Pea proteins having a milky flavor

Abstract

The present invention relates to pea proteins having a milky aromatic profile, to a method for producing said pea proteins, and to the use of said proteins for producing food or beverage products, in particular plant-based alternatives to milk.

Description

Description Title: PEA PROTEINS WITH A MILKY FLAVOR Field of invention

[0001] The invention relates to novel pea proteins with a milky aromatic universe. Another subject of the invention relates to a method for manufacturing these pea proteins. The invention also relates to the use of said proteins for the manufacture of food products. Prior art

[0002] Daily protein requirements are generally between 12 and 20% of the diet. These proteins are provided by both animal products (meat, fish, eggs, dairy products) and plant foods (cereals, legumes, algae).

[0003] In industrialized countries, protein intake is still predominantly in the form of animal protein. These proteins have good nutritional and functional properties that allow them to be used in a wide variety of food products.

[0004] However, numerous studies show that excessive consumption of animal proteins at the expense of plant proteins is one of the causes of increased cancers and cardiovascular diseases. Furthermore, animal proteins have many disadvantages, both in terms of their allergenicity (particularly proteins from milk or eggs), and on an environmental level linked to the harmful effects of intensive farming.

[0005] Thus, there is a growing demand from manufacturers for proteins of plant origin with interesting nutritional and functional properties, without presenting the disadvantages of proteins of animal origin.

[0006] Since the 1970s, the pea has been the most widely grown grain legume in Europe, and mainly in France, particularly as a protein resource for animal and human food. Peas contain approximately 27% protein by weight. The term "pea" is here considered in its broadest sense and includes in particular all wild varieties of "smooth pea" and all mutant varieties of "smooth pea" and "wrinkled pea", regardless of the uses for which said varieties are generally intended (human food, animal nutrition and / or other uses). The protein of Pea protein, mainly pea globulin, has been extracted and used industrially for many years. An example of a pea protein extraction process is patent EP1400537. In this process, the seed is ground in the absence of water (known as "dry grinding") to obtain a flour. This flour is then suspended in water at room temperature in order to proceed with the various stages of protein extraction.

[0007] Despite its undeniable qualities, pea protein suffers, compared to other proteins, from undesirable aromatic notes that can limit its use in certain applications. Moreover, while many plant-based alternatives to milk have been developed in recent years, for example from soy, but also rice or oats, plant-based alternatives to milk made from peas have so far met with little commercial success.

[0008] These aromatic notes are very specific to the pea source and distinct from other plant sources. In particular, one of the main aromatic notes that is generally found in many proteins on the market is of the "pea" type ("pea" or "beany"). This aromatic note is an undeniable obstacle in many applications, particularly food applications. Following numerous studies, it has been highlighted that one of the main causes of this unwanted pea aromatic note comes from the synthesis of volatile aldehydes and / or ketones (in particular hexanal), resulting from the action of an internal lipoxygenase on the lipids present in the pea seed, in particular during protein extraction. Saponins and 3-alkyl-2-methoxypyrazines are also categories of compounds generating these unwanted flavors ("Flavor aspects of pulse Ingredients", Wibke SU Roland, 2017). The article by Gao et al.“Effect of alkaline extraction pH on structure properties, solubility, and beany flavor of yellow pea protein isolate, Food Research International, May 2020, 131(4)” also concludes a correlation between lipoxygenase inhibition and a reduction in volatiles.

[0009] Furthermore, the protein extracted from peas also very often has a marked bitter aftertaste (or “off-note”).

[0010] Thus, to improve the taste of vegetable proteins, a well-known solution for a long time is to reduce the lipid content by the use of organic solvents, in order to consequently limit the generation of the volatiles indicated above, the use of organic solvent being able to be done on the flour or on the protein obtained directly. In this respect, we can cite application WO2021174226 which illustrates this technique. However, this document does not describe a pea protein having a milky aromatic note.

[0011] Those skilled in the art have developed several other solutions for improving the aroma of pea proteins, in particular to give them a neutral taste. A first solution is based on masking the flavor by adding compounds selected for this purpose: this solution requires the user to introduce into their formulation a compound that they did not necessarily want to introduce and also requires its labeling on the ingredient.

[0012] Another solution is described in patents US4022919 which teaches that treating pea flour with water vapor allows the production of flour with improved flavor. However, this process can be criticized for the risk of a modification of the functional qualities of the proteins obtained by thermal denaturation (for example, loss of solubility or increase in its hydration capacity) and gelation of the starch included in the flour. Here again, the document makes no mention of a milky note.

[0013] Other solutions have been explored, including, but not limited to, the selection of pea cultivars with less lipoxygenase or the pre-germination of peas prior to protein extraction.

[0014] The use of long-term soaking of peas before grinding and extraction of the protein has also been described. For example, patent application WO2015071499 teaches a process comprising soaking for several hours with lactic acid bacteria at 40°C. However, these solutions are not yet satisfactory. This long, complex process, which consumes a large amount of water due to lactic fermentation, does not yet allow the production of a pea protein with a completely neutral flavor (see Table 10 where the odor and / or taste of peas are noted in each extract) nor the production of a milky aromatic note.

[0015] We can mention patent application WO2017 / 120597 which describes a process including precipitation of the pea protein by adding salts, several washes, and recovery by centrifugation. Despite a complex process using large quantities of water (up to 30 times the quantity of peas), the "pea" and "bitter" flavors are still present in the pea protein (see graphs 18A, B and C). Here again, this document is completely silent regarding a milky aromatic note of the pea protein. Furthermore, when formulating a plant-based alternative to milk, the formulation of the finished product may also include several flavorings. However, there is an interest in being able to do without these flavorings for reasons of simplicity in the labeling of this finished product. Furthermore, these flavorings can be expensive. Finally, these flavorings can be difficult to dose to achieve the desired result.

[0016] The Applicant has also explored many other strategies to improve the taste of legume proteins, including pea. For example, documents WO2020 / 260841 and WO2020 / 240144 may be cited, which describe the manufacture of pea protein with an improved taste. In these documents, no milky note is mentioned for the taste of the pea proteins manufactured. Also, document WO2019 / 053387 in the name of the Applicant describes a process for manufacturing pea proteins with a reduced pea aromatic note, said process comprising blanching the seeds between 70 and 90°C for 2 to 4 minutes before cooling, grinding these seeds and then extracting the pea protein. This document does not describe the manufacture of pea protein with a milky aromatic note: while this aromatic note was presented (among other notes) to the panel, the latter did not retain it to characterize the taste of the protein.

[0017] The use of enzymes that modify the primary structure of the protein, such as glutaminases or proteases, can also modify the organoleptic properties of the proteins, including their taste; processes for producing modified pea proteins using such enzymes have already been described. For example, US2021 / 0401022 A1, which describes such a process, can be cited. The milky note is mentioned in Table 2 of the sensory evaluation. In addition to the fact that the pea protein obtained is modified in its primary structure, another disadvantage of using an enzyme such as glutaminase is that it transforms glutamine and produces ammonia, which consequently reduces the amount of protein nitrogen in the pea protein.

[0018] Thus, while it appears that research exists to reduce the pea taste and bitter aftertaste of the protein, or even to try to achieve a protein with the most neutral taste possible, it must be noted that none of the documents cited above have sought (and succeeded) in providing pea proteins with a milky aromatic universe while retaining the unmodified pea protein and without adding additional flavoring. Furthermore, this is also confirmed by the fact that pea proteins on the market do not have a milky aromatic universe, as demonstrated in the Examples section.

[0019] According to the present application, the term "aromatic universe" means all the aromatic descriptors determined by a trained tasting panel, which represent the aromatic profile of a product. A milky aromatic universe means that the milky note has been identified by the tasting panel among the first 3 main aromatic notes, or even as the first or second aromatic note, when the protein is tasted after suspension in water. A milky note means an aromatic note linked to milk and / or yogurt.

[0020] However, there is a need for such proteins which can be advantageously used, for example, in plant-based alternatives to milk, in order to obtain more milky organoleptic properties.

[0021] The Applicant has thus arrived, after much research, at a new manufacturing process making it possible to provide pea proteins with a very reduced pea aromatic note, a very low bitterness and also having a milky aromatic universe, and this without adding any flavoring. This is obviously an advantage for the manufacture of products such as plant-based alternatives to milk made from peas. Furthermore, as the aromatic universe of the pea protein thus obtained is unique, even in food products other than plant-based alternatives, its use can make it possible to modify the taste and flavor of the final products using pea proteins in their composition. According to a variant, the Applicant has also succeeded in obtaining new pea proteins allowing excellent texturing when used in extrusion, in particular in wet extrusion.These pea proteins are particularly advantageous for the production of meat or fish analogues. Summary of the invention

[0022] Thus, the subject of the invention is a process for manufacturing pea protein comprising the following steps: a) introduction of peas or ground peas into an aqueous solution whose temperature is between 65°C and 90°C in order to obtain a water-pea suspension or a water-ground pea suspension; b) heat treatment of the suspension obtained during step a) at a temperature between 40°C and 65°C for 1 to 10 min; c) in the case where it is a water-pea suspension, wet grinding of the water-pea suspension obtained in step b) in order to obtain an aqueous suspension of ground peas; d) extraction of a protein fraction by solid-liquid separation of the aqueous pea suspension obtained in step b) or c); e) optionally adjustment to a pH between 2.0 and 8.0, for example between 4.5 and 5.7, of said protein fraction obtained in step d);f) heat treatment of the protein fraction obtained in step e) at a temperature ranging from 65 to 90°C for a time ranging from 1 to 120 seconds to form a suspension of coagulated pea proteins; g) solid-liquid separation of the suspension of coagulated proteins obtained in step f) to form the pea protein.;

[0023] Advantageously, the extraction step d) is preceded by a step dO) of cooling the suspension is cooled to a temperature below 15°C, preferably to a temperature of 4 to 14°C, for example 10 to 12°C.

[0024] Advantageously, the cooling step dO) is carried out by passing the aqueous suspension of ground peas through a heat exchanger.

[0025] Advantageously, the method comprises, following the heat treatment step f), a cooling step f1) by rapid cooling of the suspension of coagulated proteins.

[0026] Advantageously, the method comprises a step of adjusting the pH of the pea protein to a pH of between 6 and 7.5, preferably between 6.5 and 7.5.

[0027] Advantageously, the method comprises an additional heat treatment step of the pea protein.

[0028] Advantageously, the method comprises a step of shearing the pea protein, for example by passing it through a high-pressure pump.

[0029] Advantageously, the process comprises a step of homogenization of the pea protein.

[0030] Advantageously, the process comprises a step of drying the pea protein.

[0031] Advantageously, the pH of the aqueous solution from step a) is adjusted between 8 and 10.

[0032] Advantageously, the duration of the heat treatment of the protein fraction is between 1 and 45 seconds, preferably between 1 and 10 seconds.

[0033] Advantageously, the ground peas from step a) are obtained by dry grinding.

[0034] Advantageously, a fraction rich in pea starch and / or a fraction rich in pea fiber is recovered from the insoluble part resulting from the solid-liquid separation step d).

[0035] Another subject of the invention relates to the pea protein obtainable by the process of the invention.

[0036] Advantageously, the pea protein is characterized in that at least one of its first three GATA descriptors determined according to ISO 5492:2008(en), 4.23 is a milk descriptor. This pea protein may have low bitterness, a reduced pea aromatic note and in addition a milky aromatic universe. Without being linked to a any theory, the applicant hypothesizes that this milky aromatic universe is explained by the presence of volatile compounds in the pea protein of the invention which are in different quantities and / or proportions than those of the pea proteins already known, some volatiles being able to be generated, some others reduced or even eliminated thanks to the steps of the process of the invention, in particular the combination of the heat treatment steps. This is all the more remarkable since the process does not require the use of organic solvents or the use of enzymes and that the pea proteins can also have excellent functional properties, such as high solubility and / or gelling power.

[0037] Another subject of the invention also relates to the use of said pea protein for the manufacture of food or beverage products, in particular plant-based alternatives to milk. Detailed brief of the invention

[0038] The invention relates to a method of manufacturing pea protein.

[0039] Step a)

[0040] Step a) comprises the introduction of peas into an aqueous solution. The peas used in step a) may have previously undergone steps well known to those skilled in the art, such as in particular cleaning (removal of unwanted particles such as stones, dead insects, soil residues, etc.) or even the removal of the external fibers of the pea (cellulosic outer shell) by a well-known step called dehulling. Thus, by "peas" in step a), we mean whole peas or pea cotyledons, the outer shell of which has been preferentially removed. Alternatively, ground peas (i.e. pea flour) may be used, these ground peas generally being obtained by dry grinding. Previously, the unhulled pea, the hulled pea or even the pea cotyledons can be subjected to a toasting step, that is to say a dry heat treatment of the legume seeds.This dry heat treatment may be that of application W02020 / 260841.

[0041] The aqueous solution may be water which may optionally include additives such as anti-foam or bacteriostatic compounds.

[0042] The weight ratio of quantity of peas / quantity of aqueous solution in step a) may in particular be between 0.5 and 2.

[0043] The temperature of the aqueous solution is between 65°C and 90°C. Heating can be carried out using any installation well known to those skilled in the art. such as an immersed heat exchanger. Preferably, the temperature is between 70°C and 80°C or even around 75°C.

[0044] The water-pea suspension or the water-crushed pea suspension is obtained by introducing the pea or crushed peas into the previously heated aqueous solution.

[0045] According to one variant, the pH of the aqueous solution from step a) is adjusted to between 8 and 10. This adjustment can be made by adding a base such as soda, lime or potash, preferably soda. According to another variant, the pH is not adjusted at this step.

[0046] Step b)

[0047] The method further comprises a heat treatment b) of the suspension obtained in step a) at a temperature between 40°C and 65°C for 1 to 10 minutes. The suspension may be heated or cooled to reach this temperature. Alternatively, the suspension does not undergo any heating and is directly at temperature when mixing the aqueous suspension with the peas or ground peas. Preferably, the temperature of the heat treatment is between 40 and 60°C, or even between 45 and 55°C. Preferably, the heat treatment is carried out for 2 to 4 min.

[0048] Step c)

[0049] In the case where peas are used in step a), the method comprises a step c) of wet grinding of the water-pea suspension treated in step b) in order to obtain an aqueous suspension of ground peas. Preferably, the method is carried out using peas and the wet grinding step c) is carried out by continuous passage through one or more grinders to obtain the aqueous suspension of ground peas. The grinder(s) may be any type of grinder capable of carrying out wet grinding, such as wet ball mills, conical wet mills, helical wet mills or wet grinders equipped with rotor / stator systems. According to a variant, the grinder may be the one used in the examples of document WO2019 / 053387 in the name of the Applicant. In the variant where the grinder is of the rotor-stator type, this type of grinder may allow continuous grinding by passing the water-pea suspension through said grinder.According to a preferred sub-variant, the method combines two cutting steps (pre-cutting then cutting) using different rotor-stator grinders for each of these cuts. The pre-cutting then the cutting can be carried out one after the other or, alternatively, the cutting can take place after pre-cutting then storage of the treated water-pea suspension. Such grinders are described in document WO2019 / 158589. Optionally, it is possible to carry out during this step or at the end of this step a dilution with water in order to form the aqueous pea suspension. ground. Alternatively, during grinding, water is added continuously or discontinuously to dilute the aqueous suspension. Generally, the dry matter of the aqueous suspension of ground peas ranges from 10 to 30%, for example from 15 to 25%.

[0050] Step d)

[0051] Step d) of the method consists of extracting the components of the aqueous suspension of ground peas, and in particular extracting a protein fraction by solid-liquid separation of the aqueous suspension of peas. According to a variant, before carrying out the solid-liquid separation step, a pH adjustment step of the aqueous suspension of ground peas can be carried out. Thus, the solid-liquid separation can take place after adjusting the aqueous suspension of peas to a pH ranging from 6 to 9, preferably from 8 to 9, most preferably from 8.5 to 9. This pH adjustment step can be carried out in a stirred tank. This step can be more or less long, and last for example from 1 to 240 minutes, generally from 5 to 60 minutes. To carry out the pH adjustment, it is possible to add any type of acid and / or base, organic or inorganic, or mixtures thereof.Examples of acids include hydrochloric acid, sulfuric acid, citric acid, or mixtures thereof. Examples of bases include sodium hydroxide, potassium hydroxide, or lime, and mixtures thereof. This addition of base or acid, as well as the pH measurement, can be done online. The base and / or acid can be in the form of aqueous solutions. Advantageously, before this solid-liquid separation, and preferably before the extraction step d), or even most preferably before the extraction step d) and after the heat treatment step b) or the possible wet grinding step c), the aqueous suspension of ground peas is cooled to a temperature below 15°C. This temperature can in particular range from 4 to 14°C, for example from 10 to 12°C. This cooling step (dO) can be carried out by known techniques, such as passing the aqueous suspension of ground peas through a heat exchanger.

[0052] Generally, the protein fraction is the soluble part of the aqueous suspension and the fraction rich in starch and fibers is the insoluble part. It is also possible to separate more than two insoluble fractions, and for example to recover a first insoluble fraction richer in starch and a second insoluble fraction richer in fibers. Thus, according to a variant of the method, a fraction rich in starch and / or a fraction rich in fiber is recovered from the insoluble part resulting from the solid-liquid separation step d). By fraction rich in starch and fraction rich in fiber, is generally meant a fraction comprising at least 50% starch or fibers. The methods for quantifying starch and fibers are known to those skilled in the art and specific methods are indicated later in the description. These fractions are recovered conventionally by known separation methods. The solid-liquid separation can in particular be carried out by means of at least one separation step with a decanter, in particular a centrifugal decanter, a centrifuge or even with hydrocyclones. The method can also make it possible to recover one or more fractions enriched in fibers and / or starch, which are eliminated from the suspension, and to recover the useful protein fraction following the method of the invention.

[0053] Step e)

[0054] The method also optionally comprises a step e) of adjusting said protein fraction to the pH, which may optionally be the isoelectric pH of the protein. Isoelectric pH means a pH close to which the net electrical charge of the protein in the protein fraction is zero. This pH may be adjusted to a pH between 2.0 and 8.0, for example between 4.5 and 5.7, or even between 4.8 and 5.2. The pH rectification may be carried out by adding acid, organic or inorganic, for example hydrochloric acid, sulfuric acid or citric acid or mixtures thereof. This step e) may be carried out in a tank, stirred or not. It may be more or less long, and last for example from 1 to 240 minutes, generally from 5 to 60 minutes. This addition of base or acid as well as the pH measurement may be carried out online and the acid may be in the form of an aqueous solution.

[0055] Step f)

[0056] The method also comprises a heat treatment step f) of the protein fraction at the optionally adjusted pH. This step comprises a stage of heating the coagulated protein suspension. This stage is carried out at a temperature ranging from 65 to 90°C to form a coagulated protein suspension. It can be carried out for a duration ranging from 1 to 120 seconds, preferably from 1 to 45 seconds, most preferably from 1 to 10 seconds. To carry out this heating, a heat exchanger is generally used. It can be of the type according to the indirect heating principle or according to the direct heating principle, generally by steam injection. Preferably, the heating is carried out by steam injection. Advantageously, the heat treatment step f) comprises a heating stage followed by a cooling stage of the coagulated protein suspension.In the variant where the heat treatment step f) comprises, following the stage of heating the suspension of coagulated proteins, a stage of cooling said suspension, this cooling stage is preferably obtained by rapid cooling known as "flash-cooling", leading to immediate cooling. At the end of this stage, the temperature can range from 60 to 75°C, for example between 64 and 70°C. This rapid cooling is carried out. by applying a vacuum to the coagulated protein suspension, the vacuum applied being determined according to the chosen cooling temperature.

[0057] The Applicant considers that essential steps in the process of the invention are the first heat treatment steps b) and f). Without being bound by any theory, one hypothesis is that the pea protein could comprise volatile compounds in certain proportions leading to providing it with a milky aromatic universe. It is likely that it is these first heat treatment steps b) and f), at particular temperatures, which generate this particular aromatic profile, different from that of the pea proteins already known. It is possible that these steps could lead to a higher concentration of certain volatile compounds and, conversely, a lower concentration of certain other volatile compounds, compared to the pea proteins already known. The whole would make it possible to give this milky aromatic universe, without needing to modify, for example, the primary structure of the protein.

[0058] Step g)

[0059] In the remainder of the process of the invention, the pea protein is separated from the coagulated protein suspension in step g). This solid-liquid separation can be carried out using the means indicated for the separation means indicated in step e). The pea protein formed during this step mainly comprises the proteins of the solid fraction which are separated from the liquid fraction. In the liquid fraction are generally found other proteins soluble at isoelectric pH, albumins but also soluble carbohydrates. The recovered solid fraction comprises the pea protein and is generally a concentrated aqueous suspension of pea protein. The recovered solid fraction has a dry matter which generally ranges from 25 to 50%, or from 30 to 40%.The mass composition of pea protein can vary and will generally include mainly proteins (especially in the form of globulins) but also starch, lipids, fibers, and / or sugars. This solid fraction can be diluted by adding water to make it easier to handle in the following optional steps.

[0060] Other steps

[0061] At the end of this step g), the process generally comprises a step g') of adjusting the pH of the pea protein to a pH ranging from 6 to 7.5, generally from 6.5 to 7.5. This step can be carried out by adding an inorganic or organic base, for example by adding sodium hydroxide. The pH is generally raised by adding a basic aqueous solution.

[0062] Preferably, the method comprises an additional heat treatment step of the pea protein. The temperature and time conditions can vary widely in this step, for example ranging from 70 to 140°C and lasting from 0.1 seconds to several minutes. According to a first variant of this additional heat treatment step, the temperature ranges from 70 to 90°C and its duration ranges from 0.1 seconds to 30 minutes. According to a second variant of this additional heat treatment step, the temperature ranges from 90 to 110°C and its duration ranges from 0.1 seconds to 5 minutes. According to another variant, this additional heat treatment step is carried out at a temperature ranging from 110 to 140°C for a time ranging from 0.1 to 30 seconds, preferably from 0.2 to 15 seconds, for example from 0.3 to 10 seconds. This step may have the objective of functionalizing and / or sanitizing the pea protein.To carry out this additional heat treatment step, the pea protein may be in the form of an aqueous dispersion, preferably having a dry matter content ranging from 10 to 25%, for example from 15 to 20%. Advantageously, the method of the invention comprises, following the additional heat treatment step, a cooling step f1) of the pea protein. According to a preferred variant, this cooling step is obtained by rapid cooling ("flash-cooling"). At the end of this step, the temperature may range from 60 to 100°C, for example between 70 and 90°C. In the same way, this rapid cooling step ("flash-cooling") is carried out by applying a vacuum to the aqueous dispersion of pea protein, the vacuum applied being determined according to the chosen cooling temperature.

[0063] Regarding the functionalities of the pea protein, they can be modified by the heat treatment. They are particularly likely to be impacted by the choice of the pH of the composition which is subjected to the additional heat treatment. For example, when the aqueous dispersion of pea protein has a neutral pH during the heat treatment, the solubility of the pea protein obtained after this heat treatment is higher than that of a pea protein heat-treated at a slightly lower pH. In the same way, when the aqueous dispersion of pea protein has a neutral pH during the heat treatment, the gelling power of the pea protein obtained after this heat treatment may be lower than that of a pea protein heat-treated at a slightly lower pH. This is reflected in the examples section below.

[0064] According to a variant of the process, it comprises a step of shearing the pea protein, for example by passing the aqueous dispersion of proteins through a high-pressure pump. As an example of a high-pressure pump, we can cite the high-pressure pumps marketed by the company Silverson, also called high-pressure mixers. shearing (“high shear mixer”), for example those of the UHS range. Preferably, the shearing step is carried out by a high pressure pump.

[0065] The shearing step can take place before or after the heat treatment and / or pH raising steps.

[0066] According to another variant, the method comprises a step of homogenizing the pea protein.

[0067] To carry out this homogenization step, any type of homogenizer can be used. According to the invention, it is understood to mean equipment comprising a high-pressure pump and a homogenization head in which the equipment is designed so that the product to be homogenized passes under pressure through this homogenization head. A homogenization head consists of a reduced orifice generally comprising a seat, a valve and a shock ring. The passage of the aqueous dispersion of pea proteins through the homogenizer can thus allow the homogenization of the pea protein. The homogenization can be low-pressure homogenization, high-pressure homogenization or even ultra-high-pressure homogenization. The homogenization pressure can vary widely and range, depending on the homogenization technique used, from 1 to 1000 bar, for example from 20 to 800 bar.According to one variant, the homogenization pressure ranges from 20 to 200 bar, for example from 50 to 150 bar. According to another variant, the homogenization pressure ranges from 200 to 800 bar, for example from 300 to 800 bar. According to one variant, the homogenization is a single-effect homogenization. According to another variant, the homogenization is a multiple-effect homogenization, for example a double-effect homogenization. The homogenizers that can be used are marketed, for example, by the company GEA or Tetra Pak.

[0068] The homogenization step can take place before or after the heat treatment and / or pH raising steps.

[0069] The method according to the invention may also comprise a step of drying the pea protein. Generally, this drying step is carried out so as to achieve a dry matter content greater than 80%, preferably greater than 90%, most preferably greater than 94% by weight of dry matter relative to the weight of the pea protein. Any technique well known to those skilled in the art is used for this purpose, such as freeze-drying, flash drying or drying on a drum dryer or even atomization. The method may also comprise a grinding or micronization step. Atomization is the preferred technology, in particular multiple-effect atomization. The pea protein may be in powder form. having a particle size d50, which can vary widely, for example from 10 to 500 pm, generally from 50 to 150 pm.

[0070] By "pea protein" is meant a pea extract which can be produced according to the method of the invention, the protein of which consists of pea protein. Generally, the protein content by weight is 60% or more, advantageously 80% or more, for example ranging from 80 to 95%, in particular ranging from 80 to 90%. The protein content is the N6.25 content, calculated by the Dumas method. It obviously generally includes other minor constituents other than proteins, such as starch, lipids, fibers, and / or sugars. Generally, the total starch content in the pea protein produced according to the method of the invention ranges from 0 to 20%, for example from 0 to 10%, in particular from 0.5 to 5%. This total starch content can be measured using the AOAC 996.11 method. Generally, the total fiber content can range from 0 to 20%, for example from 1 to 18%, especially from 2 to 10%. This content can be determined by AOAC Method 2017.16.Generally, the total lipid content ranges from 0 to 15%, for example, from 1 to 10%. The total lipid content can be determined by the AOAC 996.06 method in acid hydrolysis. The sugar content can range from 0 to 10%, generally from 0.5 to 5%. The sugar content can be determined by high-performance liquid chromatography (HPLC).

[0071] Pea protein may have a milky aromatic profile. Without being bound by any theory, this could be explained by the higher concentration of certain volatile compounds and, conversely, a lower concentration of certain other volatile compounds. According to one embodiment, the 3-methyl butanal content is less than 3000 ppb, for example less than 2500 ppb. According to another embodiment that can be combined with the previous embodiment, the benzaldehyde content is less than 60 ppb, for example, less than 50 ppb.

[0072] The properties of pea protein can vary widely, depending on the process parameters discussed above and as shown in the Examples section.

[0073] According to one embodiment, the dried pea protein has a solubility at pH 7 ranging from 10 to 99%. The solubility may have all intermediate amounts (i.e. 11%, 12%, 13%... 97%, 98%, 99%) and the person skilled in the art will know, on the basis of the process indications indicated above and in the Examples section, how to modify the process parameters within the ranges indicated in order to achieve the desired solubility. Advantageously, the dried pea protein has a solubility ranging from 5 to 100%, in particular from 40 to 95%. According to a first variant, the solubility ranges from 75 to 100%, for example from 80 to 95%. According to a second variant, the solubility ranges from 40 to 75%.

[0074] Solubility: Test A

[0075] As for solubility, it is determined according to the TEST A method described below: Measurement of water solubility This measurement is based on diluting the sample in distilled water, centrifuging it and analyzing the supernatant.

[0076] Operating mode: In a 400 ml beaker, introduce 150 g of distilled water at a temperature of 20°C + / - 2°C, mix with a magnetic bar and add precisely 5 g of the sample to be tested. Adjust or not the pH to the desired value with NaOH or HCl 0.1 N (pH 7). Add water to 200g. Mix for 30 minutes at 1000 rpm and centrifuge for 15 minutes at 3000 g. Collect 25 g of the supernatant. Place in a previously dried and tared crystallizer. Place in an oven at 103°C + / - 2°C for 1 hour. Then place in a desiccator (with desiccant) to cool to room temperature and weigh.

[0077] The soluble solids content, expressed in % by weight, is given by the following formula:

[0078] [Math. 1] ( = m1 - m2) x (200 + ) x 100 > = % solubility P1 x P

[0079] Or : • P = weight, in g, of the sample = 5 g • m1 = weight, in g, of the crystallizer after drying • m2 = weight, in g, of the empty crystallizer • P1 = weight, in g, of the collected sample = 25 g

[0080] According to one embodiment, the dried pea protein may have a gelling power. This gelling power may range from 1 to 500 Pa, for example from 100 to 500 Pa.

[0081] Gelling power: Test B

[0082] By "gelling power" is meant the functional property consisting of the ability of a protein composition to form a gel or a network, increasing the viscosity and generating a state of matter intermediate between the liquid and solid states. The term "gel strength" can also be used. To quantify this gelling power, it is therefore necessary to generate this network and evaluate its strength. To carry out this quantification, in the present invention, test B is used, the description of which is as follows: 1) Solubilization at 60°C + / - 2°C of the tested protein composition in water containing 15% + / - 2% dry matter and at pH 7; 2) Stirring for 5 min at 60°C + / - 2°C; 3) Cooling to 20°C + / - 2°C and stirring for 24 hours at 350 rpm; 4) Implementation of the suspension in an imposed stress rheometer equipped with a concentric cylinder; 5) Measurement of elastic moduli G' and viscous moduli G” by applying the following temperature profile: a. Phase 1: Measurement of parameter G'1 after stabilization at 20°C + / - 2°C and heating from a temperature of 20°C + / - 2°C to a temperature of 80°C + / - 2°C in 10 minutes; b. Phase 2: stabilization at a temperature of 80°C + / - 2°C for 110 minutes; c. Phase 3: cooling from a temperature of 80°C + / - 2°C to a temperature of 20°C + / - 2°C in 30 min and measurement of G'2 after stabilization at 20°C + / - 2°C; 6) Calculation of the gelling power equal to G'2 - G'1.

[0083] Preferably, the imposed stress rheometers are chosen from the DHR 2 (TA, instruments) and MCR 301 (Anton Paar) models, with a concentric cylinder type spindle. They have a Peltier effect temperature control system. To avoid evaporation problems at high temperatures, paraffin oil is added to the samples.

[0084] A "rheometer" within the meaning of the invention is a laboratory device capable of making measurements relating to the rheology of a fluid or gel. It applies a force to the sample. Generally of small characteristic dimension (very low mechanical inertia of the rotor), it allows the fundamental study of the mechanical properties of a liquid, a gel, a suspension, a paste, etc., in response to an applied force.

[0085] The so-called "imposed constraint" models allow, by applying a sinusoidal stress (oscillation mode), to determine the intrinsic viscoelastic quantities of the material, which depend in particular on time (or angular speed œ) and the temperature. In particular, this type of rheometer allows access to the complex module G*, itself allowing access to the modules G' or elastic part and G" or viscous part;

[0086] The first three steps consist of resuspending the protein in water, under precise conditions to maximize subsequent measurement.

[0087] The water chosen is preferably osmosis water, but drinking water can also be used.

[0088] Its temperature is 60°C + / - 2°C during the initial resuspension (1st and 2nd steps) then 20°C + / - 2°C after solubilization for 24 hours and cooling before measurement (3rd step). Generally speaking and unless otherwise indicated, when a temperature is given in this description, it always includes a variation of + / - 2°C, for example 20°C + / - 2°C or 80°C + / - 2°C.

[0089] A defined quantity of protein is added to said water in order to obtain a suspension titrating 15% + / - 2% in dry matter. To do this, equipment well known to those skilled in the art such as beakers and magnetic bars is used. A volume of 50 mL is stirred for at least 10 hours at 350 rpm at room temperature. Generally speaking and unless otherwise indicated, the dry matter contents given in the present description always include a variation of + / - 2%, for example 15% + / - 2%. The pH is adjusted to 7 + / - 0.5 using a pH meter and acid-base reagents, as well known in the prior art.

[0090] The fourth step is to introduce the sample into the rheometer, covering it with a thin layer of oil to limit evaporation.

[0091] The following temperature scale is then applied in the fifth step: a. Phase 1: heating from a temperature of 20°C + / - 2°C to a temperature of 80°C + / - 2°C in 10 minutes; b. Phase 2: stabilization at a temperature of 80°C + / - 2°C for 110 minutes; c. Phase 3: cooling from a temperature of 80°C + / - 2°C to a temperature of 20°C + / - 2°C in 30 min.

[0092] The measurement of the parameter G' is carried out continuously during this scale and is recorded.

[0093] The sixth and final step of test B consists of the exploitation of the recording. Two values ​​are extracted: G'1 = value of G' at the start of phase 1 after stabilization at 20°C + / - 2°C and G'2 = value of G' at the end of phase 3 after stabilization at 20°C + / - 2°C.

[0094] The gelling power is equal to G'2 - G'1.

[0095] According to one variant, the pea protein is an enzymatically modified protein. By enzymatically modified protein, the person skilled in the art means a protein whose protein structure has been deliberately modified by the addition to the protein of at least one enzyme capable of modifying the protein structure. This enzyme may be chosen from proteases, peptidases, deamidation enzymes, for example those of type EC 3.5.1 such as glutaminase or deimination enzymes, for example those of type EC 3.5.3 such as peptidylarginine deiminase. These protein modification enzymes are known to modify the physicochemical and / or organoleptic properties of the protein. For example, it is known from document WO2019 / 233920 A1 that peptidylarginine deiminase makes it possible to reduce astringency, in particular the astringency of rapeseed protein.In the case where the method comprises proteolysis of the protein-enriched protein fraction, this can make it possible to modify the degree of hydrolysis (DH) of the protein. Preferably, the degree of hydrolysis is less than 15%, advantageously less than 10%, preferably less than 6%, for example between 3 and 5%. A person skilled in the art will know how to adapt the enzymatic proteolysis conditions, or will even not carry out such a step in order to obtain the desired DH. According to a preferred variant of the invention, the pea protein is not enzymatically modified by deamidation. According to a preferred variant of the invention, the pea protein is not enzymatically modified by deamination. Glutaminase also makes it possible to carry out a deamination step. According to another preferred variant of the invention, the protein is not enzymatically modified.An advantage of the invention is that it is possible to modify the organoleptic properties of the pea protein, and in particular to give it a milky aromatic universe, without even needing to enzymatically modify the protein. The invention therefore makes it possible to provide, according to one embodiment, proteins with an unmodified primary structure.

[0096] Pea protein obtainable by the process of the invention

[0097] Another subject of the invention relates to a pea protein that can be obtained by the process of the invention. As explained previously, the protein of the invention has a unique milky aromatic profile for pea proteins. Without being bound by any theory, the applicant hypothesizes that this milky aromatic universe is explained by the presence of volatile compounds in the pea protein of the invention which are in different quantities and / or proportions than those of pea proteins already known, some volatiles being able to be generated, some others reduced or even eliminated thanks to the steps of the process of the invention, in particular the combination of heat treatment steps. This is all the more remarkable since the process requires neither the use of organic solvents nor enzymatic modification of the protein in order to obtain this milky aromatic universe. Advantageously, the pea protein capable of being obtained by the process of the invention is characterized in that at least one of its first three GATA descriptors determined according to the ISO 5492:2008(en) standard, 4.23 is a milky descriptor.

[0098] Pea protein having a milk descriptor among its first three GATA descriptors

[0099] Another subject of the invention relates to a pea protein characterized in that at least one of its first three GATA descriptors determined according to ISO 5492:2008(en), 4.23 is a milk descriptor.

[0100] Uses of Pea Protein

[0101] The invention also relates to the use of the pea protein of the invention for the manufacture of food or beverage products, in particular plant-based alternatives to milk.

[0102] Generally, the pea protein of the invention may be used in food and beverage products which may include it in an amount of up to 100% by weight based on the total dry weight of the food or beverage product, for example in an amount of from about 1% by weight to about 80% by weight based on the total dry weight of the food or beverage product. All intermediate amounts (i.e., 2%, 3%, 4%... 77%, 78%, 79% by weight based on the total weight of the food or beverage product) may be used, as may all intermediate ranges based on these amounts. These food and beverage products may be suitable for vegetarian or vegan populations.

[0103] A particularly interesting use of the protein of the invention concerns its use in beverages which have a more pleasant taste than those obtained from other commercial pea proteins. The pea protein of the invention can advantageously be used for the manufacture of beverages, in particular milk alternatives, or in other words milk substitutes. Furthermore, due to the milky aromatic note due to the ingredient, these beverages can also have a more milky aromatic note than a beverage not comprising said protein, which is an undeniable advantage for the manufacture of plant-based alternatives to milk.In addition to an improvement in the aroma, it is also possible according to the invention to obtain a more coating texture in the mouth (“mouthfeel” effect) than when other pea proteins are used, which is advantageous for drinks, and in particular for plant-based alternatives to milk because animal milks generally also have a coating texture.

[0104] In beverages, the protein content in these products can vary widely and can also be a high protein drink. The amount of protein can range, for example, from 1 to 12% in dry mass relative to the total mass of the beverage, including 3 to 10% relative to the total mass of the beverage. Beverages can be of any type and include plant-based alternatives to milk or milk substitutes, including "barista" type milks or "coffee creamers".It may also include other ready-to-drink beverages, acidic or not, such as carbonated beverages (including, but not limited to, carbonated soft drinks), non-carbonated beverages (including, but not limited to, non-carbonated soft drinks such as flavored waters, fruit juices, and sweetened or unsweetened tea or coffee-based beverages), alcoholic beverages such as beers or spirits, smoothies, beverage concentrates (including, but not limited to, liquid concentrates and syrups, and non-liquid "concentrates," such as freeze-dried and / or powdered preparations or "powder mixes"). Note that in beverages, flavorings or masking agents are generally used to reduce the pea-like flavor note or the bitter aftertaste of the protein or to flavor the beverage.One of the advantages of the pea protein of the invention is that its use in place of conventional pea proteins makes it possible to reduce this quantity of flavoring or masking agent, or even to completely remove these constituents from the drink, while maintaining a very satisfactory taste for the drink. The drinks can also include hydrocolloids; however, since pea protein provides a more coating texture, it is possible to reduce or even remove the content of hydrocolloid agents while maintaining a coating texture in the mouth.

[0105] Food products that may be affected include bakery products such as bread products (including, but not limited to, leavened and unleavened breads, sandwich breads, yeast breads and yeast-free breads such as soda breads), breads comprising all types of wheat flour, breads comprising all types of flour other than wheat flour (such as potato, rice, barley, spelt and rye flours), gluten-free breads; mixes for the preparation of such bread products; sweet bakery products (including, but not limited to, rolls, cakes, pies, pastries, waffles, crepes, muffins, pancakes, and biscuits); mixes for the preparation of such sweet bakery products;pie fillings and other sweet fillings (including, but not limited to, fruit pie fillings and nut pie fillings such as pecan pie fillings, and fillings for cookies, cakes, pastries, confectionery products and the like, such as; cream fillings); snack bars (including, but not limited to, energy, cereal, nut, and / or fruit bars).

[0106] It can also be gelled desserts such as puddings or custards and puddings. Another type of dessert can also be frozen desserts (including, but not limited to, frozen dairy desserts such as ice cream - including regular ice cream, soft-serve ice cream, and all other types of ice cream - and frozen non-dairy desserts such as non-dairy ice cream, sorbet, and others).

[0107] Other products conventionally prepared from animal milk may also comprise the pea protein of the invention to form substitutes. These may be acidified products and / or fermented with ferments, for example lactic, vegan or mesophilic ferments. These may be yogurts (including, but not limited to, full-fat, reduced-fat and fat-free yogurts, which yogurts may be free of milk proteins and lactose-free). The term "yogurts" also includes fromage frais and petits suisses. They may also be cheese substitutes such as spreadable, processed, cooked and uncooked pressed cheeses, soft cheeses, pasta filata, blue-veined cheeses; These include Emmental, string cheese, ricotta, provolone, Parmesan, Munster, mozzarella, Monterey Jack, Manchego, blue cheese, Fontina, feta, Edam, Double Gloucester, Camembert, Cheddar, Brie, Asiago, and Havarti.It can also be other products such as vegetable butters or crème fraîche.

[0108] Other products that may include the pea protein of the invention are also sauces such as salad dressings or mayonnaise or ketchup based sauces or syrups.

[0109] Also, the pea proteins of the invention may be incorporated into confectionery products (including, but not limited to, gummies, soft candies, hard candies, chocolates, caramels, and gums); sweetened and unsweetened breakfast cereals (including, but not limited to, extruded cereals, flaked cereals, and puffed cereals); and cereal coating compositions for preparing breakfast cereals. They may also be sweetened spreads (including, but not limited to, jellies, jams, nut butters such as peanut butter, spreads, and other spreadable products).

[0110] The pea proteins of the invention can also be used as a carrier or in flavor encapsulation.

[0111] Other types of foods and beverages not mentioned here but which typically include one or more proteins and may also be considered in the scope of the present invention. In particular, animal foods (such as pet foods) are explicitly contemplated.

[0112] Pea protein can also be used, possibly after texturizing, in meat substitutes such as emulsified sausages or hamburgers, or fish or seafood substitutes. It can also be used in egg replacement formulations or for the manufacture of protein products such as tofu or tempeh. Textured proteins generally mean proteins textured by extrusion, i.e., in particular, dry extrusion ("dry extrusion" or "Textured Vegetable Protein"), wet extrusion ("high moisture extrusion"). Extruders can be single-screw, twin-screw or multiple-screw extruders. In the case of twin-screw extrusion, the extrusion can be co-rotating or counter-rotating. Examples of multiple-screw extrusion include the planetary extruder or the ring extruder.We can also cite other more specific technologies such as “shear cell” technology, microextrusion or even 3D printing.

[0113] Food or beverage products may be used in particular in specialized nutrition, for example for specific populations, e.g., babies or infants, children, adolescents, adults, the elderly, athletes, people suffering from a disease. These may be meal replacement nutritional formulas, complete nutritional drinks, for example for weight management or in clinical nutrition (e.g., tube feeding or enteral nutrition).

[0114] Pea protein can be used as a sole source of protein, but can also be used in combination with other additional proteins, whether plant or animal. These additional proteins can be hydrolyzed or non-hydrolyzed. Generally, these additional proteins are in the form of concentrates or isolates. The term "plant protein" refers to all proteins derived from cereals, oilseed plants, legumes and tuberous plants, as well as all proteins derived from algae and microalgae or fungi, used alone or in mixtures, chosen from the same family or from different families. By "legume" is generally meant the family of dicotyledonous plants of the order Fabales.Several legumes are important cultivated plants, including soybeans, beans (especially mung beans), chickpeas, fava beans, peanuts, lentils, alfalfa, various clovers, fava beans, carob, licorice, and lupin. Additional legume protein can be selected from these legumes. or even be a pea protein than that of the invention. In the present application, the term "cereals" designates cultivated plants of the grass family producing edible grains, for example wheat, oats, rye, barley, corn, sorghum or rice. The tubers can be carrots, cassava, konjac, potatoes, Jerusalem artichokes, sweet potatoes. Oilseed plants are generally plants producing seeds from which oil is extracted. The oil plants can be chosen from sunflower, rapeseed, peanut, sesame, squash or flax. Animal proteins can be, for example, egg or milk proteins, such as whey proteins, casein or caseinates.The pea protein composition of the invention can thus be used in combination with one or more of these proteins or amino acids in order to improve the nutritional properties of the final product, for example to improve the PDCAAS of the protein or to provide other functionalities.

[0115] Pea protein can also be used for the manufacture of pharmaceutical products or in fermentation, for example, for the production of fungal metabolites or metabolites by cell culture.

[0116] The invention and its advantages will now be illustrated in the embodiments detailed in the examples section below. It is specified that these examples are not limiting of the present invention. Examples

[0117] Example 1: Pea protein according to the invention

[0118] Approximately 900 kg of peas were used. The outer fibers of the peas were first separated from the seeds by crushing (mechanical separation of the outer shell and the pea seed) and dehulling (sorting the outer shells and dehulled pea seeds using compressed air). Water at 75°C was used in this first part of the process: the pea seeds and water were continuously fed into a Bruynooghe brand blancher with a submerged screw. The water / pea weight ratio was approximately 1. The water inlet was made entirely at the entrance to the blancher and the peas were immediately introduced into the 75°C water. As soon as the peas were brought into contact with the water, the temperature of the water-pea suspension was approximately 55°C. The screw speed was set so that the peas passed through the blancher in 3 minutes and the temperature remained stable during this period.Water was added at the outlet of the bleacher so as to have a water / pea weight ratio of approximately 1.5. The water-pea suspension was immediately ground in continuous wet grinding by introducing water at room temperature during grinding, so as to obtain a suspension of ground peas of approximately 20% dry matter at a temperature of approximately 35°C. The suspension. of ground peas was adjusted to pH 8.5 by adding sodium hydroxide continuously and in-line. The suspension of ground peas was cooled to approximately 10°C by passing through a plate exchanger and then transferred to a stirred storage tank. This suspension of ground peas fed a decanter centrifuge (Flottweg Z3). The protein fraction was recovered in the overflow (approximately 7% dry matter). The protein fraction was adjusted with hydrochloric acid to pH 5 in a stirred tank and then heat-treated by injecting steam at 74°C into a GEA skid for approximately 3 seconds, after an initial immediate preheating step by passing through a plate exchanger. The protein fraction was then flash-cooled to 67°C. Immediately, the heat-treated protein fraction was passed through a Flottweg Z3 decanter centrifuge.The recovered protein sediment ("underflow") was diluted in hot water (80°C) so that it could be pumped. This sediment was then immediately adjusted to a dry matter content of approximately 15% and then rectified to pH 7 with sodium hydroxide. The pea protein floc was heat-treated at 130°C for 5 seconds and then flash-cooled to approximately 75°C. This pea protein floc was passed through a high-pressure homogenizer at 200 bars and then atomized in a TGE nozzle atomizer. The recovered pea protein powder was then analyzed.

[0119] Example 2: Pea protein according to the invention

[0120] Approximately 900 kg of peas were used. The outer fibers of the peas were first separated from the seeds by crushing (mechanical separation of the outer shell and the pea seed) and dehulling (sorting the outer shells and dehulled pea seeds using compressed air). Water at 75°C was used in this first part of the process: peas and water were continuously fed into a Bruynooghe brand blancher with a submerged screw. The water / pea weight ratio was approximately 1. The water inlet was made entirely at the entrance to the blancher and the peas were immediately introduced into the 75°C water. As soon as the peas were brought into contact with the water, the temperature of the water-pea suspension was approximately 52°C. The screw speed was set so that the peas passed through the blancher in 3 minutes and the temperature remained stable during this period.Water was added at the outlet of the bleacher so as to have a water / pea weight ratio of approximately 1.5. The water-pea suspension was immediately ground by continuous wet grinding by introducing water at room temperature during grinding, so as to obtain a suspension of ground peas of approximately 20% dry matter at a temperature of approximately 35°C. The suspension of ground peas was adjusted to pH 8.5 by adding sodium hydroxide continuously and in line. The ground pea suspension was cooled to approximately 10°C by passing through a plate heat exchanger and then transferred to a stirred storage tank. This ground pea suspension fed a decanter centrifuge (Flottweg Z3). The protein fraction was recovered in the overflow (approximately 7% dry matter). The protein fraction was adjusted with hydrochloric acid to pH 5 in a stirred tank and then heat-treated by injecting steam at 74°C into a GEA skid for approximately 3 seconds, after an initial immediate preheating step by passing through a plate heat exchanger. The protein fraction was then immediately cooled by rapid cooling ("flash cooling") to 67°C. Immediately, the heat-treated protein fraction was passed through a Flottweg Z3 decanter centrifuge. The recovered protein sediment (the underflow) was diluted in hot water (80°C) so that it could be pumped.This sediment was then immediately adjusted to a dry matter content of approximately 15% and then rectified to pH 6.5 with sodium hydroxide. The pea protein floc was heat-treated at 120°C for 10 seconds and then flash-cooled to approximately 75°C. This protein floc was atomized in a TGE nozzle atomizer. The recovered pea protein powder was then analyzed.

[0121] Other embodiments

[0122] Other embodiments of the invention are carried out and make it possible to obtain pea proteins with properties similar to those of Example 1. For reasons of simplicity, the table below lists the differences compared to Example 1 (if mentioned the same, no differences).

[0123] [Table 1]

[0124] Analyses

[0125] [Table 2] ;0126] Commercial pea protein

[0127] In addition to the pea protein of the invention (Example 1), the following commercial pea proteins were sensorially evaluated: • NUTRALYS® S85F (ROQUETTE® Frères) • Pisane® C9 (Cosucra) • Puris® 870 (Puris) • Profam® (ADM)

[0128] Comparative pea protein - prior art protein WQ2019 / 053387 A1

[0129] 0.8 kg of peas are used. The outer fibers of the peas are first separated from the seeds by crushing (mechanical separation of the outer shell and the pea seed) and dehulling (sorting of the outer shells and pea seeds using compressed air). The peas are placed in a container containing 1.6 L of demineralized water heated to 80°C. The temperature of 80°C is maintained for 3 minutes. The peas are separated from the aqueous solution by filtration through a sieve with a mesh size of 2 mm. The peas are then placed for 5 minutes in a second container containing 1.6 L of demineralized water whose temperature is regulated at a temperature of 7°C. This cooling is continued until the temperature of the peas is less than or equal to 10°C. The peas are separated from the aqueous solution by filtration through a sieve with a mesh size of The mesh is 2 mm. The peas, weighing 1.3 kg due to water absorption, are introduced into the enclosure of a Robocoupe Blixer 4VV type grinder. The peas are ground at maximum speed for 1.5 minutes. Then, still grinding at maximum speed, 2.7 L of demineralized water are added over a period of 3 minutes. Finally, the grinding is extended for a period of 0.5 minutes. The final result is a homogeneous ground water / pea material with a 20% DM content. This ground material is centrifuged for 5 min at 5000 g. The supernatant, concentrating the proteins, is adjusted to pH 5 then heated to 60°C for 10 min to flocculate the proteins. The protein floc is recovered by centrifuging at 5000 g for 5 min. The floc is resuspended in a volume of water to obtain a fluid suspension so that its pH can be adjusted to 7 with hydrochloric acid. This floc is then freeze-dried. A pea protein is obtained with a protein / DM content of 81% and DM content of 95%.

[0130] Comparative pea protein - prior art protein W02020 / 260841 A1

[0131] The following protein and starch extraction process is applied: - Whole peas placed in a ventilated oven under 4 conditions (2 min 80°C, 5 min 80°C, 2 min 120°C and 5 min 120°C) - Separation of external fibers and cotyledons of peas - Grinding pea cotyledons using a stone mill - Suspending the flour in water at 17% dry matter (DM), 20°C + / - 2°C and pH of 7 + / - 1 - Stir for 30 min - Separation of insolubles (starch and internal fibers) by centrifugation 1000G 5min, - Rectification to pH 5 of the supernatant - Heating at 55°C for 20 min in a container equipped with a double jacket and stirring, - Recovery of protein composition by centrifugation 5000G 5min - Rectification of pH to 7 with 1 N NaOH - Direct injection heat treatment 140°C 10 seconds - Spray drying

[0132] Sensory evaluation of the pea proteins of the invention, comparative and commercial

[0133] For each sensory test, panelists had a specific protocol to follow to rinse their mouths and avoid saturation caused by pea protein isolate solutions, to optimize the sensory analysis of this type of product. This method is described in the publication, which is incorporated by reference: Cosson, A., Delarue, J., Mabille, A.-C., Druon, A., Descamps, N., Roturier, J.-M., Souchon, I., & Saint-Eve, A. (2020). Block protocol for conventional profiling to sensory characterize plant protein isolates. Food Quality and Preference, 83, 103927.

[0134] In-water assessment

[0135] [Table 3] (1) “Sensory analysis — Methodology — General guidelines for establishing a sensory profile.” (ISO 13299:2016) (2) “Description of the sensory attributes of a sample, but without measurement of intensity” (ISO 5492:2008(en), 4.23)

[0136] Sensory analysis using the GATA methodology makes it possible to define the aromatic universes of proteins, each of which appears in the Table below:

[0137] [Table 4] ;0138] Among the proteins tested, only the protein of the invention presents a milk descriptor, which is even the first descriptor in the case of the protein of the example.

[0139] In addition, some of the comparative proteins (Profam® (ADM), Puris® 870 (Puris), Pisane® C9) present unpleasant main descriptors, such as the sulfur and / or chemical descriptor, unlike the protein of the invention.

[0140] As for the comparative pea protein of application WO2019 / 053387 A1, the milk descriptor was not noted by the panel and this protein therefore does not have a milky aromatic universe either. Similarly, the panel does not determine a milky aromatic universe for each of the 4 proteins manufactured according to application WQ2020 / 260841 A1.

[0141] Furthermore, the protein of the invention has very low pea and bitter notes, and it thus ranks at the top of the best proteins with regard to these two criteria.

[0142] Plant-based alternative to milk

[0143] Preparation

[0144] Plant-based milk alternatives were made using the recipe below:

[0145] [Table 5] ;0146] Nine liters of plant-based milk alternative are prepared using the following protocol: - 1. Disperse the powders in water heated to 70°C - 2. Hydrate the mixture with gentle stirring for 30 minutes (2500 rpm in a Silverson mixer) to form an aqueous protein solution - 3. Heat the oil to 65°C and disperse the lecithin and mix for 3 minutes. - 4. Add the oil and lecithin mixture into the aqueous solution and stir vigorously for 5 minutes (6000rpm in Silverson mixer) - 5. Sterilization: 142°C for 5 seconds - 6. Homogenization of the sterilized solution at 75°C in a high pressure homogenizer (170 bars - 1 er floor / 30 bars 2 nd floor) - 7. Cool to 4°C and bottle

[0147] Similar recipes were made with commercial pea proteins: NUTRALYS® S85F (ROQUETTE® Frères) and PURIS® Pea Protein P870 (PURIS®).

[0148] Texture and color

[0149] The plant-based milk alternatives of the invention have an excellent texture and a satisfying color.

[0150] Sensory analysis

[0151] The plant-based milk alternative of the invention has fewer pea-like aromatic notes, less astringency and bitterness than plant-based alternatives made with commercial pea proteins.

[0152] Furthermore, the plant-based alternative to milk of the invention is the only one which presents the milky note as the main aromatic note of its aromatic universe, which is explained by the milky aromatic universe of the protein of the invention.

[0153] Adding masking agents to the plant-based milk alternative

[0154] An addition of 0.08% of masking agents was made to the reference plant-based milk alternative to improve its aroma (i.e. approximately 1.3% relative to the weight of the NUTRALYS® S85F pea protein). However, even with this addition, the pea and bitter notes of the plant-based milk alternative of the invention are much weaker than those of the reference plant-based alternative comprising this masking agent. In addition, the plant-based milk alternative of the invention remains the only one to have a milky aromatic note.

[0155] Powder mix

[0156] Preparation

[0157] The powder mixes were made using the recipe below:

[0158] [Table 6] ;0159] The pea protein of the invention is evaluated as well as the commercial pea protein NUTRALYS® S85F (ROQUETTE® Frères) also in the powder mix recipe.

[0160] 40g of powdered mix is ​​placed in 325 mL of Evian® brand water.

[0161] After shaking in the shaker, we notice that in both cases after 15-25 minutes: • that no sedimentation is observed • that the amount of foam is low and very acceptable • that no lumps are observed • viscosity remains stable over time

[0162] Sensory analysis

[0163] The powdered mix made with the protein from Example 1 has a milky note identified as the most prominent by the panel. It also has a pleasant, more coating taste in the mouth than the powdered mix made from commercial pea protein.

[0164] As in the case of pea proteins evaluated in water, an improvement in taste is also noted for the powdered mixture comprising the protein of the invention. compared to that comprising the commercial product, with regard to the bitter note and the pea note which are very reduced.

[0165] Addition of masking agents to the reference powder mix

[0166] An addition of a quantity of 1.2% of masking agents was made to the reference powder mixture to improve its aromatics (i.e. approximately 1.3% relative to the weight of the pea protein). However, even if with this addition the pea and bitter notes of the reference powder mixture are improved and can be quite close to the pea and bitter notes of the powder mixture of the invention, the powder mixture of the invention remains the only one to have a milky aromatic note. Furthermore, it is thus possible to provide a powder mixture having very low pea and bitter notes, without the addition of a masking agent which adds a cost to the formulation of the powder mixture and which must also be labeled.

[0167] Plant-based alternative to pizza cheese

[0168] Preparation

[0169] The plant-based alternatives to pizza cheese were made using the recipe below:

[0170] [Table 7] ;0171] The pea protein of the invention is evaluated as well as the commercial pea protein NUTRALYS® S85F (ROQUETTE® Frères) as well.

[0172] The following protocol is applied: • Pour the water into a Stephan-type cooker Heat to 50°C • Add the powders except the citric acid • Mix for 2 minutes, stirring at 750 rpm • Adjust the pH to 4.5 using citric acid • Mix for 1 minute at the same speed and possibly readjust the pH to 4.5 • Heat to 75°C • Pour the melted mass into a silicone mold and place in the refrigerator (4°C)

[0173] Both cheeses have a high melting capacity, a desirable characteristic for this type of application. The cheeses' grateability is excellent in both cases, with the protein of the invention allowing them to be grated in a longer form than in the case of commercial protein.

[0174] Plant-based alternative to spreadable cheese

[0175] The spreadable cheeses were made using the following recipes:

[0176] [Table 8] ;0177] All cheeses made have a quantity of pea protein and water selected to include 6% protein.

[0178] In a Hotmix type mixer equipped with a butterfly type mixing blade, the following protocol was carried out: 1. Heat water to 55°C and mix at 300 rpm 2. Add the pea protein and mix for 20 minutes at 300 rpm 3. Add the other ingredients in powder form and mix for 2 minutes at 300 rpm 4. Add the oil and mix for 2 minutes at 800 rpm 5. Heat with stirring at 300 rpm to 95°C then maintain for 5 minutes at this temperature 6. Cool to 43°C and stir at 300rpm 7. Add the ferments (Vega Harmony, 0.1 mL for 500 mL) 8. Place in an oven at 43°C, until a pH of 5.0 is reached 9. Smooth using the Hotmix for 30 seconds at 300 rpm 10. Pack and store at 4°C

[0179] The fermentation time was approximately 3 hours 25 minutes for all tests. The color of the cheeses is quite satisfactory.

[0180] The cheeses of the invention exhibited an improved taste compared to those prepared from the commercial protein. Among the tests, only cheese 2 had a texture close to a commercial spreadable cheese, the other 2 being slightly more liquid and less gelled.

[0181] Yogurt without texturizer

[0182] Preparation

[0183] The yogurt was made using the recipe below:

[0184] [Table 9] ;0185] The pea protein of the invention is evaluated as well as the commercial pea protein NUTRALYS® S85F (ROQUETTE® Frères) as well.

[0186] The following protocol is applied: 1. Heat the water to 55°C 2. Add the pea protein with moderate stirring (480 rpm) and hydrate for 30 minutes 3. Add the cane sugar, mix for 5 minutes at the same stirring speed. 4. Add sunflower oil, mix for 5 minutes at 1800 rpm 5. Place the mixture in a high pressure homogenizer type NI RO PANDA heated to 60°C (first stage 105 bar, second stage 45 bar (upstream) at 150 bar 6. Pasteurization at 95°C for 10 minutes while stirring at 800 rpm 7. Cool to 42°C and add the lactic ferments 8. Maintain at 42°C until the pH is 4.6 9. Passage through an IKA Magic Lab smoother equipped with 4M and 2G modules 10. Package and store at 4°C.

[0187] The texturizer-free yogurt of the invention has a soft, even liquid texture. It appears creamier and more coating than texturizer-free yogurt made from commercial protein.

[0188] It is entirely possible to add a classic texturizing agent to improve the texture and make the yogurt more gel-like than creamy.

[0189] Emulsified vegetable sausage

[0190] A vegetable sausage model is made following the following recipe:

[0191] [Table 10]

[0192] The pea protein of the invention is tested in this model.

[0193] About 1.5 kg of emulsified sausage model is prepared by the following process:

[0194] In a Stephan mixer cooled to 4°C equipped with emulsion blades, disperse the crushed ice in water, stir at 750 rpm and place under vacuum and increase the speed to 1500 rpm.

[0195] Gradually add the oil and methylcellulose then mix under vacuum for 5 minutes at the same speed.

[0196] Add the protein and continue mixing for 5 minutes at the same speed

[0197] Add the remaining ingredients and mix at the same speed for 5 minutes

[0198] Place 140g of mixture in metal cans and seal

[0199] Heat for 1 hour at 100°C (70% relative humidity)

[0200] Cool in cold water

[0201] Freeze

[0202] For tasting, the preserves are heated in hot water (100°C for 20 minutes).

[0203] The texture of the sausages of the invention is excellent and does not have a marked taste, demonstrating that the protein of the invention can be advantageously used in this application.

[0204] Evaluation of pea protein in wet extrusion

[0205] A powder mixture is produced and consists of 3% potato starch, 5% ROQUETTE® I50M pea fiber and 92% pea protein, the proportions being given by weight.

[0206] The pea proteins tested are those of example 1, example 2 as well as the commercial pea protein NUTRALYS® F85M.

[0207] This mixture is introduced by gravity into a LEISTRITZ ZSE 27MAXX extruder from the LEISTRITZ company.

[0208] The mixture is introduced at a regulated flow rate of approximately 13.3 kg / h. A quantity of approximately 15.3 kg / h of water is also introduced. The humidity in the extruder is approximately 56%.

[0209] The wet extrusion tests are carried out on this extruder equipped with a thermoregulated die, model FDK750 from Coperion, comprising two modules of length 80 cm and passage section 50 mm x 15 mm of which the 2nd module is thermoregulated at 30°C; The extrusion screw is rotated at a speed equal to 350 rpm and sends the mixture into the die.

[0210] The temperature profile of the extruder, equipped with 15 heatable barrels, is detailed below:

[0211] [Table 11]

[0212] The textured protein thus produced is cut into 10 cm strips at the outlet of the die.

[0213] For the 3 tests, the extrusion parameters are reported below:

[0214] [Table 12] 0215] Observation of the bands

[0216] Regarding the test carried out using the protein of Example 2, the H ME bands obtained show very good fibration. These bands have numerous and fine fibers. They also show good elasticity.

[0217] As for the bands obtained from the protein of Example 1, the bands show less fibration than those of Example 2. Under the conditions of preparation of Example, the HME bands obtained from the commercial protein also show less fiberization than those of Example 2.

Claims

Demands

1. A process for manufacturing pea protein comprising the following steps: a) introducing peas or ground peas into an aqueous solution at a temperature between 65°C and 90°C to obtain a water-pea suspension or a water-ground pea suspension; b) heat-treating the suspension obtained in step a) at a temperature between 40°C and 65°C for 1 to 10 min; c) in the case of a water-pea suspension, wet-grinding the water-pea suspension obtained in step b) to obtain an aqueous suspension of ground peas; d) extracting a protein fraction by solid-liquid separation of the aqueous pea suspension obtained in step b) or c); e) optionally adjusting said protein fraction obtained in step d) to a pH between 2.0 and 8.0, for example between 4.5 and 5.7);f) heat treatment of the protein fraction obtained in step e) at a temperature of 65 to 90°C for a duration of 1 to 120 seconds to form a suspension of coagulated pea proteins; g) solid-liquid separation of the suspension of coagulated proteins obtained in step f) to form the pea protein.

2. The method according to claim 1 characterized in that the extraction step d) is preceded by a cooling step d0) of the suspension is cooled to a temperature below 15°C, preferably to a temperature of 4 to 14°C, for example 10 to 12°C.

3. The method according to claim 2 characterized in that the cooling step dO) is carried out by passing the aqueous suspension of crushed peas through a heat exchanger.

4. A process according to any one of the preceding claims characterized in that it comprises, following the heat treatment step f), a cooling step f1) by rapid cooling of the coagulated protein suspension.

5. A method according to any one of the preceding claims characterized in that it comprises a step of adjusting the pH of the pea protein to a pH between 6 and 7.5, preferably between 6.5 and 7.

5.

6. A process according to any one of the preceding claims characterized in that it comprises an additional heat treatment step of the pea protein.

7. A method according to any one of the preceding claims characterized in that it comprises a step of shearing the pea protein, for example by passing it through a high-pressure pump.

8. A process according to any one of claims 1 to 6 characterized in that it comprises a step of homogenizing the pea protein.

9. A process according to any one of the preceding claims characterized in that it comprises a step of drying the pea protein.

10. A process according to any one of the preceding claims characterized in that the pH of the aqueous solution in step a) is adjusted between 8 and 10.

11. A process according to any one of the preceding claims characterized in that the duration of the heat treatment of the protein fraction is between 1 and 45 seconds, most preferably between 1 and 10 seconds.

12. A process according to any one of the preceding claims characterized in that the ground peas of step a) are obtained by dry grinding.

13. A process according to any one of the preceding claims characterized in that a pea starch-rich fraction and / or a pea fibre-rich fraction is recovered from the insoluble part obtained from the solid-liquid separation step d).

14. Pea protein that can be obtained by the process according to any one of the preceding claims.

15. Pea protein according to claim 14 characterized in that it is not enzymatically modified by deamidation, preferably not enzymatically modified.

16. Pea protein according to claim 14 or 15 characterized in that at least one of its first three GATA descriptors determined according to ISO 5492:2008(en), 4.23 is a milk descriptor.

17. Use of pea protein according to any one of claims 14 to 16 for the manufacture of food or beverage products, in particular plant-based alternatives to milk.

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