comprises fractionating said ground peas into a fraction comprising at least 50% by weight of protein based on the total dry matter of said fraction. As used herein, the term "fractionation" refers to a process by which at least some of the proteins contained in the peas are separated from the rest of the pea.It should be understood that, when referring to the fractionation step, in some embodiments, not all, but nevertheless most of the individual proteins are separated, such that, preferably, at least 50% by weight, preferably at least 60% by weight of the proteins, based on the total protein content of the ground peas, are separated. Providing an aqueous composition comprising pea proteins in step (a) can be achieved by any means known in the art, such as fractionating ground peas into a protein fraction. Fractionating the ground peas into a fraction comprising proteins can be achieved by any means known in the art, such as adding a suitable base or a salt. Preferably, the ground peas are fractionated by adjusting the pH of the ground peas. Preferably, the ground peas are fractionated by increasing the pH of an aqueous composition comprising ground peas. Preferably, the fractionation step (c1) comprises adjusting the pH of the ground peas to a pH of at least 6, preferably at least 7, more preferably at least 8 and at most 9. Preferably, the fractionation step (c1) comprises increasing the pH of an aqueous composition comprising ground peas. In a preferred embodiment, the pH of the composition is adjusted to a pH of at least 6, more preferably at least 7.In another preferred embodiment, the pH of the composition is adjusted to a value in the range of pH 6 to pH 9, more preferably from pH 7 to pH 9, such as at least 7.0, for example, at least 7.1, for example, at least 7.2, for example, at least 7.3, for example, at least 7.4, for example, at least 7.5, for example, at least 7.6, for example, at least 7.7, for example, at least 7.8, for example, at least 7.9, for example, at least 8.0, for example, at least 8.1, for example, at least 8.2, for example, at least 8.3, for example, at least 8.4, for example, at most 8.5, for example, at most 8.6, for example, at most 8.7, for example, at most 8. 8, for example, at most 8, 9, for example, at most 9, 0, most preferably in the range of pH 7.5 to pH 8.5, most preferably pH 8 or approximately pH 8.Preferably, this pH adjustment is made in an aqueous composition comprising ground peas having a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%. In one embodiment, the dry matter content of the ground peas is adjusted to the aforementioned dry matter content by adding water accordingly. This pH adjustment can be made using any suitable base, such as sodium hydroxide, calcium hydroxide, potassium hydroxide, and the like. In a preferred embodiment, the pH of the compositions containing ground peas is adjusted by adding sodium hydroxide. In a preferred embodiment, after pH adjustment, the protein fraction is separated from the aqueous composition comprising ground peas by decantation or by using a hydrocyclone, preferably by decantation, and preferably by centrifugal decantation (i.e., by means of a decantation centrifuge), wherein the protein fraction is the supernatant, and the sediment is a fraction comprising, among other things, the remaining ground peas and some residual protein. In one embodiment, more than one fractionation step may be carried out sequentially.For example, after decantation, the sediment can be suspended in an aqueous solution (preferably an aqueous solution, which preferably has a pH similar to or higher (preferably pH 8.5 or approximately pH 8.5) than in the first fractionation stage) and subjected to a decantation stage, to recover additional proteins in the supernatant. It should be understood that the process of grinding the peas can be carried out simultaneously with the fractionation of the ground peas, or alternatively, the process of grinding the peas can be carried out before the fractionation stage. It should be understood that the protein-comprising fraction may also include additional constituents, notably those that become soluble through or remain soluble through the fractionation step. In a preferred embodiment, the concentration (based on dry weight) of protein in the protein-comprising fraction is at least 50% by weight, preferably at least 60% by weight, such as at least 55% by weight and at most 80% by weight, for example, from 60% to 78% by weight. In one embodiment, the fraction comprising proteins comprises at least 1.0% dry matter based on the total weight of the composition, preferably at least 2.0% dry matter, more preferably at least 3.0% dry matter, such as, for example, at least 4.0% dry matter, such as, for example, at least 5.0% dry matter. In another embodiment, the fraction comprising proteins comprises from 1.0% to 40% of dry matter, preferably from 2.0% to 30% of dry matter, more preferably from 3.0% to 20% of dry matter, more preferably from 3.0% to 15% of dry matter, such as from 3.0% to 10%. In one embodiment, the dry matter of the fraction comprising the protein comprises at least 50% by weight of pea protein, preferably at least 60% by weight of pea protein, more preferably at least 65% by weight of pea protein, such as, for example, at least 70% by weight, such as at least 55% by weight and at most 80% by weight, or between 60% by weight and 80% by weight, or between 60% by weight and 78% by weight. In some embodiments, in a further step, the fraction comprising the protein, also referred to herein as the aqueous composition comprising pea proteins, is subjected to at least one heat treatment, preferably said fraction comprising protein is subjected to a temperature of at least 30 °C, for example, at least 40 °C, for example, at least 50 °C, for example, said fraction comprising protein is subjected to a temperature in the range of 30 °C to 90 °C, more preferably in the range of 50 °C to 80 °C, even more preferably in the range of 55 °C to 75 °C, such as, for example, 55 °C, 60 °C, 65 °C, 70 °C or 75 °C. In one embodiment, the heat treatment is from 50°C to 60°C, for example, from 55°C to 65°C, for example, from 60°C to 70°C, for example, from 65°C to 75°C, for example, from 70°C to 80°C. The person skilled in the art will understand that such heat treatment may be pasteurization.Pasteurization is a well-known technique and can involve heat treatment at a specific temperature or temperature range for a specific time or time interval. Those skilled in the art will understand that, generally, as the heat treatment temperature increases, the duration of the heat treatment decreases. Step (b) of the present process comprises isolating said pea proteins from said aqueous composition comprising pea proteins (i.e., from said protein-comprising fraction). As used herein, the term "isolated" or "isolation" may refer to a process that separates the proteins from said proteins comprising the fraction. The term "concentration" may also be used interchangeably with "isolation." Accordingly, in one embodiment, in step (b) of the method according to the invention or as described above, the pea proteins are concentrated from said aqueous composition comprising pea proteins. Preferably, said isolation or concentration step may be carried out using precipitation, flocculation, filtration, and / or chromatography, or a combination thereof. This document also describes a method for extracting pea protein, comprising the following steps: (a) providing an aqueous composition comprising pea proteins, wherein said composition is obtained by a method comprising the steps of: (a1) grind peas, preferably shelled peas; (b1) fractionating said ground peas to obtain at least a fraction comprising proteins, thereby forming an aqueous composition comprising pea proteins; (b) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins preferably using precipitation, flocculation, filtration and / or chromatography; (c) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; (d) subject said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature of at least 75 °C. Preferably, the aqueous suspension comprising pea proteins in step (c) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment can be adjusted to this extent by dilution with water. In one embodiment, the isolation or concentration of said pea proteins from said aqueous composition comprising pea proteins can be carried out using precipitation, flocculation, filtration and / or chromatography. Preferably, the proteins are isolated or concentrated by isoelectric precipitation or ultrafiltration. In a preferred embodiment, the isolation or concentration of pea proteins of said composition comprises at least one step of isoelectric precipitation of said proteins. Preferably, the pH of the composition comprising the pea proteins is adjusted to the isoelectric point of the proteins. As used herein, the term "isoelectric point" refers to the pH at which the proteins have a net ionic charge of 0, or substantially 0 (i.e., the sum of the positive and negative charges is 0, or substantially 0).While it is understood that the isoelectric point of individual proteins can vary, as used herein, the isoelectric pH of protein compositions refers to the pH of the composition at which the overall charge of the proteins in the composition is 0, or substantially 0. The isoelectric pH of proteins and protein compositions can be determined using techniques known in the art. In this document, the isoelectric pH is defined as the pH at which the nitrogen solubility index is lowest. In a preferred embodiment, the pH of the composition comprising the proteins is adjusted in the range of 4.0 to 5.8, preferably from 4.5 to 5.5, such as, for example, 4.0, 4.1, 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8.The pH can be adjusted by adding an acid, such as sulfuric or hydrochloric acid. At the isoelectric point, most proteins precipitate or aggregate. In certain embodiments, the isolation of precipitated or aggregated proteins is carried out by separating a liquid fraction from an insoluble fraction, the latter comprising the precipitated or aggregated pea proteins. The separation of the precipitated or aggregated proteins can be carried out by decantation, preferably centrifugal decantation. In a preferred embodiment, the dry matter content (by weight) after the separation of the precipitated or aggregated proteins ranges from 20% to 40%, such as, for example, at least 25%, at least 26%, at least 27%, at least 28%, at least 29%, 30%, 31%, 32%, 33%, 34%, or 35%, preferably at least 27% and at most 38%, based on the total weight of the precipitated or aggregated proteins.The dry matter content can be further adjusted, for example, by adding an aqueous solution to the precipitated or aggregated proteins, thus obtaining a composition of precipitated proteins, preferably water, preferably potable water, i.e., water suitable for human consumption. Preferably, the dry matter content can be adjusted to vary from 10% to 25%, preferably from 15% to 20%, such as, for example, at least 15%, for example, at least 16%, preferably at least 17%, 18%, 19%, or 20%, based on the total weight of the precipitated protein composition. Optionally, the protein isolation process can be repeated at least once more. Preferably, the protein concentration step is performed only once. In a preferred embodiment, the precipitated or aggregated proteins are preferably resuspended in an aqueous solution, preferably water, preferably potable water, i.e., water suitable for human consumption. The dry matter content preferably ranges from 10% to 25%, preferably from 15% to 20%, such as, for example, at least 15%, for example, at least 16%, 17%, 18%, 19%, or 20% of the resuspended protein composition. According to the invention, the pH of the composition comprising the reconstituted proteins is adjusted (if necessary) or maintained in a range of 4.0 to 5.8, preferably from pH 4.5 to 5.5, such as, for example, pH 4.5, 4, 6, 4, 7, 4, 8, 4, 9, 5, 0, 5, 1, 5, 2, 5, 3, 5, 4, 5, 5. For this purpose, for example, sodium hydroxide or sulfuric acid can be used to adjust the pH to the desired level. Accordingly, obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8 in step (c) of the method described above comprises adjusting or maintaining the pH of the aqueous suspension to vary from 4.0 to 5.8, preferably from pH 4.5 to 5.5, such as, for example, pH 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5.Preferably, this pH adjustment is carried out in an aqueous composition comprising reconstituted proteins having a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%. In one embodiment, the dry matter content of the composition is adjusted to the above-mentioned dry matter content by adding water accordingly. In step (d) as described herein, said aqueous suspension having a pH in the range of 4.0 to 5.8 is subjected to heat treatment at a temperature of at least 75 °C, preferably the aqueous suspension is subjected to a temperature of at least 77 °C, preferably at least 78 °C, preferably at least 80 °C, even more preferably at least 85 °C, even more preferably at least 90 °C, for example at least 95 °C, preferably at most 160 °C, even more preferably at most 210 °C. Preferably, said proteins are subjected to heat treatment at a temperature in the range of 75 °C to 210 °C, preferably in the range of 85 °C to 160 °C, more preferably in the range of 90 °C to 150 °C. Heat treatment can be advantageously carried out by means of one or more heat exchangers or by direct or indirect steam injection.In one embodiment, the duration of the heat treatment is at least 0.01 seconds, preferably in the range of 0.01 seconds to 20 minutes, and preferably in the range of 10 seconds to 10 minutes. Those skilled in the art will appreciate that the higher the temperature, the shorter the duration of the heat treatment. For example, the heat treatment may be at a temperature in the range of 115°C to 210°C for a time in the range of 0.01 seconds to 15 seconds. Alternatively, for example, the heat treatment may be at a temperature in the range of 95°C to 115°C for a time in the range of 15 seconds to 5 minutes. Alternatively, for example, the heat treatment may be at a temperature in the range of 75°C to 95°C for a time in the range of 5 minutes to 15 minutes.In a preferred embodiment, the heat treatment is carried out at a temperature in the range of 75°C to 110°C, or more preferably, at a temperature in the range of 80°C to 100°C, for a time in the range of 2 to 10 minutes, or preferably, for a time in the range of 5 to 8 minutes. In another preferred embodiment, the heat treatment is carried out at a temperature in the range of 130°C to 150°C for a time in the range of 1 to 8 seconds. After heat treatment, the protein-containing compositions can be held at a temperature in the range of 70°C to 90°C, preferably in the range of 70°C to 85°C, before drying. According to the invention, in step (d) of the method according to the invention as described herein, said aqueous suspension having a pH in the range of 4.0 to 5.8 is subjected to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s ± 1 s. Preferably, the heat treatment time decreases when the heat treatment temperature increases. In one embodiment, the aqueous suspension, having a pH in the range of 4.0 to 5.8 at a temperature in the range of 75°C to 210°C, can be dried after step (d) of the method according to the invention as described herein. Drying can be carried out by any means known in the art, such as hot air application, evaporation, freeze-drying, contact drying, steam drying, dielectric drying, roller drying, flash drying, etc. In a preferred embodiment, the aqueous suspension, having a pH in the range of 4.0 to 5.8 at a temperature in the range of 75°C to 210°C, is dried by spray drying. Optionally, the proteins can be granulated using techniques known in the art. In certain embodiments, the pea proteins in the aqueous composition comprising pea proteins in step (a) of the methods according to the invention as described herein may be derived from ground peas. In one embodiment, said ground peas are produced from peas that have been hydrated, or said peas are dry-ground and then hydrated. In another embodiment, these ground peas have been fermented prior to milling. When whole peas undergo fermentation before milling, the fermenting microorganisms, as well as fermentation byproducts such as lactic acid and secreted compounds like enzymes, which can affect downstream processing, are advantageously removed and easily and cost-effectively separated from the peas after fermentation. Furthermore, unexpectedly, fermenting whole peas drastically reduces the monosaccharide, disaccharide, and / or oligosaccharide content, particularly monomeric or dimeric sugars such as glucose, fructose, sucrose, galactose, and / or flatulent sugars such as raffinose, stachyose, and verbascose, all of which are present in the peas. This is all the more surprising given the limited duration of fermentation in some embodiments. As used herein, the term "sugar" or "free sugar" refers to monosaccharides, disaccharides, and / or oligosaccharides consisting of up to 10 monomer units. In some embodiments, reference to "total sugars" or "total free sugars" encompasses all monosaccharides, disaccharides, and / or oligosaccharides consisting of up to 10 monomer units. In other embodiments, a specific subset of sugars is specified. In one embodiment, an aqueous composition comprising peas is subjected to fermentation, preferably in the presence of one or more lactic acid bacteria. Preferably, the peas being fermented are unground (i.e., whole) peas. However, in one embodiment, the peas may be split peas. In one embodiment, the peas are round when harvested and dried. After pod removal, the natural split at the cotyledon of the seed can be separated manually or mechanically, resulting in "split peas." The peas, as used herein, can be sorted before fermentation. For example, stones or larger plant material, as well as damaged peas, can be removed from the peas to be used according to the invention. In such embodiments where peas are subjected to fermentation, the peas, preferably dried peas, preferably shelled peas, such as dried shelled peas, are suspended in an aqueous solution. In a preferred embodiment, the aqueous solution is water. In one embodiment, the water may be potable water or well water that has been treated to make it potable. The water used is preferably potable water, i.e., water suitable for human consumption. In some embodiments, the amount of peas added to the aqueous solution to reconstitute the aqueous composition comprising peas preferably varies from 150 to 500 kg of peas per m3 of aqueous composition comprising peas, i.e., for 150 to 500 kg of peas, an aqueous solution is added until a final volume of 1 m3 is reached. In one embodiment, the aqueous composition comprising the peas at the beginning of fermentation has a pH of at least 6.0, preferably at least 6.2, for example at least 6.4, as measured in the aqueous composition comprising the peas after said composition has been ground. In a preferred embodiment, the peas that come into contact with the aqueous composition are naturally harvested and dry, or in another embodiment, the peas may be fresh peas. Preferably, the peas are dried peas and have a dry matter content (by weight) of at least 80% (i.e., at least 80 g of dry matter per 100 g total weight of the dried peas), more preferably at least 85%, for example, at least 90%, for example, at least 95%, such as, for example, in the range of 80% to 95%, for example, 85% to 95%, for example, 90% to 95%. As used herein, the term "fermentation" has its usual meaning in this field. By way of further guidance, fermentation is a microbiological metabolic process involving the conversion of sugar to acids and / or gases using yeast and / or bacteria. Subjecting an aqueous composition comprising peas to fermentation, as used herein, may therefore refer to incubating the aqueous composition comprising peas with bacteria and / or yeast, preferably lactic acid bacteria, under conditions suitable for the bacteria and / or yeast to be metabolically active. As used herein, "lactic acid bacteria" refers to a population of Gram-positive, low-GC, acid-tolerant, generally non-spore-forming, non-respiratory cocci or bacilli that are associated by their common metabolic and physiological characteristics and that produce lactic acid as the principal metabolic end product of carbohydrate fermentation. These bacteria are commonly found in dairy products and decaying plants. As used herein, lactic acid bacteria may be non-pathogenic in the sense that they do not cause harm or lead to adverse effects when ingested.Preferably, the lactic acid bacteria as used herein are one or more bacterial genera selected from Lactobacillus, Pediococcus, Lactococcus, Leuconostoc, Streptococcus, Aerococcus, Carnobacterium, Enterococcus, Oenococcus, Sporolactobacillus, Tetragenococcus, Vagococcus and Weisella and combinations thereof.Most preferably, lactic acid bacteria are Lactobacillus sp, preferably selected from the group consisting of Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosae, Lactobacillus pontis, Lactobacillus acid, Lactobacillus plantarum, Lactobacillus helveticus, Lactobacillus buchneri, Lactobacillus delbrueckii, and Lactobacillus casei, and mixtures of the same, for example of the group consisting of Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosa, Lactobacillus, ponnacillus Lactobacillus acidophilus and mixtures of the same, for example of the group consisting of Lactobacillus fermentum, Lactobacillus crispatus, Lactobacillus panis, Lactobacillus mucosae, Lactobacillus pontis and mixtures of the same, for example dichabacillus es fermentus Lactobacillus, o Lactobacillus fermentus crispatus.In some embodiments, fermentation can be spontaneous (i.e., fermentation in which no fermenting microorganisms are deliberately added, but fermentation is carried out by microorganisms, preferably lactic acid bacteria, that occur naturally on / within the peas and / or in the environment) or inoculated (i.e., fermentation in which fermenting microorganisms, preferably lactic acid bacteria, are deliberately added). Fermentation can also be carried out by transferring part or all of the aqueous fraction from one fermentation stage to the next fermentation to be initiated, for example, by transferring at least 1 / 10 of the first fermentation volume to at least a second fermentation stage. In a preferred embodiment, the fermentation is anaerobic (not strictly anaerobic).In a preferred embodiment, said Lactobacillus fermentum is Lactobacillus fermentum LMG 6902 or LMG 18026. In a preferred embodiment, said Lactobacillus Crispatus is Lactobacillus Crispatus LMG 12005. In a preferred embodiment, said Lactobacillus is Lactobacillus acidbacillus acidophilus LMG 8151. In one embodiment, the aqueous composition comprising peas is subjected to fermentation until the pH in the peas is at most 5.5, preferably at most 5.0, more preferably ranging from 3.5 to 5, preferably as measured at room temperature in 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section.In one embodiment, the aqueous composition comprising peas is subjected to fermentation until the pH in the peas varies from 3.5 to 4.5, for example, from 4.0 to 5.0, preferably from 4.5 to 5.5, such as, for example, at least 3.5, for example, at least 3.75, for example, at least 4.0, for example, at least 4.25, for example, at least 4.50, for example, at least 4.75, for example, at most 5.0, for example, at most 5.25, for example, at most 5.5, preferably, as measured at room temperature in 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section. In one embodiment, the dried peas have a pH of at least 6.0, preferably in the range of 6.0 to 7.10 before fermentation, such as, for example, at least 6.0, for example, at least 6.1, for example, at least 6.2, for example, at least 6.3, for example, 6.4, for example, 6.5, for example, 6.6, for example, 6.7, for example, 6.8, for example, 6.9, for example, 7.10, preferably in the range of 6.25 to 6.75, preferably, as measured at room temperature on 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section. In one embodiment, the aqueous composition comprising peas is subjected to fermentation until the pH in the peas decreases by at least 1 pH unit, preferably by at least 1.5 pH units, such as, for example, at least 1, for example, at least 1, 1, for example, at least 1, 2, for example, at least 1, 3, for example, at least 1, 4, for example, at least 1, 5, for example, at least 1, 6, for example, at least 1, 7, for example, at least 1, 8, for example, at least 1, 9, for example, at least 2, for example, at least 2, 1, for example, at least 2, 2, for example, at least 2, 3, for example, at least 2, 4, for example, at least 2, 5, for example, at least 2, 6, for example, at least 2, 7, by for example, at least 2, 8, for example, at least 2, 9, for example, at least 3 pH units, preferably as measured at room temperature on 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section.In another embodiment, the aqueous composition comprising peas is subjected to fermentation until the pH in the peas decreases by 1 pH unit to 3 pH units, preferably by 1.5 pH units to 3 pH units, such as, for example, by 1.5 pH units to 2.5 pH units, or by 2.0 pH units to 3.0 pH units, preferably, as measured at room temperature in 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section. By way of example, and without limitation, at the beginning of fermentation, the pH in the peas may be 6.5, and at the end of fermentation, the pH in the peas may be 5.0, preferably, as measured at room temperature in 1 g of said peas that have been ground and then suspended in 9 g of water, as described in the experimental section. In one embodiment, the aqueous composition comprising peas is subjected to fermentation for at least 3 h, preferably at least 4 h, more preferably at least 6 h. In another embodiment, the aqueous composition comprising peas is subjected to fermentation for a period in the range of 3 to 24 h, preferably in the range of 4 to 24 h, more preferably in the range of 4 to 20 h, such as, for example, at least 3 h, for example, at least 4 h, for example, at least 5 h, for example, at least 6 h, for example, at least 7 h, for example, at least 8 h, at least 9 h, approximately 10 h, approximately 11 h, approximately 12 h, approximately 13 h, approximately 14 h, for example, at most 15 h, for example, at most 16 h, for example, at most 17 h, for example, at most 18 h, for example, at most 19 h, for example, at most 20 h, for example, at most 21 h, for example, at most 22 h, for example, at most 23 h, for example, at most 24 h.The expert will appreciate that, for example, spontaneous fermentations can take longer than fermentations carried out by adding bacteria, given the different amounts of microorganisms at the start of the fermentation. In one embodiment, the aqueous composition comprising peas is fermented at a temperature optimum for the fermenting microorganism, preferably at a temperature that is at most 5 °C higher or lower than the optimum temperature for the fermenting microorganism. The optimum temperatures for bacteria and / or yeasts as defined herein are known in the art. For further guidance, and without limitation, an optimum temperature as defined herein refers to the temperature at which growth is maximized. In a further embodiment, the aqueous composition comprising peas is fermented at a temperature of at least 30 °C, for example, in the range of 30 °C to 50 °C, preferably in the range of 35 °C to 45 °C.In another embodiment, the aqueous composition comprising peas is subjected to fermentation at a temperature in the range of 30 °C to 40 °C, 35 °C to 45 °C, or 40 °C to 50 °C, preferably 40 °C, or approximately 40 °C. In one embodiment, the aqueous composition comprising peas is subjected to fermentation in the presence of fermenting microorganisms, such as bacteria and / or yeasts, preferably comprising one or more lactic acid bacteria, more preferably, said lactic acid bacteria being selected from the group comprising one or more Lactobacillus sp. In one embodiment, the fermentation is carried out in the presence of one or more of the above-specified microorganisms, preferably lactic acid bacteria, at a concentration in the range of 10² CFU / ml to 10¹⁰ CFU / ml of said aqueous composition comprising the peas, such as at least 10⁴ CFU / ml, for example, at least 10⁵ CFU / ml, for example, at least 10⁶ CFU / ml, for example, at least 10⁷ CFU / ml, for example, at least 10⁸ CFU / ml, for example, at least 10⁹ CFU / ml of said aqueous composition comprising the peas.Colony-forming units (CFU) are well-known in this field and can be determined, for example, by plate counting. It should be understood that "CFU / ml" refers to the number of CFU per ml of the total aqueous composition comprising peas, i.e., including the peas themselves. In another embodiment, the aqueous composition comprising peas is subjected to fermentation in the presence of fermenting microorganisms, preferably comprising one or more lactic acid bacteria, preferably comprising one or more Lactobacillus sp., wherein the microorganisms, preferably lactic acid bacteria, are added to a concentration of at least 102 CFU / ml of aqueous composition comprising peas. In one embodiment, the peas at the end of fermentation and before the milling stage have a dry matter content (by weight) in the range of 35% to 60%, preferably from 35% to 60%, for example from 40% to 50%, such as, for example, at least 40%, for example, at least 41%, at least 42%, for example, at least 43%, for example, at least 44%, for example, at least 45%, for example, at least 46%, for example, at least 47%, approximately 48%, approximately 49%, for example, at most 50%, for example, at most 55%, for example, at most 60% based on the total weight of the peas at the end of fermentation, i.e., after the peas have been isolated from the aqueous composition. In a further embodiment, the peas are fermented until they have a dry matter content (by weight) in the range of 35% to 60%, preferably 35% to 55%, for example 40% to 50%, such as, for example, at least 40%, for example, at least 41%, at least 42%, for example, at least 43%, for example, at least 44%, for example, at least 45%, for example, at least 46%, for example, at least 47%, approximately 48%, approximately 49%, for example, at most 50%, for example, at most 55%, for example, at most 60% based on the total weight of the peas at the end of fermentation, i.e., after the peas have been isolated from the aqueous composition.In this embodiment, the peas preferably have a dry matter content (by weight) before fermentation, or at the beginning of fermentation, of at least 80% (i.e., at least 80 g of dry matter per 100 g total weight of the dried peas), more preferably at least 85%, for example, at least 90%, for example, at least 95%, such as, for example, in the range of 80% to 95%, for example, 85% to 95%, for example, 90% to 95%. In one embodiment, the peas that have undergone fermentation are ground. For this purpose, in one embodiment, the peas may be removed from the aqueous solution after fermentation and then ground. Preferably, the peas are washed or rinsed after fermentation and before grinding. The washing or rinsing may be carried out with an aqueous solution, preferably water, such as tap water or treated well water, preferably potable water, i.e., water suitable for human consumption. In a preferred embodiment, the method for extracting pea protein from Pisum sativum ssp. comprises the following steps: (i) provide peas; (ii) grind said peas; (iii) fractionating said ground peas in the presence of an aqueous solution to obtain at least one aqueous composition comprising pea proteins; (iv) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins; (v) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; and (vi) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature in the range of 75 °C to 210 °C; wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5; wherein step (d) comprises subjecting said precipitated pea proteins to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s ± 1 s. Preferably, the aqueous suspension comprising pea proteins in step (v) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment can be adjusted to this extent by dilution with water. In a preferred embodiment, the method for extracting pea protein from Pisum sativum ssp. comprises the following steps: (i) subjecting an aqueous composition comprising peas to fermentation, preferably in the presence of one or more lactic acid bacteria; (ii) grind said peas; (iii) fractionating said ground peas in the presence of an aqueous solution to obtain at least one aqueous composition comprising pea proteins; (iv) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins; (v) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; and (vi) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature in the range of 75 °C to 210 °C; wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5; wherein step (d) comprises subjecting said precipitated pea proteins to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s ± 1 s. Preferably, the aqueous suspension comprising pea proteins in step (v) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment can be adjusted to this extent by dilution with water. In a preferred embodiment, the method for extracting pea protein from Pisum sativum ssp. comprises the following steps: (i1) provide an aqueous composition comprising pea proteins; (ii1) isolating or concentrating said pea proteins from said aqueous composition comprising pea proteins, preferably using isoelectric precipitation, preferably adjusting the pH of said aqueous composition to a pH in the range of 4.0 to 5.8; (iii1) obtaining said pea proteins isolated or concentrated as an aqueous suspension having a pH in the range of 4.0 to 5.8; (iv1) optionally adjust the dry matter content of the aqueous suspension to a value in the range of 10% to 25%, preferably 15% to 20%; (v1) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature in the range of 75°C to 210°C; wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5; wherein step (d) comprises subjecting said precipitated pea proteins to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s ± 0.01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 s ± 1 s; (vi1) drying said aqueous suspension having a pH in the range of 4.0 to 5.8, preferably obtaining a pea protein composition having a pH in the range of 4.0 to 5.8, as measured at room temperature in 10 g of pea protein composition suspended in 90 g of water. Preferably, the aqueous suspension comprising pea proteins in step (iii1) has a dry matter content of at most 45%, preferably at most 40%, preferably at most 35%, preferably at most 30%, preferably at most 25%, and in one embodiment can be adjusted to this extent by dilution with water. Pea protein extracts obtained by the methods according to the present invention as described herein have different characteristics, such as different biochemical and / or organoleptic characteristics, as well as a difference in the values of the parameters associated with quality compared to known pea proteins of the prior art. Accordingly, in one aspect, the present invention covers pea protein extracts and pea protein compositions obtained by or that can be obtained by the methods according to the invention as described herein. In a further aspect, the invention relates to a pea protein composition comprising at least 60% by weight of protein based on the total dry matter of the composition, wherein said pea protein composition has a nitrogen solubility index at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition, and preferably a nitrogen solubility index at pH 7.0 of at most 11%, preferably at most 10%, preferably at most 9%, preferably at most 8%. In a preferred embodiment, said composition is obtained by the method of the invention. In a further aspect, the invention relates to a pea protein composition having a gel strength at pH 6 of at most 100 g, preferably at most 75 g, and even more preferably at most 50 g. In another aspect, the invention relates to pea proteins having a gel strength at pH 6 in the range of 10 g to 100 g, preferably in the range of 10 g to 75 g, and even more preferably in the range of 10 g to 50 g. In a further aspect, the invention relates to a pea protein composition comprising at least 60% by weight of protein based on the total dry matter of the composition, wherein said pea protein composition has a nitrogen solubility index at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition, and preferably an NSI at pH 7.0 of at most 11%, preferably at most 10%, preferably at most 9%, preferably at most 8%, and a gel strength at pH 6 of at most 100g, preferably at most 75g, even more preferably at most 50g.In another aspect, the invention relates to pea proteins having a gel strength at pH 6 in the range of 10 ga 100 g, preferably in the range of 10 ga 75 g, even more preferably in the range of 10 ga 50 g. In additional aspects, the invention relates to pea proteins having one or more, preferably all, characteristics A to H as indicated in Table 1. Table 1 In preferred embodiments, the pea proteins have any of the following combinations of features from Table 1: A, B, C, D, E, F, G, H, A+B, A+C, A+D, A+E, A+F, A+G, A+H, B+C, B+D, B+E, B+G, B+H, B+D, B+H, B+D, B+H, B+D C+E, C+F, C+G, C+H, D+E, D+F, D+G, D+H, E+F, E+G, E+H, F+G, F+H, G+H, A+B+C, A+B+D, A+B+E, A+B+F, A+B+G, A+B+H, A+C+D, A+C+F, A+C+G, A+C+G, A+C+G, A+C+G, A+C+G A+C+H, A+D+E, A+D+F, A+D+G, A+D+H, A+E+F, A+E+G, A+E+H, A+F+G, A+F+H, A+G+H, B+C+D, B+C+E, B+C+F, B+C+G, B+C+H, B+D+E, B+D+G, B+D+G, B+C+H B+D+H, B+E+F, B+E+G, B+E+H, B+F+G, B+F+H, B+G+H, C+D+E, C+D+F, C+D+G, C+D+H, C+E+F, C+E+G, C+E+H, C+F+G, C+F+H, D+G+H, D+G+H, D+E+H, D+F+G, D+F+H, D+G+H, E+F+G, E+F+H, E+G+H, F+G+H, A+B+C+D, A+B+C+E, A+B+C+F, A+B+C+G, A+B+C+H, A+B+D+E, A+F+D+G, A+B+D+B, A+B+D+E A+B+D+H, A+B+E+F, A+B+E+G, A+B+E+H, A+B+F+G, A+B+F+H, A+B+G+H, A+C+D+E, A+C+D+F, A+C+D+G, A+C+D+H, A+C+E+F, A+C+E+H, A+C+E+H, A+C+E+H, A+C+E+H, A+C+E+H, A+C+E+H A+C+F+G, A+C+F+H, A+C+G+H, A+D+E+F, A+D+E+G, A+D+E+H, A+D+F+G, A+D+F+H, A+D+G+H, A+E+F+G, A+E+F+H, A+E+G+H,A+F+G+H, B+C+D+E, B+C+D+F, B+C+D+G, B+C+D+H, B+C+E+F, B+C+E+G, B+C+E+H, B+C+F+G, B+C+F+H, B+C+G+H, B+D+E+F, B+D+E+G, B+D+E+H, B+D+F+G, B+D+F+H, B+D+G+H, B+E+F+G, B+E+F+H, B+E+G+H, B+F+G+H, C+D+E+F, C+D+E+G, C+D+E+H, C+D+F+G, C+D+F+H, C+D+G+H, C+E+F+G, C+E+F+H, C+E+G+H, C+F+G+H, D+E+F+G, D+E+F+H, D+E+G+H, D+F+G+H, E+F+G+H, A+B+C+D+E, A+B+C+D+F, A+B+C+D+G, A+B+C+D+H, A+B+C+E+F, A+B+C+E+G, A+B+C+E+H, A+B+C+F+G, A+B+C+F+H, A+B+C+G+H, A+B+D+E+F, A+B+D+E+G, A+B+D+E+H, A+B+D+F+G, A+B+D+F+H, A+B+D+G+H, A+B+E+F+G, A+B+E+F+H, A+B+E+G+H, A+B+F+G+H, A+C+D+E+F, A+C+D+E+G, A+C+D+E+H, A+C+D+F+G, A+C+D+F+H, A+C+D+G+H, A+C+E+F+G, A+C+E+F+H, A+C+E+G+H, A+C+F+G+H, A+D+E+F+G, A+D+E+F+H, A+D+E+G+H, A+D+F+G+H, A+E+F+G+H, B+C+D+E+F, B+C+D+E+G, B+C+D+E+H, B+C+D+F+G, B+C+D+F+H, B+C+D+G+H, B+C+E+F+G, B+C+E+F+H, B+C+E+G+H, B+C+F+G+H, B+D+E+F+G, B+D+E+F+H, B+D+E+G+H, B+D+F+G+H, B+E+F+G+H, C+D+E+F+G, C+D+E+F+H, C+D+E+G+H, C+D+F+G+H, C+E+F+G+H, D+E+F+G+H, A+B+C+D+E+F, A+B+C+D+E+G, A+B+C+D+E+H, A+B+C+D+F+G,A+B+C+D+F+H, A+B+C+D+G+H, A+B+C+E+F+G, A+B+C+E+F+H, A+B+C+E+G+H, A+B+C+F+G+H, A+B+D+E+F+G, A+B+D+E+F+H, A+B+D+E+G+H, A+B+D+F+G+H, A+B+E+F+G+H, A+C+D+E+F+G, A+C+D+E+F+H, A+C+D+E+G+H, A+C+D+F+G+H, A+C+E+F+G+H, A+D+E+F+G+H, B+C+D+E+F+G, B+C+D+E+F+H, B+C+D+E+G+H, B+C+D+F+G+H, B+C+E+F+G+H, B+D+E+F+G+H, C+D+E+F+G+H, A+B+C+D+E+F+G, A+B+C+D+E+F+H, A+B+C+D+E+G+H, A+B+C+D+F+G+H, A+B+C+E+F+G+H, A+B+D+E+F+G+H, A+C+D+E+F+G+H, B+C+D+E+F+G+H, A+B+C+D+E+F+G+H., The expert will understand that when "pea proteins" is referred to in some embodiments, a composition is being described that predominantly, but not exclusively, comprises pea proteins. Residual impurities may be present in such compositions. Such residual impurities may include, for example, minerals, sugars, etc. In a preferred embodiment, the term "pea proteins" preferably refers to a composition comprising (on a total dry matter basis) at least 60% by weight of protein, preferably at least 75% by weight of protein, and more preferably at least 80% by weight.In another preferred embodiment, the term pea protein refers to a pea protein extract or a pea protein composition comprising (based on the total dry matter of the composition) from 70% by weight to 98% by weight of protein, preferably from 75% by weight to 98% by weight of protein, more preferably from 80% by weight to 98% by weight of protein, more preferably from 85% by weight to 98% by weight, even more preferably from 88% by weight to 98% by weight. Also described herein is a composition comprising pea proteins obtained by, or obtainable by, the methods according to the invention as described herein. In a preferred embodiment, such a composition is an edible composition. As used herein, and as will be understood by those skilled in the art, an "edible" composition refers to a composition that is suitable for human or animal consumption. Preferably, such a composition is a food or feed, more preferably a bakery food product or a confectionery food product. In a preferred embodiment, such a food product is a biscuit, bread, cake, waffle, fudge, extruded cereal, or bar. Accordingly, in a further aspect, the present invention relates to the use of pea protein extract as described herein, in particular, pea protein extract obtained or obtainable according to the methods described herein, in food products or feed. In a preferred embodiment, the food products are bakery or confectionery products. The pea protein extract as described herein can, for example, partially or completely replace other proteins in food or food products, such as, for example, proteins of animal origin, such as milk proteins. Particularly suitable applications of the pea protein extract as described herein can be, for example, in processes for preparing bakery or confectionery products. In a further aspect, the invention relates to the use of pea protein extract as described herein, in particular, pea protein extract obtained or obtainable according to the methods described herein for clarifying or clarifying liquids, such as brews and beverages. As used herein, the terms "clarify" and "clarify" have their usual meanings in this field. For the sake of further guidance, and without limitation, the term "clarify" refers to a process by which, for example, insoluble (suspended) elements are removed from a liquid by the addition of a clarifying agent. The addition of a clarifying agent may cause insoluble elements to aggregate, but it may also cause certain soluble elements to form larger particles (for example, proteins), which can be easily removed, such as by filtration or centrifugation. In one embodiment, the liquid to be clarified is a beverage, i.e., a liquid suitable for human or animal consumption.In a particularly preferred embodiment, said beverage is a fermented beverage, such as an alcoholic beverage, preferably wine (including, but not limited to, white wine, rosé wine, Champagne, Port, Sherry, etc.). Uses of pea proteins as described herein according to the invention are also contemplated for clarifying fermented beverages or beverages other than wine. The aspects and embodiments of the invention are further supported by the following non-limiting examples. Examples Protocols Unless otherwise specified, in the examples below, all parameters are measured as defined in this section. The measurement of parameters as defined in this section also represents, in preferred embodiments, the method for measuring such parameters according to the invention as described in the respective aspects and embodiments of the detailed description above. Unless otherwise specified, in the examples below, all parameters are measured as defined in this section. The measurement of parameters as defined in this section also represents, in preferred embodiments, the method for measuring such parameters according to the invention as indicated in the respective aspects and embodiments of the preceding detailed description. pH measurement in dried peas or aqueous composition comprising peas or ground peas The pH was measured using a WTW SERIES Inolab Termil 740 pH meter. The device was calibrated with buffer solutions at pH 4.01 (WTW Technical Buffer pH 4.01, Model STP4, Order No. 108706) and pH 7 (WTW Technical Buffer pH 7.00, Model STP7, Order No. 108708). When measuring the pH of the aqueous composition, excluding the peas, a sample of the aqueous solution was taken directly from the fermentation vessel. The pH of the sample was measured once the value stabilized. When measuring the pH of peas, the peas were taken from the fermentation vessel. The peas were drained in a colander and then placed on absorbent paper for two minutes to remove excess juice. The peas were then ground for one minute using a blender (Magic Bullet, Homeland Housewares). One gram of the ground peas was suspended in 9 grams of deionized water (water conductivity <15 J S). The suspension was ground again using the blender. Finally, the pH of the suspension was measured (at room temperature) once the value had stabilized. When measuring the pH of dried peas, the peas were dry-ground for one minute using a grinder (Kenwood). Five grams of the ground dried peas were suspended in 95 g of deionized water (water conductivity <15 J S). The suspension was then homogenized on a stirring plate for one minute. The pH of the suspension was measured once the value stabilized. pH measurement in protein powder extract The pH was measured using a WTW pH / Cond 340I / SET pH meter. The instrument was calibrated with buffer solutions at pH 4.01 (WTW Technical Buffer pH 4.01, Model STP4, Order No. 108706) and pH 7 (WTW Technical Buffer pH 7.00, Model STP7, Order No. 108708). 5.0 g of protein extract powder were introduced into a 100 mL beaker and prepared to 50 g (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g) with demineralized water at room temperature. The suspension was stirred for 5 minutes on a stirring plate (Stuart US151) at intensity 4. The pH of the suspension (at room temperature) was measured under stirring once the value stabilized. pH measurement in protein suspension The pH was measured using a WTW pH / Cond 340i / SET pH meter. The instrument was calibrated with buffer solutions at pH 4.01 (WTW Technical Buffer pH 4.01, Model STP4, Order No. 108706) and pH 7 (WTW Technical Buffer pH 7.00, Model STP7, Order No. 108708). 50 mL of protein suspension were placed in a 100 mL beaker without further dilution. The pH of the sample (at room temperature) was measured once the value stabilized. pH measurement of food products The pH meter (Knick Portavo 902 PH) was calibrated using buffer solutions at pH 4.01 (WTW Technical Buffer pH 4.01, model STp4, order no. 108706) and pH 7 (WTW Technical Buffer pH 7.00, model STP7, order no. 108708). The pH was measured by inserting the probe of the pH meter (Knick Portavo 902 PH) directly into the product (liquid food product, paste, dough, etc.) at room temperature. For solid food products, a 50% dilution was prepared in demineralized water, and the solution was analyzed. After stabilization, the pH value was recorded. Enumeration of lactic acid bacteria The sample dilutions were performed with EPT Dilucups 9 ml Led techno. The medium used was MRS agar (according to De Man, Rogosa, and Sharpe), Merck Cat. No. 1.10661.0500. The peas or pea suspension were ground using a Magic Bullet blender (Homeland Housewares). When analyzing a sample of the aqueous composition excluding peas, a sample was taken directly from the fermentation vessel. One milliliter of sample was plated. If a dilution was required, 1 milliliter of sample was added to the dilution cup, and this step was repeated until the correct dilution was achieved. Then, 1 milliliter of the diluted sample was plated. The Petri dishes were incubated for 48 hours at 45°C. When analyzing a pea sample, whole peas were taken from the fermentation vessel. The peas were drained in a sieve and then placed on absorbent paper for two minutes to remove excess juice. The peas were then ground for one minute. The ground peas were suspended (1 g of peas in 9 g of deionized water) in deionized water (conductivity <15 J S). The suspension was then blended. One milliliter of the suspension was placed on a Petri dish. If dilution was required, 1 ml of the suspension was added to the dilution container (dilucup), and this step was repeated until the correct dilution was achieved. Then, 1 ml of the diluted sample was plated. The Petri dishes were incubated for 48 hours at 45 °C. Determination of dry matter Total dry matter was determined gravimetrically as the residue remaining after drying. Moisture was evaporated from the sample by oven drying. Five grams of sample were weighed onto a pre-weighed, dry aluminum plate (Ohaus precision balance, capacity 410 g, sensitivity 0.001 g). The sample was placed in an oven at 103 °C until the residual weight remained constant (at least 24 h). The sample was cooled in a desiccator for 1 hour and then immediately weighed. The results are expressed as % (g of dry matter per 100 g of sample). Dry matter (%) = (m3 - m1) / (m2 - ml) x 100 m1 = weight of the dry aluminum plate (in g) m2 = weight of the aluminum plate with the sample before drying (in g) m3 = weight of the aluminum plate with the sample after drying (in g) Determination of dry matter content of food products The dry matter content of the food products was determined in duplicate after drying 5 g of sample at 104 °C overnight. Ash determination The ash content was determined gravimetrically as the residue remaining after heating in a muffle furnace at high temperature. Moisture was evaporated from the sample by oven drying. Two grams of sample were weighed into a pre-weighed, dry porcelain crucible (Ohaus precision balance, capacity 410 g, sensitivity 0.001 g). The crucible was placed in a muffle furnace at 550 °C for 24 h. It was then placed in an oven at 103 °C for 1 h and subsequently in a desiccator for 1 h. After cooling, the crucible was weighed. Results are expressed as % (g of ash per 100 g of sample). Ash (%) = (m3 - m1) / (m2-m1) x 100 m1 = weight of the crucible (in g) m2 = weight of crucible with sample (in g) m3 = weight of the crucible with ashes (in g) Determination of protein content by the Dumas method The instrument (Leco FP2000) was calibrated using EDTA sold by Leco under reference 502092. The quantities of EDTA weighed for calibration ranged from 0.08 g to 0.50 g (0.08 g, 0.15 g, 0.25 g, 0.35 g, 0.40 g, 0.50 g). Samples of 0.3 g to 1 g were weighed on a precision balance (Sartorius BP61S, capacity 61 g, sensitivity 0.1 mg) and placed in a ceramic jar. The ceramic jar was automatically placed in a 1200 °C oven where the sample was burned in a combustion tube by pyrolysis under controlled oxygen flow. Nitrogen compounds are converted to N2 and NOx, while other volatile decomposition compounds are retained through adsorbent filters and a series of purification reagents. All nitrogen compounds are reduced to molecular N, which is quantitatively determined by a thermal conductivity detector. The nitrogen content is then calculated using a microprocessor. The results are expressed as a percentage of protein (% N*6, 25): % nitrogen = g of nitrogen per 100 g of sample % protein = % nitrogen x 6.25 Determination of nitrogen content in ISN samples by the Dumas method The instrument (Leco FP2000) was calibrated using a 15 mg / ml glycine solution (glycine powder marketed by Merck under reference 1.04201.1000). The amounts of 15 mg / ml glycine solution weighed for calibration ranged from 0.1 g to 1.8 g (0.1 g, 0.4 g, 0.7 g, 1.1 g, 1.4 g, 1.8 g). 1 g to 1.8 g of sample were weighed on a precision balance (Sartorius BP61S, capacity 61 g, sensitivity 0.1 mg) and placed in a ceramic jar covered by a nickel insert. The ceramic jar was automatically placed in a 1200 °C oven where the sample was burned in a combustion tube by pyrolysis under controlled oxygen flow. Nitrogen compounds are converted to N2 and NOx, while other volatile decomposition compounds are retained through adsorbent filters and purification reagent series.All nitrogen compounds are reduced to molecular N, which is quantitatively determined by a thermal conductivity detector. The nitrogen content is then calculated using a microprocessor. The results were expressed as a percentage of nitrogen: % nitrogen = g of nitrogen per 100 g of sample Determination of the nitrogen solubility index (NSI) After dispersing proteins in demineralized water, the nitrogen solubility index was determined by measuring the ratio between the percentage of nitrogen in the supernatant after centrifugation and the percentage of nitrogen in the starting suspension. The method was used with a protein powder extract containing 90–99% dry matter (by weight) and was performed one month after drying the protein extract. The measurement was taken at room temperature. 9.0 g of sample were introduced into a 400 ml beaker and diluted to 300 g (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g) with demineralized water at room temperature. The suspension was homogenized with a spoon and then stirred for 5 minutes on a hot plate (Stuart US151) at intensity 4. 10 ml of the starting suspension were collected and the nitrogen content was analyzed using a Leco FP 2000 protein analyzer. The suspension was divided into two 150 ml beakers; the pH was raised in one and lowered in the other. The pH of the suspension was adjusted to pH 3, 5, 4, 5, 5, 5, 6, 5, 7, and 8 using 1N HCl or 1N NaOH (WTW pH / Cond 340i / SET pH meter). For each pH adjustment, the pH value was recorded once stabilized, and 10 mL of the suspension was collected in a 10 mL centrifuge tube. Aliquots of the suspension at different pH levels were centrifuged for 15 min at 6000 rpm (ALC 4239 R centrifuge).The different supernatants were collected and analyzed to determine the nitrogen content in a Leco FP 2000 protein analyzer. For each pH tested, the nitrogen solubility index was calculated according to the following expression:. % nitrogen solubility index = % nitrogen in supernatant / % nitrogen in starting solution x 100 Determination of the isoelectric pH of the fraction comprising protein 300 g of a protein fraction with a protein content of 1% by weight (based on the total weight of the protein fraction) was introduced into a 400 ml beaker at room temperature. The suspension was stirred for 5 minutes on a stirrer (Stuart US151) at intensity 4. 10 ml of the starting suspension was collected and its nitrogen content was analyzed using a Leco FP 2000 protein analyzer. The suspension was then divided into two 150 ml beakers; the pH was raised in one and lowered in the other. The pH of the suspension was adjusted to pH 3, 5, 3, 75, 4, 0, 4, 25, 4, 5, 4, 75, 5, 0, 5, 25, 5, 5, 5, 75, 6, 0, 6, 25, 6, 5, 6, 75 and 7, 0 with 1N HCl or 1N NaOH (WTW pH / Cond 340i / SET pH meter). For each pH adjustment, the pH value was recorded once stabilized and 10 ml of the suspension was collected in a 10 ml centrifuge tube.Aliquots of the suspension at different pH were centrifuged for 15 min at 6000 rpm (ALC 4239 R centrifuge). The different supernatants were collected and analyzed to determine the nitrogen content using a Leco FP 2000 protein analyzer. For each pH tested, the nitrogen solubility index was calculated according to the following expression: % nitrogen solubility index = % nitrogen in supernatant / % nitrogen in starting solution x 100 The isoelectric pH was determined as the pH at which the nitrogen solubility index was lowest. Sugar determination The sample was prepared using an Eppendorf Centrifuge 5417R and NANOSEP 100k OMEGA centrifuge devices. The peas or pea suspension were ground using a blender, Magic Bullet, Homeland Housewares. When analyzing a sample of the aqueous composition excluding peas, a sample was taken directly from the fermentation vessel. The sample was diluted 20-fold (1 g of pea juice in 19 g of deionized water) with deionized water (conductivity <15 J S). 0.5 mL of this dilution was placed in a filtration Eppendorf tube and centrifuged at 14,000 rpm for 10 minutes. The filtrate was then used for sugar analysis. When preparing a pea sample, whole peas were taken from the fermentation vessel. The peas were drained in a sieve and then placed on absorbent paper for two minutes to remove excess juice. The peas were then ground for one minute. The ground peas were suspended (1 g of peas in 9 g of deionized water) in deionized water (conductivity <15 J S). The suspension was then blended. The suspension was diluted 8-fold (1 g of pea suspension in 8 g of deionized water) with deionized water (conductivity <15 J S). 0.5 mL of this dilution was placed in a filtration Eppendorf tube and centrifuged at 14,000 rpm for 10 minutes. The filtrate was then used for sugar analysis. For sugar analysis, a Thermo Scientific Dionex ICS 5000 chromatographic system was used with the Chromeleon 6.80 SR11 Build 3161 software. Separation was performed using a 4 mm x 250 mm Carbopac PA100 (with protective cover) at 40 °C. Elution was carried out with 40 mM NaOH at a flow rate of 1 mL / min. The injection volume was 10 JL. Quadruple pulse detection was used for PAD detection. Calibration was performed with appropriate standard solutions, which varied for each of the following sugars: The concentration of the standard sugar solution (Est1, 2, 3 and 4) (mg / l) is provided in the table below. Acidity measurement Acidity was measured using an Inolab Termil 740 WTW Series pH meter. The device was calibrated with buffer solutions at pH 4.01 (WTW Technical Buffer pH 4.01, Model STP4, Order No. 108706) and pH 7 (WTW Technical Buffer pH 7.00, Model STP7, Order No. 108708). The peas or pea suspension were ground using a blender, Magic Bullet, Homeland Housewares. When measuring the acidity of the "pea juice", a sample (A) was taken directly from the fermentation vessel. Sample (A) was weighed. 1 mol / l of sodium hydroxide solution (C) (No. 1.09137.1000 TitriPURR; Density = d = 1.04 kg / L) was slowly added until the pH of the sample stabilized at pH 7 for at least two minutes. The mass of sodium hydroxide (B) was then calculated. Acidity (mEq / kg) = (B* (C / d) / A) *1000 When measuring the acidity of the peas, whole peas were taken from the fermentation vessel. The peas were drained in a colander and then placed on absorbent paper for two minutes to remove excess juice. The peas were then ground for one minute. The ground peas were suspended (1 g of peas in 9 g of deionized water) in deionized water (conductivity <15 µS). The suspension was then blended. A pea suspension was obtained. An exact amount of the pea suspension (A') was weighed. 1 mol / l of sodium hydroxide solution (C) (No. 1.09137.1000 TitriPURR; Density = d = 1.04 kg / L) was slowly added until the pH of the suspension stabilized at pH 7 for at least two minutes. The mass of sodium hydroxide (B') was then calculated. Acidity (mEq / kg) = (B' * (C7d) / (A710) ) *1000 Determination of viscosity with the Brookfield DVII viscometer The viscosity of a protein suspension is determined using a Brookfield DVII viscometer by measuring its resistance to flow imposed by the rotation of a cylindrical probe. This resistance causes a spring attached to the sensor of a drive system to rotate. The viscosity value, expressed in centipoise (cP), is proportional to the percentage of torsion indicated by the viscometer and a multiplicative factor that depends on the probe used and its rotation speed. The method was used on a protein powder extract with a dry matter content of 90–99% (by weight) and was performed one month after the protein extract was dried. The measurement was taken at room temperature. A 13.5% protein (w / w) suspension was prepared. 75 g of sample (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g) were weighed into a 250 mL beaker, and the required amount of demineralized water was weighed into a 1 L plastic beaker, both at room temperature. The powder was suspended in water with mechanical stirring (IKA, EURO-ST.P CV) at 700 rpm for 5 minutes using an 80 cm diameter solvent (commercially sold by Roth, reference A322.1). The pH of the suspension was measured under stirring (WTW pH / Cond 340i / SET pH meter). Stirring was stopped for 3 minutes, and the viscosity of the suspension was measured at three different locations using a Brookfield DVII+Pro viscometer at 50 rpm. The probe used for the measurement was chosen from SO1 to SO7, so that the percentage of twist was between 20% and 80%. The viscosity value was recorded after 4 seconds of probe rotation.The suspension was again subjected to mechanical stirring for 5 minutes at 700 rpm, during which time the pH was adjusted to 6.4 with 3N HCl. Stirring was stopped for 3 minutes, and the viscosity of the suspension was measured in the same manner as before. Similarly, the viscosity of the suspension was measured at pH 6.2, 6.0, and 5.8 after 5 minutes of stirring at 700 rpm and 3 minutes of settling. When the initial pH of the 13.5% protein suspension was equal to or less than 5.8, the pH was raised to pH 7.5 with 3N NaOH, instead of being reduced with 3N HCl. Determination of apparent density and density after settling The bulk density of a powder is the ratio of the mass of an uncompacted powder sample to its volume, including the contribution of the interparticle void volume. The density after settling was obtained by mechanically compacting a graduated cylinder containing the powder sample. Both the bulk density and the density after settling are expressed in grams per milliliter (g / ml). The method was used for protein extract powder, and the measurement was performed at room temperature. 60 g of powder were weighed into a 250 ml graduated cylinder (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g). The volume of powder was measured before stirring. The apparent density was calculated as follows: Apparent density = m / V1 m = mass of protein extract powder (expressed in g) V1 = Volume of powder without settling (expressed in ml) Sixty g of powder were weighed into a 250 ml graduated cylinder (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g). The graduated cylinder was placed in the center of a sedimentation apparatus (Retsch) and shaken for 12 minutes at intensity 60. The volume of powder was measured after shaking. The density after settling was calculated as follows: Density after settling = m / V2 m = mass of protein extract powder (expressed in g) V2 = Volume of settled powder (expressed in ml) Determination of gel strength Gel strength was determined by the maximum resistance of a gel to compression applied by a probe guided by a texture analyzer. Protein gel formation consisted of preparing a protein suspension that was subjected to heat treatment followed by cooling. Gel concentration was expressed in g N. The method was used with a powdered protein extract with a dry matter content of 90–99% (by weight) and was performed one month after the protein extract was dried. Measurements were taken at room temperature. A 13.5% protein (w / w) suspension was prepared. 75 g of sample (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g) were weighed into a 250 mL beaker, and the required amount of demineralized water was weighed into a 1 L plastic beaker, both at room temperature. The powder was suspended in water with mechanical stirring (IKA, EURO-ST.P CV) at 700 rpm for exactly 10 minutes using an 80 cm diameter solvent (commercially sold by Roth under reference A322.1). The pH of the suspension was adjusted to 6.0 with 3N HCl or 3N NaOH according to the initial pH of the suspension (WTW pH / Cond 340 µg / s Et pH meter). The suspension was poured into two 220 ml glass flasks which were placed in a water bath at 80 °C for 1 h. The glass flasks were cooled for 10 minutes in a water bath at room temperature and then placed for 16 hours in a cold room at 4 °C.The glass flasks were placed at room temperature for 15 minutes to bring them to room temperature. Gel strength was measured using a TA-XT2i texture analyzer (Stable Micro Systems, Ltd) with a 5 kg compression load cell and a conical probe (P45C Cone 45° Perspex). Gel strength was the maximum force recorded at the end of the penetration test, expressed in g. TA-XT2i configuration: Measure the force in compression - hold until the moment Pre-test speed: 2 mm / s Test speed: 1 mm / s Post-test speed: 1 mm / s Penetration distance: 35 mm Trigger type: Auto - 3 g Time 10 s Powder flow measurement The rheological behavior of a powder is characterized by measuring its resistance to flow. Flowability was measured using a Brabender microviscoamylograph (MVA). Twenty grams of sample (Ohaus ARC120 balance, sensitivity 0.01 g, capacity 3100 g) were weighed into the measuring vessel of the instrument. The measurement was performed for 5 minutes at 20 °C using a cooling water bath. The vessel's rotation speed was set to 75 rpm and the measurement interval to 70 cmg. The instrument measured the force required to maintain the vessel's rotation speed at 75 rpm. The results correspond to the average of the measurements recorded during the last minute of the test and are expressed in Brabender units (BU). The lower the result, the higher the free-flowing powder. Determination of wettability Wettability is defined as the time in seconds required for all particles of a powder to become wetted when placed on the surface of water. A powder sample is considered wetted when it has sunk below the water's surface or has a wet appearance. One gram of powder sample was weighed into a glass beaker. One hundred milliliters of demineralized water at room temperature were introduced into a 250-milliliter beaker (9 cm high, 7 cm in diameter). The test portion was poured from the glass beaker onto the water's surface. The time was recorded from the start of the powder transfer until all particles were wetted. Results are expressed in seconds. Color measurement The L*a*b* coordinates were measured at 20 °C using a CR5 chromium meter (Konica Minolta TA Sensing, Europe). L* denotes lightness on a scale of 0-100 from black to white; a*, (+) red or (-) green; yb*, (+) yellow or (-) blue. Apparatus: - CR5 chromameter (Konica Minolta TA Sensing Europe). - Petri dish CR-A502 Procedure: Sample preparation - The Petri dish was filled with the sample to be analyzed on a uniform surface. Method The Petri dish was placed in the apparatus in the specifically reserved location and the analysis of the results began. - The L*a*b* values are given by the chromameter (average of 3 measurements). Water activity Water activity is a measure of the energy state of water in a system. It is defined as the vapor pressure of water in a substance divided by that of pure water at the same temperature; therefore, pure distilled water has a water activity of exactly one. The determination of water activity (aw) was performed using a Rotronic Hygroskop DT, Krautli. A cell was filled with the sample to be characterized and placed in the measuring chamber (Rotronic Hygroskop DT, Krautli). After stabilization, the water activity value was recorded. Sensory analysis for proteins in solution Sensory evaluation was conducted by a trained panel of five members. Panelists were trained in the recognition of six characteristics (sweetness, bitterness, metallic taste, salinity, acidity, umami, and astringency). A descriptive analysis based on 4% dispersion was performed. After discussion to reach a consensus, the descriptive terms most relevant to characterizing the appearance, texture, and flavor of the solutions were selected. Sensory analysis for baked goods Sensory evaluation was conducted by a trained panel of five members. The panelists' training focused on recognizing six characteristics: sweetness, bitterness, metallic taste, saltiness, acidity, umami, and astringency. A descriptive analysis of the finished products was performed. After discussion to reach a consensus, the descriptive terms most relevant to characterizing the appearance, texture, and flavor of the products were selected. Oven expansion capacity: The expansion capacity of the cookies was determined by measuring the length and width of 20 cookies with a caliper. The average value was determined and expressed in mm. Cookie hardness: The hardness of the cookies is defined as the force required to break a cookie with a knife. The cookie hardness was assessed using the Ta-XT2i texture analyzer. Apparatus: - TA-XT2i Texture Analyzer (Stable Micro Systems, Ltd) - Compression load cell, 25 kg - Blade set with knife (HDP / BSK) Procedure: - Position the upper limit of the crosshead so that the Warner Bratzler blade is 1 mm above the sample surface - TA-XT2i configuration: Measuring compression force - back to top Pre-test speed: 3 mm / s Test speed: 2 mm / s Speed after the test: 10 mm / s Penetration distance: 5 mm Trigger type: Auto - 3 g The penetration test begins. The results were recorded by the texture analyzer and displayed on a graph. Results The hardness of the biscuit was the maximum force recorded during the test (expressed as "maximum force"). The test results were obtained from 20 samples and the average value was calculated. Cookie crisp: The crispness of the biscuit is defined as the number of peaks recorded during compression of a biscuit by a piston. The crispness texture of the biscuit was evaluated using the Ta-XT2i texture analyzer as described below. Apparatus: - TA-XT2i Texture Analyzer (Stable Micro Systems, Ltd) - Compression load cell, 25 kg - Piston T1 (9 cm long - 0.5 cm in diameter) Procedure: - Position the upper limit of the crosshead so that the piston is 1 mm above the sample surface - TA-XT2i configuration: Measuring compression force - back to top Pre-test speed: 2 mm / s Test speed: 0.1 mm / s Post-test speed: 5 mm / s Penetration distance: 4 mm Trigger type: Auto - 3 g The penetration test begins. The results were recorded by Texture Analyzer and displayed in a graph. Results The crispness of the cookie was measured by the number of peaks recorded during the test (expressed as "crispy"). The test results were obtained from 20 samples and the average value was calculated. Yeast index for sourdough This test evaluates the ability of a bread dough to develop during fermentation: After kneading, the dough was removed from the mixer and left to rest for 10 minutes. Seven small loaves (30 g each) were taken and shaped into small balls by hand. After shaping, they were placed in graduated cylinders. The initial height (Vi) was recorded. The graduated cylinders were placed in a fermentation cabinet at 32 °C / 100% relative humidity for 35 minutes. At the end of the test, the cylinders were removed from the cabinet and the final height after the test (Vf) was recorded. - The fermentation index (LI) was the difference in volume between the beginning and the end of the test: LI = (Vf-Vi) x 3, 14 x r2 (where r is the radius of the graduated cylinder) Bread crumb hardness The hardness of the bread crumb was determined using a texture analyzer (TA XT2i, Stable Micro Systems, UK). Two 12.5 mm thick slices were compressed with a 36 mm diameter stainless steel cylindrical probe, penetrating up to 50% (distance = 6 mm) of their original height at a crosshead speed of 1 mm / s. Apparatus: - TA-XT2i Texture Analyzer (Stable Micro Systems, Ltd) - Compression load cell, 5 kg - P36R probe, diameter, radius, aluminum AACC Procedure: - Position the upper limit of the crosshead so that the probe is 1 mm above the sample surface - TA-XT2i configuration: Measuring compression force - back to top Pre-test speed: 1 mm / s + test speed: 1.7 mm / s Speed after the test: 10 mm / s Penetration distance: 6 mm Trigger type: Auto - 5 g The penetration test begins. The results were recorded by the texture analyzer and displayed on a graph. Results - The hardness of the bread crumb was defined as the strength after 2.21 s (expressed as "bread crumb hardness" in g) - The test results were obtained from 20 samples and the average value was calculated. Bread volume The bread volume was determined by the rapeseed displacement method (AACC Standard 10-05) in five replicates. The average specific volume (volume / weight) was calculated. Hardness of the bars The hardness of the bars was defined as the maximum force recorded during compression of the bars by a piston. The hardness of the bars was evaluated using the Ta-XT2i texture analyzer as described below. Apparatus: - TA-XT2i Texture Analyzer (Stable Micro Systems, Ltd) - Compression load cell, 5 kg - Piston 52 mm long - 5.7 mm in diameter) Procedure: - Position the upper limit of the crosshead so that the piston is 1 mm above the sample surface - TA-XT2i configuration: Measuring compression force - Return to the beginning Pre-test speed: 2 mm / s Test speed: 0.5 mm / s Post-test speed: 5 mm / s Penetration distance: 10 mm Trigger type: Auto - 3 g The penetration test begins. The results were recorded by Texture Analyzer and displayed in a graph. Results - The hardness of the bars was the maximum force recorded during the test (expressed as "hardness of the bars") - The test results were obtained from 12 samples and the average value was calculated. Example 1: Method for extracting pea protein according to an embodiment of the present invention This example was performed following the protocol as schematically represented in Figure 1. Step 1 - Preparation of pea protein concentrates: The dry-harvested peas, referred to herein as "dried peas" (having a dry matter content (based on weight) of approximately 87.7%), were sieved and destoned by passing them through a destoner. Subsequently, the peas were shelled in a sheller. The peas were then fermented with lactic acid bacteria (Lactobacillus fermentum). Up to this point, the peas were soaked intermittently in potable water. The potable water was treated with well water to be safe for human consumption in accordance with European Directive 98 / 83 / EC. In subsequent batches, part of the fermentation medium (aqueous phase excluding peas) from a previous batch was used as an inoculum for further fermentation. The peas were fermented in the presence of 10⁸ CFU of lactic acid bacteria per ml of aqueous composition comprising peas. 400 kg of peas per m³ of the total volume of aqueous composition comprising peas were placed in a container. Fermentation was carried out anaerobically in a closed container without degassing at a temperature of 40 °C, until a pH of 4.2 was reached in the peas.During fermentation, the aqueous phase in the fermentation vessel was recirculated at approximately 20 m³ / hour. The peas were fermented for approximately 540 minutes. At the end of fermentation, the peas had absorbed water equal to approximately their initial mass before fermentation and had a dry matter content of approximately 45% (based on weight). After fermentation, the peas were removed from the fermentation medium. They were then placed in a perforated rotating drum and washed to remove any remaining fermentation medium. After washing, the peas underwent wet milling. During milling, additional potable water was added so that the final composition had a dry matter content of approximately 25% (by weight). During the milling stage, the pH was adjusted to approximately 8.0 by adding sodium hydroxide. After milling, the ground pea paste was subjected to centrifugal decantation. The supernatant containing soluble proteins and impurities (also referred to herein as the aqueous composition comprising pea proteins) had a dry matter content of approximately 4% (by weight). The aqueous composition comprising pea proteins was subsequently subjected to heat treatment at 75 °C for 15 seconds in a plate heat exchanger. Subsequently, the pea proteins were concentrated by isoelectric precipitation. For this purpose, the pH of the aqueous composition comprising pea proteins was adjusted to 4.7 with sulfuric acid. The precipitated / aggregated proteins were separated by centrifugal decantation. The resulting pea protein concentrate was obtained as an aqueous suspension with a dry matter content of approximately 25% (weight-based). Potable water was added to reach a dry matter content of 13% (weight-based). Stage 2 - Preparation of pea protein extracts from the concentrates of stage 1: Next, the pH of the aqueous suspension was adjusted to pH 5.3 with sodium hydroxide. The suspension was then subjected to heat treatment by heating it to approximately 90 °C using a plate heat exchanger and maintaining the aqueous suspension at a temperature of approximately 90 °C for 7 min. Finally, the aqueous suspension was spray-dried. The inlet temperature of the spray dryer was approximately 190 °C and the outlet temperature was approximately 72 °C. Example 2: The effect of acidification and heat treatment on the properties of pea protein extracts Step 1 - Preparation of pea protein concentrates: Dry-harvested peas, referred to herein as "dried peas" (having a dry matter content (based on weight) of approximately 87%), were sieved and destoned by passing them through a destoner. Subsequently, the peas were shelled in a sheller. The peas were then fermented with lactic acid bacteria (Lactobacillus fermentum). Up to this point, the peas were soaked intermittently in potable water. In subsequent batches, part of the fermentation medium (aqueous phase excluding peas) from a previous batch was used as an inoculum for the subsequent fermentation. The peas were fermented in the presence of 10⁸ CFU of lactic acid bacteria per ml of aqueous composition comprising peas. 400 kg of peas per m³ of the total volume of aqueous composition comprising peas were placed in a vessel. Fermentation was carried out anaerobically in a closed, non-degassed vessel at a temperature of 40 °C until a pH of 4.6 was reached in the peas. During fermentation, the aqueous phase in the fermentation vessel was recirculated at approximately 20 m³ / hour. The peas were fermented for a duration of approximately 480 min.At the end of fermentation, the peas had absorbed water in an amount approximately equal to their initial mass before fermentation and had a dry matter content of approximately 47% (based on weight). After fermentation, the peas were removed from the fermentation medium. They were then placed in a perforated rotating drum and washed to remove any remaining fermentation medium. After washing, the peas underwent wet milling. During milling, additional potable water was added so that the final composition had a dry matter content of approximately 27% (by weight). During the milling stage, the pH was adjusted to approximately 8 by adding sodium hydroxide. After milling, the ground pea paste was subjected to centrifugal decantation. The supernatant containing soluble proteins and impurities (also referred to herein as the aqueous composition comprising pea proteins) had a dry matter content of approximately 4.5% (by weight). The aqueous composition comprising pea proteins was subsequently subjected to heat treatment at 75 °C for 15 seconds in a plate heat exchanger. Subsequently, the pea proteins were concentrated by isoelectric precipitation. For this, the pH of the aqueous composition comprising pea proteins was adjusted to 4.7 with sulfuric acid. The precipitated / aggregated proteins were separated by centrifugal decantation. The resulting pea protein concentrate was obtained as an aqueous suspension with a dry matter content of approximately 25% (by weight). Step 2 - Preparation of pea protein extracts from the concentrates of step 1. Different pea protein extracts were prepared from the pea protein concentrate described above. Extract (A) was obtained by adjusting the dry matter content of the aqueous suspension obtained in step 1 to approximately 15% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 7.5; and after heating to a temperature of approximately 98°C, the temperature was held at approximately 95°C for approximately 6.5 minutes; and then the suspension was spray-dried to obtain a powder having a dry matter content of approximately 95% (by weight). Extract (B) was obtained by adjusting the dry matter content of a prepared aqueous suspension as described in step 1 to approximately 12.5% (by weight); and spray-drying said aqueous suspension without pH adjustment (the pH remained at 4.7) and without further heat treatment. The extract (C) was obtained by adjusting the dry matter content of a prepared aqueous suspension as described in step 1 to approximately 12.5% (by weight); followed by heat treatment of the suspension at a temperature of approximately 90°C for approximately 7 minutes without adjusting the pH (the pH remained at 4.5), and then spray-drying the aqueous suspension to obtain powder with a dry matter content of approximately 95% (by weight). Extract (D) was obtained by adjusting the dry matter content of an aqueous suspension prepared as described in step 1 to approximately 12.5% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 5.4; and subsequent heat treatment at a temperature of approximately 90°C for approximately 7 minutes, and then spray-drying the suspension to obtain a powder having a dry matter content of approximately 95% (by weight). The gel strength, density after settling and bulk density, flowability and wettability of the protein extracts (A) to (D) were measured. The results are shown in Table 2. The strength of the gel at pH 6 is represented in Figure 2. Table 2 The nitrogen solubility index (NSI) of each extract as a function of pH is given in Table 3 and shown in Figure 3. Table 3 The measured viscosity for each extract at different pH is given in Table 4 and the viscosity profile is shown in Figure 4. Table 4 Example 3: Characterization of an extract according to an embodiment of the invention Step 1 - Preparation of pea protein concentrates: Dry-harvested peas, referred to herein as "dried peas" (having a dry matter content (based on weight) of approximately 87%), were sieved and destoned by passing them through a destoner. Subsequently, the peas were shelled in a sheller. The peas were then fermented with lactic acid bacteria (Lactobacillus fermentum). Up to this point, the peas were soaked intermittently in potable water. In subsequent batches, part of the fermentation medium (aqueous phase excluding peas) from a previous batch was used as an inoculum for the subsequent fermentation. The peas were fermented in the presence of 10⁸ CFU of lactic acid bacteria per ml of aqueous composition comprising peas. 400 kg of peas per m³ of the total volume of aqueous composition comprising peas were placed in a vessel. Fermentation was carried out anaerobically in a closed, non-degassed vessel at a temperature of approximately 40 °C, until a pH of 4.7 was reached in the peas. During fermentation, the aqueous phase in the fermentation vessel was recirculated at approximately 20 m³ / hour.The peas were fermented for a duration of approximately 430 min. At the end of fermentation, the peas had absorbed water in an amount of approximately their initial mass before fermentation and had a dry matter content of approximately 47% (based on weight). After fermentation, the peas were removed from the fermentation medium. They were then placed in a perforated rotating drum and washed to remove any remaining fermentation medium. After washing, the peas underwent wet milling. During milling, additional potable water was added so that the final composition had a dry matter content of approximately 25% (by weight). During the milling stage, the pH was adjusted to approximately 8 by adding sodium hydroxide. After milling, the ground pea paste was subjected to centrifugal decantation. The supernatant containing soluble proteins and impurities (also referred to herein as the aqueous composition comprising pea proteins) had a dry matter content of approximately 4% (by weight). The aqueous composition comprising pea proteins was subsequently subjected to heat treatment at 75 °C for 15 seconds in a plate heat exchanger. Subsequently, the pea proteins were concentrated by isoelectric precipitation. For this, the pH of the aqueous composition comprising pea proteins was adjusted to 4.8 with sulfuric acid. The separation of the precipitated / aggregated proteins was carried out by centrifugal decantation. The resulting pea protein concentrate was obtained as an aqueous suspension with a dry matter content of approximately 25% (by weight). Step 2-Preparation of pea protein extracts. The extract (E) was obtained by adjusting the dry matter content of the aqueous suspension obtained in step 1 to approximately 16% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 7.4; and subsequent heat treatment at a temperature of approximately 90°C for approximately 7 minutes; then spray-drying the suspension to obtain a powder having a dry matter content of approximately 95% (by weight). Extract the pea protein concentrate (F) prepared according to the invention as described in Example 1. The extract (G) was obtained by adjusting the dry matter content of the aqueous suspension obtained in step 1 to approximately 16% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 6.1; and subsequent heat treatment of the suspension at a temperature of approximately 98°C for approximately 7 minutes; and then by spray drying the suspension to obtain a powder having a dry matter content of approximately 95% (by weight). For each extract, the wettability, flowability, density after settling, and apparent density properties were measured. The results are given in Table 5. Table 5 The color of pea protein extracts E, F, and G was evaluated. The results are shown in Table 6. Table 6 The pH and gel strength at pH 6 were measured for each extract. The results are shown in Table 7. Table 7 The nitrogen solubility index (NSI) of each extract as a function of pH is given in Table 8 and shown in Figure 5. Table 8 The viscosity measured for each extract at different pH is given in Table 9. Table 9 The sensory characteristics of each extract were determined after dispersion in running water at 4% by weight and the results are given in Table 10. Table 10 Example 4: Use of pea proteins according to the invention in the clarification of wines Wine clarification is done to reduce cloudiness and improve brightness and flavor. A positively charged protein solution (pH <pHi) al vino (pH 2, 8 a 4, 0) . En presencia de partículas de vino cargadas negativamente, las cargas eléctricas se neutralizan y los coloides hidrofílicos estables se vuelven inestables, lo que da como resultado su precipitación. Commonly used clarifying agents in wine presentation include gelatin, egg albumin, casein, and vegetable proteins. Clarifying adjuvants such as silica (silicon dioxide) and tannins are also frequently used. Different types of pea proteins were evaluated at two different concentrations (5 g / hl and 10 g / hl) in 12° alcoholic solutions, at pH 3, 2, 4 °C, in the presence of tannins or SiO2. The absorbance of the solutions was measured after standing (from 1 h to 96 h). The procedure was as follows: 1750 g of water (1750 ml) were added to a 2-liter beaker. A volumetric flask was filled with 250 ml of 96% ethanol. The ethanol was added to the water and thoroughly mixed. The pH of the resulting solution was adjusted to 3.2 with 1 M HCl (the weight was recorded). Tannins or silicon dioxide were added to the solution and thoroughly mixed. The solution was covered and allowed to stand for 1 h. Pea proteins were then added, marking the start of the incubation period (t = 0 h). The solution was stored at 4 °C. Sampling: The sampling was performed as follows: A plastic syringe was filled with 30 ml of the solution, taken from the center of the beaker without stirring the solution, and a cuvette for measuring absorbance was filled with the solution. The absorbance at 420 nm was recorded using a spectrometer. The solution was then filtered using a 0.45 µm Whatman filter. The absorbance of the filtrate was measured at 420 nm. Turbidity was measured using the following equation: Turbidity = absorbance before filtration - absorbance after filtration 1. Protein concentrations of 5 and 10 g / hl with tannins as adjuvants Several solutions were prepared. The tannins were used at a concentration of 0.3 ml / l. The White T (also called Control T) was the negative control with tannins (without any clarifying agent). The tannins were a ready-to-use solution: ST Solution from the Institut Oenologique de Champagne consisting of a solution of tannic acid (CAS number: 1401-55-4) and copper sulfate. Perle T was the positive control with tannins (also known as Perle), and also contained as a clarifying agent 0.115 g / hl of Colle Perle (hydrolyzed gelatin from the Institut Oenologique de Champagne). Extracts E and F prepared in Example 3 were used as pea proteins. Solution A comprised the White T solution and the pea protein from extract E. Solution B comprised the White T solution and the pea protein from extract F. The turbidity of the solutions after different incubation times at 4 °C was measured as described above. The results are shown in Table 11 and Figure 7. The turbidity of the solutions after 96 h of incubation is shown in Figure 6. Table 11 2. Protein concentration of 5 g / hl with SiO₂ as an adjuvant SiO2 was used at 0.6 ml / l. Blank S (also known as Control S) was the negative control with SiO2 (without clarifying agents) Perle S was the positive control with SI₂O₂ and contains 0.115 g / hl of Colle Perle (hydrolyzed gelatin provided by the Institut Oenologique de Champagne) Extracts E and F prepared in Example 3 were used as pea proteins. Solution A1 comprised the White S solution and the pea protein from extract E. Solution B1 comprised Blank S and pea protein from extract F. The turbidity of the solutions after an incubation time other than 4 °C was measured as described above. The results are shown in Table 12 and Figure 9. The turbidity of the solutions after 96 h of incubation is shown in Figure 8. Table 12 Effect of adjuvants at a protein concentration of 5 g / hl Table 13 and Figure 10 show the effect of the different adjuvants tested in steps 1 and 2 after 96 h of incubation at 4 °C, compared to solutions containing only the proteins and no adjuvants (none). Pea proteins at 5 g / hl in 12° alcoholic solutions, at pH 3, 2, 4 °C, were prepared as follows: 1750 g of water (= 1750 ml) were added to a 2-liter beaker. A volumetric flask was filled with 250 ml of 96° ethanol. The ethanol was added to the water and mixed thoroughly. The pH of the resulting solution was adjusted to 3.2 with 1 M HCl (the weight was noted). The pea proteins were added. The solution was stored at 4 °C. Table 13 4. Comparison with other pea proteins (without adjuvants) Solution A2 comprised a 12° alcoholic solution and pea protein from extract E. Solution B2 comprised a 12° alcoholic solution and pea protein from extract F. Solution C1 to F1 comprised a 12° alcoholic solution and commercial pea proteins. The different extracts are shown in Table 14. The turbidity of the solutions was measured after different incubation times. The effect on turbidity is shown in Table 15 and Figure 11. Table 14 Table 15 Example 5: Food products comprising pea proteins according to the invention The inclusion of pea protein in various food products was evaluated. 1. Cookies Cookie doughs were prepared. Extract E (not according to the invention) and Extract F (according to the invention), as prepared in Example 3, were used as pea proteins. Tests were performed to evaluate the pH of the cookie dough prepared with Extract E, and / or to modify the pH of the dough prepared with Extract F and different acidity regulators and raising agents. 1a) The dough was prepared as shown in Table 16 Table 16 An analysis of the mass is given in Table 17. Table 17 1b) The dough was prepared as shown in Table 18. A dough was prepared (Table 18) in which the amount of water added to the dough prepared with extract F was reduced. An optimal water reduction of 3% was found, resulting in a dough with excellent texture and lamination capacity. For the dough prepared with extract E, it was found that it was not possible to reduce the water content as the dough became too hard. Table 18 An analysis of the mass is given in Table 19 The cookies were prepared using the dough from trials 3 and 4. They were baked in an Eloma Backmaster oven at 150 °C for 20 minutes and cooled to room temperature before packaging. Table 20 shows an analysis of cookies prepared with the respective doughs from trial 3 (cookie A) and trial 4 (cookie B). Table 20 2. Protein-enriched bread The loaves were prepared using either pea protein extract G as prepared in Example 3, or pea protein extract F. The loaf recipes are provided in Table 21. In addition to identical doughs prepared with the pea proteins according to the invention (extract F) and the pea proteins not according to the invention (G), several adaptations were made (reduction of water content by 5% for F with or without adjustment of pH of the dough; as well as decrease of water content for G). Table 21 The mixer used was a spiral mixer (Vema QR24 type). After kneading, the dough was removed from the mixer and left to rest for 10 minutes. The dough was divided into 500g rolls, which were shaped in the first round and then elongated by hand. The bread was placed in pre-greased metal tins and stored for 1 hour and 15 minutes in a controlled fermentation cabinet (32°C). Oven: The bread was baked at 200°C for 60 minutes in a deck oven (Salva Modular). 20 minutes before the end of baking, the steam vent was opened. The bread was then cooled to room temperature and packaged in appropriate packaging. The dough was prepared according to the recipes above in Table 21 and evaluated as shown in Table 22. Table 22 It was observed that the dough prepared with pea protein extract F, when the water content was reduced, was less sticky, had good elasticity, and was easier to work with. For the dough prepared with extract G, it was not possible to reduce the water content by more than 2%; otherwise, the dough became too stiff. The fermentation index of the dough was measured. Table 23 and Figure 12 show the fermentation index for the respective doughs. Table 23 The quality of the prepared bread was evaluated. The results are shown in Table 24. Measurements of bread volume and bread crumb hardness are shown in Figures 13 and 14, respectively. Table 24 3. Dulce de leche bars The dulce de leche bars were prepared using extracts E and F as prepared in Example 3. The dulce de leche bar recipes are shown in Table 25. Table 25 The process for preparing the bars was as follows - Melt the fat at 45°C in a water bath - Mix the syrups and add the fat - Mix the powders in a Hobart - Add the syrups and stir for a few minutes until you obtain a homogeneous paste The dough was placed in a plastic bag and spread out, then left to rest overnight. - Cut the bars and cover them with chocolate It has been observed that the mixture (B) containing extract F according to the invention takes less time to homogenize than the mixture (A), approximately 2 minutes less. The pH, Aw (water activity) and hardness of the respective dulce de leche bars over time (months) were measured and the results are illustrated respectively in Tables 26, 27 and 28. The hardness of the dulce de leche bar was also measured and the results are shown in Figure 15. Table 26 Table 27 Table 28 The sensory analysis of the respective dulce de leche bars is illustrated in Table 29. Table 29 Example 6: Characterization of an extract according to an embodiment of the invention (without fermentation step) Step 1 - Preparation of pea protein concentrates: Dry-harvested peas, referred to herein as "dried peas" (having a dry matter content (based on weight) of approximately 87%), were sieved and destoned by passing them through a destoner. Subsequently, the peas were shelled in a sheller. The peas were dry-milled to obtain pea flour. Potable water was added to the pea flour so that the final composition had a dry matter content of approximately 25% (by weight). Subsequently, the pH was adjusted to approximately 8 by the addition of sodium hydroxide. After pH adjustment, the pea paste was subjected to centrifugal decantation. The supernatant containing soluble proteins and impurities (also referred to herein as the aqueous composition comprising pea proteins) had a dry matter content of approximately 4% (by weight). The aqueous composition comprising pea proteins was subsequently subjected to heat treatment at 75 °C for 15 seconds in a plate heat exchanger. Subsequently, the pea proteins were concentrated by isoelectric precipitation. For this, the pH of the aqueous composition comprising pea proteins was adjusted to 4.8 with sulfuric acid. The precipitated / aggregated proteins were separated by centrifugal decantation. The resulting pea protein concentrate was obtained as an aqueous suspension with a dry matter content of approximately 25% (by weight). Stage 2 - Preparation of pea protein extracts from the concentrates of stage 1: The extract (H) was obtained by adjusting the dry matter content of the aqueous suspension obtained in step 1 to approximately 18% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 5.4; and subsequent heat treatment at a temperature of approximately 85°C for approximately 7 minutes; then spray-drying the suspension to obtain a powder having a dry matter content of approximately 95% (by weight). Extract (I) was obtained by adjusting the dry matter content of the aqueous suspension obtained in step 1 from approximately 17% (by weight) after the addition of water; followed by adjusting the pH of the suspension with sodium hydroxide to achieve a pH of approximately 5.4; and subsequent heat treatment was performed by direct steam injection at a temperature of approximately 140 °C for approximately 4 seconds; and then spray-drying the suspension at 90 °C to obtain a powder having a dry matter content of approximately 96% (by weight). The gel strength, density after settling and bulk density, flowability and wettability of the protein extracts (H) and (I) were measured. The results are shown in Table 30. Table 30 The nitrogen solubility index (NSI) of both extracts as a function of pH is shown in Table 31 and is shown in Figure 16. Table 31 The viscosity measured for both extracts at different pH is given in Table 32. Table 32 Example 7: Comparative studies of peas fermented with different strains of Lactobacillus (Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus Crispatus LMG 12005 or Lactobacillus Acidophilus LMG 8151) The dry-harvested peas, referred to herein as "dried peas" (having a dry matter content (based on the total weight of dried peas) of approximately 87%), were sieved and destoned by passing them through a destoner. Subsequently, the peas were shelled in a sheller. The peas were then fermented with lactic acid bacteria (Lactobacillus fermentum LMG 6902, Lactobacillus fermentum LMG 18026, Lactobacillus crispatus LMG 12005, or Lactobacillus acidophilus LMG 8151). 2000 g of peas were soaked in 3663 g of sterilized demineralized water at 40 °C in a container. The fermentation medium, comprising the aforementioned bacterial strains, was added simultaneously. The container was placed in a thermostatically controlled water bath, and a pump was added to recirculate the aqueous phase at approximately 250 ml / min. For Lactobacillus fermentum LMG 6902 and Lactobacillus fermentum LMG 18026 (both obtained from BCCM / lMG Laboratorium voor Microbiologie, Universiteit Gent (UGent) Belgium), the fermentation medium was prepared as described in the procedure provided by the BCCM (F109C Revival of lyophilized cultures; recommended medium 66). Then 37 ml of the fermentation medium were added to the container. For Lactobacillus crispatus LMG 12005 (50 Bn) and Lactobacillus Acidophilus LMG 8151 (100 Bn) (both obtained from THT sa Gembloux, Belgium), the fermentation medium was prepared by putting 37 g of Lactobacillus flakes directly into the container. The peas were fermented in the presence of approximately 10⁸ CFU of lactic acid bacteria per ml of aqueous composition comprising peas. The fermentation was carried out in a closed container without degassing at a temperature of approximately 40 °C. Figures 17-20 illustrate respectively the evolution of sugar content, pH, acidity and lactic acid bacteria concentration as a function of fermentation time.
Claims
1. A method for extracting pea proteins, comprising the steps of: (a) providing an aqueous composition comprising pea proteins; (b) isolating said pea proteins from said aqueous composition comprising pea proteins; (c) obtaining said isolated pea proteins as an aqueous suspension having a pH in the range of 4.0 to 5.8; and (d) subjecting said aqueous suspension having a pH in the range of 4.0 to 5.8 to a temperature in the range of 75°C to 210°C; wherein step (b) comprises adjusting the pH of said aqueous composition comprising pea proteins to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.5; wherein step (d) comprises subjecting said precipitated pea proteins to heat treatment at a temperature in the range of 115 °C to 210 °C for a time in the range of 15 s 0,01 s; at a temperature in the range of 95 °C to 115 °C for a time in the range of 5 min to 15 s; at a temperature in the range of 75 °C to 95 °C for a time in the range of 15 min to 5 min; at a temperature in the range of 75 °C to 110 °C for a time in the range of 10 min to 2 min; at a temperature in the range of 80 °C to 100 °C for a time in the range of 8 min to 5 min; or at a temperature in the range of 130 °C to 150 °C for a time in the range of 8 to 1 s.
2. The method according to claim 1, wherein isolating pea proteins from said aqueous composition of step (b), comprises concentrating said pea proteins.
3. The method according to claim 1 or 2, wherein step (b) comprises at least one step of precipitation, flocculation, filtration and / or chromatography.
4. The method according to any one of claims 1 to 3,wherein step (b) comprises isoelectric precipitation.
5. The method according to any one of claims 1 to 4, wherein step (c) comprises adjusting or maintaining the pH of the aqueous suspension to a value in the range of 4.0 to 5.8, preferably in the range of 4.5 to 5.
5.
6. The method according to any one of claims 1 to 5, wherein said aqueous composition comprising pea proteins in step (a) has a pH of at least 6, preferably in the range of 6.0 to 9.0, preferably in the range of 6.5 to 8.
5.
7. The method according to any one of claims 1 to 6, wherein prior to step (a) an aqueous composition comprising peas is subjected to fermentation in the presence of lactic acid bacteria.
8. The method according to claim 7,wherein said fermentation is carried out in the presence of one or more Lactobacillus sp.
9. The method according to any one of claims 1 to 8, wherein before or during step (b) said aqueous composition comprising pea proteins, or said pea proteins are subjected to heat treatment, preferably pasteurization; said protein-comprising fraction is subjected to a temperature of at least 30 °C, for example, at least 40 °C, for example, at least 50 °C, for example, said protein-comprising fraction is subjected to a temperature in the range of 30 °C to 90 °C, more preferably in the range of 50 °C to 80 °C, even more preferably in the range of 55 °C to 75 °C.
10. Pea protein extract obtainable by the method according to any one of claims 1 to 9.
11. Pea protein composition comprising at least 60% by weight of protein based on the total dry matter of the composition,wherein said pea protein composition has a nitrogen solubility index at pH 7.0 of at most 15%, as measured in an aqueous composition comprising 3% by weight of said pea protein composition based on the total weight of the aqueous composition.
12. Pea protein composition according to claim 11, wherein said composition has a pH in the range of 4.0 to 5.8, as measured at room temperature in 10 g of pea protein composition suspended in 90 g of water.
13. Use of the pea protein extract according to claim 10 or the pea protein composition according to claim 11 or 12 in food or feed products, preferably in bakery and confectionery products, or for clarifying liquids.