WO2017127927A1 - Produit protéique a base de légumes secs à ph ajusté - Google Patents

Produit protéique a base de légumes secs à ph ajusté Download PDF

Info

Publication number
WO2017127927A1
WO2017127927A1 PCT/CA2017/050081 CA2017050081W WO2017127927A1 WO 2017127927 A1 WO2017127927 A1 WO 2017127927A1 CA 2017050081 W CA2017050081 W CA 2017050081W WO 2017127927 A1 WO2017127927 A1 WO 2017127927A1
Authority
WO
WIPO (PCT)
Prior art keywords
solution
protein
pulse protein
product
pulse
Prior art date
Application number
PCT/CA2017/050081
Other languages
English (en)
Inventor
Kevin I. Segall
Martin Schweizer
Original Assignee
Burcon Nutrascience (Mb) Corp.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority claimed from US15/006,312 external-priority patent/US11134705B2/en
Application filed by Burcon Nutrascience (Mb) Corp. filed Critical Burcon Nutrascience (Mb) Corp.
Priority to US16/071,603 priority Critical patent/US20190075819A1/en
Publication of WO2017127927A1 publication Critical patent/WO2017127927A1/fr

Links

Classifications

    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • 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
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
    • A21D13/00—Finished or partly finished bakery products
    • A21D13/06—Products with modified nutritive value, e.g. with modified starch content
    • A21D13/064—Products with modified nutritive value, e.g. with modified starch content with modified protein content
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • A21D2/264—Vegetable proteins
    • A21D2/266—Vegetable proteins from leguminous or other vegetable seeds; from press-cake or oil bearing seeds
    • 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 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
    • A23C11/06—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing non-milk proteins
    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/426—Addition of proteins, carbohydrates or fibrous material from vegetable origin other than sugars or sugar alcohols
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
    • A23L2/52—Adding ingredients
    • A23L2/66—Proteins

Definitions

  • the present invention relates to pH-adjusted pulse protein products, preferably isolates.
  • the pulse protein product is formed by a method which comprises:
  • steps (f) alternatively from steps (b) to (e), optionally, diluting and then adjusting the pH of the combined aqueous pulse protein solution and residual pulse protein source to a pH of about 1.5 to about 4.4, preferably about 2 to about 4, then separating the acidified, preferably clear, pulse protein solution from residual pulse protein source,
  • the low pH of the pulse protein products may not be ideal for other food applications, for example, foods having a neutral or near neutral pH.
  • the protein product already in a neutral or near neutral form.
  • Commercial pulse protein products are commonly provided at neutral or near neutral pH.
  • the optionally concentrated and optionally diafiltered aqueous protein solution resulting from the aforementioned US Patent Applications Nos. 13/103,528, 13/289,264, 13/556,357 and 13/642,003 or a solution prepared by rehydrating dried pulse protein product from the process of the aforementioned US Patent Applications Nos. 13/103,528, 13/289,264, 13/556,357 and 13/642,003 is adjusted to a pH in the range of about 6 to about 8, preferably about 6.5 to about 7.5 and either the resulting product is dried or any precipitate which forms is separated and dried.
  • the pH adjusted solution may be heat treated and then the resulting product dried or any precipitate which forms is separated and dried.
  • the heat treatment step serves to modify the functional properties of the protein product, namely lowering the solubility of the protein and increasing the water binding capacity of the material.
  • the pulse protein products provided herein have a clean flavour and are useful in food applications under neutral or near neutral conditions.
  • the pH adjusted pulse protein products of the present invention have a cleaner flavour than conventional pulse protein products and can replace the conventional pulse protein products in various food products, including the types mentioned above, to provide food products having improved flavour.
  • the pH adjusted pulse protein products of the present invention are also highly useful in food and beverage applications having a pH of between about 6 and about 8 such as dairy analogue products, dairy alternative products and products that are dairy/plant ingredient blends.
  • the pH adjusted pulse protein products of the present invention are particularly useful in dairy analogue or dairy alternative beverages which are formulated and prepared to have organoleptic and/or nutritional properties similar to cow's milk.
  • Such beverages are typically prepared at a pH of about 7 to about 7.5, typically contain protein, optionally contain fat which is stabilized against separation by a homogenization step and optionally contain added vitamins and minerals.
  • the acidic pulse protein product prepared by the process of the aforementioned US Patent Applications Nos.
  • a method of producing the pulse protein product which comprises:
  • the pulse protein solution produced according to the procedure of above-noted US Patent Applications may be processed to produce the pH-adjusted pulse protein products provided herein. Accordingly, in a further aspect of the present invention, there is provided a method of producing the pulse protein product , which comprises:
  • the heat treatment of the pH-adjusted solution generally is effected at a temperature of about 70° to about 160°C for about 2 seconds to about 60 minutes, preferably about 80° to about 120°C for about 15 seconds to about 15 minutes, more preferably about 85° to about 95°C for about 1 to about 5 minutes.
  • Providing the pulse protein product with a neutral pH of about 6 to about 8 facilitates the use of the product in applications having neutral or near neutral pH, eliminating the need to include in the application formulation, pH elevating ingredients to counteract the low pH of the pulse protein product.
  • the pulse protein products presented herein have a clean flavour and are useful in food applications under neutral or near neutral conditions.
  • pulse protein isolates having a protein content of at least about 90 wt% (N x 6.25) on a dry weight basis (d.b.), preferably at least about 100 wt%
  • pulse protein products of lesser purity may be provided and used having similar properties to the pulse protein isolate.
  • Such lesser purity products may have a protein concentration of at least about 60 wt% (N x 6.25) d.b.
  • the pulse protein products provided herein are novel. Accordingly, in another aspect of the present invention, there is provided a pulse protein product having a protein content of at least about 60 wt%, preferably at least about 90 wt%, more preferably at least about 100 wt%, (N x 6.25) on a dry weight basis (d.b.) having a natural pH in aqueous solution of about 6 to about 8, preferably about 6.5 to about 7.5 and which lacks the characteristic flavours of current commercial pulse protein products.
  • the invention includes a food composition comprising the pulse protein product provided herein.
  • the pulse protein product having a protein content of at least about 60 wt% (N x 6.25) d.b., with a natural pH in aqueous solution of about 6 to about 8 and which has a clean flavour has a phytic acid content of less than about 1.5 wt%, preferably less than about 0.5 wt%.
  • a pulse protein product having a protein content of at least about 60 wt% (N x 6.25) d.b., having a molecular weight profile, determined by the method described in Example 15, which is:
  • a pulse protein product having a protein content of at least about 60 wt% (N x 6.25) d.b., having a viscosity reading for a 10% protein w/w solution thereof in water, which is less than about 30 cP, as determined by the method described in Example 17.
  • the pulse protein product produced according to the process herein lacks the characteristic green and/or beany and/or vegetable flavours of current commercial pulse protein products and is suitable for use in a wide variety of conventional applications of protein products, including but not limited to protein fortification of processed foods and beverages, emulsification of oils, as a body former in baked goods and foaming agent in products which entrap gases.
  • the pulse protein product may be formed into protein fibers, useful in meat analogs and may be used as an egg white substitute or extender in food products where egg white is used as a binder.
  • the pulse protein product may also be used in nutritional supplements.
  • the pulse protein product may also be used in dairy analogue or dairy alternative products or products that are dairy/plant ingredient blends. Other uses of the pulse protein product are in pet foods, animal feed and in industrial and cosmetic applications and in personal care products.
  • the initial step of the process of providing the pulse protein products involves solubilizing pulse protein from a pulse protein source.
  • the pulses to which the invention may be applied include, but are not limited to lentils, chickpeas, dry peas and dry beans.
  • the pulse protein source may be pulses or any pulse product or by-product derived from the processing of pulses.
  • the pulse protein source may be a flour prepared by grinding an optionally dehulled pulse.
  • the pulse protein source may be a protein-rich pulse fraction formed by dehulling and grinding a pulse and then air classifying the dehulled and ground material into starch-rich and protein-rich fractions.
  • the pulse protein product recovered from the pulse protein source may be the protein naturally occurring in pulses or the proteinaceous material may be a protein modified by genetic manipulation but possessing characteristic hydrophobic and polar properties of the natural protein.
  • Protein solubilization from the pulse protein source material is effected most conveniently using calcium chloride solution, although solutions of other calcium salts, may be used. In addition, other alkaline earth metal compounds may be used, such as magnesium salts. Further, extraction of the pulse protein from the pulse protein source may be effected using calcium salt solution in combination with another salt solution, such as sodium chloride. Additionally, extraction of the pulse protein from the pulse protein source may be effected using water or other salt solution, such as sodium chloride, with calcium salt subsequently being added to the aqueous pulse protein solution produced in the extraction step. Precipitate formed upon addition of the calcium salt is removed prior to subsequent processing.
  • concentration of the calcium salt solution increases, the degree of solubilization of protein from the pulse protein source initially increases until a maximum value is achieved. Any subsequent increase in salt concentration does not increase the total protein solubilized.
  • concentration of calcium salt solution which causes maximum protein solubilization varies depending on the salt concerned. It is usually preferred to utilize a concentration value less than about 1.0 M, and more preferably a value of about 0.10 to about 0.15 M.
  • the salt solubilization of the protein is effected at a temperature of from about ⁇ to about 100°C, preferably about 15°C to about 65°C, more preferably about 20° to about 35°C, preferably accompanied by agitation to decrease the solubilization time, which is usually about 1 to about 60 minutes. It is preferred to effect the solubilization to extract substantially as much protein from the pulse protein source as is practicable, so as to provide an overall high product yield.
  • the extraction of the protein from the pulse protein source is carried out in any manner consistent with effecting a continuous extraction of protein from the pulse protein source.
  • the pulse protein source is continuously mixed with the calcium salt solution and the mixture is conveyed through a pipe or conduit having a length and at a flow rate for a residence time sufficient to effect the desired extraction in accordance with the parameters described herein.
  • the salt solubilization step is effected in a time of about 1 minute to about 60 minutes, preferably to effect solubilization to extract substantially as much protein from the pulse protein source as is practicable.
  • the solubilization in the continuous procedure is effected at temperatures between about 1° and about 100°C, preferably between about 15°C and about 65°C, more preferably between about 20° and about 35°C.
  • the extraction is generally conducted at a pH of about 4.5 to about 11, preferably about 5 to about 7.
  • the pH of the extraction system may be adjusted to any desired value within the range of about 4.5 to about 11 for use in the extraction step by the use of any convenient food grade acid, usually hydrochloric acid or phosphoric acid, or food grade alkali, usually sodium hydroxide, as required.
  • the concentration of pulse protein source in the calcium salt solution during the solubilization step may vary widely. Typical concentration values are about 5 to about 15% w/v.
  • the protein extraction step with the aqueous salt solution has the additional effect of solubilizing fats which may be present in the pulse protein source, which then results in the fats being present in the aqueous phase.
  • the protein solution resulting from the extraction step generally has a protein concentration of about 5 to about 50 g/L, preferably about 10 to about 50 g/L.
  • the aqueous calcium salt solution may contain an antioxidant.
  • the antioxidant may be any convenient antioxidant, such as sodium sulfite or ascorbic acid.
  • the quantity of antioxidant employed may vary from about 0.01 to about 1 wt% of the solution, preferably about 0.05 wt%.
  • the antioxidant serves to inhibit oxidation of any phenolics in the protein solution.
  • the aqueous phase resulting from the extraction step then may be separated from the residual pulse protein source, in any convenient manner, such as by employing a decanter centrifuge, followed by disc centrifugation and/or filtration, to remove residual pulse protein source material.
  • the separation step may be conducted at any temperature within the range of about 1° to about 100°C, preferably about 15° to about 65°C, more preferably about 50° to about 60°C.
  • the optional dilution and acidification steps described below may be applied to the mixture of aqueous pulse protein solution and residual pulse protein source, with subsequent removal of the residual pulse protein source material by the separation step described above.
  • the separated residual pulse protein source may be dried for disposal or further processed, such as to recover starch and/or residual protein.
  • Residual protein may be recovered by re-extracting the separated residual pulse protein source with fresh calcium salt solution and the protein solution yielded upon clarification combined with the initial protein solution for further processing as described below.
  • the separated residual pulse protein source may be processed by a conventional isoelectric precipitation process or any other convenient procedure to recover residual protein.
  • the aqueous pulse protein solution may be treated with an anti-foamer, such as any suitable food-grade, non-silicone based anti-foamer, to reduce the volume of foam formed upon further processing.
  • an anti-foamer such as any suitable food-grade, non-silicone based anti-foamer
  • the quantity of anti-foamer employed is generally greater than about 0.0003% w/v.
  • the anti-foamer in the quantity described may be added in the extraction steps.
  • the separated aqueous pulse protein solution may be subject to a defatting operation, if required, as described in US Patents Nos. 5,844,086 and 6,005,076, assigned to the assignee hereof and the disclosures of which are incorporated herein by reference.
  • defatting of the separated aqueous pulse protein solution may be achieved by any other convenient procedure.
  • the aqueous pulse protein solution may be treated with an adsorbent, such as powdered activated carbon or granulated activated carbon, to remove colour and/or odour compounds.
  • an adsorbent such as powdered activated carbon or granulated activated carbon
  • Such adsorbent treatment may be carried out under any convenient conditions, generally at the ambient temperature of the separated aqueous protein solution.
  • powdered activated carbon an amount of about 0.025% to about 5% w/v, preferably about 0.05% to about 2% w/v, is employed.
  • the adsorbing agent may be removed from the pulse protein solution by any convenient means, such as by filtration.
  • the resulting aqueous pulse protein solution may be diluted with water generally with about 0.1 to about 10 volumes, preferably about 0.5 to about 2 volumes, in order to decrease the conductivity of the aqueous pulse protein solution to a value of generally below about 105 mS, preferably about 4 to about 21 mS.
  • Such dilution is usually effected using water, although dilute salt solutions, such as sodium chloride or calcium chloride, having a conductivity up to about 3 mS, may be used.
  • the water with which the pulse protein solution is mixed generally has the same temperature as the pulse protein solution, but the water may have a temperature of about 1° to about 100°C, preferably about 15° to about 65°C, more preferably about 50° to about 60°C.
  • the optionally diluted pulse protein solution then is adjusted in pH to a value of about 1.5 to about 4.4, preferably about 2 to about 4, by the addition of any suitable food grade acid, such as hydrochloric acid or phosphoric acid, to result in an acidified aqueous pulse protein solution, preferably a clear acidified aqueous pulse protein solution.
  • the acidified aqueous pulse protein solution has a conductivity of generally below about 110 mS for a diluted pulse protein solution, or generally below about 115 mS for an undiluted pulse protein solution, in both cases preferably about 4 to about 26 mS.
  • the aqueous pulse protein solution and the residual pulse protein source material may be optionally diluted and acidified together and then the acidified aqueous pulse protein solution is clarified and separated from the residual pulse protein source material by any convenient technique as discussed above.
  • the acidified aqueous pulse protein solution may optionally be defatted, optionally treated with an adsorbent and optionally treated with defoamer as described above.
  • the acidified aqueous pulse protein solution may be subjected to a heat treatment to inactivate heat labile anti-nutritional factors, such as trypsin inhibitors, present in such solution as a result of extraction from the pulse protein source material during the extraction step.
  • a heating step also provides the additional benefit of reducing the microbial load.
  • the protein solution is heated to a temperature of about 70° to about 160°C, preferably about 80° to about 120°C, more preferably about 85° to about 95°C, for about 10 seconds to about 60 minutes, preferably about 10 seconds to about 5 minutes, more preferably about 30 seconds to about 5 minutes.
  • the heat treated acidified pulse protein solution then may be cooled for further processing as described below, to a temperature of about 2° to about 65°C, preferably about 50°C to about 60°C.
  • the optionally diluted, acidified and optionally heat treated pulse protein solution is not transparent it may be clarified by any convenient procedure, such as filtration or centrifugation.
  • the resulting acidified aqueous pulse protein solution may be adjusted to a pH of about 6 to about 8, preferably about 6.5 to about 7.5, as described below, optionally further processed as described below and then dried to produce a pulse protein product.
  • the acidified aqueous pulse protein solution may be processed prior to the pH adjustment step.
  • the acidified aqueous pulse protein solution may be concentrated to increase the protein concentration thereof while maintaining the ionic strength thereof substantially constant. Such concentration generally is effected to provide a concentrated pulse protein solution having a protein concentration of about 50 to about 300 g/L, preferably about 100 to about 200 g/L.
  • the concentration step may be effected in any convenient manner consistent with batch or continuous operation, such as by employing any convenient selective membrane technique, such as ultrafiltration or diafiltration, using membranes, such as hollow-fibre membranes or spiral-wound membranes, with a suitable molecular weight cutoff, such as about 1,000 to about 1,000,000 Daltons, preferably about 1,000 to about 100,000 Daltons, having regard to differing membrane materials and configurations, and, for continuous operation, dimensioned to permit the desired degree of concentration as the aqueous protein solution passes through the membranes.
  • any convenient selective membrane technique such as ultrafiltration or diafiltration
  • membranes such as hollow-fibre membranes or spiral-wound membranes
  • a suitable molecular weight cutoff such as about 1,000 to about 1,000,000 Daltons, preferably about 1,000 to about 100,000 Daltons
  • the low molecular weight species include not only the ionic species of the salt but also low molecular weight materials extracted from the source material, such as carbohydrates, pigments, low molecular weight proteins and anti- nutritional factors, such as trypsin inhibitors, which are themselves low molecular weight proteins.
  • the molecular weight cut-off of the membrane is usually chosen to ensure retention of a significant proportion of the protein in the solution, while permitting contaminants to pass through having regard to the different membrane materials and configurations.
  • the concentrated pulse protein solution then may be subjected to a diafiltration step using water or a dilute saline solution.
  • the diafiltration solution may be at its natural pH or at a pH equal to that of the protein solution being diafiltered or at any pH value in between.
  • Such diafiltration may be effected using from about 1 to about 40 volumes of diafiltration solution, preferably about 2 to about 25 volumes of diafiltration solution.
  • further quantities of contaminants are removed from the aqueous pulse protein solution by passage through the membrane with the permeate. This purifies the aqueous protein solution and may also reduce its viscosity.
  • the diafiltration operation may be effected until no significant further quantities of contaminants and visible colour are present in the permeate or until the retentate has been sufficiently purified so as, when pH adjusted, optionally further processed then dried, to provide a pulse protein isolate with a protein content of at least about 90 wt% (N x 6.25) d.b.
  • Such diafiltration may be effected using the same membrane as for the concentration step.
  • the diafiltration step may be effected using a separate membrane with a different molecular weight cut-off, such as a membrane having a molecular weight cut-off in the range of about 1,000 to about 1,000,000 Daltons, preferably about 1,000 to about 100,000 Daltons, having regard to different membrane materials and configuration.
  • the diafiltration step may be applied to the acidified aqueous protein solution prior to concentration or to partially concentrated acidified aqueous protein solution. Diafiltration may also be applied at multiple points during the concentration process. When diafiltration is applied prior to concentration or to the partially concentrated solution, the resulting diafiltered solution may then be additionally concentrated. The viscosity reduction achieved by diafiltering multiple times as the protein solution is concentrated may allow a higher final, fully concentrated protein concentration to be achieved.
  • the concentration step and the diafiltration step may be effected herein in such a manner that the pulse protein product subsequently recovered contains less than about 90 wt% protein (N x 6.25) d.b., such as at least about 60 wt% protein (N x 6.25) d.b.
  • N x 6.25) d.b. wt% protein
  • This protein solution may then be pH adjusted, optionally further processed as described below and dried to provide a pulse protein product with lower levels of purity.
  • An antioxidant may be present in the diafiltration medium during at least part of the diafiltration step.
  • the antioxidant may be any convenient antioxidant, such as sodium sulfite or ascorbic acid.
  • the quantity of antioxidant employed in the diafiltration medium depends on the materials employed and may vary from about 0.01 to about 1 wt%, preferably about 0.05 wt%. The antioxidant serves to inhibit the oxidation of any phenolics present in the pulse protein solution.
  • the optional concentration step and the optional diafiltration step may be effected at any convenient temperature, generally about 2° to about 65°C, preferably about 50° to about 60°C, and for the period of time to effect the desired degree of concentration and diafiltration.
  • the temperature and other conditions used to some degree depend upon the membrane equipment used to effect the membrane processing, the desired protein concentration of the solution and the efficiency of the removal of contaminants to the permeate.
  • pulses contain anti-nutritional trypsin inhibitors.
  • the level of trypsin inhibitor activity in the final pulse protein product can be controlled by the manipulation of various process variables.
  • heat treatment of the acidified aqueous pulse protein solution may be used to inactivate heat-labile trypsin inhibitors.
  • the partially concentrated or fully concentrated acidified aqueous pulse protein solution may also be heat treated to inactivate heat labile trypsin inhibitors.
  • the heat treatment is applied to the partially concentrated acidified pulse protein solution, the resulting heat treated solution may then be additionally concentrated.
  • the concentration and/or diafiltration steps may be operated in a manner favorable for removal of trypsin inhibitors in the permeate along with the other contaminants. Removal of the trypsin inhibitors is promoted by using a membrane of larger pore size, such as 30,000 to 1,000,000 Da, operating the membrane at elevated temperatures, such as about 30° to about 65°C, preferably about 50° to about 60°C and employing greater volumes of diafiltration medium, such as 10 to 40 volumes.
  • Acidifying and membrane processing the pulse protein solution at a lower pH, such as 1.5 to 3, may reduce the trypsin inhibitor activity relative to processing the solution at higher pH, such as 3 to 4.4. Further, a reduction in trypsin inhibitor activity may be achieved by exposing pulse materials to reducing agents that disrupt or rearrange the disulfide bonds of the inhibitors. Suitable reducing agents include sodium sulfite, cysteine and N-acetylcysteine.
  • the addition of such reducing agents may be effected at various stages of the overall process.
  • the reducing agent may be added with the pulse protein source material in the extraction step, may be added to the clarified aqueous pulse protein solution following removal of residual pulse protein source material, may be added to the diafiltered retentate before or after pH adjustment or may be dry blended with the dried pulse protein product.
  • the addition of the reducing agent may be combined with the heat treatment step and membrane processing steps, as described above.
  • the optionally concentrated and optionally diafiltered protein solution may be subject to a further defatting operation, if required, as described in US Patents Nos. 5,844,086 and 6,005,076.
  • defatting of the optionally concentrated and optionally diafiltered protein solution may be achieved by any other convenient procedure.
  • the optionally concentrated and optionally diafiltered aqueous protein solution may be treated with an adsorbent, such as powdered activated carbon or granulated activated carbon, to remove colour and/or odour compounds.
  • an adsorbent such as powdered activated carbon or granulated activated carbon
  • Such adsorbent treatment may be carried out under any convenient conditions, generally at the ambient temperature of the protein solution.
  • powdered activated carbon an amount of about 0.025% to about 5% w/v, preferably about 0.05% to about 2% w/v, is employed.
  • the adsorbent may be removed from the pulse protein solution by any convenient means, such as by filtration.
  • a pasteurization step may be effected on the pulse protein solution prior to pH adjustment.
  • Such pasteurization may be effected under any desired pasteurization conditions.
  • the optionally concentrated and optionally diafiltered pulse protein solution is heated to a temperature of about 55° to about 70°C, preferably about 60° to about 65°C, for about 30 seconds to about 60 minutes, preferably about 10 minutes to about 15 minutes.
  • such pasteurization may be carried out at about 70 to about 85°C for about 10 to about 60 seconds.
  • the pasteurized pulse protein solution may then be cooled for further processing, preferably to a temperature of about 25° to about 40°C.
  • the acidified aqueous pulse protein solution, the partially concentrated pulse protein solution or the concentrated pulse protein solution described above, following optional dilution with about 0.1 to about 6 volumes of water, preferably about 1 to about 4 volumes of water, may be adjusted to a pH about 6 to about 8, preferably about 6.5 to about 7.5.
  • the entire sample then may be dried or any precipitated solids may be collected by centrifugation and only these dried to form the product.
  • the pH 6 to 8 solution may be heated to a temperature of about 70° to about 160°C, for about 2 seconds to about 60 minutes, preferably about 80° to about 120°C, for about 15 seconds to about 15 minutes, more preferably about 85° to about 95°C, for about 1 to about 5 minutes, prior to drying the entire sample or collecting any precipitated solids by centrifugation and drying these to form the product.
  • the acidified aqueous pulse protein solution may be adjusted in pH to about 6 to about 8, preferably about 6.5 to about 7.5 prior to the optional concentration and optional diafiltration steps above.
  • the pH adjusted protein solution resulting from the optional concentration and optional diafiltration steps may then be dried or centrifuged to collect any insoluble pulse protein material, which may be dried.
  • the pH adjusted protein solution resulting from the optional concentration and optional diafiltration steps may be heat treated and then dried or centrifuged to collect any insoluble pulse protein material, which may be dried.
  • the acidified aqueous pulse protein solution is dried without any pH adjustment.
  • the dried pulse protein product then may be redissolved in water and the pH of the resulting acidic aqueous solution is raised to a pH of about 6 to about 8, preferably 6.5 to about 7.5, in any convenient manner, such as by the use of aqueous sodium hydroxide solution, prior to drying.
  • any precipitate formed on adjustment of the pH to about 6 to about 8 is recovered by centrifugation and these solids are dried to yield a pulse protein product.
  • the pH 6 to 8 solution may be heated to a temperature of about 70°C to about 160°C, for about 2 seconds to about 60 minutes, preferably about 80° to about 120°C, for about 15 seconds to about 15 minutes, more preferably about 85° to about 95°C, for about 1 to about 5 minutes, prior to drying the entire sample, or in yet another alternative procedure, recovering by centrifugation and drying only any insoluble solids present in the heat treated sample.
  • the dry pulse protein product has a protein content of at least about 60 wt% (N x 6.25) d.b.
  • the dry pulse protein product is an isolate with a high protein content, in excess of about 90 wt% protein, preferably at least about 100 wt% protein (N x 6.25) d.b.
  • the remaining soluble protein fraction may also be processed to form a pulse protein product.
  • the soluble fraction may be dried directly or may be further processed by membrane concentration and/or diafiltration and/or heat treatment prior to drying.
  • pea protein concentrate prepared by air classifying flour made by grinding yellow split peas
  • 300 L of 0.15 M CaCl 2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution.
  • the residual solids were removed by centrifugation to produce 262 L of centrate having a protein content of 3.47 % by weight.
  • This centrate was added to 317 L of water and the pH of the sample lowered to 3.27 with HCl that had been diluted with an equal volume of water.
  • the diluted and acidified centrate was further clarified by filtration to provide a protein solution with a protein content of 1.23% by weight.
  • the filtered protein solution was reduced in volume from 583 L to 60 L by concentration on a PES membrane, having a molecular weight cutoff of 10,000 Daltons, operated at a temperature of about 56°C. At this point the acidified protein solution, with a protein content of 10.14% by weight, was diafiltered with 600 L of RO water, with the diafiltration operation conducted at about 59°C. The resulting diafiltered solution had a weight of 58.36 kg and a protein content of 9.16% by weight.
  • a 18.86 kg sample of the concentrated protein solution which represented a yield of 24.1% of the filtered protein solution, was diluted with 18.92 kg of water and then treated with an aqueous sodium hydroxide solution to raise the pH of the sample to 7.00 and a precipitate formed.
  • a 1 kg aliquot of the pH adjusted sample was centrifuged at 6,500 g and the precipitate collected and freeze dried to form a product called YP03-L07-11A YP701N having a protein content of 106.33 wt% (N x 6.25) on a dry weight basis.
  • the remainder of the pH adjusted sample was spray dried and then freeze dried to further reduce the moisture content and to form a product called YP03-L07-11A YP701N2 having a protein content of 102.02 wt% (N x 6.25) on a dry weight basis.
  • This Example is another illustration of the preparation of a pH adjusted pea protein isolate.
  • the filtered protein solution was reduced in volume from 470 L to 66 L by concentration on a polyethersulfone (PES) membrane, having a molecular weight cutoff of 10,000 Daltons, operated at a temperature of approximately 58°C.
  • PES polyethersulfone
  • the protein solution, with a protein content of 4.75 wt % was diafiltered with 132 L of RO water, with the diafiltration operation conducted at approximately 59°C.
  • the diafiltered protein solution was then concentrated to 28 L and diafiltered with an additional 140 L of RO water, with the diafiltration operation conducted at approximately 60°C.
  • the concentrated protein solution, having a protein content of 10.13 wt% was diluted with RO water to a protein content of 4.58 wt%.
  • This Example contains an evaluation of the solubility in water of the pea protein isolates produced by the methods of Examples 1 and 2. Protein solubility was evaluated using a modified version of the procedure of Morr et al., J. Food Sci. 50: 1715- 1718.
  • This Example contains an evaluation of the water binding capacity of the pea protein isolates produced by the methods of Examples 1 and 2.
  • Protein powder (1 g) was weighed into centrifuge tubes (50 ml) of known weight. To this powder was added approximately 20 ml of reverse osmosis purified (RO) water at the natural pH. The contents of the tubes were mixed using a vortex mixer at moderate speed for 1 minute. The samples were incubated at room temperature for 5 minutes then mixed with the vortex mixer for 30 seconds. This was followed by incubation at room temperature for another 5 minutes followed by another 30 seconds of vortex mixing. The samples were then centrifuged at 1,000 g for 15 minutes at 20°C. After centrifugation, the supernatant was carefully poured off, ensuring that all solid material remained in the tube. The centrifuge tube was then re-weighed and the weight of water saturated sample was determined.
  • RO reverse osmosis purified
  • WBC Water binding capacity
  • WBC (ml/g) (mass of water saturated sample - mass of initial sample)/(mass of initial sample x total solids content of sample)
  • This Example contains an evaluation of the phytic acid content of the protein products prepared as described in Examples 1 and 2. Phytic acid content was determined using the method of Latta and Eskin (J. Agric. Food Chem, 28: 1313-1315). The YP03-L07-11A YP701N2 was tested after spray drying but prior to the freeze drying step.
  • This Example illustrates the preparation of a pulse protein isolate by conventional isoelectric precipitation.
  • the washed precipitate was then collected by centrifugation. A total of 30.68 kg of washed precipitate was obtained with a protein content of 22.55 wt%. This represented a yield of 81.9% of the protein in the clarified extract solution.
  • An aliquot of 15.34 kg of the washed precipitate was combined with 15.4 kg of RO water and then the pH of the sample adjusted to about 7 with sodium hydroxide solution. The pH adjusted sample was then spray dried to yield an isolate with a protein content of 90.22% (N x 6.25) d.b.
  • the product was designated YP12-K13-12A conventional IEP pH 7.
  • This Example is a sensory evaluation of the YP03-L07-12A YP701N product prepared as described in Example 1 with the conventional pea protein isolate product prepared as described in Example 6.
  • Samples were presented for sensory evaluation as a 2% protein w/v dispersion in purified drinking water. A small amount of food grade sodium hydroxide solution was incorporated when preparing the samples so that the pH of each was 7. Samples were presented blindly to an informal panel of 7 panelists who were asked to identify which sample had a cleaner flavour and which sample they preferred the flavour of.
  • This Example is a sensory evaluation of the YP03-L07-12A YP701N2 product prepared as described in Example 1 with the conventional pea protein isolate product prepared as described in Example 6.
  • Samples were presented for sensory evaluation as a 2% protein w/v dispersion in purified drinking water. A small amount of food grade sodium hydroxide solution was incorporated when preparing the samples so that the pH of each was 7. Samples were presented blindly to an informal panel of 7 panelists who were asked to identify which sample had a cleaner flavour and which sample they preferred the flavour of.
  • This Example is a sensory evaluation of the YP07-C20-12A YP701N2 product prepared as described in Example 2 with the conventional pea protein isolate product prepared as described in Example 6.
  • Samples were presented for sensory evaluation as a 2% protein w/v dispersion in purified drinking water. A small amount of food grade sodium hydroxide solution was incorporated when preparing the samples so that the pH of each was 7. Samples were presented blindly to an informal panel of 6 panelists who were asked to identify which sample had a cleaner flavour and which sample they preferred the flavour of.
  • This Example describes the production of a dairy alternative beverage using the product of Example 2 or Nutralys S85F (Roquette America Inc., Keokuk, IA), a commercial pea protein isolate recommended for use in applications including dairy-type products.
  • Example 10 This Example is a sensory evaluation of the dairy alternative beverages produced in Example 10.
  • This Example is another illustration of the preparation of pH adjusted pea protein isolates.
  • the fine residual solids were removed by centrifugation using a disc stack centrifuge to produce 'k' L of centrate having a protein content of T % by weight and a conductivity of 'm' mS.
  • 'n' L of centrate was combined with ⁇ ' L of RO water and the pH of the sample lowered to 'p' with HC1 that had been diluted with an equal volume of water, 'q' L of acidified protein solution was clarified using a Membralox ceramic microfiltration membrane, having a pore size of 0.80 um, operated at about 'r' °C until 's' L of permeate (clarified, acidified protein solution) was collected.
  • the ' protein solution, having a protein content of 'u' wt% was reduced in volume from 'v' L to 'w' L by concentration on a polyethersulfone (PES) membrane, having a molecular weight cutoff of 1,000 daltons, operated at a temperature of approximately 'x' °C.
  • PES polyethersulfone
  • the protein solution, with a protein content of 'y' wt% was diafiltered with 'z' L of RO water, with the diafiltration operation conducted at approximately 'aa' °C.
  • the diafiltered protein solution was then concentrated to 'ab' kg at about 'ac' °C.
  • the concentrated protein solution having a protein content of 'ad' wt% represented a yield of 'ae' wt% of the ' protein solution
  • 'af kg of the concentrated protein solution was diluted with 'ag' L RO water and then adjusted in pH to 'ah' with 'ai' solution and then an aliquot spray dried to yield a product found to have a protein content of 'aj ' wt% (N x 6.25) d.b.
  • the product was given designation 'ak' YP701N2.
  • This Example is another illustration of the preparation of pH adjusted pea protein isolates.
  • the acidified protein solution having a protein content of 'f % by weight, was reduced in volume from 'g' L to 'h' L by concentration on a polyethersulfone membrane, having a molecular weight cut-off of 1,000 daltons, operated at a temperature of about 'i' °C.
  • the protein solution with a protein content of 'j ' wt% was diafiltered with 'k' L of RO water, with the diafiltration operation conducted at about T °C.
  • the diafiltered protein solution was then further concentrated to 'm' L, the resulting protein solution having a protein content of 'n' wt%, represented a yield of ⁇ ' wt% of the acidified protein solution.
  • the concentrated and diafiltered protein solution was pasteurized at about 72°C for 16 seconds then 'p' kg of the pasteurized, concentrated and diafiltered protein solution was diluted with 'q' L of RO water and adjusted in pH to 'r' with NaOH/KOH solution, 's' of the pH adjusted sample was then spray dried to yield a product found to have a protein content of 't' wt% (N x 6.25) d.b.
  • the product was given designation 'u' YP701N2.
  • the parameters 'a' to 'u' are set forth in the following Table 6. Table 6 - Parameters for the production of the pH adjusted pea protein isolates
  • This Example contains an evaluation of the phytic acid content of protein products produced as described in Examples 12 and 13. Phytic acid content was determined using the method of Latta and Eskin (J. Agric. Food Chem., 28: 1313-1315).
  • Example 15 This Example illustrates the molecular weight profile of the pulse protein products prepared as described in Examples 1, 2 and 12 as well as the molecular weight profile of some commercial yellow pea protein products (Pisane C9 (Cosucra Groupe Warcoing S.A., Belgium), Pea Protein YS 85% (The Scoular Company, Minneapolis, MN (manufactured by Yantai Shuangta Food Co., LTD, Jinling Town, Zhaoyuan City, Shangdong province, China) and Empro E86 (Emsland Group, Emlichheim, Germany). These protein products are among the most highly purified pea protein ingredients currently commercially available.
  • a standard curve was prepared using a Biorad protein standard (Biorad product #151-1901) containing proteins with known molecular weights between 17,000 Daltons (myoglobulin) and 670,000 Daltons (thyroglobulin) with Vitamin B12 added as a low molecular weight marker at 1,350 Daltons.
  • a 0.9 % w/v solution of the protein standard was prepared in water, filtered with a 0.45 um pore size filter disc then a 50 aliquot run on the column using a mobile phase of 0.05M phosphate/0.15M NaCl, pH 6 containing 0.02% sodium azide. The mobile phase flow rate was 1 mL/min and components were detected based on absorbance at 280 nm. Based on the retention times of these molecules of known molecular weight, a regression formula was developed relating the natural log of the molecular weight to the retention time in minutes.
  • the above regression formula relating molecular weight and retention time was used to calculate retention times that corresponded to molecular weights of 100,000 Da, 15,000 Da, 5,000 Da and 1,000 Da.
  • the HPLC ProStar system was used to calculate the peak areas lying within these retention time ranges and the percentage of protein ((range peak area/total protein peak area) x 100) falling in a given molecular weight range was calculated. Note that the data was not corrected by protein response factor.
  • This Example contains an evaluation of the colour in solution and the haze level of solutions of the pulse products prepared according Examples 1, 2, 12 and 13 as well as the commercial pea protein products Propulse (Nutri-Pea, Portage la Prairie, MB), Nutralys S85F (Roquette America, Inc., Keokuk, IA), Pisane C9 (Cosucra Groupe Warcoing, S.A., Belgium), Pea Protein YS 85% (The Scoular Company, Minneapolis, MN (manufactured by Yantai Shuangta Food Co., LTD, Jinling Town, Zhaoyuan City, Shangdongzhou, China), HarvestPro Pea Protein 85 (Glanbia Nutritionals, Inc., Fitchburg, WI) and Empro E86 (Emsland Group, Emlichheim, Germany).
  • Propulse Nutri-Pea, Portage la Prairie, MB
  • Nutralys S85F Rosucra Groupe Warcoing, S.A., Belgium
  • Solutions of the protein products were prepared by dissolving sufficient protein powder to supply 0.48 g of protein in 15 ml of RO water.
  • the pH of the solutions was measured with a pH meter and the colour and haze level assessed using a HunterLab ColorQuest XE instrument operated in transmission mode. The results are shown in the following Table 9.
  • This Example contains an evaluation of the viscosity in solution of the pulse products prepared according Examples 12 and 13 as well as the commercial pea protein products Nutralys S85F (Roquette America, Inc., Keokuk, IA), HarvestPro Pea Protein 85 (Glanbia Nutritionals, Inc., Fitchburg, WI) and Empro E86 (Emsland Group, Emlichheim, Germany).
  • the pulse protein products of the present invention provided 10% protein w/w solutions having lower viscosity than 10% protein w/w solutions of the commercial pulse protein products evaluated.
  • the present invention provides procedures for producing pulse protein products with neutral or near neutral pH values that can substitute for conventional pulse protein products in a variety of food application. Modifications are possible within the scope of this invention.

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Nutrition Science (AREA)
  • Biochemistry (AREA)
  • Molecular Biology (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • General Health & Medical Sciences (AREA)
  • Peptides Or Proteins (AREA)

Abstract

La présente invention concerne une solution aqueuse d'un produit protéique à base de légumes secs présentant une teneur en protéines d'au moins environ 60 % en poids (N x 6,25) en poids sec, qui est soluble en milieux aqueux à un pH inférieur à environ 4,4 et thermostable dans cette plage de pH, dont le pH est ajusté à un pH compris entre environ 6 et environ 8. Le produit obtenu est ensuite traité par séchage du produit, récupération et séchage de toute la matière protéique de légumes secs précipitée, traitement thermique puis séchage du produit, ou traitement thermique du produit et récupération et séchage de toute la matière protéique de légumes secs précipitée.
PCT/CA2017/050081 2012-07-10 2017-01-26 Produit protéique a base de légumes secs à ph ajusté WO2017127927A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
US16/071,603 US20190075819A1 (en) 2012-07-10 2017-01-26 Ph adjusted pulse protein product

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US15/006,312 US11134705B2 (en) 2012-07-10 2016-01-26 pH adjusted pulse protein product
US15/006,312 2016-01-26

Publications (1)

Publication Number Publication Date
WO2017127927A1 true WO2017127927A1 (fr) 2017-08-03

Family

ID=59396949

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/CA2017/050081 WO2017127927A1 (fr) 2012-07-10 2017-01-26 Produit protéique a base de légumes secs à ph ajusté

Country Status (1)

Country Link
WO (1) WO2017127927A1 (fr)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2020256908A1 (fr) * 2019-06-18 2020-12-24 Corn Products Development, Inc. Émulsifiants protéiques d'impulsion
WO2021174017A1 (fr) * 2020-02-26 2021-09-02 Eat Just, Inc. Isolation de protéines de légume sec par ultrafiltration

Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5520935A (en) * 1991-03-07 1996-05-28 Novo Nordisk A/S Method for production of pea protein hydrolyzate
WO2012015303A1 (fr) * 2010-07-28 2012-02-02 Unifine Food & Bake Ingredients B.V. Agent de glaçage pour produits de boulangerie
WO2014008578A1 (fr) * 2012-07-10 2014-01-16 Burcon Nutrascience (Mb) Corp. Produit protéique à base de légumes secs à ph régulé
WO2014008580A1 (fr) * 2012-07-09 2014-01-16 Burcon Nutrascience (Mb) Corp. Mélanges de dessert congelés utilisant des produits de protéine de légumineuse
WO2014190418A1 (fr) * 2013-05-30 2014-12-04 Burcon Nutrascience (Mb) Corp. Production de produits de protéine de légumes secs dotés d'une astringence réduite
WO2016015151A1 (fr) * 2014-07-28 2016-02-04 Burcon Nutrascience (Mb) Corp. Préparation de produits de protéines de légumineuses ("yp810")

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5520935A (en) * 1991-03-07 1996-05-28 Novo Nordisk A/S Method for production of pea protein hydrolyzate
WO2012015303A1 (fr) * 2010-07-28 2012-02-02 Unifine Food & Bake Ingredients B.V. Agent de glaçage pour produits de boulangerie
WO2014008580A1 (fr) * 2012-07-09 2014-01-16 Burcon Nutrascience (Mb) Corp. Mélanges de dessert congelés utilisant des produits de protéine de légumineuse
WO2014008578A1 (fr) * 2012-07-10 2014-01-16 Burcon Nutrascience (Mb) Corp. Produit protéique à base de légumes secs à ph régulé
WO2014190418A1 (fr) * 2013-05-30 2014-12-04 Burcon Nutrascience (Mb) Corp. Production de produits de protéine de légumes secs dotés d'une astringence réduite
WO2016015151A1 (fr) * 2014-07-28 2016-02-04 Burcon Nutrascience (Mb) Corp. Préparation de produits de protéines de légumineuses ("yp810")

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2020256908A1 (fr) * 2019-06-18 2020-12-24 Corn Products Development, Inc. Émulsifiants protéiques d'impulsion
WO2021174017A1 (fr) * 2020-02-26 2021-09-02 Eat Just, Inc. Isolation de protéines de légume sec par ultrafiltration

Similar Documents

Publication Publication Date Title
US10021896B2 (en) Production of pulse protein product with reduced astringency
CA2878482C (fr) Produit proteique a base de legumes secs a ph regule
US10327456B2 (en) pH adjusted soy protein isolate and uses
US20230240322A1 (en) Preparation of pulse protein products ("yp810")
AU2013284306B2 (en) Soy protein product with neutral or near neutral pH ("S701N2")
WO2020061698A1 (fr) Produit de protéines de légumineuse à ph ajusté
US11134705B2 (en) pH adjusted pulse protein product
US20230345966A1 (en) Soy protein product with neutral or near neutral ph ("s701n2")
WO2017127927A1 (fr) Produit protéique a base de légumes secs à ph ajusté
US20190021364A1 (en) Ph adjusted pulse protein product

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 17743522

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 17743522

Country of ref document: EP

Kind code of ref document: A1