Improved pea albumins, methods for their preparation and applications thereof

Description

[0001] The present invention relates to a pea albumin characterized in that its emulsifying activity is improved, as it can emulsify more than 600 ml of corn oil per gram of albumin. It also relates to a process for obtaining said pea albumin according to the invention. Finally, it relates to the use of said pea albumin according to the invention in industrial applications, particularly in the food, cosmetic, and pharmaceutical industries.

[0002] Since the 1970s, the pea has been the most widely cultivated legume in Europe, particularly in France, notably as a protein source for both animal and human consumption. Peas contain approximately 27% protein by weight. The term "pea" is used here 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 their intended uses: human consumption, animal feed, and / or other applications.

[0003] Among the constituents of peas, the most valued today are starch, fiber, and protein, also known as high-value components. The corresponding valorization process begins by creating a flour suspension by mixing pea flour and water in a mixer. After extracting the starch and fiber from this mixture by centrifugation, a protein-rich fraction, or light fraction, is obtained. From this fraction, isolates are obtained by selectively precipitating proteins at their isoelectric point; the aim is to insolubilize a protein of interest rich in globulins. A separation operation is then performed on this flour suspension, or "milk," notably by thermocoagulation, the objective of which is to insolubilize a protein of interest composed of globulins.At this stage of the process, it is necessary to carry out a separation, notably by centrifugal decantation, in order to isolate the composition very rich in globulins, also called the "floc." The supernatant constitutes what those skilled in the art generally refer to as the "soluble fractions."

[0004] It is important to clarify first that the term "soluble fractions" is a misnomer, as this fraction contains a number of insoluble particles, such as various colloids, but also, and especially, proteins. These soluble fractions must first be concentrated by evaporation so that the insoluble compounds, particularly the proteins, can be recovered. Currently, soluble fractions are underutilized; they are used almost exclusively as a source of nitrogen in fermentation and as a nutritious feed for livestock once they have been enriched with fiber.

[0005] However, it must be noted that the overall yield of the process leading from the initial pea to the globulin-rich composition, the floc, is far from reaching 100%. It is estimated that at an industrial scale, between 5% and 25%, but more generally around 20% by weight, of the proteins initially contained in the starting pea are found within the soluble fractions.

[0006] Several studies have been conducted to recover this protein fraction, mainly albumin, present in this soluble fraction. The document "Pilot scale recovery of proteins from a pea whey discharge by ultrafiltration" (Lei (Leigh) Gao, Lebensm.-Wiss. u.-Technol., vol 34, pp. 149-158, 2001) focuses on the recovery of pea albumins by centrifugation followed by ultrafiltration, then neutralization at pH 7 and atomization.

[0007] Patent Application WO 2006 / 052003 relates to a process for preparing soluble polypeptides from a liquid effluent from pea processing, by membrane filtration, then neutralization by adding calcium carbonate and drying.

[0008] The Applicant has also developed a process described in patent application WO2014118449 based on the succession of a) centrifugation or microfiltration, b) then ultrafiltration, c) and finally possibly reverse osmosis in order to recover an albumin-rich fraction.

[0009] Emulsifying properties are classically evaluated by two indices: emulsifying activity (EA) and emulsion stability (ES) (Boye et al. 2010a). Emulsifying activity (EA) is defined as the maximum amount of oil that can be dispersed in an aqueous solution containing a defined amount of emulsifier before the emulsion breaks down or undergoes phase inversion (Sherman, 1995).

[0010] Dairy albumins are known for their significant emulsifying activity. Despite the progress made to date, the emulsifying activity of pea albumins is promising but remains below that of dairy albumin fractions, which remain the benchmark.

[0011] The article "Pilot-scale recovery of proteins from a pea whey discharge by ultrafiltration" (Lei (Leigh) Gao, Lebensm.-Wiss. u.-Technol., vol. 34, pp. 149-158, 2001) shows in Table 3 that the emulsifying activity, or emulsifying capacity, of pea albumin is significantly lower than that of soy or milk albumin: its emulsifying activity is half that of egg albumin. This article also notes that the foaming capacity, i.e., the product's propensity to form foam, is excellent. While this property may be advantageous for certain applications, it is contrary to the properties sought in the present invention. Indeed, foam formation can be problematic when these compounds undergo membrane filtration, requiring the addition of a chemical antifoaming agent.Due to their lower emulsifying activity, pea albumins cannot completely replace milk proteins, and in particular milk albumins, in several food applications such as processed meats or coffee whiteners, or even in certain pharmaceutical or cosmetic applications. Several approaches to improve this emulsifying activity have been proposed. "Foaming and emulsifying properties of pea albumin fractions and partial characterisation of surface-active components" (Lu et al., J.Sci.Food.Agric., 80:1964-1972, 2000) indicates that the emulsifying properties of pea albumin are maximal at acidic pH and that a complex fractionation process would be necessary to access a sub-fraction called Pa2 to improve the emulsifying properties of pea albumins. Other complex and costly strategies involve, for example, enzymatic hydrolysis or chemical modifications.These approaches, however, remain complicated and costly.

[0012] It is to the Applicant's credit that she was able to isolate a pea albumin with improved emulsifying activity, designed a simple process to obtain it, and developed food, cosmetic, and pharmaceutical applications with said improved pea albumin, which until now had been impossible to implement with previously known vegetable albumins.

[0013] A first object of the present invention is a pea albumin characterized in that its emulsifying activity is greater than 600 ml of corn oil per gram of albumin. Preferably, the emulsifying activity will be greater than 800 ml of corn oil per gram of albumin. More preferably, the emulsifying activity will be greater than 1000 ml of corn oil per gram of albumin.

[0014] Pea albumin in this application means the water-soluble protein fraction extracted during the aqueous fractionation process of the different constituents of the pea (see for example the applicant's patent EP1400537).

[0015] Emulsifying activity is defined as the maximum amount of oil that can be dispersed in an aqueous solution containing a defined amount of emulsifier before the emulsion breaks down or undergoes phase inversion (Sherman, 1995). To quantify this activity, the Applicant has developed a test that allows for easy, rapid, and reproducible quantification. This process involves the following steps: 1. 0.2 g of the product sample is dispersed in 20 ml of water. 2. The solution is homogenized using an Ultraturax IKA T25 for 30 seconds at a speed of 9500 revolutions per minute (rpm). 3. 20 ml of corn oil marketed under the name AMPHORA by CARGILL is added and homogenized under the same conditions as in step 2. 4. Centrifuge for 5 minutes at 3100 g. a. If a good emulsion is obtained, i.e., without rupture or phase inversion of the emulsion, the test is repeated at step 1, increasing the quantities of water and corn oil by 50%. b. If a poor emulsion is obtained, for example a phase shift, a break or phase inversion of the emulsion, the test is repeated at step 1, reducing the quantities of water and corn oil by 50%.

[0016] The maximum quantity of oil (Qmax in ml) that can be emulsified is thus determined iteratively.

[0017] Emulsifying activity is therefore the maximum amount of corn oil that can be emulsified per gram of product. Activité émulsifiante = Qmax / 0 , 2 * 100

[0018] A second object of the present invention consists of a process for treating a soluble fraction of peas to obtain a pea albumin comprising: a. The supply of a soluble pea fraction b. Followed by a vacuum degassing step of the soluble pea fraction c. Followed by a microfiltration or centrifugation step of the degassed soluble fraction leading to a microfiltration permeate or a centrifugation supernatant d. Followed by an ultrafiltration step of the preceding microfiltration permeate or centrifugation supernatant, leading to an ultrafiltration retentate e. Followed by an optional reverse osmosis step of the ultrafiltration permeate leading to a reverse osmosis permeate and retentate f. Followed by pH neutralization of the retentates obtained in steps d) or e) g. Followed by UHT heat treatment of the retentate neutralized in step f) h. Followed by drying of the heat-treated retentate from step g).

[0019] The first step therefore consists of providing a soluble fraction of peas. By soluble fraction of peas, we mean the residual solution obtained after extraction of starch, internal fibers and globulins from an aqueous milk of pea flour (see for example the applicant's patent EP1400537).

[0020] The second step consists of a vacuum degassing stage. The aim here is to remove dissolved gases from the soluble pea fraction through vacuum treatment. A suitable device could be, for example, the SPX DEROX skid. The soluble fraction is subjected to an inlet temperature, for example, between 45°C and 55°C, preferably around 50°C, and to low-pressure conditions. The applied "vacuum" corresponds, for example, to a pressure between 0.05 bar and 0.15 bar, preferably around 0.1 bar. This step eliminates the need for the traditional addition of an antifoaming agent, which degrades the functional properties of the albumin.

[0021] The third step of the process according to the invention is a microfiltration or centrifugation step which takes place directly on the degassed soluble pea fractions obtained from the previous step. The purpose of this step is, in particular, to isolate a protein fraction rich in albumins.

[0022] When the third step is centrifugation, a person skilled in the art may use any equipment that allows separation using centrifugal force, such as a centrifuge, a horizontal decanter, a plate centrifuge, or a deslimer.

[0023] When the third stage is microfiltration, it is preferably a tangential flow membrane microfiltration. More specifically, tangential flow microfiltration is preferably carried out with ceramic membranes having a porosity of 0.01 µm to 1 µm, preferably of 0.05 µm to 0.5 µm.

[0024] Optionally, this microfiltration or centrifugation step may be preceded by a flocculation step of the insoluble particles contained in the soluble fraction of starch plants, by any technique otherwise known to a person skilled in the art.

[0025] The fourth step of the process according to the invention consists of an ultrafiltration step (d), carried out on the microfiltration permeate or on the centrifugation supernatant. This step yields, on the one hand, an ultrafiltration retentate rich in albumins, and on the other hand, an ultrafiltration permeate rich in sugars and salts. Optionally, a concentration step can be added upstream of this ultrafiltration step to reduce the amount of water and facilitate the ultrafiltration step. For this purpose, those skilled in the art could, for example, use an evaporator or reverse osmosis.

[0026] In particular, it is recommended to carry out ultrafiltration using membranes with a cut-off threshold between 5 and 20 kiloDaltons (KDa), preferably 5 or 10 KDa, with the transmembrane pressure maintained below 4 bars.

[0027] The process according to the present invention may then include an optional fifth step: reverse osmosis performed on the ultrafiltration permeate. The Applicant recommends performing this osmosis with membranes having a sodium chloride rejection rate of between 97 and 99.9%.

[0028] The sixth step consists of neutralizing the retentate from the previous step by adding a base while stirring. The retentate is adjusted to a pH between 6 and 8. Preferably, the pH of the retentate is adjusted to between 6.5 and 7.5. Preferably, the base used is sodium hydroxide, potassium hydroxide, or ammonia. Preferably, sodium hydroxide is used. Note that the use of carbonate should be avoided as it has a detrimental effect on the taste of the albumin fraction obtained.

[0029] The seventh step consists of a UHT heat treatment of the previously neutralized retentate. The treatment temperature is between 130°C and 150°C, preferably 140°C. The treatment time is between 5 and 15 seconds, preferably 10 seconds.

[0030] The eighth step is the final drying of the retentate using any technique known to those skilled in the art. Preferably, a single-effect atomizer should be used.

[0031] The third and final object of the present invention is the use of said pea albumin to emulsify large quantities of oil in food applications such as non-dairy coffee whitener, particularly where dairy proteins are completely replaced; UHT beverages rich in protein and lipids intended for clinical nutrition, particularly with total or partial replacement of dairy proteins; or ice cream, particularly with total or partial replacement of dairy proteins. The albumin according to the present invention also opens up possibilities for applications in the pharmaceutical and cosmetic fields.

[0032] The following examples help to better illustrate the Demand, without however limiting its scope. EXAMPLES Example 1

[0033] This example illustrates the production of a pea albumin according to the prior art WO2014118449 which we will call PA.

[0034] The first step is obtaining the soluble fraction of the pea. Pea flour is initially prepared by grinding hulled forage peas in an ALPINE-type hammer mill equipped with a 100 µm screen. 300 kg of flour at 87% dry matter are then soaked in water to a final concentration of 25% dry matter, at a pH of 6.5. 1044 kg of flour suspension at 25% dry matter, yielding 261 kg of dry flour, are then introduced with 500 kg of water into a 14-stage hydrocyclone battery. The flour suspension is introduced at stage 5. This separation results in a light phase, which corresponds to the outlet of stage 1. This phase consists of a mixture of proteins, internal fibers, and soluble fibers.

[0035] This light phase exiting the hydrocyclones contains a mixture totaling 142 kg on a dry matter basis: fibers, approximately 14.8% by weight, or 21 kg dry matter; proteins, approximately 42.8% by weight, or 60.8 kg dry matter; and solubles, approximately 42.4% by weight, or 60.2 kg dry matter. This fraction has a dry matter content of 11.4%. The fibers are separated using Westfalia-type centrifugal decanters employed in an industrial potato starch processing unit. The light phase exiting the centrifugal decanter contains a mixture of proteins and solubles, while the heavy phase contains the pea fibers. The heavy phase contains 105 kg of fiber at 20% dry matter. It is observed that almost all of the fibers are recovered in this fraction.

[0036] As for the protein and solubles fraction, it contains 1142 kg of a solution mixture of solubles and proteins (6% dry matter fraction). The proteins are flocculated at their isoelectric point by adjusting the light phase at the outlet of the centrifugal decanter to a pH of 4.5 and heating to 50 °C.

[0037] The proteins thus flocculated are left for 10 minutes in a maturation tank. After precipitation of the proteins, a centrifugal decantation is carried out, which allows the recovery, after drying, of sediment containing 56 kg of globulin-type proteins (86% of Nx6.25 on dry matter) at 93% dry matter and a soluble fraction containing albumins, sugars and salts, measuring 2.5g per 100g of dry matter of which 27% is protein.

[0038] This soluble pea fraction is then pumped through a microfiltration unit equipped with Inside Ceram® ceramic membranes with a porosity of 0.14 µm (19 channels of 4.5 mm). Throughout the filtration process, the temperature is regulated at 60°C and the transmembrane pressure is maintained between 0.4 and 0.6 bar. 707 liters of microfiltration permeate, with a concentration of 2.5 g / 100 g DM, and 1768 liters of microfiltration retentate, also with a concentration of 2.5 g / 100 g DM, are thus recovered.

[0039] 550 liters of microfiltration permeate are pumped through an ultrafiltration unit. The ultrafiltration unit is equipped with KERASEP® BX ceramic membranes, marketed by NOVASEP, with a cut-off pressure of 15 kDa (7 channels of 6 mm). Throughout the filtration process, the temperature is regulated at 60°C and the transmembrane pressure is maintained between 1 and 3 bar.

[0040] 467 liters of ultrafiltration permeate, with a concentration of 2.2 g / 100 g dry matter, and 33 liters of retentate are recovered. The PA ultrafiltration retentate is atomized using a single-effect spray-dryer. The inlet temperature is set at 190°C and the outlet temperature is between 85 and 90°C.

[0041] The composition of the final albumin fraction (atomized PA ultrafiltration retentate) is given in the table below: Dry matter content 93,9 % Protein content (Nx6.25) 97 g / 100 g of dry matter Ash content 0,1 g / 100 g of dry matter Example 2

[0042] This example illustrates the production of a pea albumin according to the invention which we will call PA_INV.

[0043] The process is similar until the soluble fraction of peas is obtained, following the steps described in the first paragraph of example 1.

[0044] The soluble fraction of peas thus obtained is first degassed by passing it over an SPX DEROX skid. The operating parameters of said SPX DEROX skid are as follows: Supply pressure bar 0,88 Outlet pressure bar 2,73 Supply temperature °C 50,5 Outlet temperature °C 42,8 Condenser temperature °C 37 Empty instruction bar 0,1 Tank level setting % 60 Draw-off flow rate to NA7 L / H 750 O2 dissolved entry mg / L 9 O2 output dissolved mg / L 0,1

[0045] Proper degassing is monitored by measuring dissolved oxygen at the inlet and outlet.

[0046] Then, this degassed soluble pea fraction is pumped through a microfiltration unit equipped with Inside Ceram® ceramic membranes having a porosity of 0.14 µm (19 channels of 4.5 mm). Throughout the filtration process, the temperature is regulated at 60°C and the transmembrane pressure is maintained between 0.4 and 0.6 bar.

[0047] The permeate is pumped through an ultrafiltration unit. The ultrafiltration unit is equipped with KERASEP® BX type ceramic membranes marketed by NOVASEP and having a cut-off threshold of 15 kDa (7 channels of 6 mm). Throughout the filtration, the temperature is regulated at 60°C and the transmembrane pressure is maintained at a value between 1 and 3 bar.

[0048] Three successive diafiltrations are performed, consisting of repeating three times the addition of a volume of decarbonated potable water to a volume of retentate, followed by ultrafiltration until the permeate dry matter content is less than 0.5% DM.

[0049] The ultrafiltration retentate obtained is then rectified under agitation to pH 6.8 by adding 50% concentrated sodium hydroxide.

[0050] A UHT heat treatment is then applied to the neutralized ultrafiltration retentate consisting of passing it over a VOMATEC skid, at a temperature of 140°C for a contact time of about ten seconds and then flashing it under vacuum at about 90°C.

[0051] The solution obtained from the UHT heat treatment is then atomized using a single-effect spray-dryer. The inlet temperature is set at 190°C and the outlet temperature is between 85 and 90°C.

[0052] The resulting pea albumin powder is called PA_INV. Its composition is given in the table below: Dry matter content 94,4 % Protein content (Nx6.25) 94 g / 100 g of dry matter Ash content 2,5 g / 100 g of dry matter Example 3

[0053] This example aims to describe the protocol used to measure the emulsifying activity (EA) of pea albumins obtained previously in Examples 1 (according to the prior art) and 2 (according to the invention): 1. 0.2 g of the product sample is dispersed in 20 ml of water. 2. The solution is homogenized using an Ultraturax IKA T25 for 30 seconds at a speed of 9500 rpm. 3. 20 ml of corn oil marketed under the name AMPHORA by CARGILL is added and homogenized under the same conditions as in step 2. 4. Centrifuge for 5 minutes at 3100 g. a. If a good emulsion is obtained, i.e., without phase separation or inversion, the test is repeated from step 1, increasing the amounts of water and corn oil by 50%. b. If a poor emulsion is obtained, for example, phase separation, separation, or inversion, the test is repeated from step 1, decreasing the amounts of water and corn oil by 50%.

[0054] The maximum quantity of oil (Qmax in ml) that can be emulsified is thus determined iteratively.

[0055] Emulsifying activity is therefore the maximum amount of corn oil that can be emulsified per gram of product. Activité émulsifiante = Qmax / 0 , 2 * 100 Example 4

[0056] This example aims to present the comparison of the two pea albumins PA (Example 1, according to the prior art) and PA_INV (Example 2, according to the invention) as well as several commercial reference albumins, vegetable and dairy, and globulins. Emulsifying Activity (ml of oil / g of product) Egg white powder Egg albumins 1225 WPC 392 whey protein concentrate 1301 Skimmed Milk Powder skimmed milk powder 1185 Sodium Caseinate supplier 1 sodium caseinate 782 NUTRALYS S85F Pea globulins 786 NUTRALYS S85 PLUS Pea globulins 195 PA Pea albumins according to the prior art 564 PA_INV Pea albumins according to the invention 1314

[0057] It is clear that with the albumins according to the invention, emulsifying activity values ​​are more than double those of prior art pea albumins. These values ​​allow for applications similar to those possible with animal proteins such as egg or milk albumins. Example 5: Use of albumins obtained according to the invention in food applications such as coffee coloring (English: coffee-whitener)

[0058] This example illustrates the possibilities of food applications offered by pea albumin according to the invention by presenting results of production of "coffee-whitener" (milk substitutes for coffee) aimed at the total replacement of traditionally used sodium caseinates.

[0059] The compositions of the different mixtures are given in the table below, as a percentage by weight of the final composition. To prepare them, the following procedure must be followed: Heat the coconut oil to 80°C while stirring and add DIMODAN HP to solubilize the monoglycerides. Heat 90% of the water to 50°C and add the proteins while stirring. Solubilize the phosphate salts in the remaining 10% of the water. Add the phosphate salt solution and glucose syrup to the container with the aqueous protein solution. Pre-emulsify the DIMODAN HP / oil solution with a homogenizer for 5 minutes at 10,000 rpm. Mix the two solutions in a homogenizer at 160 bar and 75°C until an emulsified solution is obtained. Pasteurize for 5 seconds at 80°C.

[0060] To quantify the emulsion quality, particle size is measured using a MALVERN Particle Size Analyser 3000. Dmode represents the average size of the emulsified particles.

[0061] It is clear that only pea albumin according to the invention PA_INV allows the obtaining of emulsified particles with an average size of less than one micron. Example 6: Use of albumins obtained according to the invention in food applications such as UHT ready-to-drink beverages, for dietary, sports or clinical nutrition (Ready To Drink or RTD)

[0062] This example illustrates the potential food applications of pea albumin according to the invention by presenting results for the production of UHT "ready-to-drink" beverages for mainstream, dietary, sports, or clinical nutrition, aiming for the partial replacement (approximately 50%) of traditionally used sodium caseinates. The example presents compositions containing approximately 10% protein by weight, but pea albumin according to the invention is also suitable for compositions with protein content ranging from 5% to 15% by weight, or even 20% by weight. Similarly, higher oil contents are possible; those skilled in the art can simply adapt the recipe using pea albumin according to the invention. Given the emulsifying properties of the albumins according to the invention, a complete replacement of milk proteins is also conceivable.

[0063] The compositions of the different mixtures are given in the table below, as mass percentages of the final composition. To prepare them, the following procedure must be followed: Dry mixing of powdered products (proteins, maltodextrins and sucrose), heating of water to 50°C, addition of the previously prepared powder mix, dispersion with a Silverson type high-shear stirrer for 30 min, at 50°C, under 3500 RPM, addition of vanilla flavoring, Place the lecithin and oil in a separate container; stir and heat to 50°C, After 30 min of hydration, add this lecithin / oil solution to the first mixture (proteins, maltodextrins and sucrose) using a high-shear stirrer for 5 min (10000 rpm), Homogenization at 200 bar and 75°C in two stages (30% in the second stage), Carry out a UHT treatment at 142°C for 5 s, Cool and store at 4°C.

[0064] To quantify the emulsion quality, particle size is measured using a MALVERN Particle Size Analyser 3000. Dmode represents the average size of the emulsified particles.

[0065] It is clear that only pea albumin according to the PA_INV invention allows us to obtain a Dmode as good (less than 1 micron) as the reference obtained with caseins of dairy origin. Example 7: Use of the albumins obtained according to the invention in food applications such as "pea milk" or "plant-based milk", intended for daily consumption

[0066] This example illustrates the possibilities of food applications offered by pea albumin according to the invention by presenting production results of "pea milk" or "plant milk" type drinks intended for daily consumption.

[0067] The compositions of the different mixtures are given in the table below. To prepare them, follow this procedure: Mix the water and gellan gum in water at 90°C until completely dissolved, stirring if necessary. Cool to 70°C. Add the remaining ingredients, except for the oil, sunflower lecithin, and vanilla flavoring, stirring until completely dissolved, stirring if necessary. Heat the sunflower oil and add the lecithin. Add the oil / lecithin mixture and vanilla flavoring while stirring with a high-shear mixer. Homogenize the solution at 75°C using a high-pressure homogenizer at 270 bar (1st stage) and 30 bar (2nd stage). Sterilize by UHT treatment at 142°C for 5 seconds. Package and store at 4°C.

[0068] To quantify the emulsion quality, particle size is measured using a MALVERN Particle Size Analyser 3000. Dmode represents the average size of the emulsified particles.

[0069] It is clear that only pea albumin according to the invention PA_INV makes it possible to obtain a Dmode as good (less than 1 micron) as the reference obtained with pea globulin. Pea albumin of the prior art does not allow for a Dmode of the emulsified globules less than 1 micron, and similar to the reference globulins: only pea albumin according to the present invention makes this possible.

Claims

1. Pea albumin characterized in that its emulsifying activity is greater than 600 ml of corn oil per gram of albumin, the emulsifying activity being determined according to the measurement method described in the description.

2. The pea albumin according to claim 1, of which the emulsifying activity is greater than 800 ml of corn oil per gram of albumin, the emulsifying activity being determined according to the measurement method described in the description.

3. The pea albumin according to claim 2, of which the emulsifying activity is greater than 1000 ml of corn oil per gram of albumin, the emulsifying activity being determined according to the measurement method described in the description.

4. A method for processing a pea soluble fraction making it possible to obtain a pea albumin according to any of the preceding claims, comprising: a. Providing a pea soluble fraction b. Followed by a step of vacuum degassing the pea soluble fraction c. Followed by a step of microfiltration or centrifugation of the degassed soluble fraction leading to a microfiltration permeate or to a centrifugation supernatant, d. Followed by a step of ultrafiltration of the microfiltration permeate or of the centrifugation supernatant, leading to an ultrafiltration retentate, e. Followed by an optional step of reverse osmosis of the ultrafiltration permeate leading to a permeate and to a retentate from the reverse osmosis. f. Followed by pH neutralization of the retentates obtained in steps d) or e) to a pH of between 6.5 and 7.5, g. Followed by UHT-type heat treatment, at a temperature of between 130°C and 150°C, preferably 140°C, for a treatment time of between 5 and 15 seconds, preferably around 10 seconds, of the neutralized retentate from step f) h. Followed by drying of the heat-treated retentate from step g)5. The method according to claim 4, characterized in that step f) is carried out by adding a base selected from soda, potash or ammonia, preferentially soda.

6. The method according to any of the preceding claims, characterized in that the drying in step h) is carried out by single-action atomization.

7. Use of pea albumin according to any of claims 1 to 3 for producing food formulations8. The use of pea albumin according to claim 7 to produce a coffee whitener.

9. The use of pea albumin according to claim 7 to produce a ready-to-drink beverage.

10. The use of pea albumin according to any of claims 1 to 3 to produce cosmetic or pharmaceutical formulations.