WO2023166491A1 - Fonctionnalisation alcaline de compositions de protéines à base de plantes - Google Patents

Fonctionnalisation alcaline de compositions de protéines à base de plantes Download PDF

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Publication number
WO2023166491A1
WO2023166491A1 PCT/IB2023/052018 IB2023052018W WO2023166491A1 WO 2023166491 A1 WO2023166491 A1 WO 2023166491A1 IB 2023052018 W IB2023052018 W IB 2023052018W WO 2023166491 A1 WO2023166491 A1 WO 2023166491A1
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WIPO (PCT)
Prior art keywords
plant
casein
protein
protein isolate
animal
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PCT/IB2023/052018
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English (en)
Inventor
Jochen Weiss
Hanna Salminen
Laura SCHEUER
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University Of Hohenheim
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Publication of WO2023166491A1 publication Critical patent/WO2023166491A1/fr

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    • 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
    • A23L19/00—Products from fruits or vegetables; Preparation or treatment thereof
    • 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
    • A23C20/00—Cheese substitutes
    • 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
    • A23J1/008—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from microorganisms
    • 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
    • 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
    • A23J3/04—Animal proteins
    • A23J3/08—Dairy proteins
    • A23J3/10—Casein
    • 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
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/20—Proteins from microorganisms or unicellular algae
    • 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
    • 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
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/185—Vegetable proteins

Definitions

  • compositions suitable for use in food products comprising one or more plant protein isolates having fiber structures analogous to animal proteins, methods of making plant protein fiber networks, and methods of use thereof, wherein the compositions provide textures to the food products comparable to animal-based food products.
  • the present disclosure is based, at least in part, on the discovery that plant proteins, in contrast to animal proteins, undergo reversable structural changes under alkaline conditions.
  • the alkaline environment causes the multimeric structure of plant proteins to solubilize into functionalized, reactive proteins capable of reforming into network of fiber structures ⁇ similar to that of animal proteins.
  • the present disclosure provides novel compositions suitable for use in food products wherein the compositions herein have textures comparable to an animalbased food product.
  • compositions provided herein may comprise at least one plant protein isolate.
  • compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution.
  • compositions disclosed herein may form reactive plant proteins when stored in an alkaline buffer solution. Reactive plant proteins may form fiber structures and/or networks analogous to animal proteins in the alkaline buffer solution and/or after the alkaline buffer solution is neutralized.
  • An alkaline buffer solution may be neutralized by reducing the pH of the buffer solution, adding one or more additional proteins, or a combination thereof.
  • Reducing the pH of the buffer solution may be performed in one or more series of steps, wherein each step comprises titrating the buffer solution to a pH lower than the pH resulting from the step proceeding it.
  • an additional protein added to the reactive plant proteins may be an animal protein, a plant protein, or a combination thereof.
  • the additional protein added to the reactive plant proteins may be a hydrolysate of an animal protein, of a plant protein, or a combination thereof.
  • compositions herein may comprise at least one plant protein isolate wherein the total concentration of the at least one plant protein isolate may be at least about 1% w/w. In some embodiments, compositions herein may comprise at least one plant protein isolate wherein the total concentration of the at least one plant protein isolate may be about 1% w/w to about 20% w/w.
  • compositions herein may comprise an alkaline buffer solution having a pH equal to or higher than about 11. In some embodiments, compositions herein may comprise an alkaline buffer solution that can comprise water. In some embodiments, compositions herein may comprise an alkaline buffer solution that can comprise at least about 1 % w/w water. In some embodiments, compositions herein may comprise an alkaline buffer solution that can comprise about 1% w/w to about 99% w/w water.
  • compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution for at least about 1 hour. In some embodiments, compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution for at least about 1 hour to at least about 48 hours.
  • compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution at a temperature of at least about 4 °C. In some embodiments, compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution at a temperature of about 4 °C to about 140 °C. In some embodiments, compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may be stored in an alkaline buffer solution at a temperature of about 20 °C to about 30 °C.
  • compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may comprise a natural protein isolate, a recombinant protein isolate, or any combination thereof. In some embodiments, compositions herein may comprise at least one plant protein isolate wherein the at least one plant protein isolate may comprise one or more proteins present in a crude plant material. In some embodiments, compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material can comprise vegetables, fruits, seeds, legumes, grains, or any combination thereof. In some embodiments, compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material may comprise pulses.
  • compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material may comprise legumes.
  • compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material may comprise chickpeas, green peas, yellow peas, black eyed peas, pinto beans, kidney beans, black beans, mung beans, soybeans, adzuki beans, fava beans, edamame, green lentils, red lentils, black lentils, lupins, peanuts, or any combination thereof.
  • compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material may comprise peas.
  • compositions herein may comprise one or more proteins present in a crude plant material wherein the crude plant material may comprise yellow peas.
  • compositions herein may comprise at least one plant protein isolate stored in an alkaline buffer solution wherein the at least one plant protein isolate can comprise at least about 10% reactive protein. In some embodiments, compositions herein may comprise at least one plant protein isolate stored in an alkaline buffer solution wherein the at least one plant protein isolate can comprise about 10% to about 100% reactive protein.
  • compositions comprising a plant-based fiber structure herein may comprise at least one plant protein isolate stored at a pH equal to or higher than about 11. In some embodiments, compositions comprising a plant-based fiber structure herein may comprise at least one pea protein isolate stored at a pH equal to or higher than about 11. In some embodiments, compositions comprising a plant-based fiber structure herein may comprise at least one pea protein isolate stored at a pH equal to or higher than about 11 for about 12 hours to about 48 hours.
  • compositions comprising a plant-based fiber structure herein may be in a solid structure. In some embodiments, compositions comprising a plant-based fiber structure herein may be a gel. In some embodiments, compositions comprising a plant-based fiber structure herein may be in a solid structure that resembles an animal-based food product. In accordance with these embodiments, an animal-based food product comprising a plant-based fiber structure herein may resemble an animal-based meat product, an animal-based dairy product, or any combination thereof.
  • plant-based fiber structures herein may comprise at least about 10% w/w moisture content. In some embodiments, plant-based fiber structures herein may comprise about 10% w/w to about 75% w/w moisture content.
  • plant-based fiber structures herein may comprise at least one fiber having a diameter of at least about 1.5 mm. In some embodiments, plant-based fiber structures herein may comprise at least one fiber having a diameter of about 1.5 mm to about 8 mm. In some embodiments, plant-based fiber structures herein may comprise at least one fiber having a length of at least about 2 mm. In some embodiments, plant-based fiber structures herein may comprise at least one fiber having a length of about 2 mm to about 40 mm.
  • compositions herein having a plant-based fiber structure may comprise at least one property of animal-based food product. In some embodiments, compositions herein having a plant-based fiber structure may comprise at least one property of animal-based food product selected from a group consisting of an animal-based meat product, an animal-based dairy product, or any combination thereof. In some embodiments, plant-based fiber structures herein may be in a solid structure with a water dispersion equal to that of an animal-based food product. In some embodiments, plant-based fiber structures herein may be in a solid structure with a tensile strength equal to that of an animal-based food product.
  • plant-based fiber structures herein may comprise an anisotropic structure.
  • compositions comprising a plant-based fiber structure herein may change form following alkalinization of the one or more plant proteins that comprises the plantbased fiber structure.
  • alkalinization of the one or more plant proteins that comprise the plant-based fiber structure herein may occur at a pH ranging from about 9 to about 12.
  • alkalinization of the one or more plant proteins that comprise the plant-based fiber structure herein may occur at a pH equal to or higher than about 11.
  • compositions comprising a plant-based fiber structure herein may change form after neutralizing the pH of the composition.
  • the pH of the composition may be neutralized at a pH ranging from about 6 to about 8.
  • compositions comprising a plant-based fiber structure herein may comprise at least one pea protein isolate, wherein the at least one pea protein isolate may comprise a natural pea protein or a recombinant pea protein.
  • compositions comprising a plant-based fiber structure herein may further comprise at least one other isolated protein.
  • compositions comprising a plant-based fiber structure herein may further comprise a casein protein.
  • compositions comprising a plant-based fiber structure herein may further comprise a casein protein wherein the casein protein may be isolated from an animal source.
  • compositions comprising a plant-based fiber structure herein may further comprise a casein protein wherein the casein protein may be prepared recombinantly in one or more non- animal sources.
  • one or more non-animal sources suitable for preparing recombinant proteins may comprise a genetically modified plant, a genetically modified bacteria, a genetically modified yeast, or any combination thereof.
  • one or more non-animal sources suitable for preparing recombinant proteins may comprise a genetically modified yeast.
  • the casein protein may comprise one or more casein or casein subunit proteins including one or more of a-casein, as 1 -casein, as2-casein, P-casein, K-casein, para-K-casein or any combination thereof.
  • At least one casein subunit may comprise one or more casein subunits that is free from or substantially free from one of the other subunits, for example comprising a-casein, K-casein (and/or para-K-casein), and/or a combination thereof, free, or substantially free of b-casein; alternatively, the casein subunit(s) may comprise a-casein, P-casein, and/or a combination thereof, free of K-casein or para-K-casein.
  • the present disclosure provides methods of making a plant-based fiber structure.
  • methods herein may comprise incubating at least one plant protein isolate stored in a buffer solution.
  • methods herein may comprise incubating at least one pea protein isolate stored in a buffer solution.
  • methods herein may comprise incubating at least one pea protein isolate stored in a buffer solution for at least 12 hours, wherein the buffer solution has a pH equal to or higher than about 11.
  • the least one pea protein isolate may be stored in a buffer solution for about 12 hours to about 48 hours.
  • at least one pea protein isolate may be stored in a buffer solution having a pH ranging from about 11 to about 14.
  • methods herein may comprise incubating at least one pea protein isolate stored in a buffer solution at a temperature of about 20 °C to about 30 °C.
  • methods of making a plant-based fiber structure may generate a plant-based fiber structure that can mimic at least one property of an animal-based food product comprising an animal-based meat product, an animal-based dairy product, or any combination thereof.
  • the least one property of an animal-based food product may comprise color, smell, taste, plasticity, breaking strength, mouth feel, or any combination thereof.
  • the current disclosure include a food product comprising: (a) at least one plant protein isolate stored in an alkaline buffer for at least 1 hr prior to incorporation into the food product; (b) a protein isolate selected from a casein protein isolate, a whey protein isolate, or a combination thereof; wherein the pH of the food product is between 6-8.
  • the food product is a meat replica selected from a meat, poultry or seafood replica.
  • the food product is a non-dairy milk product selected from a milk, yogurt, ice cream, butter, cheese.
  • the food product is a liquid or gel composition, selected from a beverage, stew, sauce, paste, spread, or soup.
  • the at least one plant protein isolate is a pea protein isolate.
  • the food product further comprises one or more of at an additional protein, a fat, a non-animal-based fat, non-animal- based matrixes, non-animal-based edible fibrous components, emulsifiers, plasticizers, thickeners, surfactants, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives, dietary fibers, gluten, and mixtures thereof.
  • the current disclosure also encompasses a method of making a food product, the method comprising: obtaining at least one plant protein isolate stored in an alkaline buffer for at least 1 hr; combining the plant protein isolate with a protein isolate selected from casein protein isolate, a whey protein isolate, or a combination thereof.
  • the food product is a meat replica selected from a meat, poultry or sea food replica.
  • the food product is a non-dairy milk product selected from a milk, yogurt, ice cream, butter, cheese.
  • the food product is a liquid or gel composition, selected from a beverage, stew, sauce, paste, spread, or soup.
  • the method further comprises combining the composition with one or more of an additional protein, a fat, a non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, emulsifiers, plasticizers, thickeners, surfactants, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives, dietary fibers, gluten, and mixtures thereof.
  • an additional protein e.g., a fat, a non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, emulsifiers, plasticizers, thickeners, surfactants, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives,
  • FIG. 1 are photographs of the pea protein isolate powder PISANE C9, the pea protein isolate powder PURIS Pea 870, micellar casein powder, a s -casein, and micellar casein concentrate.
  • Fig. 2 depicts a representative schematic of sample preparation according to storage times.
  • Fig. 3 depicts representative phase diagrams of PISANE C9, P-casein reduced micellar casein powder, and a mixture thereof wherein structure formation was assessed by visual appearance, in the first screening phase.
  • Fig. 4 depicts a representative schematic of sample preparation according to pH and storage times.
  • FIG. 5A depict representative images of a PISANE C9 solution immediately after pH adjustment to pH 11.
  • FIG. 5B depict representative images of a PISANE C9 solution after pH adjustment to pH 11 after 24 hours at 25 °C.
  • Fig. 6A depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder with 0 hr of mixing for both, wherein structure formation was assessed by visual appearance.
  • Fig. 6B depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6C depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6D depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6E depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6F depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6G depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 6H depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 61 depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7A depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder with 0 hr of mixing for both, wherein structure formation was assessed by visual appearance.
  • Fig. 7B depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7C depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7D depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7E depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7F depicts representative phase diagrams of a mixture of PISANE C9 and P-casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7G depicts representative phase diagrams of a mixture of PISANE C9 and P-casein P- casein reduced micellar casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 7H depicts representative phase diagrams of a mixture of PISANE C9 and P-casein P- casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 71 depicts representative phase diagrams of a mixture of PISANE C9 and a s -casein P- casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8A depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder with 0 hr of mixing for both, wherein structure formation was assessed by visual appearance.
  • Fig. 8B depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8C depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with no prior mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8D depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8E depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8F depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8G depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein P-casein reduced micellar casein powder, after addition of casein after 0 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 8H depicts representative phase diagrams of a mixture of PURIS Pea 870 and P-casein P-casein reduced micellar casein powder, after addition of casein after 24 hours of mixing and PISANE C9 with 24 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 81 depicts representative phase diagrams of a mixture of PURIS Pea 870 and a s -casein P-casein reduced micellar casein powder, after addition of casein after 48 hours of mixing and PISANE C9 with 48 hours of mixing, wherein structure formation was assessed by visual appearance.
  • Fig. 9A depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 with P-casein micellar casein powder, wherein structure formation was assessed by visual appearance.
  • Fig. 9B depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 with a s-casein powder, wherein structure formation was assessed by visual appearance.
  • Fig. 9C depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 with P-casein reduced micellar casein concentrate, wherein structure formation was assessed by visual appearance.
  • Fig. 10A depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 (10%) wherein structure formation was assessed by visual appearance.
  • Fig. 10B depicts representative images of structure formation and phase diagrams of mixtures of PURIS Pea 870 (10%), wherein structure formation was assessed by visual appearance.
  • FIG. 11A depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 with P-casein micellar casein powder, wherein structure formation was assessed by visual appearance.
  • Fig. 11B depicts representative images of structure formation and phase diagrams of mixtures of PISANE C9 with a s -casein powder, wherein structure formation was assessed by visual appearance.
  • Fig. 11C depicts representative images of structure formation and phase diagrams of mixtures of or PURIS Pea 870 with 0-casein micellar casein powder, wherein structure formation was assessed by visual appearance.
  • Fig. 12 depicts a representative schematic of sample preparation according to pH and storage times after acid hydrolysis of casein at pH 2.
  • Fig. 13A depicts representative phase diagrams of a mixture of PISANE C9 and casein concentrate after PISANE C9 was stored for 24 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13B depicts representative phase diagrams of a mixture of PISANE C9 and casein concentrate after PISANE C9 was stored for 48 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13C depicts representative phase diagrams of a mixture of PURIS Pea 870 and casein concentrate after PURIS Pea 870 was stored for 24 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13D depicts representative phase diagrams of a mixture of PURIS Pea 870 and casein concentrate after PURIS Pea 870 was stored for 48 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13E depicts representative phase diagrams of a mixture of PISANE C9 and casein powder after PISANE C9 was stored for 24 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13F depicts representative phase diagrams of a mixture of PISANE C9 and casein powder after PISANE C9 was stored for 48 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13G depicts representative phase diagrams of a mixture of PURIS Pea 870 and casein powder after PURIS Pea 870 was stored for 24 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 13H depicts representative phase diagrams of a mixture of PURIS Pea 870 and casein powder after PURIS Pea 870 was stored for 48 h at pH 2, wherein structure formation was assessed by visual appearance.
  • Fig. 14A depict representative phase diagrams of samples with previous acidification of casein at pH 2 for 48 hours, of PISANE C9 x micellar casein powder.
  • Fig. 14B depict representative phase diagrams of samples with previous acidification of PURIS Pea 870 x micellar casein powder.
  • Fig. 14C depict representative phase diagrams of samples with previous acidification of casein at pH 2 for 48 hours, of PISANE C9 x micellar casein concentrate.
  • Fig. 14D depict representative phase diagrams of samples with previous acidification of casein at pH 2 for 48 hours, of PURIS Pea 870 x micellar casein concentrate at pH 2-11.
  • Fig. 15A depict representative phase diagrams of samples with previous homogenization of both protein solutions and acidification of casein at pH 2 of PISANE C9 x micellar casein powder for 24 hours.
  • Fig. 15B depict representative phase diagrams of samples with previous homogenization of both protein solutions and acidification of casein at pH 2 of PISANE C9 x micellar casein powder for 48 hours.
  • Fig. 15C depict representative phase diagrams of samples with previous homogenization of both protein solutions and acidification of casein at pH 2 of PISANE C9 x micellar casein concentrate at pH 2-11 for 24 hours.
  • Fig. 15D depict representative phase diagrams of samples with previous homogenization of both protein solutions and acidification of casein at pH 2 of PISANE C9 x micellar casein concentrate at pH 2-11 for 48 hours.
  • Fig. 16A depicts representative microscopic images of samples of pea protein (PISANE C9) (10% w/w), a mixture of pea protein (5% w/w) and casein concentrate (5% w/w) and casein concentrate (5% w/w) (total protein content 10% w/w) stored at pH 2-6 for 0 to 24 hrs.
  • the scale bar is 200 pm.
  • Fig. 16B depicts representative microscopic images of samples of pea protein (PISANE C9) (10% w/w), a mixture of pea protein (5% w/w) and casein concentrate (5% w/w) and casein concentrate (5% w/w) (total protein content 10% w/w) stored at pH 7-11 for 0 to 24 hrs. The scale bar is 200 pm.
  • Fig. 17A depicts representative microscopic images of pea protein (PISANE C9) mixed with cis-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 17B depicts representative microscopic images of pea protein (PISANE C9) mixed with as-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 17C depicts representative microscopic images of pea protein (PISANE C9) mixed with as-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 17D depicts representative microscopic images of pea protein (PISANE C9) mixed with as-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 17E depicts representative microscopic images of pea protein (PISANE C9) mixed with as-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 17F depicts representative microscopic images of pea protein (PISANE C9) mixed with as-casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7- 11.
  • Fig. 18A depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 18B depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 18C depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 18D depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 18E depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 18F depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19A depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19B depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1 : 1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19C depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1:1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19D depicts representative microscopic images of pea protein (PISANE C9) mixed with p-casein reduced micellar casein powder at a ratio 1:1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19E depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1:1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 19F depicts representative microscopic images of pea protein (PISANE C9) mixed with P-casein reduced micellar casein powder at a ratio 1:1 (total protein content 10% w/w) for indicated times at pH ranges 7-11.
  • Fig. 20A depicts representative microscopic images of samples of micellar casein powder (5% w/w) mixed with pea protein (PISANE C9) (5% w/w) after being hydrolyzed at pH 2-4 for 24 hours and 48 hours at a ratio 1: 1 (total protein content 10% w/w).
  • the scale bar is 200 pm.
  • Fig. 20A depicts representative microscopic images of samples of micellar casein powder (5% w/w) mixed with pea protein (PISANE C9) (5% w/w) after being hydrolyzed at pH 4-8 for 24 hours and 48 hours at a ratio 1: 1 (total protein content 10% w/w).
  • the scale bar is 200 pm.
  • Fig. 20A depicts representative microscopic images of samples of micellar casein powder (5% w/w) mixed with pea protein (PISANE C9) (5% w/w) after being hydrolyzed at pH 8-11 for 24 hours and 48 hours at a ratio 1: 1 (total protein content 10% w/w).
  • the scale bar is 200 pm.
  • Fig. 21A depicts representative microscopic images of samples of micellar casein (5% w/w) mixed with pea protein (PURIS Pea 870) (5% w/w) after being hydrolyzed at pH 2-6 for 24 hours and 48 hours at a ratio 1: 1 (total protein content 10% w/w).
  • the scale bar is 200 pm.
  • Fig. 21B depicts representative microscopic images of samples of micellar casein (5% w/w) mixed with pea protein (PURIS Pea 870) (5% w/w) after being hydrolyzed at pH 7-11 for 24 hours and 48 hours at a ratio 1: 1 (total protein content 10% w/w).
  • the scale bar is 200 pm.
  • Fig. 22A depicts representative microscopic images of individual protein samples of pea protein isolate PISANE C9, pea protein isolate PURISpea 870, a s -casein powder, micellar casein powder, and casein concentrate respectively at indicated pH and storage time.
  • Fig. 22B depicts representative microscopic images of individual protein samples of pea protein isolate PISANE C9, pea protein isolate PURISpea 870, a s -casein powder, micellar casein powder, and casein concentrate respectively at indicated pH and storage time.
  • Fig. 22C depicts representative microscopic images of individual protein samples of pea protein isolate PISANE C9, pea protein isolate PURISpea 870, a s -casein powder, micellar casein powder, and casein concentrate respectively at indicated pH and storage time.
  • Plant proteins are mainly made of globular proteins which form multimers covalently linked together whereas animal (i.e. meat) proteins have a complex hierarchical construction of fibrous protein bundles. While animal proteins form flexible fibrous protein networks, the globular plant proteins are made up of polypeptide chains that fold into a densely packed shape. Because plant proteins cannot endogenously form fibrous protein networks like animal proteins, the plant proteins must be modified to undergo a structural change in order to reveal reactive side chains, thus allowing for novel protein-protein interactions to emerge. As used herein, plant proteins that undergo “a structural change” refer to a plant protein having a protein structure different than its native structure (e.g., globular protein structure).
  • a plant protein subjected to any of the methods disclosed herein may have a structural change in its primary protein structure, its secondary protein structure, its tertiary protein structure, its quaternary protein structure, or any combination thereof.
  • Modifications to the plant protein refers to methods resulting in changes in the protein structure. Such structural changes expose reactive proteins thereby creating new or improved functional properties that may mimic animal proteins. Such functional properties can include, but are not limited to gelation, solubility, thermal stability, emulsification, foamability, and the like. Examples of modifications to plant proteins may include, but are not limited to, physical, chemical, biological perturbations, or a combination thereof.
  • the present disclosure is based, at least in part, on the discovery that plant proteins undergo a structural change, especially in the alkaline range. As such, the present disclosure provides functionalized plant proteins with one or more improved or new functional properties resulting from chemical modification (i.e., alkalinization) of the plant protein.
  • supramolecular structures are formed in the acidic range (e.g. the casein micelle in milk, or the formation of fiber structure in meat after slightly acidifying and the addition of salt) so that the proteins become reactive. Solid products (sausage or cheese) result after heating. Plant proteins exist as pairs, trimers or hexamers, and due to their different chemical structure, do not dissolve in the acidic range, but instead dissolve at higher pH values, where they would thus produce reactive proteins.
  • the present disclosure demonstrates that plant proteins dissolved during storage in an alkaline buffer are capable of forming network structures before and after lowering the pH (i.e., neutralization).
  • the present disclosure thus provides compositions that form structures from plant extracts which are analogous to structures formed from animal proteins.
  • functionalized plant proteins disclosed herein may form proteinaceous networks that resemble an animal tissue, such an animal connective tissues and/or an animal muscle.
  • Functionalized plant proteins prepared as disclosed herein may form fibrous proteinaceous networks that mimic the fiber-like structures which contribute to the textural qualities of animalbased foods. Accordingly, the present disclosure also provides compositions suitable for use in plant-based food products having at least one property of an animal-based food product.
  • the term “about,” can mean relative to the recited value, e.g., amount, dose, temperature, time, percentage, etc., ⁇ 10%, ⁇ 9%, ⁇ 8%, ⁇ 7%, ⁇ 6%, ⁇ 5%, ⁇ 4%, ⁇ 3%, ⁇ 2%, or ⁇ 1%.
  • the terms “comprising,” “including,” “encompassing” and “having” are used interchangeably in this disclosure.
  • the terms “comprising,” “including,” “encompassing” and “having” mean to include, but not necessarily be limited to the things so described.
  • w/w refers to proportions by weight and means the ratio of the weight of one substance in a composition to the total weight of the composition, or the weight of one substance in the composition to the weight of another substance of the composition.
  • a reference to a composition that comprises plant protein totaling 10% w/w of the composition means that 10% of the composition's weight is composed of plant protein (e.g., such a composition having a weight of 100 mg would contain 10 mg of plant protein) and the remainder of the weight of the composition (e.g., 90 mg in this example) is composed of other ingredients.
  • nucleic acid refers to deoxyribonucleic acids (DNA) or ribonucleic acids (RNA) and polymers thereof in either single- or double-stranded form. Unless specifically limited, the term encompasses nucleic acids containing known analogues of natural nucleotides that have similar binding properties as the reference nucleic acid and are metabolized in a manner similar to naturally occurring nucleotides. Unless otherwise indicated, a particular nucleic acid sequence also implicitly encompasses conservatively modified variants thereof (e.g., degenerate codon substitutions), alleles, orthologs, SNPs, and complementary sequences as well as the sequence explicitly indicated.
  • DNA deoxyribonucleic acids
  • RNA ribonucleic acids
  • degenerate codon substitutions may be achieved by generating sequences in which the third position of one or more selected (or all) codons is substituted with mixed-base and/or deoxy inosine residues (Batzer et al., Nucleic Acid Res. 19:5081 (1991); Ohtsuka et al., J. Biol. Chem. 260:2605-2608 (1985); and Rossolini et al., Mol. Cell. Probes 8:91-98 (1994)).
  • peptide refers to a compound comprised of amino acid residues covalently linked by peptide bonds.
  • a protein or peptide must contain at least two amino acids, and no limitation is placed on the maximum number of amino acids that can comprise a protein's or peptide's sequence.
  • Polypeptides include any peptide or protein comprising two or more amino acids joined to each other by peptide bonds.
  • the term refers to both short chains, which also commonly are referred to in the art as peptides, oligopeptides and oligomers, for example, and to longer chains, which generally are referred to in the art as proteins, of which there are many types.
  • Polypeptides include, for example, biologically active fragments, substantially homologous polypeptides, oligopeptides, homodimers, heterodimers, variants of polypeptides, modified polypeptides, derivatives, analogs, fusion proteins, among others.
  • a polypeptide includes a natural peptide, a recombinant peptide, or a combination thereof.
  • “recombinant” refers to a cell, nucleic acid, protein, or vector, which has been modified due to the introduction of an exogenous nucleic acid or the alteration of a native nucleic acid.
  • compositions suitable for use in food products herein comprising have one or more plant-based fiber structures.
  • plant-based fiber structure includes a matrix of plant proteins. In the area of plant-based food products, the structure of proteins plays an essential role; however, plant proteins usually do not form network or fiber structures and are relatively unreactive, so that matrix formation to produce solid foods with interesting textures is presently problematic in the field.
  • plant-based fiber structures herein may comprise one or more plant proteins. Plant-based fiber structures disclosed herein may comprise one or more plant proteins wherein the one or more plant proteins may exist as pairs, trimers, hexamers, or any combination thereof.
  • Plant proteins for use in the plant-based fiber structures herein may be sourced from raw plant material.
  • the term “raw plant material” as used herein can refer to crude plant material that can be converted by processing according to the present disclosure into a new and useful product such as protein isolate containing proteins originally present in the crude plant material.
  • Raw plant materials may include material derived from plants.
  • the raw plant material may be sourced from a non-genetically modified, commoditized, hybridized, or genetically modified plant.
  • Raw plant materials can include, but are not limited to, vegetables, fruits, seeds, legumes, grains, or any combination thereof.
  • raw plant materials suitable for use herein may include soybeans, other beans, legumes, lentils, peas, and any combination thereof.
  • Non-limiting examples of legumes may include chickpea, green pea, yellow pea, black eyed peas, pinto bean, kidney bean, black bean, mung bean, soybean, adzuki bean, fava bean, edamame, green lentil, red lentil, black lentil, lupin, peanut, and combinations thereof.
  • Pulses may also be used herein as raw plant materials.
  • Exemplarily pulses include, non-soybean, non-peanut legumes, such as peas, beans, lentils, and chickpeas.
  • raw plant materials can include peas.
  • pea means the mostly small spherical seed of the pod fruit Pisum sativum.
  • Peas suitable for use herein may be from varieties of Pisum sativum.
  • Non-limiting examples of peas suitable for use herein may be field peas, yellow peas, green peas, and/or wrinkled peas that are grown to produce dry peas that are shelled from the mature pod.
  • peas suitable for use herein may be yellow peas.
  • plant proteins for use in the plant-based fiber structures herein may be a plant protein isolated from a plant material.
  • isolated or “isolating” may refer to a process which separates proteins from said protein comprising fraction.
  • any method of preparing a protein isolate from plant material known in the art is suitable for use herein.
  • Nonlimiting examples of preparing protein isolates from plants can include precipitation, flocculation, filtration, chromatography, alkali extraction/isoelectric precipitation (AE-IP), salt extractiondialysis (SE), micellar precipitation (MP), and the like.
  • Plant proteins for use in the plant-based fiber structures herein may be from a genetically modified non-animal source.
  • a genetically modified non-animal source may be a genetically modified plant, a genetically modified bacteria, a genetically modified yeast, or any combination thereof.
  • plant proteins herein may be recombinant plant proteins.
  • recombinant plant proteins refers to plant proteins recombinantly produced using polypeptide expression techniques (e.g., heterologous expression techniques using bacterial cells, insect cells, fungal cells such as yeast, plant cells such as tobacco, soybean, or Arabidopsis, or mammalian cells).
  • recombinant plant proteins herein may be a polypeptide encoded from a polynucleotide, wherein the polynucleotide may have an endogenous (i.e., wild-type) nucleic acid sequence for a plant protein derived from a plant source as described herein.
  • recombinant plant proteins disclosed herein may be isolated from proteins used in preparing the recombinant plant proteins. Non-limiting examples of preparing isolated recombinant plant proteins can include precipitation, filtration, chromatography, and the like.
  • the plant protein isolates herein may predominantly, but not exclusively comprise the plant protein of interest. Residual impurities may be present in such plant protein isolates. Residual impurities may include but are not limited to minerals, sugars, carbohydrates, and the like.
  • a plant protein isolate herein may comprise at least about 70 wt % plant proteins to at least about 99% wt % plant proteins.
  • a plant protein isolate herein may comprise at least about 70 wt %, at least about 75 wt %, at least about 80 wt %, at least about 85 wt %, at least about 90 wt %, at least about 95 wt %, or at least about 99 wt % plant proteins.
  • a plant protein isolate herein may comprise about 90 wt %, about 91 wt %, about 92 wt %, about 93 wt %, about 94 wt %, about 95 wt %, about 96 wt %, about 97 wt %, about 98 wt %, or about 99 wt % plant proteins.
  • a plant protein isolate (e.g., a pea protein isolate) disclosed herein may comprise at least about 40% dry weight plant protein to at least about 99% dry weight plant protein.
  • a plant protein isolate herein may comprise about 40% dry weight plant protein to about 99% dry weight plant protein, about 60% dry weight plant protein to about 99% dry weight plant protein, or about 60% dry weight plant protein to about 98% dry weight plant protein.
  • a plant protein isolate herein may comprise at least one plant protein with a molecular weight of less than about 100 Daltons, less than about 75 Daltons, less than about 50 Daltons, less than about 40 Daltons, less than about 30 Daltons, less than about 20 Daltons, or less than about 10 Daltons.
  • a plant protein isolate (e.g., a pea protein isolate) herein may comprise at least one plant protein having a PDCAAS of about 0.6 to about 1.0, about 0.7 to about 1.0, about 0.8 to about 1.0, or about 0.9 to about 1.0.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein may have one or more reactive proteins.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein may have one or more reactive proteins that forms a plant-based fiber structure by forming a chemical bond with another reactive protein.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein may have at least about 5% (e.g., at least about 5%, at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 99%) reactive proteins of the total protein.
  • a plant protein isolate herein e.g., a pea protein isolate
  • Reactive proteins comprising a plant protein isolate disclosed herein may form a plant-based fiber structure in response to an alkaline condition.
  • an “alkaline condition” can refer to an environment having a pH higher than about 10.
  • reactive proteins comprising a plant protein isolate herein e.g., a pea protein isolate
  • Plant protein isolates herein may form an isotropic (e.g., yogurtlike) or an anisotropic (e.g., fibrous structures) gel immediately after exposure to the alkaline condition.
  • reactive proteins comprising a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition after less than about 1 minute, less than about 10 minutes, less than about 30 minutes, less than about 1 hour, less than about 2 hours, less than about 6 hours, less than about 12 hours, less than about 24 hours, less than about 36 hours, or less than about 48 hours.
  • Reactive proteins comprising a plant protein isolate herein may also form a plant-based fiber structure in response to an alkaline condition at a temperature of about 0 °C to about 160 °C, about 2 °C to about 150 °C, about 4 °C to about 140 °C, about 6 °C to about 130 °C, about 8 °C to about 120 °C, about 10 °C to about 110 °C, about 12 °C to about 100 °C, about 14 °C to about 95 °C, about 16 °C to about 90 °C, about 18 °C to about 85 °C, or about 20 °C to about 80 °C.
  • reactive proteins comprising a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition at room temperature (i.e., about 25 °C ⁇ 3 °C).
  • reactive proteins comprising a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition under pressure.
  • a plant-based fiber structure may be formed in response to an alkaline condition under absolute pressure ranging from about 1 bar to about 3 bar.
  • a plant-based fiber structure may be formed in response to an alkaline condition under absolute pressure of about 1 bar, about 1.5 bar, about 2 bar, about 2.5 bar, or about 3 bar.
  • a plant-based fiber structure may be formed in response to an alkaline condition under absolute pressure of about 2 bar and a temperature of about 121 °C.
  • Plant protein isolates herein may form a plant-based fiber structure after exposure to a solution having a pH of about 10, a pH of about 11, a pH of about 12, a pH of about 13, or a pH of about 14.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein may form a plant-based fiber structure in less than about 1 minute, less than about 10 minutes, less than about 30 minutes, less than about 1 hour, less than about 2 hours, less than about 6 hours, less than about 12 hours, less than about 24 hours, less than about 36 hours, or less than about 48 hours after exposure to a solution having a pH of at least about 11.
  • a plant protein isolate herein may form a plant-based fiber structure after exposure to a solution having a pH of at least about 11 at a temperature of about 0 °C to about 100 °C, about 5 °C to about 95 °C, about 10 °C to about 90 °C, about 15 °C to about 85 °C, or about 20 °C to about 80 °C.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition wherein the plant-based fiber structure forms a solid structure.
  • a plant protein isolate herein e.g., a pea protein isolate
  • a plant protein isolate herein e.g., a pea protein isolate
  • Plant protein isolates herein may form a plant-based fiber structure in response to an alkaline condition wherein the plant-based fiber structure is viscous. Viscosity can be measured by methods known in the art, such as for example via a viscometer.
  • a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition wherein the plant-based fiber structure has a viscosity of about 10 centipoise (cps) to about 5,000,000 cps, about 50 cps to about 3,000,000 cps, about 100 cps to about 2,000,000 cps, or about 500 cps to about 1,000,000 cps.
  • cps centipoise
  • a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition wherein the plant-based fiber structure has a viscosity of about 50,000 cps to about 2,000,000 cps, about 75,000 cps to about 1,000,000 cps, or about 100,000 cps to about 500,000 cps.
  • a plant protein isolate herein may form a plant-based fiber structure in response to an alkaline condition wherein the plant-based fiber structure has a viscosity of about 50 cps to about 100,000 cps, about 100 cps to about 80,000 cps, or about 150 cps to about 60,000 cps.
  • Plant protein isolates herein stored in an alkaline condition may increase gelation time to form a plant-based fiber structure.
  • gelation time is the amount of time it takes for the composition comprising a plant protein isolate herein to transform into a gel.
  • a plant protein isolate herein (e.g., a pea protein isolate) in an alkaline condition may have a gelation time of less than about 1 minute, less than about 10 minutes, less than about 30 minutes, less than about 1 hour, less than about 2 hours, less than about 6 hours, less than about 12 hours, less than about 24 hours, less than about 36 hours, or less than about 48 hours.
  • Plant-based fiber structures formed in an alkaline condition may be stable at a temperature of about 0 °C to about 100 °C, about 5 °C to about 95 °C, about 10 °C to about 90 °C, about 15 °C to about 85 °C, or about 20 °C to about 80 °C.
  • a plant-based fiber structure formed in an alkaline condition herein may be stable at room temperature (i.e., about 25 °C ⁇ 3 °C).
  • a plant-based fiber structure formed in an alkaline condition herein may be stable at about a temperature of at least 4 °C for about 1 day, about 3 days, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 2 months, about 4 months, about 5 months, about 6 months, about 1 year, or about 2 years.
  • a plant-based fiber structure formed in an alkaline condition herein may be stable at room temperature (i.e., about 25 °C ⁇ 3 °C) for about 1 day, about 3 days, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 2 months, about 4 months, about 5 months, about 6 months, about 1 year, or about 2 years.
  • a plant-based fiber structure formed in an alkaline condition herein may be stable after the pH of the condition is changed to a pH of about 6 to about 14, about 7 to about 12, or about 8 to about 11.
  • a plant-based fiber structure formed in an alkaline condition herein may be stable after the pH of the condition is changed to a pH of about 6.0, about 6.5, about 7.0, about 7.5, about 8.0, or about 8.5.
  • a plant-based fiber structure formed in an alkaline condition herein may be stable for about 1 day, about 3 days, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 2 months, about 4 months, about 5 months, about 6 months, about 1 year, or about 2 years after the pH of the condition is changed to a pH of about 6 to about 10 (e.g., about 6, about 7, about 8, about 9, about 10).
  • a plant-based fiber structure formed in an alkaline condition herein may be stable for about 1 day, about 3 days, about 5 days, about 1 week, about 2 weeks, about 3 weeks, about 4 weeks, about 2 months, about 4 months, about 5 months, about 6 months, about 1 year, or about 2 years after the pH of the condition is changed to a pH of about 6.0, about 6.5, about 7.0, about 7.5, about 8.0, or about 8.5.
  • Plant-based fiber structures formed in an alkaline condition herein may comprise at least about 5% w/w moisture content (e.g., at least about 5%, at least about 10%, at least about 20%, at least about 30%, at least about 40%, or at least about 50% w/w moisture content).
  • a plant-based fiber structure formed in an alkaline condition herein may comprise about 5% to about 99% w/w moisture content, about 10% to about 95% w/w moisture content, or about 15% to about 90% w/w moisture content.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise about 5%, about 10%, about 20%, about 30%, about 40%, about 50%, about 60%, about 70%, about 80%, about 90%, or about 99% w/w moisture content.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise about 20%, about 25%, about 30%, about 35%, about 40%, about 50%, about 55%, about 60%, about 65%, about 70%, or about 75% w/w moisture content.
  • a dehydrated plant-based fiber structure formed in an alkaline condition herein may comprise less than about 25% w/w moisture content (e.g., less than about 25% w/w moisture, less than about 20% w/w moisture, less than about 15% w/w moisture, less than about 10% w/w moisture, less than about 5% w/w moisture, less than about 1% w/w moisture, less than about 0.5% w/w moisture).
  • a dehydrated plant-based fiber structure formed in an alkaline condition herein may be rehydrated.
  • a rehydrated plant-based fiber structure formed in an alkaline condition disclosed herein may comprise at least about 5% w/w moisture content (e.g., at least about 5%, at least about 10%, at least about 20%, at least about 30%, at least about 40%, or at least about 50% w/w moisture content).
  • Plant-based fiber structures formed in an alkaline condition herein may retain moisture content when the plant-based fiber structure is heated.
  • a plant-based fiber structure formed in an alkaline condition herein may retain moisture content when the plant-based fiber structure is heated to at least about 40 °C (e.g., at least about 40 °C, at least about 50 °C, at least about 60 °C, at least about 70 °C, at least about 80 °C, at least about 100 °C, at least about 110 °C, at least about 120 °C, at least about 140 °C).
  • a plant-based fiber structure formed in an alkaline condition herein may retain moisture content when the plantbased fiber structure is heated to a temperature ranging from about 10 °C to about 140 °C, about 20 °C to about 130 °C, about 30 °C to about 120 °C, about 40 °C to about 110 °C, about 50 °C to about 100 °C, about 60 °C to about 90 °C, or about 70 °C to about 80 °C.
  • a plant-based fiber structure formed in an alkaline condition herein may retain moisture content when the plant-based fiber structure is heated to about 40 °C, about 45 °C, about 50 °C, about 55 °C, about 60 °C, about 65 °C, about 70 °C, about 75 °C, about 80 °C, about 85 °C, about 90 °C, about 95 °C, about 100 °C, about 105 °C, about 110 °C, about 115 °C, about 120 °C, about 125 °C, about 130 °C, about 135 °C, or about 140 °C.
  • a plantbased fiber structure formed in an alkaline condition herein may lose about 1% to about 40% moisture content (e.g., about 1%, about 5%, about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%) when the plant-based fiber structure is heated.
  • moisture content e.g., about 1%, about 5%, about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%
  • a plant-based fiber structure formed in an alkaline condition herein may lose about 1% to about 40% moisture content (e.g., about 1%, about 5%, about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%) when the plant-based fiber structure is heated to at least about 40 °C (e.g., at least about 40 °C, at least about 50 °C, at least about 60 °C, at least about 70 °C, at least about 80 °C, at least about 90 °C, at least about 100 °C, at least about 110 °C, at least about 120 °C, at least about 130 °C, at least about 140 °C).
  • at least about 40 °C e.g., at least about 40 °C, at least about 50 °C, at least about 60 °C, at least about 70 °C, at least about 80 °C, at least about 90 °C, at least about 100 °C, at least about 110 °C, at least
  • Plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure resembling that of an animal muscle.
  • An animal muscle for comparison to the plant-based fiber structures formed herein can include, but are not limited to muscle fibers of a cow, a sheep, a goat, a pig, a horse, a camel, a chicken, a turkey, a duck, and the like.
  • Plant-based fiber structures formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a diameter similar to that of an animal muscle.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a diameter of at least about 0.5 mm (e.g., at least about 0.5 mm, at least about 1.0 mm, at least about 1.5 mm, at least about 2.0 mm, at least about 3.0 mm, at least about 4.0 mm, at least about 5.0 mm).
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a diameter ranging from about 0.5 mm to about 10 mm, about 1.0 mm to about 9 mm, or about 1.5 mm to about 8 mm.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a diameter of about 0.5 mm, about 1.0 mm, about 1.5 mm, about 2.0 mm, about 2.5 mm, about 3.0 mm, about 3.5 mm, about 4.0 mm, about 4.5 mm, about 5.0 mm, about 5.5 mm, about 6.0 mm, about 6.5 mm, about 7.0 mm, about 7.5 mm, about 8.0 mm, about 8.5 mm, about 9.0 mm, about 9.5 mm, or about 10 mm.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a length similar to that of an animal muscle.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a length of at least about 0.5 mm (e.g., at least about 0.5 mm, at least about 1.0 mm, at least about 1.5 mm, at least about 2.0 mm, at least about 3.0 mm, at least about 4.0 mm, at least about 5.0 mm).
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a length ranging from about 0.5 mm to about 50 mm, about 1.0 mm to about 45 mm, or about 2.0 mm to about 40 mm.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise a fiber structure having at least one or more fibers having a length of about 0.5 mm, about 1.0 mm, about 2.0 mm, about 3.0 mm, about 4.0 mm, about 5.0 mm, about 6.0 mm, about 7.0 mm, about 8.0 mm, about 9.0 mm, about 10 mm, about 15 mm, about 20 mm, about 25 mm, about 30 mm, about 35 mm, about 40 mm, about 45 mm, or about 50 mm.
  • Plant-based fiber structure formed in an alkaline condition herein may comprise solid structure with a water dispersion equal to that of an animal-based food product.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a homogeneous dispersion of water particles throughout the structure.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a heterogeneous dispersion of water particles throughout the structure.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a dispersion of water particles throughout the structure wherein the water particles may have a diameter averaging between about 1 m to about 20 m, about 2 pm to about 15 pm, or about 3 pm to about 10 pm in size.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a dispersion of water particles throughout the structure wherein the water particles may have a diameter averaging about 1 pm, about 2 pm, about 3 pm, about 4 pm, about 5 pm, about 6 pm , about 7 pm, about 8 pm, about 9 pm, about 10 pm, about 11 pm, about 12 pm, about 13 pm, about 14 pm, about 15 pm, about 16 pm, about 17 pm, about 18 pm, about 19 pm, or about 20 pm in size.
  • Plant-based fiber structure formed in an alkaline condition herein may comprise solid structure with a tensile strength equal to that of an animal-based food product. Methods of measuring tensile strength known in the art are suitable for use herein, including use of a texture analyzer.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a tensile strength ranging from about 0.05 kPa to about 10 kPa.
  • a plant-based fiber structure formed in an alkaline condition herein may comprise solid structure having a tensile strength of about 0.05 kPa, about 0.1 kPa, about 0.5 kPa, about 1 kPa, about 1.5 kPa, about 2 kPa, about 2.5 kPa, about 3 kPa, about 3.5 kPa, about 4 kPa, about 4.5 kPa, about 5 kPa, about 5.5 kPa, about 6 kPa, about 6.5 kPa, about 7 kPa, about 7.5 kPa, about 8 kPa, about 8.5 kPa, about 9 kPa, about 9.5 kPa, or about 10 kPa.
  • Plant-based fiber structures formed in an alkaline condition herein may comprise solid structure with a hardness equal to that of an animal-based food product. Methods of measuring hardness known in the art are suitable for use herein, including use of a texture analyzer. In some embodiments, plant-based fiber structures herein may comprise a solid structure having a hardness ranging from about 150 kPa to about 1000 kPa.
  • plant-based fiber structures herein may comprise a solid structure having a hardness of about 150 kPa, about 175 kPa, about 200 kPa, about 225 kPa, about 250 kPa, about 275 kPa, about 300 kPa, about 325 kPa, about 350 kPa, about 375 kPa, about 400 kPa, about 425 kPa, about 450 kPa, about 475 kPa, about 500 kPa, about 525 kPa, about 550 kPa, about 575 kPa, about 600 kPa, about 625 kPa, about 650 kPa, about 675 kPa, about 700 kPa, about 725 kPa, about 750 kPa, about 775 kPa, about 800 kPa, about 825 kPa, about 850 kPa, about 875 kPa,
  • Plant-based fiber structures formed in an alkaline condition herein may be combined with one or more proteins.
  • a plant-based fiber structure herein may be first formed in an alkaline condition followed by addition of one or more proteins.
  • a plant-based fiber structure herein may be first formed in an alkaline condition followed by addition of one or more proteins wherein the addition of the one or more proteins lowers the pH of the condition.
  • a plant-based fiber structure herein may be first formed in an alkaline condition followed by addition of one or more proteins wherein the addition of the one or more proteins lowers the pH of the condition to a pH of about 6 to about 9.
  • a plant-based fiber structure herein may be first formed in an alkaline condition followed by addition of one or more proteins wherein the addition of the one or more proteins lowers the pH to a pH of about 6.0, about 6.5, about 7.0, about 7.5, about 8.0, or about 8.5.
  • the pH may be further adjusted to a range of about 6 to about 8.5 using any food-grade organic or inorganic buffer including but not limited to potassium metaphosphate, potassium phosphate, potassium phosphate dibasic anhydrous, potassium phosphate monobasic, potassium phosphate tribasic, potassium phosphate dibasic heptahydrate, monobasic sodium acetate, sodium citrate anhydrous and dihydrate, ammonium hydroxide, sodium hydroxide, sodium bicarbonate, sodium carbonate, ammonium carbonate, calcium carbonate, borate, glycine, Tris, Bis-Tris propane, bicine, HEPES, TESm MOBS, DIPSO, TAPS, triethanolamine (TEA), pyrophosphate, HEPPSO, tricine, hydrazine, glycylclycine, 2-amino-2- methyl- 1,3 -propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, tri
  • the buffer is an alkaline buffer for example: ammonium hydroxide, sodium hydroxide, sodium carbonate, ammonium carbonate, calcium carbonate, glycine, TAPS, pyrophosphate, tricine, hydrazine, glycylclycine, 2-amino-2-methy 1-1,3 - propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, or tris(hydroxymethyl)aminomethane (THAM).
  • alkaline buffer for example: ammonium hydroxide, sodium hydroxide, sodium carbonate, ammonium carbonate, calcium carbonate, glycine, TAPS, pyrophosphate, tricine, hydrazine, glycylclycine, 2-amino-2-methy 1-1,3 - propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, or tris(hydroxymethyl)aminomethane (T
  • Plant-based fiber structures formed in an alkaline condition herein may be combined with one or more proteins wherein the one or more proteins is a plant-based protein, an animal-based protein, or a combination thereof.
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more proteins wherein the one or more proteins is a recombinantly produced plant-based protein, a recombinantly produced animal-based protein, or a combination thereof.
  • Plant-based fiber structures formed in an alkaline condition herein may be combined with one or more proteins wherein the one or more proteins is a casein protein isolate, a whey protein isolate, wheat gluten, soy protein concentrate or pea vicilin or pea legumin or a combination thereof.
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more proteins wherein the one or more proteins is a casein protein isolate wherein the casein protein isolate may comprise alpha-casein peptides, beta-casein peptides, kappa-casein peptides, or any combination thereof.
  • a casein protein isolate for use herein may be derived and/or produced from micellar casein, acid casein, hydrolyzed casein, rennet casein or any combination thereof.
  • Micellar casein is ultrafiltered casein extracted from milk without acidification.
  • Acid casein is a dry free flowing high-quality protein food ingredient that has been isolated from skim milk.
  • Hydrolysed casein is a soluble, enzymatic digest of casein. Rennet casein is produced by the controlled precipitation of casein from pure, pasteurized skim milk through the action of rennet.
  • a casein protein isolate for use herein may be a recombinantly produced casein protein.
  • Plant-based fiber structures formed in an alkaline condition herein may be combined with one or more proteins in a ratio of about 1 :1.
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more proteins wherein the about of plant-based fiber structure may be about 1% w/w to about 10% w/w (e.g., about 1% w/w, about 2% w/w, about 3% w/w, about 4% w/w, about 5% w/w, about 6% w/w, about 7% w/w, about 8% w/w, about 9% w/w, about 10% w/w) and the total protein amount of the one or more proteins may be about 1 % w/w to about 10% w/w (e.g., about 1% w/w, about 2% w/w, about 3% w/w, about 4% w/w, about 5% w/w, about 6% w
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more proteins wherein the about of plant-based fiber structure may be about 5% w/w and the total protein amount of the one or more proteins may be about 5% w/w.
  • Plant-based fiber structure compositions herein may have at least one plant protein isolate as disclosed herein. In some embodiments, plant-based fiber structure compositions herein may have at least one pea protein isolate as disclosed herein. In some other embodiments, compositions herein may comprise about 5% to about 99% (e.g., about 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99%) by weight of the composition of one or more pea protein isolate disclosed herein.
  • a buffer solution for use herein can be any solution suitable for use in a food product.
  • plant-based fiber structure compositions herein may have at least one plant protein isolate as disclosed herein in a buffer solution.
  • plant-based fiber structure compositions herein may have at least one pea protein isolate as disclosed herein in a buffer solution.
  • buffer solutions for use herein may comprise water.
  • buffer solutions for use herein may comprise at least about 1% w/w water (e.g., at least about 1% w/w water, at least about 5% w/w water, at least about 10% w/w water, at least about 20% w/w water, at least about 30% w/w water, at least about 40% w/w water, at least about 50% w/w water).
  • buffer solutions herein may comprise about 1% to about 99% w/w water, about 5% to about 95% w/w water, or about 10% to about 90% w/w water.
  • buffer solutions herein may comprise about 1% w/w water, about 5% w/w water, about 10% w/w water, about 20% w/w water, about 30% w/w water, about 40% w/w water, about 50% w/w water, about 60% w/w water, about 70% w/w water, about 80% w/w water, about 90% w/w water, or about 99% w/w water.
  • Compositions herein may also include a buffer solution having one or more buffering agents wherein “buffering agents” are compounds used to resist change in pH upon dilution or addition of acid or alkali.
  • Buffering agents for use herein can include, by way of example and without limitation, potassium metaphosphate, potassium phosphate, potassium phosphate dibasic anhydrous, potassium phosphate monobasic, potassium phosphate tribasic, potassium phosphate dibasic heptahydrate, monobasic sodium acetate, sodium citrate anhydrous and dihydrate, ammonium hydroxide, sodium hydroxide, sodium bicarbonate, sodium carbonate, ammonium carbonate, calcium carbonate, borate, glycine, Tris, Bis-Tris propane, bicine, HEPES, TESm MOBS, DIPSO, TAPS, triethanolamine (TEA), pyrophosphate, HEPPSO, tricine, hydrazine, glycylclycine, 2-amino-2-methyl-l,3-propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, tris(hydroxymethyl)aminomethane (THAM), and other materials known to
  • the buffer is an alkaline buffer for example: ammonium hydroxide, sodium hydroxide, sodium carbonate, ammonium carbonate, calcium carbonate, glycine, TAPS, pyrophosphate, tricine, hydrazine, glycylclycine, 2-amino-2-methyl- 1,3-propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, or tris(hydroxymethyl)aminomethane (THAM).
  • any food-grade organic or inorganic buffer can be used.
  • compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more buffering agents by total weight of the composition.
  • the amount of one or more buffering agents may depend on the desired pH level of compositions herein.
  • compositions disclosed herein may have a pH ranging from about 9 to about 14 (e.g., about 9, about 10, about 11, about 12, about 13, about 14).
  • buffer solutions herein may have a pH ranging from about 10 to about 12 (e.g., about 10.0, about 10.5, about 11.0, about 11.5, about 12.0).
  • buffer solutions herein may have a pH ranging from about 5 to about 8 (e.g., about 5.0, about 5.5, about 6.0, about 6.5, about 7.0, about 7.5, about 8.0). In some other embodiments, buffer solutions herein may have a pH ranging from about 10 to about 12 (e.g., about 10.0, about 10.5, about 11.0, about 11.5, about 12.0) until a plant-based fiber structure is formed, then the buffer solutions herein may be changed to have a pH ranging from about 5 to about 8 (e.g., about 5.0, about 5.5, about 6.0, about 6.5, about 7.0, about 7.5, about 8.0). [0158] The present disclosure also provides methods of making a plant-based fiber structure.
  • Methods herein may comprise incubating at least one plant protein isolate as disclosed herein in a buffer solution disclosed herein.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution for about 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14, or about 11 to about 13.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH of at least about 10, at least about 11, at least about 12, at least about 13, or at least about 14.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH of about 10, about 10.5, about 11, about 11.5, about 12, about 12.5, about 13, about 13.5, or about 14.
  • plant protein isolate herein e.g., pea protein isolate
  • the buffer solution may have a pH of about 10, about 10.5, about 11, about 11.5, about 12, about 12.5, about 13, about 13.5, or about 14.
  • Methods of making plant-based fiber structures may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution at a temperature of about 0 °C to about 100 °C, about 5 °C to about 95 °C, about 10 °C to about 90 °C, about 15 °C to about 85 °C, or about 20 °C to about 80 °C.
  • methods herein may comprise incubating at least one plant protein isolate (e.g., pea protein isolate) in a buffer solution at a temperature of about 10 °C, about 15 °C, about 20 °C, about 25 °C, about 30 °C, or about 35 °C.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution at room temperature (i.e., about 25 °C ⁇ 3 °C).
  • Methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours.
  • a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours at a temperature of about 0 °C to about 100 °C, about 5 °C to about 95 °C, about 10 °C to about 90 °C, about 15 °C to about 85 °C, or about 20 °C to about 80 °C.
  • a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours at a temperature of about 0 °C to about 100 °C, about 5 °C to about 95 °C, about 10 °C to about 90 °C
  • Other methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution wherein the buffer solution may have a pH ranging from about 10 to about 14 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours.
  • methods herein may comprise incubating at least one plant protein isolate herein (e.g., pea protein isolate) in a buffer solution for at least 12 hours, wherein the buffer solution has a pH equal to or higher than about
  • Plant protein isolates herein may be stored in a buffer solution for about 12 hours to about 48 hours. In some other embodiments, at least one plant protein isolate herein may be stored in a buffer solution having a pH ranging from about 11 to about 14. In some embodiments, at least one plant protein isolate herein may be stored in a buffer solution and incubated at a temperature of about 10 °C, about 15 °C, about 20 °C, about 25 °C, about 30 °C, or about 35 °C. In some other embodiments, at least one plant protein isolate herein may be stored in a buffer solution and incubated at a temperature of about 20 °C to about 30 °C.
  • methods herein may comprise incubating at least one plant protein isolate herein in a buffer solution wherein the buffer solution may have a pH of about 11 for at least 1 minute, at least 30 minutes, at least 1 hour, at least 2 hours, at least 6 hours, at least 12 hours, or at least 48 hours at a temperature of about 10 °C, about 15 °C, about 20 °C, about 25 °C, about 30 °C, or about 35 °C.
  • compositions herein can be used for producing meat substitute food products (“meat replicas”).
  • a “meat replica” refers to a food product having a realistic meat-like appearance without containing an animal-based competent.
  • Compositions herein can be used as a materials in and in methods of making meat replicas, including, but not limited to ground meat replicas (e.g., ground beef, ground chicken, ground turkey, ground lamb, or ground pork), as well as replicas of cuts of meat and fish.
  • the current disclosure also encompasses a method of making a food product, the method comprising: a) obtaining or having obtained at least a plant protein isolate stored in an alkaline buffer for at least 1 hr; combining the plant protein isolate with a protein isolate selected from casein protein isolate, a whey protein isolate, or a combination thereof.
  • the plant protein isolate stored in an alkaline buffer may comprise a pea protein isolate.
  • the protein isolate is casein.
  • the casein is a micellar casein, acid casein, hydrolyzed casein, rennet casein or any combination thereof.
  • the casein in micellar casein.
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more additional protein isolates (for example: casein, or whey protein), in a weight ratio of the plant protein isolate to additional protein isolate (for example, casein or whey protein) ranging from about 1 : 10 to about 10: 1, or about 1 :5 to about 5:1.
  • additional protein isolates for example: casein, or whey protein
  • a plant-based fiber structure formed in an alkaline condition herein may be combined with one or more additional protein isolates (for example: casein, or whey protein), in a weight ratio of the plant protein isolate to additional protein isolate (for example, casein or whey protein) ranging from about 1 : 1 to about 1 :2, or 1 :2 to about 1:3, 1:3 to about 1 :4, or 1:4 to about 1 :5, or 1: 1 to about 2: 1, or 2: 1 to about 3:1, or 3: 1 to about 4: 1, or 4: 1 to about 5:1 ratio by weight.
  • additional protein isolates for example: casein, or whey protein
  • the composition as disclosed herein comprises about 5% (w/w) to about 20% (w/w) of each of the at least a plant protein isolate and the protein isolate. In some aspects, the composition comprises about 5% (w/w), or about 6% (w/w), or about 7% (w/w), or about 8% (w/w), or about 9% (w/w), or about 10% (w/w), or about 11% (w/w), or about 12% (w/w), or about 13% (w/w), or about 14% (w/w), or about 15% (w/w), or about 16% (w/w), or about 17% (w/w), or about 18% (w/w), or about 19% (w/w), or about 20% (w/w) of each of the at least a plant protein isolate and the protein isolate.
  • the composition may have a pH ranging from about 5 to about 8.5.
  • the addition of the protein isolate to the pea protein isolate lowers the pH of the composition to a pH of about 6.0, about 6.5, about 7.0, about 7.5, about 8.0, or about 8.5.
  • the pH of the composition may be further adjust to a pH ranging from about 5 to about 8.5, or about 5.5 to about 8, or about 6 to about 7.5, or about 6.5 to about 7.
  • the pH of the composition can be adjusted using any food-grade organic or inorganic buffer.
  • the method of making the food product further comprises subjecting the composition at least one pea protein isolate subjected to an alkaline buffer and a protein isolate to one or more of a fermentation, cooking, pressurized cooking, extrusion, low-shear, or high shear extrusion process.
  • the composition is subjected to an extrusion process.
  • an “extrusion” refers to a process in which a material is pushed under compressive stresses through a deformation control element such as a die to form a product. The process of extrusion is usually accomplished by using equipment referred to in the art as an extruder.
  • the extruder as used herein may comprise a single screw extruder or a twin-screw extruder, or a combination thereof. It may be a single screw “wet” extruder (with or without the preconditioner), single screw “dry” extruder (with or without the preconditioner), single-screw interrupted flight extruder (with or without a preconditioner), and twin-screw extruder (with or without a preconditioner).
  • the current disclosure encompasses use of extruders with a wide range of configurations and attachments.
  • the composition may be further combined with additional ingredients for example additional proteins for example a heme-protein, or soy protein, or combination thereof, a fat (milk based like butter), a non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, emulsifiers, plasticizers, thickeners, surfactants, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives, dietary fibers, gluten, and mixtures thereof.
  • the casein may be a recombinant casein.
  • methods of making food products may include combining the compositions herein with non-animal-based fat, non-animal-based matrixes, non- animal-based edible fibrous components, or any combination thereof.
  • Methods of making food products may also include combining the compositions herein with non- animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, or any combination thereof wherein the addition of the composition herein provides a meat-like appearance to the meat substitute.
  • methods of making food products may include combining the compositions herein with additional proteins, non- animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, or any combination thereof wherein the addition of the composition herein provides a meat-like taste to the meat substitute.
  • methods of making food products may include combining the compositions herein with additional non-animal-based proteins, non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, or any combination thereof wherein the addition of the composition herein provides a meat-like smell to the meat substitute.
  • the additional non-animal-based proteins is a heme-protein, soy protein.
  • the non-animal-based fat may be selected from soybean oil, canola oil, corn oil, sunflower oil, safflower oil, flaxseed oil, almond oil, peanut oil, fish oil, algal oil, palm oil, palm stearin, palm olein, palm kernel oil, fractionated palm kernel oil (including Medium Chain Triglyceride (MCT) oil made from palm kernel oil), high oleic soybean, canola, sunflower or safflower oils, acai oil, almond oil, amaranth oil, apricot seed oil, argan oil, avocado seed oil, babassu oil, ben oil, blackcurrant seed oil, Borneo tallow nut oil, borage seed oil, buffalo gourd oil, carob pod oil, cashew oil, castor oil, coconut oil, fractionated coconut oil (including Medium Chain Triglyceride (MCT) oil made from coconut oil),
  • MCT Medium Chain Tri
  • the meat replica food product may further comprise one or more optional ingredients, non-limiting examples of such ingredients include emulsifiers, surfactants, plasticizers, thickeners, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives, dietary fibers, and mixtures thereof.
  • emulsifiers include but are not limited to lecithin, or soy lecithin.
  • Nonlimiting examples of surfactant/solvent components include, Polyoxyethylene sorbitan monostearate (Tween 60), sorbitan monooleate (SMO or Span 80), sorbitan monostearate(SMS or Span 60), glyceryl monooleate (GMO), glyceryl monostearate (GMS) glyceryl monopalmitate (GMP), polyglyceryl ester of lauric acid - polyglyceryl polylaurate (PGPL), polyglyceryl ester of stearic acid - polyglyceryl polystearate (PGPS), polyglyceryl ester of oleic acid (PGPO) - polyglyceryl polyoleate (PGPO), and polyglyceryl ester of ricinoleic acid (PGPR) - polyglyceryl polyricinoleate (PGPR).
  • Tween 60 Polyoxyethylene sorbitan monostearate
  • SMO or Span 80 sorbitan
  • Non-limiting examples of plasticizers include glycerin or propylene glycol or a combination thereof.
  • Non-limiting examples of thickeners include but not limited to guar gum, pectin, xanthan gum, agar, alginic acid and its salts, carboxymethyl cellulose, carrageenan and its salts, gums, modified starches, pectins, processed Eucheuma seaweed, sodium carboxymethyl cellulose, tara gum.
  • Non-limiting examples of plasticizers include but are not restricted to polysaccharides and galactomannans such as starch, modified starch, maltodextrin, carrageenan, guar gum, alginin, agar, grain flour mix, carboxymethyl cellulose, pectin, locust beam gum and xanthan gum.
  • Non-limiting examples of sugars/sweeteners include but are not limited to stevia, sucralose, sugar alcohols, sucrose, glucose, fructose, and aspartame.
  • Non-limiting examples of a suitable colorant include FD&C colors, such as blue no. 1, blue no. 2, green no. 3, red no. 3, red no. 40, yellow no. 5, yellow no.
  • natural colors such as roasted malt flour, caramel coloring, annatto, chlorophyllin, cochineal, betanin, turmeric, saffron, paprika, lycopene, elderberry juice, pandan, butterfly pea and the like, titanium dioxide, and any suitable food colorant known to the skilled artisan.
  • binding agents include but are not restricted to Examples of suitable binding agents include but are not limited to purees (e.g., bean puree, sweet potato puree, pumpkin puree, applesauce, yam puree, banana puree, plantain puree, date puree, prune puree, fig puree, zucchini puree, carrot puree, coconut puree), native or modified starches (e.g., starches from grains, starches from tuber, potato starch, sweet potato starch, corn starch, waxy corn starch, tapioca starch, tapioca, arrowroot starch, taro starch, pea starch, chickpea starch, rice starch, waxy rice starch, lentil starch, barley starch, sorghum starch, wheat starch, and physical or chemical modifications thereof (including, e.g., pre-gelatinized starch, acetylated starch, phosphate bonded starch, carboxymethylated starch, hydroxypropylated starch), flour
  • beta-glucans e.g., from bacteria [e.g., curdlan], oat, rye, wheat, yeast, barley, algae, mushroom
  • gums e.g., xanthan gum, guar gum, locust bean gum, gellan gum, gum arabic, vegetable gum, tara gum, tragacanth gum, konjac gum, fenugreek gum, gum karaya, gellan gum, high-acetyl gellan gum, lowacetyl gellan gum
  • native or relatively folded (i.e., not fully in the native functional state but not fully denatured) proteins e.g., fava protein, lentil protein, pea protein, ribulose-1,5- bisphosphate carboxylase/oxygenase, chickpea protein, mung bean protein, pigeon pea protein,
  • stabilizing agents include but are not limited to polymeric biosurfactants, amphipathic polysaccharides (e.g., methylcellulose), lipopolysaccharides, proteins (e.g., pea protein, soy protein, chickpea protein, algae protein, yeast protein, potato protein, lentil protein), or mannoprotein.
  • suitable stabilizing agents include animal meat flavor, an animal meat oil, spice extracts, spice oils, natural smoke solutions, natural smoke extracts, yeast extract, and shiitake extract. Additional flavoring agents may include onion flavor, garlic flavor, or herb flavors.
  • Herbs that may be added include basil, celery leaves, chervil, chives, cilantro, parsley, oregano, tarragon, and thyme.
  • Nonlimiting examples of flavor enhancers include glucose, fructose, ribose, arabinose, glucose-6- phosphate, fructose-6-phosphate, fructose- 1,6-diphosphate, inositol, maltose, sucrose, maltodextrin, glycogen, sugars associated with nucleotides, molasses, animal meat flavor, an animal meat oil, spice extracts, spice oils, natural smoke solutions, natural smoke extracts, yeast extract, and shiitake extract.
  • Additional flavoring agents may include onion flavor, garlic flavor, or herb flavors.
  • Herbs that may be added include basil, celery leaves, chervil, chives, cilantro, parsley, oregano, tarragon, and thyme or mixtures thereof.
  • Non-limiting examples of dietary fiber component may include vegetable fibers from carrots, bamboo, peas, broccoli, potatoes, sweet potatoes, corn, whole grains, alfalfa, collard greens, celery, celery root, parsley, cabbage, squash, green beans, common beans, black beans, red beans, white beans, beets, cauliflower, nuts, apple peels, oats, wheat or plantain, or mixtures thereof.
  • Non-limiting examples of dietary fibers including but not limited to pea fiber, oat fiber, bamboo fiber, rice bran, waxy maize, bean fiber, beet fiber, guar gum, pectin, carrageenan, apple fiber, citrus fiber, carrot fiber, barley fiber, psyllium husk, soy fiber, sesame flour, flaxseed fiber, nuts, garcinia fiber, chicory fiber, and fenugreek fiber and combinations thereof.
  • Non-limiting examples of vitamins that can be used include Vitamins A, C, and E.
  • Non-limiting examples of minerals that may be added include the salts of aluminum, ammonium, calcium, magnesium, and potassium
  • Non-limiting examples of pH regulators include food-grade organic or inorganic buffer (including but not limited to potassium metaphosphate, potassium phosphate, potassium phosphate dibasic anhydrous, potassium phosphate monobasic, potassium phosphate tribasic, potassium phosphate dibasic heptahydrate, monobasic sodium acetate, sodium citrate anhydrous and dihydrate, ammonium hydroxide, sodium hydroxide, sodium bicarbonate, sodium carbonate, ammonium carbonate, calcium carbonate, borate, glycine, Tris, Bis-Tris propane, bicine, HEPES, TESm MOBS, DIPSO, TAPS, triethanolamine (TEA), pyrophosphate, HEPPSO, tricine, hydrazine, glycylclycine, 2-amino-2- methyl- 1,3 -propanediol (AMPD), HEPBS
  • the buffer is an alkaline buffer for example: ammonium hydroxide, sodium hydroxide, sodium carbonate, ammonium carbonate, calcium carbonate, glycine, TAPS, pyrophosphate, tricine, hydrazine, glycylclycine, 2-amino-2-methy 1-1,3 - propanediol (AMPD), HEPBS, taurine, methylamine, piperadine, CABS, or tris(hydroxymethyl)aminomethane (THAM), but non-buffering agents like malic acid, tartaric acid, succinic acid, lactic acid.
  • alkaline buffer for example: ammonium hydroxide, sodium hydroxide, sodium carbonate, ammonium carbonate, calcium carbonate, glycine, TAPS, pyrophosphate, tricine, hydrazine, glycylclycine, 2-amino-2-methy 1-1,3 - propanediol (AMPD), HEPBS, taurine
  • Non-limiting examples of preservatives include but are not limited to hydroxybenzoate, nitrite, nitrate, sorbic acid, sodium sorbate, sorbates lactic acid, celery extract, propionic acid, benzoic acid, and sodium propionate.
  • a meat-like appearance, taste, or smell may be a beef-like appearance, taste, or smell, a poultry-like appearance, taste, or smell, a seafood-like appearance, taste, or smell, a game-like appearance, taste, or smell, a pork-like appearance, taste, or smell, or any combination thereof.
  • methods of making food products may include combining the compositions herein with non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, or any combination thereof wherein the addition of the composition herein provides a meat like texture to the meat substitute.
  • methods of making food products may include combining the compositions herein with non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, or any combination thereof wherein the addition of the composition herein provides a fat like (i.e., gel like) texture to the meat substitute.
  • a composition herein added to a food product e.g., meat replicas
  • a composition herein added to a food product e.g., meat replicas
  • Food products contemplated herein include meat, poultry and seafood analogs comprising as a component the disclosed compositions.
  • Non-limiting examples of food products comprising the compositions disclosed herein include products mimicking ground meat, meatloaf mix, steaks, pinwheels, sausages, salami, jerky, bacon, pork boneless rib meat, chicken cutlets, tenders, drumsticks, or hams, soups or stews.
  • Non-limiting examples of poultry analog food products include vegan chicken, mock chicken, vegan turkey, and compositions mimicking nuggets, cutlets, breasts, slices or strips sourced from chicken, quail, duck, ostrich, turkey, bantam, or geese.
  • Non-limiting examples of seafood analog include fish, clams, oysters, mussels, lobsters, shrimp, crab, echinoderms analogs.
  • the compositions described herein may be formulated to mimic any real meat, poultry, or seafood product, such as ground meat, ground meat patties, ground meat meatballs, meat steaks, meat sausage, meat jerky strips, ground chicken, poultry slices, fish fillets, seafood cutlets, seafood pies, salmon burgers, fish sticks, crab cakes, fish burgers, fish cakes, sushi, chowder, bisques, rolls and seafood stews or any combination thereof.
  • the compositions described herein may be formed as any such product formed from real beef, poultry, or seafood.
  • the present disclosure expressly contemplates, for example, plant-based food compositions in the form of plant-based beef, which may take the form of a ground beef patty or slider, a ground beef meatbail, a beef sausage or hot dog, a cut of beef, corned beef, or a dried beef strip.
  • the meat alternative formulation described herein may alternatively be prepared in the form taken by other real meat products such as meat (beef, chicken, or turkey) nuggets or strips, meat loaf or meat cake forms, canned seasoned meat, sliced meat, sausage of any size, or processed meats such as salami, bologna, luncheon meat and the like.
  • the meat alternative formulation, after cooking may provide the color, the flavor, and the texture of cooked meat which is pleasurable and palatable to the consumer.
  • the methods of making food-products may include combining the compositions with various ingredients to be used in meat replicas sold in a form such as “ground meat”, burgers/patties, or other forms, for example comparable to Impossible® Burger (from ImpossibleTM Foods), Beyond Burger® (from Beyond Meat®), Veggie Chik Patty® (from Morningstar Farms®), and Plant-Based Patties from Good & GatherTM.
  • Impossible® Burger from ImpossibleTM Foods
  • Beyond Burger® from Beyond Meat®
  • Veggie Chik Patty® from Morningstar Farms®
  • Plant-Based Patties from Good & GatherTM for example comparable to Impossible® Burger (from ImpossibleTM Foods), Beyond Burger® (from Beyond Meat®), Veggie Chik Patty® (from Morningstar Farms®), and Plant-Based Patties from Good & GatherTM.
  • poultry, meat and seafood analog products that may include compositions provided herein include products like Veggie Meal Starters® from Morningstar Farms®, such as Veggie CHIK’N Nugget, Veggie Popcorn CHIK’N, Veggie CHIK’N Strips, Veggie Grillers®, Veggie Buffalo, beef analogue products made by Beyond Meat® products such as Beyond Beef® Crumbles, Beyond Beef® Ground Beef, and Beyond Beef® Sausage, or fish analog products made by Good Catch like salmon burgers, fish sticks, fish fillets, crab cakes, fish burgers and fish cakes.
  • Veggie Meal Starters® from Morningstar Farms®
  • Veggie CHIK’N Nugget Nugget
  • Veggie Popcorn CHIK’N Veggie CHIK’N Strips
  • Veggie Grillers® Veggie Buffalo
  • beef analogue products made by Beyond Meat® products such as Beyond Beef® Crumbles, Beyond Beef® Ground Beef, and Beyond Bee
  • compositions disclosed here may also be incorporated into beverages, liquids, gels, pastes, sauces, powder or cubes, soup or stew bases.
  • the compositions may comprise a composition as disclosed herein mixed with other ingredients to form a non-dairy milk product for example cheese replica, icecreams and yogurt.
  • a “cheese substitute” or “cheese replica” can be any non-dairy product that serves a role as food or in food that is commonly served by traditional dairy cheese.
  • a cheese “substitute” or “replica” can be a product that shares visual, olfactory, textural or taste characteristics of cheese such that an ordinary human observer of the product is induced to think of traditional dairy cheese.
  • Non-dairy milk products herein refer to an emulsion comprising proteins and fats or a solution or suspension of proteins, sometimes further comprising other solutes that might include carbohydrates, salts and other small molecules that contribute to flavor, texture, emulsion stability, protein solubility or suspension stability, or its ability to support growth of microbial cultures used in making cheese replicas, yogurt replicas, or other replicas of cultured dairy products.
  • methods of making food products may include combining the compositions herein with one or more oils or fats isolated from plant sources, recombinant or synthetic sources.
  • oils or fats isolated from plant sources can be, but are not limited to, triglycerides, monoglycerides, diglycerides, sphingosides, glycolipids, lecithin, lysolecithin, phospholipids such as phosphatidic acids, lysophosphatidic acids, phosphatidyl cholines, phosphatidyl inositols, phosphatidyl ethanolamines, or phosphatidyl serines; sphingolipids such as sphingomyelins or ceramides; sterols such as stigmasterol, sitosterol, campesterol, brassicasterol, sitostanol, campestanol, ergosterol, zymost
  • Methods of making food products may include combining the compositions herein with non-dairy oils or fats to form a non-dairy milk.
  • methods of making food products may include combining the compositions herein with one or more oils or fats also isolated from plant sources, in a colloidal suspension, solution or emulsion to form the non-dairy milk for making a cheese replica.
  • methods of making food products may include combining the compositions herein with at least one additional ingredient.
  • At least additional ingredient suitable for use herein can include, but is not limited to, additional protein, for example a heme-protein, or soy protein, or combination thereof, a non-animal-based fat, non-animal-based matrixes, non-animal-based edible fibrous components, emulsifiers, surfactants, binding agents, emulsifiers, plasticizers, thickeners, surfactants, sugars, coloring agents, binding agents, stabilizing agents, flavor enhancers, flavoring agents, fragrance enhancers, nutritional supplements (e.g. vitamins, minerals, antioxidants), essential oils, pH regulators, preservatives, dietary fibers, gluten, and mixtures thereof.
  • compositions herein may provide food having at least one characteristic of dairy-based food compositions.
  • non-dairy milk products contemplated herein include milk, yogurt, ice cream, butter, cheese, and the like.
  • compositions herein may provide food having least one characteristic of dairy-based cheese compositions.
  • methods of making food products using the compositions herein can form a non-covalent linked protein network, similar to that formed by casein in natural, dairy-based cheese, which is weakened, but not eliminated, at increased temperatures.
  • methods of making food products (e.g., non-dairy milk products, cheese replicas) using the compositions herein can form a gel-like structure which can form a melted-cheese like structure at higher temperatures.
  • methods of making food products (e.g., non-dairy milk products, cheese replicas) using the compositions herein can form a gel-like structure which can form a melted-cheese like structure at higher temperatures and return to the gel-like structure upon cooling.
  • methods of making food products e.g., non-dairy milk products, cheese replicas
  • the compositions herein can have at least one of the following characteristics of dairy-based cheeses: moisture, hardness, gumminess, cohesiveness, brittleness, adhesiveness, meltability, and/or stretchability.
  • Food products contemplated herein may comprise about 1% to about 99% (e.g., about 1%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99%) of any of the compositions herein by weight.
  • food products e.g., meat replicas, non-dairy milk products
  • food products e.g., meat replicas, non-dairy milk products
  • food products may comprise about 1% to about 99% (e.g., about 1%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99%) of any of the pea isolated proteins herein by weight and at least one additional isolated protein, wherein the total amount of protein may comprise about 1% to about 99% (e.g., about 1%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99%) by weight.
  • Example 1 Methods of Preparing Materials and Solutions and Characterization Thereof [0181]
  • materials and solutions were prepared for analysis herein.
  • two pea protein isolates were used in the methods exemplified herein: PISANE C9 and PURIS Pea 870.
  • the pea protein isolate PISANE C9 was obtained from Cosucra Groupe Warcoing S.A. (Warcoing, Belgium).
  • Pea protein isolate PURIS Pea 870 was purchased from Cargill, Inc. (Minneapolis, USA).
  • Beta (P)-casein reduced micellar casein concentrate, alphas (a s )-casein, and P-casein reduced micellar casein powder were donated by the Department of Soft Matter Science and Dairy Technology (University of Hohenheim, Stuttgart, Germany). Hydrochloric acid (32%), sodium hydroxide pellets, and tris(hydroxymethyl)aminomethane (THAM) were purchased from Carl Roth GmbH & Co. KG (Karlsruhe, Germany). To measure the protein content of liquid protein samples according to methods disclosed herein, absorbent for liquid samples (DumaS orbXE, C. Gerhardt GmbH & Co. KG, Kbnigswinter, Germany) was used. Double deionized water was used throughout the exemplary methods disclosed herein.
  • the following nitrogen conversion factors were used: A standard factor of N x 6.25 and specific conversion factors of N x 5.36 for pea protein and N x 6.36 for casein.
  • Pea protein isolate PISANCE C9 pea protein isolate PURIS pea 870, micellar casein powder (diafiltered), a s -casein, and micellar casein concentrate (diafiltered) were characterized according to the methods described herein, as provided in Table 1 and further shown in Fig. 1.
  • the pea proteins and micellar casein had a protein content of approximately 67%
  • a s -casein had a protein content of 82%
  • micellar casein concentrate had a protein content of 19% (Table. 1).
  • All proteins characterized in a 10% solution in water (H2O) were in a pH range between 5.4 and 7.4 (Table. 1).
  • Table 1 Characterization of pea protein and casein powder and concentrate Example 2. Visual Analysis of Structure Formation in Pea and Micellar Casein Samples [0186] In an exemplary method, visual appearance and consistency of samples were assessed according to the methods described herein. The assessments determine consistency (e.g., gel, liquid) with possible aggregate formation (e.g., with flocs) and phase separation (e.g., 1 -phase, 2- phase).
  • consistency e.g., gel, liquid
  • possible aggregate formation e.g., with flocs
  • phase separation e.g., 1 -phase, 2- phase
  • the pea protein isolate and micellar casein (10% w/w protein) solution alone were adjusted to pH 2-11 by using HC1 and NaOH solutions (1 N, 3 N, and 10 N).
  • the samples were stirred for 10 minutes before the pH was adjusted to 2-11 by using HC1 and NaOH solutions (1 N, 3 N, and 10 N).
  • Fig. 3 shows structure formation in pea and micellar casein samples.
  • the pea protein isolate and casein (10% w/w protein) solutions alone were adjusted to pH 7-11 by using HC1 and NaOH solutions (1 N, 3 N, and 10 N).
  • the solutions alone were stored for 0 hours, 24 hours, and 48 hours at 25 °C in the dark before mixing.
  • the mixing pattern is displayed in Fig. 4. After mixing according to the patterns shown in Fig.
  • Fig. 5A shows PISANE C9 (10% w/w protein immediately after pH adjustment to pH 11 and Fig. 5B shows the same sample after 24 hours at 25 °C.
  • Figs. 6-11 show structure formation in pea and micellar casein samples.
  • the casein (10% w/w protein) solution was adjusted to pH 2 by using HQ solution (IO N) and stored in the dark for 24 hours and 48 hours.
  • the samples were adjusted to pH 2-11 by using HC1 and NaOH solutions (1 N, 3 N, and 10 N).
  • Fig. 13 shows visual analysis of casein samples were mixed with an aqueous pea protein isolate solution after the casein samples were stored at pH 2 for 24 hours or 48 hours.
  • the samples with the same pea protein isolate mixed with casein after 24 hours of acid hydrolysis did not differ significantly from the ones with 48 hours of acid hydrolysis.
  • All samples from pH 2 to 5 exhibited a formation of white flakes, which were slightly bigger the lower the pH.
  • Samples in the pH range from 6 to 10 were mostly liquid and smooth without any visible particles.
  • the samples with PISANE C9 exhibited a phase separation at pH 3, 4, 5 and 6 after 24 hours and 48 hours, respectively.
  • the isoelectric point (pl) of caseins is around 4.6 and the pl of major pea proteins at 4.5, presumably resulting in precipitation of the proteins.
  • the difference in solubility between the two pea protein isolates used may be related to potentially different proportions of pea protein subunits, such as vicilin, legumin and covicilin, which have differing molecular sizes and pl.
  • Figs. 14A-14D show phase diagrams of samples with previous acidification of casein at pH 2 for 48 hours of PISANE C9 x micellar casein powder (Fig. 14A), PURIS Pea 870 x micellar casein powder (Fig. 14B), PISANE C9 x micellar casein concentrate (Fig. 14C) and PURIS Pea 870 x micellar casein concentrate (Fig. 14D) at pH 2-11.
  • Figs. 15A-15D show phase diagrams of samples with previous homogenization of both protein solutions and acidification of casein at pH 2 for 24 hours and 48 hours, of PISANE C9 x micellar casein powder (Figs. 15A-15B) and PISANE C9 x micellar casein concentrate (Figs. 15C-15D) at pH 2-11.
  • Tables 2-7 provide visual descriptions for each sample prepared as described in this exemplary method.
  • Table 3 Visual description of aqueous 10% (w/w) mixture of pea protein isolate PISANE C9 (5% (w/w)) and micellar casein (5% (w/w))
  • Table 4 Visual description of aqueous 10% (w/w) mixture of pea protein isolate PURISpea 870 (5% (w/w)) and micellar casein (5% (w/w)).
  • Table 6 Visual description of samples of pea protein isolate PISANE C9 and PURIS Pea 870 with P-casein reduced micellar casein powder (after being stored for 24 h and 48 h at pH2).
  • Table 7 Visual description of samples of pea protein isolate PISANE C9 and PURIS Pea 870 with P-casein reduced micellar casein concentrate (after being stored for 24h and 48h at pH2).
  • Example 3 Microscopic Analysis of Structure Formation in Pea and Micellar Casein Samples [0196]
  • microscopic appearance and consistency of samples were assessed according to the methods described herein.
  • Samples were prepared according to the methods depicted in Figs. 2, 4, and 12. As a first screening, microscopic images were collected of samples of: 1) pea protein (PISANE C9) (10% w/w); 2) a mixture of pea protein (5% w/w) casein concentrate (5% w/w); and 3) casein concentrate (5% w/w) where the total protein content of each sample was 10% w/w.
  • Fig. 16 shows microscopic images collected from each sample at pH 2-11 after 0 hours or 24 hours of storage.
  • FIG. 17 shows images from a PISANE C9 pea protein (5% w/w) and cis-casein powder (5% w/w) mixture at varying storage times and varying pHs.
  • Figs. 18 and 19 show images from a PISANE C9 pea protein (5% w/w) and [3-casein reduced micellar powder (5% w/w) mixture at varying storage times and varying pHs.
  • Foodstuff prototypes containing plant protein isolates stored in alkaline buffer solutions are analyzed with respect to texture, rheology, stretchability and moisture content.
  • the prototypes produced contain the plant protein isolates at different percentages, as well as fats, starches, and/or water. All ingredients and methods used are food grade and readily available.
  • Rheological Behavior - Temperature sweeps evaluate the melting ability of foodstuff prototype samples, specifically evaluating the ability of the samples to soften and flow as temperature is increased from 5 °C to 100 °C. The melting profiles of each sample are plotted and differences in melting behavior between samples is determined. Amplitude sweeps performed at 50 °C are performed to examine the rheological properties (linear viscoelastic region and the critical or yield strain value) of the samples when the fat content is sufficiently melted. This ensures that the properties analyzed are primarily attributed to the protein content of the samples.
  • Texture Profile Analysis (TPA) - TPA involves a double compression of the samples that mimic the action of chewing. This makes the technique highly reliable when it comes to mechanically determining values for different sensory properties of solid or semi-solid foods. In this work, the values for hardness, springiness, chewiness, and gumminess for all samples are compared. Since the texture is relevant at both low and high temperatures, testing at a range of temperatures, such as 5 °C, 50 °C, and 150 °C, allows for direct comparison of both low and high temperature functionality of all samples.
  • the samples are stirred before the pH is adjusted to 2-11 by using HC1 and NaOH solutions (1 N, 3 N, and 10 N).
  • the mix is fed to a 40 kg capacity twin-screw extruder with speed of 25 kg/hour. Screw speed of 300 rpm is settled and temperatures profile 60 °C— >175 °C— >130 °C used in six temperature sections. The mass is let shortly to cool through 10 cm long die.
  • the post extrusion treatment is carried out by moisturizing the texturized food product with water where the share of water to the dry material is between 1: 1.0 to 1:5.
  • the texturized food product is placed in a liquid and fermented or, alternatively, the food product is hydrated, wetted or soaked for between 1-48 hours before further processing.
  • the brewed (or alternatively, hydrated, wetted or soaked) texturized food product is further treated with amylase and processed with high-speed mixing for 1 -60 minutes.
  • an additional high pressure-cooking step is performed in an autoclave or in a pressurized cooking device, preferably having a pressure of at least 2 bar, for 10 to 60 minutes (even more preferably, for around 25 minutes or for between 30 to 60 minutes, such as for 35 to 45 minutes).
  • the treated food product may be baked or cooked in a baking or cooking step, preferably in an oven or in a steam oven, at a temperature of between 110 and 130° C., most preferably around 121° C.
  • This post extrusion treatment further improves pleasant sensory properties of the texturized food products.
  • the example above shows the use of twin-screw extruder, it should be understood that extrusion processes are very diverse and manufacturing of extruded textured food products comprising functionalized plant proteins can be prepared via use of any acceptable model of type food processing extruder.

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Abstract

La présente invention concerne des compositions appropriées pour une utilisation dans des produits alimentaires, les compositions fournissant des textures aux produits alimentaires comparables à des produits alimentaires d'origine animale. Des modes de réalisation de l'invention concernent des compositions ayant une structure de fibre à base de plante capable de subir des changements structuraux dans des conditions alcalines.
PCT/IB2023/052018 2022-03-03 2023-03-03 Fonctionnalisation alcaline de compositions de protéines à base de plantes WO2023166491A1 (fr)

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Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0626175A2 (fr) * 1993-05-28 1994-11-30 Abbott Laboratories Produit entérale nutritif
WO2015071498A1 (fr) * 2013-11-18 2015-05-21 Cosucra Groupe Warcoing S.A. Procédé d'extraction de protéines de pois
US9149063B2 (en) * 2010-05-20 2015-10-06 Roquette Freres Method for preparing alkaline hydrolysates of plant proteins
US20170105438A1 (en) * 2015-10-20 2017-04-20 SAVAGE RIVER, INC. dba BEYOND MEAT Meat-like food products
US20190297927A1 (en) * 2018-04-03 2019-10-03 World Food Holdings, Llc Gluten free pasta and pasta-like products and usage of such

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0626175A2 (fr) * 1993-05-28 1994-11-30 Abbott Laboratories Produit entérale nutritif
US9149063B2 (en) * 2010-05-20 2015-10-06 Roquette Freres Method for preparing alkaline hydrolysates of plant proteins
WO2015071498A1 (fr) * 2013-11-18 2015-05-21 Cosucra Groupe Warcoing S.A. Procédé d'extraction de protéines de pois
US20170105438A1 (en) * 2015-10-20 2017-04-20 SAVAGE RIVER, INC. dba BEYOND MEAT Meat-like food products
US20190297927A1 (en) * 2018-04-03 2019-10-03 World Food Holdings, Llc Gluten free pasta and pasta-like products and usage of such

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Title
"Department of Soft Matter Science and Dairy Technology", UNIVERSITY OF HOHENHEIM
BATZER ET AL., NUCLEIC ACID RES., vol. 19, 1991, pages 5081
OHTSUKA ET AL., J. BIOL. CHEM., vol. 260, 1985, pages 2605 - 2608
ROSSOLINI ET AL., MOL. CELL. PROBES, vol. 8, 1994, pages 91 - 98

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