WO2023232295A1 - Proteines de pois presentant un arome lacte - Google Patents
Proteines de pois presentant un arome lacte Download PDFInfo
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- WO2023232295A1 WO2023232295A1 PCT/EP2023/025265 EP2023025265W WO2023232295A1 WO 2023232295 A1 WO2023232295 A1 WO 2023232295A1 EP 2023025265 W EP2023025265 W EP 2023025265W WO 2023232295 A1 WO2023232295 A1 WO 2023232295A1
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- pea
- protein
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- peas
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
- A23C11/103—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins containing only proteins from pulses, oilseeds or nuts, e.g. nut milk
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
- A23C11/103—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins containing only proteins from pulses, oilseeds or nuts, e.g. nut milk
- A23C11/106—Addition of, or treatment with, microorganisms
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C20/00—Cheese substitutes
- A23C20/02—Cheese substitutes containing neither milk components, nor caseinate, nor lactose, as sources of fats, proteins or carbohydrates
- A23C20/025—Cheese substitutes containing neither milk components, nor caseinate, nor lactose, as sources of fats, proteins or carbohydrates mainly containing proteins from pulses or oilseeds
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/22—Working-up of proteins for foodstuffs by texturising
- A23J3/225—Texturised simulated foods with high protein content
- A23J3/227—Meat-like textured foods
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/22—Working-up of proteins for foodstuffs by texturising
- A23J3/26—Working-up of proteins for foodstuffs by texturising using extrusion or expansion
Definitions
- the subject of the invention is new pea proteins presenting a milky aromatic universe. Another subject of the invention relates to a process for manufacturing these pea proteins. The invention also relates to the use of said proteins for the manufacture of food products.
- pea is the grain legume which has developed the most in Europe and mainly in France, in particular as a protein resource for animal but also human food. Peas contain approximately 27% protein by weight.
- the term “pea” is considered 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”. (“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 mainly pea globulin, has been extracted and used industrially for many years.
- a process for extracting pea protein we can cite patent EP1400537. In this process, the seed is ground in the absence of water (a process known as “dry grinding”) to obtain flour. This flour is then suspended in water at room temperature in order to then proceed with the different stages of protein extraction.
- aromatic notes are very specific to the pea source and distinct from other plant sources.
- one of the main aromatic notes which is generally found in many proteins on the market is of the “pea” or “beany” type.
- This aromatic note is an undeniable obstacle in many applications, particularly food.
- 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 S. U. 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 that there is a correlation between the inhibition of lipoxygenase and a reduction in volatiles. .
- the protein extracted from peas also very often has a marked bitter aftertaste (or “off-note”).
- enzymes modifying the primary structure of the protein can also modify the organoleptic properties of proteins, including their taste; processes for producing modified pea proteins using such enzymes have already been described.
- the milky note is mentioned in Table 2 of the sensory evaluation.
- 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 from pea protein.
- aromatic universe we mean 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 was 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.
- milky note we mean an aromatic note linked to milk and/or yogurt.
- proteins which can be advantageously used, for example, in plant-based alternatives to milk, in order to obtain more milky organoleptic properties.
- the Applicant has thus arrived after numerous research at a new manufacturing process making it possible to provide pea proteins having a very reduced pea aromatic note, also very low bitterness and also presenting a milky aromatic universe, and this without adding flavor. This is obviously an advantage for the manufacture of products such as plant-based alternatives to pea-based milk. Furthermore, as the aromatic universe of the pea protein thus obtained is unique, even in food products other than plant 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 manufacture of meat or fish analogues.
- the subject of the invention is a process for manufacturing pea protein comprising the following steps: a) introducing 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-crushed 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 crushed peas; d) extraction of a protein fraction by solid-liquid separation of the aqueous pea suspension obtained in step b) or c); e) optionally adjusting 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
- the cooling step dO) is carried out by passing the aqueous suspension of crushed peas through a heat exchanger.
- the process comprises, following the heat treatment step f), a cooling step f1) by rapid cooling of the suspension of coagulated proteins.
- the process 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.
- the process comprises an additional heat treatment step of the pea protein.
- the process comprises a step of shearing the pea protein, for example by passing it through a high pressure pump.
- the process comprises a step of homogenizing the pea protein.
- the process comprises a step of drying the pea protein.
- the pH of the aqueous solution of step a) is adjusted between 8 and 10.
- the duration of the heat treatment of the protein fraction is between 1 and 45 seconds, most preferably between 1 and 10 seconds.
- the ground peas from step a) are obtained by dry grinding.
- 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).
- Another subject of the invention relates to the pea protein capable of being obtained by the process of the invention.
- the pea protein is characterized in that at least one of its first three GATA descriptors determined according to standard ISO 5492:2008(en), 4.23 is a milk descriptor.
- This pea protein can have low bitterness, a reduced pea aromatic note and also 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 quantities and/or proportions different from those of pea proteins already known, certain volatiles can be generated, certain 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 does not require the use of organic solvents or the use of enzymes and the pea proteins can also have excellent functional properties, such as solubility and/or high gelling power.
- Another subject of the invention also relates to the use of said pea protein for the manufacture of food products or drinks, in particular plant-based alternatives to milk.
- the invention relates to a process for manufacturing pea protein.
- 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 (elimination of unwanted particles such as stones, dead insects, soil residue, etc. .) or even the elimination of the external fibers of the pea (external cellulosic covering) by a well-known step called dehulling or “dehulling”.
- steps well known to those skilled in the art, such as in particular cleaning (elimination of unwanted particles such as stones, dead insects, soil residue, etc. .) or even the elimination of the external fibers of the pea (external cellulosic covering) by a well-known step called dehulling or “dehulling”.
- peas in step a
- ground peas i.e. pea flour
- these ground peas usually being obtained by dry grinding.
- the unshelled pea, the peeled 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.
- the aqueous solution may be water which may possibly include additives such as in particular anti-foam or bacteriostatic compounds.
- the ratio by weight of quantity of peas/quantity of aqueous solution in step a) can in particular be between 0.5 and 2.
- 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 a submerged heat exchanger. Preferably, the temperature is between 70°C and 80°C or even approximately 75°C.
- the water-pea suspension or the water-crushed pea suspension is obtained by introducing the pea or crushed peas into the aqueous solution previously heated.
- the pH of the aqueous solution of step a) is adjusted between 8 and 10. This adjustment can be done by adding a base such as soda, lime or potash, preferably soda. According to another variant, the pH is not adjusted at this step.
- the process 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 can be heated or cooled to reach this temperature.
- the suspension does not undergo any heating and is directly at temperature when mixing the aqueous suspension with the peas or crushed peas.
- the heat treatment temperature is between 40 and 60°C, or even between 45 and 55°C.
- the heat treatment is carried out for 2 to 4 min.
- the process comprises a step c) of wet grinding of the water-pea suspension treated in step b) in order to obtain an aqueous suspension of crushed peas.
- the process is carried out from peas and step c) of wet grinding is carried out by continuous passage through one or more grinders to obtain the aqueous suspension of crushed peas.
- the grinder(s) may be any type of grinder capable of carrying out wet grinding, such as ball wet grinders, conical wet grinders, helical wet grinders or wet grinders equipped with rotor/stator systems.
- the crusher can be that used in the examples of document WO2019/053387 in the name of the Applicant.
- this type of grinder can allow continuous grinding by passing the water-pea suspension through said grinder.
- the process combines two cutting stages (pre-cut then cutting) using different rotor-stator grinders for each of these cuts.
- the pre-cut then the cut can be carried out one after the other or, alternatively the cut can take place after pre-cut then storage of the treated water-pea suspension.
- Such crushers are described in document WO2019/158589.
- a dilution with water during this step or at the end of this step in order to form the aqueous suspension of peas. crushed.
- water is added continuously or discontinuously to dilute the aqueous suspension.
- dry matter of the aqueous suspension of crushed peas ranges from 10 to 30%, for example from 15 to 25%.
- Step d) of the process consists of the extraction of the components from the aqueous suspension of crushed peas, and in particular the extraction of a protein fraction by solid-liquid separation of the aqueous suspension of peas.
- a stage of adjusting the pH of the aqueous suspension of crushed peas can be carried out before carrying out the solid-liquid separation stage.
- the solid-liquid separation can take place after adjusting the aqueous pea suspension to a pH ranging from 6 to 9, preferably from 8 to 9, most preferably from 8.5 to 9.
- This stage of pH adjustment can be done in a stirred tank. This stage can be more or less long, and last for example from 1 to 240 minutes, generally from 5 to 60 minutes.
- the base and/or the acid can be in the form of aqueous solutions.
- the aqueous suspension of crushed 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 for example passing the aqueous suspension of crushed peas through a heat exchanger.
- the protein fraction is the soluble part of the aqueous suspension and the fraction rich in starch and fiber is the insoluble part. It is also possible to separate more than two insoluble fractions, and for example recover a first insoluble fraction richer in starch and a second insoluble fraction richer in fiber. Thus, according to a variant of the process, 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).
- starch-rich fraction and fiber-rich fraction we generally mean a fraction comprising at least 50% starch or fiber.
- the starch and fiber quantification methods are known to those skilled in the art and specific methods are indicated later in the description. These fractions are recovered classically 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.
- a decanter in particular a centrifugal decanter, a centrifuge or even with hydrocyclones.
- the process can also make it possible to recover one or more fractions enriched in fibers and/or starch, which are eliminated from the suspension, and recover the useful protein fraction following the process of the invention.
- 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 we mean a pH close to which the net electric charge of the protein of the protein fraction is zero.
- This pH can 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 can be carried out by adding an acid, organic or inorganic, for example hydrochloric acid, sulfuric acid or citric acid or their mixtures.
- This step e) can be done in a tank, stirred or not. It can 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 can be done online and the acid can be in the form of an aqueous solution.
- the process also includes a heat treatment step f) of the protein fraction at the possibly adjusted pH.
- This step includes a stage of heating the suspension of coagulated proteins. This stage is carried out at a temperature ranging from 65 to 90°C to form a suspension of coagulated proteins. 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.
- a heat exchanger is generally used. It can be type according to the principle of indirect heating or according to the principle of direct heating, generally by steam injection. Preferably, heating is carried out by steam injection.
- the heat treatment step f) comprises a heating stage followed by a cooling stage of the suspension of coagulated proteins.
- this stage of cooling is preferably obtained by rapid cooling known under the name "flash - cooling”, leading to immediate cooling.
- flash - cooling leading to immediate cooling.
- the temperature can range from 60 to 75°C, for example between 64 and 70°C.
- This rapid cooling is achieved by applying a vacuum to the suspension of coagulated proteins, the applied vacuum being determined as a function of the chosen cooling temperature.
- the Applicant considers that essential steps in the process of the invention are the first heat treatment steps b) and f). Without being linked to any theory, one hypothesis is that pea protein could include 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 already known pea proteins. 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 already known pea proteins. The whole would make it possible to create this milky aromatic universe, without the need to modify, for example, the primary structure of the protein.
- the pea protein is separated from the suspension of coagulated proteins 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.
- the recovered solid fraction includes pea protein and is generally a concentrated aqueous suspension of pea protein.
- the solid fraction recovered has a dry matter which generally ranges from 25 to 50%, or even from 30 to 40%.
- the mass composition of pea protein can vary and will generally mainly include proteins (notably in the form of globulins) but also starch, lipids, fibers, and/or sugars. This solid fraction can be diluted by adding water to be more easily handled in the following optional steps.
- 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. Raising the pH is generally done by adding a basic aqueous solution.
- the process comprises an additional heat treatment step of the pea protein.
- the temperature and time conditions can vary widely in this step, for example going 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 second to 30 minutes.
- the temperature ranges from 90 to 110°C and its duration ranges from 0.1 seconds to 5 minutes.
- 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 at 10 seconds.
- This step may aim to functionalize and/or sanitize the pea protein.
- the pea protein can be in the form of an aqueous dispersion, preferably having a dry matter ranging from 10 to 25%, for example from 15 to 20%.
- the process of the invention comprises, following the additional heat treatment step, a step of cooling f1) of the pea protein.
- this cooling step is obtained by rapid cooling (“flash-cooling”).
- the temperature can range from 60 to 100°C, for example between 70 and 90°C.
- this rapid cooling step (“flash-cooling”) is carried out by applying a vacuum to the aqueous dispersion of pea protein, the applied vacuum being determined as a function of the chosen cooling temperature.
- pea protein can be modified by 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 heat treatment, the solubility of the pea protein obtained after this heat treatment is greater than that of a pea protein heat treated at a slightly lower pH. In the same way, when the aqueous dispersion of pea proteins has a neutral pH during 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 pH slightly lower. This is reflected in the examples section below.
- the process comprises a step of shearing the pea protein, for example by passing the aqueous dispersion of proteins through a high pressure pump.
- a high pressure pump we can cite the high pressure pumps marketed by the company Silverson, also called high pressure mixer.
- shear (“high shear mixer”), for example those from the UHS range.
- the shearing step is carried out by a high pressure pump.
- the shearing step can take place before or after the heat treatment and/or pH rise steps.
- the process comprises a step of homogenizing the pea protein.
- any type of homogenizer can be used.
- 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 homogenizing head consists of a reduced orifice generally comprising a seat, a valve and a shock ring. Passing the aqueous dispersion of pea proteins through the homogenizer can thus allow the homogenization of the pea protein.
- 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.
- 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 which can be used are marketed for example by the company GEA or Tetra Pak.
- the homogenization step can take place before or after the heat treatment and/or pH rise steps.
- the process according to the invention may also include 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, such as for example freeze-drying, drying by flash drying or on a drying drum or even atomization.
- the process may also include a grinding or micronization step.
- Atomization is the preferred technology, especially multiple-effect atomization.
- Pea protein can 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.
- 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.
- the protein content by weight is 60% or more, advantageously 80% or more, for example ranges from 80 to 95%, in particular ranges from 80 to 90%.
- the protein content is N6.25, calculated by the Dumas method. It obviously generally includes other minority constituents other than proteins, such as starch, lipids, fibers, and/or sugars.
- 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.
- 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 the 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 acid hydrolysis method.
- the sugar content can range from 0 to 10%, generally 0.5 to 5%. The sugar content can be determined by high performance liquid chromatography (HPLC).
- Pea protein can have a milky aromatic profile. Without being linked to any theory, this could be explained by the higher concentration of certain volatile compounds and, conversely, a lower concentration of certain other volatile compounds.
- the content of 3-methyl butanal is less than 3000 ppb, for example less than 2500 ppb.
- the benzaldehyde content is less than 60 ppb, for example, less than 50 ppb.
- pea protein The properties of pea protein can vary widely, depending on the process parameters explained previously and as appears in the Examples section.
- the dried pea protein has a solubility at pH 7 ranging from 10 to 99%.
- the solubility may be all intermediate amounts (i.e. 11%, 12%, 13%...97%, 98%, 99%) and those skilled in the art will know based on the process guidance. indicated above and in the Examples section modify the process parameters within the ranges indicated in order to achieve the desired solubility.
- 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
- This measurement is based on the dilution of the sample in distilled water, its centrifugation and the analysis of the supernatant.
- the dried pea protein may have gelling power.
- This gelling power can range from 1 to 500 Pa, for example from 100 to 500 Pa.
- gelling power is meant the functional property consisting of the capacity of a protein composition to form a gel or a network, increasing the viscosity and generating a state of matter intermediate between liquid and solid states. .
- gel strength we can also use the term “gel strength”. 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:
- 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;
- Phase 2 stabilization at a temperature of 80°C +/- 2°C for 110 minutes;
- 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;
- the imposed stress rheometers are chosen from the DHR 2 (TA, instruments) and MCR 301 (Anton Paar) models, with a concentric cylinder type mobile. They have a Peltier effect temperature regulation system. In order to avoid evaporation problems at high temperatures, paraffin oil is added to the samples.
- a “rheometer” within the meaning of the invention is a laboratory device capable of making measurements relating to the rheology of a fluid or a gel. It applies a force to the sample. Generally of small characteristic dimension (very low mechanical inertia of the rotor), it makes it possible to fundamentally study the mechanical properties of a liquid, a gel, a suspension, a paste, etc., in response to a force applied.
- the first three steps consist of resuspension of the protein in water, under precise conditions making it possible to maximize the subsequent measurement.
- the water chosen is preferably osmosis water, but drinking water can also be used.
- a defined quantity of protein is added to said water in order to obtain a suspension measuring 15% +/- 2% in dry matter.
- we use equipment well known to those skilled in the art such as beakers and magnetic bars. Shake a volume of 50mL for a minimum of 10 hours at 350 rpm at room temperature. Generally speaking and unless otherwise indicated, the dry matter contents given in this 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.
- the fourth step consists of introducing the sample into the rheometer by covering it with a thin layer of oil in order to limit evaporation.
- 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; vs. Phase 3: cooling from a temperature of 80°C +/- 2°C to a temperature of 20°C +/- 2°C in 30 min.
- pea protein is an enzymatically modified protein.
- enzymatically modified protein those skilled in the art mean 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 can be chosen from proteases, peptidases, deamidation enzymes, for example those of EC 3.5.1 type such as glutaminase or deimination enzymes, for example those of EC 3.5.3 type such as peptidylarginine deiminase.
- These protein modification enzymes are known to modify the physicochemical and/or organoleptic properties of the protein.
- peptidylarginine deiminase makes it possible to reduce astringency, in particular the astringency of rapeseed protein.
- this can make it possible to modify the degree of hydrolysis (DH) of the protein.
- the degree of hydrolysis is less than 15%, advantageously less than 10%, preferably less than 6%, for example between 3 and 5%.
- 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 allows a deamination step to be carried out. According to another preferred variant of the invention, the protein is not enzymatically modified.
- the protein of the invention has a unique milky aromatic profile for pea proteins.
- 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 quantities and/or proportions different than those already known pea proteins, certain volatiles can be generated, certain 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 as the process requires neither the use of organic solvents nor to enzymatically modify the protein in order to to obtain this milky aromatic universe.
- 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 standard ISO 5492:2008(en), 4.23 is a milk descriptor .
- 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 standard ISO 5492:2008(en), 4.23 is a milk descriptor.
- the invention also relates to the use of the pea protein of the invention for the manufacture of food products or drinks, in particular plant-based alternatives to milk.
- the pea protein of the invention can be used in food products and drinks which can include it in an amount of up to 100% by weight relative to the total dry weight of the product.
- food or beverage product for example in an amount ranging from approximately 1% by weight to approximately 80% by weight relative to the total dry weight of the food or beverage product. All intermediate amounts (i.e. 2%, 3%, 4%...77%, 78%, 79% by weight relative to the total weight of the food or beverage product) may be used, from same as all intermediate ranges based on these quantities.
- These food and drink products can be adapted to vegetarian or vegan populations.
- a particularly interesting use of the protein of the invention concerns its use in drinks 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 drinks, in particular alternatives to milk, or in other words milk substitutes.
- these drinks can also have a more milky aromatic note than a drink not including said protein, which is an undeniable advantage for the manufacture of plant-based alternatives. with milk.
- the protein content in these products can vary widely and can also be a high protein drink.
- the quantity of protein can range for example from 1 to 12% by dry mass relative to the total mass of the drink, in particular from 3 to 10% relative to the total mass of the drink.
- the drinks can be of any type and include plant-based alternatives to milk or milk substitutes, including “barista” type milks or even “coffee creamers”.
- They may also be other beverages, acidic or not, ready to drink such as carbonated drinks (including, but not limited to, carbonated soft drinks), non-carbonated drinks (including, but not limited to, limited to non-carbonated soft drinks such as flavored waters, fruit juices and sweetened or unsweetened tea or coffee-based drinks), alcoholic drinks such as beers or strong alcohols, smoothies , beverage concentrates (including, but not limited to, liquid concentrates and syrups as well as non-liquid “concentrates”, such as freeze-dried and/or powdered preparations or “powder mixes”).
- carbonated drinks including, but not limited to, carbonated soft drinks
- non-carbonated drinks including, but not limited to, limited to non-carbonated soft drinks such as flavored waters, fruit juices and sweetened or unsweetened tea or coffee-based drinks
- alcoholic drinks such as beers or strong alcohols
- smoothies beverage concentrates (including, but not limited to, liquid concentrates and syrups as well as non-liquid “concentrates”, such as freeze-dried and/or
- pea protein of the invention is that its use instead of conventional pea proteins makes it possible to reduce this quantity of flavor or masking agent, or even makes it possible to completely remove these constituents from the drink, while while maintaining a very satisfying taste for the drink.
- Beverages may also include hydrocolloids; however, as pea protein provides a smoother texture, it is possible to reduce or even eliminate the content of hydrocolloid agents while maintaining a smooth texture in the mouth.
- Food products which may be affected include bakery products such as bread products (including, but not limited to, leavened and unleavened breads, sandwich breads, yeast breads and breads without yeast such as baking soda breads), breads comprising all types of wheat flour, breads comprising all types of flour other than wheat (such as potato flour, rice flour, barley, spelled and rye), gluten-free breads; mixtures for the preparation of said bread products; sweet baked goods (including, but not limited to, rolls, cakes, pies, pastries, waffles, crepes, muffins, pancakes, and cookies); mixtures for the preparation of said sweet bakery products; pie fillings and other sweet fillings (including but not limited to fruit pie fillings and nutty pie fillings such as pecan pie fillings, as well as cookie fillings, cakes, pastries, confectionery products and others, such as cream fillings); snack bars (including, but not limited to, energy, cereal, nut, and/or fruit bars).
- bread products including, but not
- 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 cream ice cream - and frozen non-dairy desserts such as non-dairy ice cream, sorbet and others).
- Other products conventionally prepared from animal milk can also include the pea protein of the invention to form substitutes.
- These may be products acidified and/or fermented with ferments, for example lactic, vegan or mesophilic ferments.
- This may include yogurt (including, but not limited to, full-fat, reduced-fat and fat-free yogurt, which may be milk protein-free and lactose-free).
- yogurt also includes white cheeses and petit suisses.
- cheese substitutes such as spreadable, processed, cooked and uncooked pressed cheeses, soft cheeses, filata cheeses, blue-veined cheeses; These can be Emmental, string cheese, ricotta, provolone, parmesan, munster, mozzarella, monterey jack, Manchego, blue, fontina, feta, edam, double Gloucester, camembert, Cheddar, brie, asiago and Havarti. It can also be other products such as vegetable butters or crème Letter.
- the pea proteins of the invention can be incorporated into confectionery products (including, but not limited to, gummies, soft candies, hard candies, chocolates, caramels and the erasers) ; sweetened and unsweetened breakfast cereals (including, but not limited to, extruded cereals, flaked cereals and puffed cereals); and cereal coating compositions for the preparation of breakfast cereals. They may also include sweetened spreads (including, but not limited to, jellies, jams, nut butters such as peanut butter, spreads and other spreads).
- pea proteins of the invention can also be used as a support or in flavor encapsulation.
- Pea protein can also be used, possibly after texturing, in meat substitutes such as emulsified sausages or hamburgers, or even fish or seafood substitutes. It can also be used in formulations egg replacement or for the manufacture of protein products such as tofu or tempeh.
- textured proteins we generally mean proteins textured by extrusion, that is to say 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.
- Food products or drinks can in particular be used in specialized nutrition, for example for specific populations, for example for babies or infants, children, adolescents, adults, the elderly, athletes, people suffering from an illness. These may include meal replacement nutritional formulas, complete nutritional drinks, for example for weight management or even in clinical nutrition (for example tube feeding or enteral nutrition).
- Pea protein can be used as the sole source of protein, but can also be used in combination with other additional plant or animal proteins. These additional proteins may be hydrolyzed or non-hydrolyzed. Generally, these additional proteins come in the form of concentrates or isolates.
- the term "vegetable 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, selected in the same family or in different families.
- legume we generally mean the family of dicotyledonous plants of the order Fabales.
- legumes are important cultivated plants including soya, beans including mung bean, chickpea, faba bean, peanut, cultivated lentil, cultivated alfalfa, various clovers, broad beans, carob, licorice and lupine.
- the additional legume protein can be chosen from these legumes or even be a pea protein than that of the invention.
- the term "cereals” refers to cultivated plants of the grass family producing edible grains, for example wheat, oats, rye, barley, corn, sorghum or rice.
- Tubers can be carrots, cassava, konjac, potatoes, Jerusalem artichokes, sweet potatoes.
- Oilseed plants are generally plants that produce seeds from which oil is extracted.
- Oilseed 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 association 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 features.
- Pea protein can also be used for the manufacture of pharmaceutical products or even in fermentation, for example for the production of fungal metabolites or metabolites by cell culture.
- Example 1 Pea protein according to the invention
- the screw speed is set so that the peas pass through the blancher in 3 minutes and the temperature remains stable during this period.
- Water was added at the outlet of the blancher 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 the grinding, so as to obtain a suspension of ground peas of approximately 20% dry matter at a temperature of approximately 35 °C.
- Suspension of crushed peas was adjusted to pH 8.5 by adding sodium hydroxide continuously and online.
- the crushed pea suspension was cooled to approximately 10°C by passing it through a plate exchanger and then transferred to a stirred storage tank. This suspension of crushed peas fed a centrifugal decanter (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 stirring tank and then heat treated by injection of steam at 74°C into a GEA skid for approximately 3 seconds, after a first step of immediate preheating by passage in a plate exchanger.
- the protein fraction was then instantly cooled (“flash cooling”) to 67°C.
- the heat-treated protein fraction was passed through a Flottweg Z3 centrifugal decanter.
- 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 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 cooled instantly by flash cooling to approximately 75°C.
- This pea protein floc was passed through a high pressure homogenizer at 200 bars and then atomized in a TGE brand nozzle atomizer.
- the recovered pea protein powder was then analyzed.
- Example 2 Pea protein according to the invention
- the screw speed is set so that the peas pass through the blancher in 3 minutes and the temperature remains stable during this period.
- Water was added at the outlet of the blancher 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 the grinding, so as to obtain a suspension of ground peas of approximately 20% dry matter at a temperature of approximately 35 °C.
- the crushed pea suspension was adjusted to pH 8.5 by adding sodium hydroxide continuously and online. There Suspension of crushed peas was cooled to approximately 10°C by passing through a plate exchanger and then transferred to a stirred storage tank. This suspension of crushed peas fed a centrifugal decanter (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 stirring tank and then heat treated by injection of steam at 74°C into a GEA skid for approximately 3 seconds, after a first step of immediate preheating by passage in a plate exchanger.
- the protein fraction was then cooled immediately by rapid cooling (“flash cooling”) to 67°C.
- the heat-treated protein fraction was passed through a Flottweg Z3 centrifugal decanter.
- the protein sediment (the underflow) recovered was diluted in hot water (80°C) so that it could be pumped. This sediment was then immediately adjusted to a dry matter 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 cooled by flash cooling to approximately 75°C. This protein floc was atomized in a TGE brand nozzle atomizer.
- peas 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 husk and the pea seed) and dehulling (sorting the outer husk 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, the temperature of which is regulated at a temperature of 7°C.
- the peas are separated from the aqueous solution by filtration through a sieve of which 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.
- still grinding at maximum speed add 2.7 L of demineralized water over a period of 3 minutes.
- the grinding is continued for a period of 0.5 minutes.
- the supernatant, concentrating the proteins, is adjusted to pH5 then heated at 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 in order to be able to correct its pH to 7 with hydrochloric acid. This floc is then freeze-dried.
- a pea protein containing 81% protein/DM and 95% DM is obtained.
- 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 2 criteria.
- the vegetable alternatives to milk of the invention have an excellent texture and a satisfactory color.
- the plant-based alternative to milk of the invention has fewer pea aromatic notes, less astringency and bitterness than plant-based alternatives made with commercial pea proteins.
- 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 milk protein. invention.
- Powder mix (“Powder mix”)
- pea protein of the invention is evaluated as well as the commercial pea protein NUTRALYS® S85F (ROQUETTE® Frées) also in the powder mixture recipe.
- the powder mixture made with the protein of Example 1 has a milky note identified as the most important by the panel. It also has a pleasant, smoother appearance in the mouth than the powdered mixture made from commercial pea protein.
- the pea protein of the invention is evaluated as well as the commercial pea protein NUTRALYS® S85F (ROQUETTE® Frées) as well.
- the cheeses both have a significant melting capacity, a characteristic sought after for this type of application.
- the ability of the cheeses to be grated is excellent in both cases, the protein of the invention allowing it to be grated in a longer form than in the case of the commercial protein.
- the cheeses of the invention presented an improved taste compared to that prepared from 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.
- the yogurt without texturizer of the invention has a flexible or even liquid texture. It appears creamier and smoother than yogurt without texturizer made from commercial protein.
- a vegetable sausage model is made by following the following recipe:
- the preserves are reheated in hot water (100°C for 20 minutes).
- a mixture of powders is produced and consists of 3% potato starch, 5% ROQUETTE® I50M pea fiber as well as 92% pea protein, the proportions being given by weight.
- the pea proteins tested are those of Example 1, Example 2 as well as the commercial pea protein NUTRALYS® F85M.
- This mixture is introduced by gravity into a LEISTRITZ ZSE 27MAXX extruder from the LEISTRITZ company.
- the mixture is introduced with 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%.
- thermoregulated die model FDK750 from the Coperion brand, comprising two modules of length 80 cm and passage section 50 mm x 15 mm, the 2nd module of which is thermoregulated at 30°C;
- the extrusion screw is rotated at a speed equal to 350 rpm and sends the mixture into the die.
- the textured protein thus produced is cut at the outlet of the die into 10 cm strips.
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Abstract
Description
Claims
Priority Applications (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP23731092.5A EP4514140A1 (fr) | 2022-06-03 | 2023-06-05 | Proteines de pois presentant un arome lacte |
| CA3257766A CA3257766A1 (fr) | 2022-06-03 | 2023-06-05 | Pea proteins having a milky flavor |
| CN202380047604.9A CN119384226A (zh) | 2022-06-03 | 2023-06-05 | 具有奶味的豌豆蛋白质 |
| US18/871,346 US20250325000A1 (en) | 2022-06-03 | 2023-06-05 | Pea proteins having a milky flavor |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FR2205390 | 2022-06-03 | ||
| FR2205390A FR3136144A1 (fr) | 2022-06-03 | 2022-06-03 | Proteines de pois presentant un univers aromatique lacte |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2023232295A1 true WO2023232295A1 (fr) | 2023-12-07 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/EP2023/025265 Ceased WO2023232295A1 (fr) | 2022-06-03 | 2023-06-05 | Proteines de pois presentant un arome lacte |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US20250325000A1 (fr) |
| EP (1) | EP4514140A1 (fr) |
| CN (1) | CN119384226A (fr) |
| CA (1) | CA3257766A1 (fr) |
| FR (1) | FR3136144A1 (fr) |
| WO (1) | WO2023232295A1 (fr) |
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|---|---|---|---|---|
| US4022919A (en) | 1975-02-14 | 1977-05-10 | The Griffith Laboratories, Limited | Removal of bitter flavor from pea flour |
| EP1400537A1 (fr) | 2002-09-18 | 2004-03-24 | Roquette FrÀ¨res | Procédé d'extraction des composants de la farine de pois |
| WO2007017572A1 (fr) * | 2005-08-05 | 2007-02-15 | Roquette Freres | Composition de proteines de pois |
| WO2015071499A1 (fr) | 2013-11-18 | 2015-05-21 | Cosucra Groupe Warcoing S.A. | Procédé d'extraction de protéines de pois |
| WO2017120597A1 (fr) | 2016-01-07 | 2017-07-13 | Ripple Foods, Pbc | Succédanés de produit ou constituants de tels succédanés et procédés pour les fabriquer |
| WO2019053387A1 (fr) | 2017-09-15 | 2019-03-21 | Roquette Freres | Protéines de pois dont la flaveur est améliorée, procédé de fabrication et utilisations industrielles |
| WO2019158589A1 (fr) | 2018-02-14 | 2019-08-22 | Endeco Gmbh | Procédé et dispositif pour la décomposition de légumineuses |
| WO2019233920A1 (fr) | 2018-06-07 | 2019-12-12 | Dsm Ip Assets B.V. | Utilisation de peptidylarginine déiminase pour obtenir un aliment amélioré |
| WO2020240144A1 (fr) | 2019-05-29 | 2020-12-03 | Roquette Freres | Proteine de legumineuse co-atomisee a flaveur reduite |
| WO2020260841A1 (fr) | 2019-06-28 | 2020-12-30 | Roquette Freres | Procédé de production de protéine de légumineuse |
| WO2021174226A1 (fr) | 2020-02-28 | 2021-09-02 | Impossible Foods Inc. | Substances et procédés pour la production de protéines |
| US20210401022A1 (en) | 2020-06-24 | 2021-12-30 | Puris Proteins, LLC | Non-soy, legume, protein material and method of making such |
-
2022
- 2022-06-03 FR FR2205390A patent/FR3136144A1/fr active Pending
-
2023
- 2023-06-05 US US18/871,346 patent/US20250325000A1/en active Pending
- 2023-06-05 EP EP23731092.5A patent/EP4514140A1/fr active Pending
- 2023-06-05 CA CA3257766A patent/CA3257766A1/fr active Pending
- 2023-06-05 WO PCT/EP2023/025265 patent/WO2023232295A1/fr not_active Ceased
- 2023-06-05 CN CN202380047604.9A patent/CN119384226A/zh active Pending
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| Publication number | Priority date | Publication date | Assignee | Title |
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| US4022919A (en) | 1975-02-14 | 1977-05-10 | The Griffith Laboratories, Limited | Removal of bitter flavor from pea flour |
| EP1400537A1 (fr) | 2002-09-18 | 2004-03-24 | Roquette FrÀ¨res | Procédé d'extraction des composants de la farine de pois |
| WO2007017572A1 (fr) * | 2005-08-05 | 2007-02-15 | Roquette Freres | Composition de proteines de pois |
| WO2015071499A1 (fr) | 2013-11-18 | 2015-05-21 | Cosucra Groupe Warcoing S.A. | Procédé d'extraction de protéines de pois |
| WO2017120597A1 (fr) | 2016-01-07 | 2017-07-13 | Ripple Foods, Pbc | Succédanés de produit ou constituants de tels succédanés et procédés pour les fabriquer |
| WO2019053387A1 (fr) | 2017-09-15 | 2019-03-21 | Roquette Freres | Protéines de pois dont la flaveur est améliorée, procédé de fabrication et utilisations industrielles |
| WO2019158589A1 (fr) | 2018-02-14 | 2019-08-22 | Endeco Gmbh | Procédé et dispositif pour la décomposition de légumineuses |
| WO2019233920A1 (fr) | 2018-06-07 | 2019-12-12 | Dsm Ip Assets B.V. | Utilisation de peptidylarginine déiminase pour obtenir un aliment amélioré |
| WO2020240144A1 (fr) | 2019-05-29 | 2020-12-03 | Roquette Freres | Proteine de legumineuse co-atomisee a flaveur reduite |
| WO2020260841A1 (fr) | 2019-06-28 | 2020-12-30 | Roquette Freres | Procédé de production de protéine de légumineuse |
| WO2021174226A1 (fr) | 2020-02-28 | 2021-09-02 | Impossible Foods Inc. | Substances et procédés pour la production de protéines |
| US20210401022A1 (en) | 2020-06-24 | 2021-12-30 | Puris Proteins, LLC | Non-soy, legume, protein material and method of making such |
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Also Published As
| Publication number | Publication date |
|---|---|
| EP4514140A1 (fr) | 2025-03-05 |
| CA3257766A1 (fr) | 2023-12-07 |
| US20250325000A1 (en) | 2025-10-23 |
| FR3136144A1 (fr) | 2023-12-08 |
| CN119384226A (zh) | 2025-01-28 |
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