US20140193547A1 - Methods and compositions for consumables - Google Patents

Methods and compositions for consumables Download PDF

Info

Publication number
US20140193547A1
US20140193547A1 US14/152,499 US201414152499A US2014193547A1 US 20140193547 A1 US20140193547 A1 US 20140193547A1 US 201414152499 A US201414152499 A US 201414152499A US 2014193547 A1 US2014193547 A1 US 2014193547A1
Authority
US
United States
Prior art keywords
protein
proteins
meat
isolated
purified
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Abandoned
Application number
US14/152,499
Other languages
English (en)
Inventor
Patrick O'reilly Brown
Marija Vrljic
Ranjani Varadan
Michael Eisen
Sergey Solomatin
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Impossible Foods Inc
Original Assignee
Maraxi Inc
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Maraxi Inc filed Critical Maraxi Inc
Priority to US14/152,499 priority Critical patent/US20140193547A1/en
Assigned to MARAXI, INC. reassignment MARAXI, INC. ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: BROWN, PATRICK O'REILLY, EISEN, MICHAEL, SOLOMATIN, Sergey, VARADAN, Ranjani, VRLJIC, Marija
Assigned to IMPOSSIBLE FOODS INC. reassignment IMPOSSIBLE FOODS INC. CHANGE OF NAME (SEE DOCUMENT FOR DETAILS). Assignors: MARAXI, INC.
Publication of US20140193547A1 publication Critical patent/US20140193547A1/en
Priority to US14/752,540 priority patent/US20150289541A1/en
Priority to US15/985,694 priority patent/US20190008192A1/en
Priority to US17/531,491 priority patent/US20220071250A1/en
Abandoned legal-status Critical Current

Links

Images

Classifications

    • 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
    • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
    • A23L27/20—Synthetic spices, flavouring agents or condiments
    • A23L27/26—Meat flavours
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
    • A23D7/00—Edible oil or fat compositions containing an aqueous phase, e.g. margarines
    • A23D7/005—Edible oil or fat compositions containing an aqueous phase, e.g. margarines characterised by ingredients other than fatty acid triglycerides
    • A23D7/0053—Compositions other than spreads
    • 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
    • A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
    • 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
    • A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
    • A23J1/007—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials from leafy vegetables, e.g. alfalfa, clover, grass
    • 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
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/18—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from yeasts
    • 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
    • A23J3/22—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
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/20—Animal feeding-stuffs from material of animal origin
    • A23K10/24—Animal feeding-stuffs from material of animal origin from blood
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/30—Animal feeding-stuffs from material of plant origin, e.g. roots, seeds or hay; from material of fungal origin, e.g. mushrooms
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/158—Fatty acids; Fats; Products containing oils or fats
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/424—Addition of non-meat animal protein material, e.g. blood, egg, dairy products, fish; Proteins from microorganisms, yeasts or fungi
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/426—Addition of proteins, carbohydrates or fibrous material from vegetable origin other than sugars or sugar alcohols
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/428—Addition of flavours, spices, colours, amino acids or their salts, peptides, vitamins, yeast extract or autolysate, nucleic acid or derivatives, organic acidifying agents or their salts or acidogens, sweeteners, e.g. sugars or sugar alcohols; Addition of alcohol-containing products
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/43—Addition of vegetable fats or oils; Addition of non-meat animal fats or oils; Addition of fatty acids
    • 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
    • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
    • A23L27/20—Synthetic spices, flavouring agents or condiments
    • 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
    • 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
    • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
    • A23L5/10—General methods of cooking foods, e.g. by roasting or frying
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • Animal farming has a profound negative environmental impact. Currently it is estimated that 30% of Earth's land surface is dedicated to animal farming and that livestock account for 20% of total terrestrial animal biomass. Due to this massive scale animal farming accounts for more than 18% of net greenhouse gas emissions. Animal farming may be the largest human source of water pollution, and animal farming is by far the world's largest threat to biodiversity. It has been estimated that if the worlds human population could shift from a meat containing diet to a diet free of animal products, 26% of Earth's land surface would be freed for other uses. Furthermore the shift to a vegetarian diet would massively reduce water and energy consumption.
  • Hunger is a worldwide problem, yet the world's 4 major commodity crops (soybeans, maize, wheat, and rice) already supply more than 100% of the human population's requirements for calories and protein, including every essential amino acid.
  • Plant based meat substitutes have largely failed to cause a shift to a vegetarian diet.
  • the current state of the art for meat substitute compositions involves the extrusion of soy/grain mixture, resulting in products which largely fail to replicate the experience of cooking and eating meat.
  • Common limitations of these products are a texture and mouthfeel that are more homogenous than that of equivalent meat products.
  • the products must largely be sold pre-cooked, with artificial flavors and aromas built in, they fail to replicate aromas, flavors, and other key features associated with cooking meat.
  • these products appeal mainly to a limited consumer base that is already committed to vegetarianism/veganism, but have failed to appeal to the larger consumer segment accustomed to eating meat.
  • the invention provides a meat substitute composition comprising a protein content, wherein one or more isolated and purified proteins accounts for 10% or more of said protein content by weight, wherein said meat substitute composition accurately mimics the taste, texture, or color of a meat product derived from animal sources.
  • the meat substitute composition accurately mimics the color of said meat product in its raw state and in a cooked state after cooking.
  • the one or more isolated and purified proteins accounts for 25% or more of said protein content by weight.
  • the one or more isolated and purified proteins accounts for 50% or more of said protein content by weight.
  • the one or more isolated and purified proteins accounts for 75% or more of said protein content by weight.
  • the one or more isolated and purified proteins accounts for 90% or more of said protein content by weight.
  • gluten does not account for 10% or more of said protein content by weight.
  • each of said isolated, purified proteins is separately isolated and purified.
  • the meat substitute composition comprises 1-7 isolated and purified proteins.
  • said 1-7 isolated and purified proteins are each isolated from different plant species.
  • the meat substitute comprises less than 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 individual proteins isolated from one or more plant species.
  • said protein content comprises no more than trace amounts of any other proteins derived from the one or more plant species.
  • said one or more isolated and purified proteins are selected from the group consisting of leghemoglobin, non-symbiotic hemoglobin, hemoglobin, myoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, triose phosphate isomerases, phosphoglycerate kinases, phosphoglycerate mutases, enolases, pyruvate kinases, glyceraldehyde-3-phosphate dehydrogena
  • said one or more isolated and purified proteins are not isolated from an animal.
  • said one or more isolated and purified proteins are isolated from a single plant source.
  • said one or more isolated and purified proteins are isolated from multiple plant sources.
  • said genetically modified organism is a genetically modified bacteria or yeast organism.
  • said isolated, purified protein has been formed into fibers.
  • said fibers resemble skeletal muscle fibers.
  • said fibers are asymmetric fibers.
  • the meat substitute composition further comprises one or more isolated and purified iron-containing proteins.
  • said one or more isolated and purified iron-containing proteins is selected from the group consisting of hemoglobin, myoglobin, leghemoglobin, non-symbiotic hemoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 1.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 2.
  • SEQ ID NO 2 MIDQKEKELI KESWKRIEPN KNEIGLLFYA NLFKEEPTVS VLFQNPISSQ SRKLMQVLGI LVQGIDNLEG LIPTLQDLGR RHKQYGVVDS HYPLVGDCLL KSIQEYLGQG FTEEAKAAWT KVYGIAAQVM TAE.
  • said iron-containing protein comprises an amino acid sequence with at least 80% homology to SEQ ID NO 2.
  • said iron-containing protein comprises an amino acid sequence with at least 90% homology to SEQ ID NO 2.
  • said iron-containing protein comprises an amino acid sequence with at least 98% homology to SEQ ID NO 2.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 3.
  • said iron-containing protein comprises an amino acid sequence with at least 80% homology to SEQ ID NO 3.
  • said iron-containing protein comprises an amino acid sequence with at least 90% homology to SEQ ID NO 3.
  • said iron-containing protein comprises an amino acid sequence with at least 98% homology to SEQ ID NO 3.
  • the isolated and purified proteins are assembled into one or more gels.
  • the meat substitute composition further comprises one or more fats.
  • said one or more fats are derived from a plant source.
  • the invention provides a meat substitute product that comprises an indicator that indicates cooking progression from a raw state to a cooked state, wherein said meat substitute product is derived from non-animal sources.
  • said indicator is a visual indicator that accurately mimics the color transition of a meat product during said cooking progression.
  • said color transition is from red to brown.
  • said color transition is from pink to white or tan.
  • said visual indicator transitions from a translucent to opaque color during said cooking progression.
  • the indicator is an olfactory indicator that indicates cooking progression.
  • said olfactory indicator is one or more volatile odorants released during cooking.
  • said indicator comprises one or more isolated, purified iron-containing proteins.
  • said one or more isolated, purified iron-containing proteins is in a reduced state before cooking.
  • said one or more isolated and purified iron-containing proteins is selected from the group consisting of hemoglobin, myoglobin, leghemoglobin, non-symbiotic hemoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 1.
  • said one or more isolated and purified iron-containing proteins are not isolated from an animal. In some embodiments compositions of the invention do not contain any proteins from an animal.
  • said one or more isolated and purified iron-containing proteins are isolated from one or more plant sources.
  • said one or more isolated, purified proteins are isolated from the root nodules, roots, seeds, leaves, or stems of said one or more plant sources.
  • said one or more plant sources are soy or pea plants.
  • said one or more plant sources comprises one or more plants of the legume family.
  • said one or more isolated and purified iron carrying proteins in a reduced or oxidized state has a similar UV-VIS profile to a myoglobin protein derived from an animal source when in an equivalent reduced or oxidized state.
  • the difference between the peak absorbance wavelength of said one or more isolated and purified iron-containing proteins and the peak absorbance wavelength of myoglobin derived from an animal source is less than 5%.
  • said one or more isolated, purified proteins are isolated from a genetically modified organism.
  • said genetically modified organism is a genetically modified bacteria or yeast organism.
  • the meat substitute product contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the meat substitute product additionally contains less than 1% wheat gluten.
  • said meat substitute product contains no wheat gluten.
  • said meat substitute product contains no soy protein isolate.
  • said meat substitute product contains no soy protein concentrate.
  • said meat substitute product contains no soy protein.
  • said meat substitute product contains less than 5% carbohydrates.
  • said meat substitute product contains no tofu.
  • said meat substitute product contains no tofu, and no wheat gluten.
  • said meat substitute product contains no soy protein, and no wheat gluten.
  • said meat substitute product contains no animal products and less than 5% carbohydrates.
  • said meat substitute product contains less than 1% cellulose.
  • said meat substitute product contains less than 5% insoluble carbohydrates.
  • said meat substitute product contains no soy protein, and less than 1% cellulose.
  • said meat substitute product contains no soy protein, and less than 5% insoluble carbohydrates.
  • said meat substitute product contains no wheat gluten, and less than 1% cellulose.
  • said meat substitute product contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the invention provides a muscle tissue replica comprising a protein content, wherein said protein content comprises one or more isolated and purified proteins, wherein said muscle tissue replica approximates the taste, texture, or color of an equivalent muscle tissue derived from an animal source.
  • said one or more isolated and purified proteins accounts for at least 50% of said protein content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 40% of said protein content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 30% of said protein content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 20% of said protein content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 10% of said protein content by weight.
  • said one or more isolated and purified proteins accounts for at least 50% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 40% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 30% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 20% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 10% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 5% of said composition content by weight. In some embodiments, said one or more isolated and purified proteins accounts for at least 1% of said composition content by weight.
  • said protein content is derived from one or more non-animal sources.
  • said one or more non-animal sources is a plant source.
  • said one or more non-animal sources is a genetically modified yeast or bacteria.
  • each of said one or more isolated proteins is isolated and purified separately.
  • said one or more isolated proteins are selected from the group consisting of hemoglobin, myoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, triose phosphate isomerases, phosphoglycerate kinases, phosphoglycerate mutases, enolases, pyruvate kinases, glyceraldehyde-3-phosphate dehydrogenases, pyruvate decarboxylases, actins,
  • said seed storage protein is moong bean 8S protein.
  • said protein content is suspended in a gel.
  • said protein content is in the form of a gel.
  • said gel comprises an isolated, purified cross-linking enzyme.
  • said isolated, purified cross-linking enzyme is selected from the group consisting of transglutaminase, lysyl oxidases, and amine oxidases.
  • said isolated, purified cross-linking enzyme is transglutaminase.
  • said protein content has been assembled into fibers.
  • said fibers are arranged isotropically.
  • said fibers are asymmetric fibers.
  • the muscle tissue replica further comprises one or more isolated and purified iron-containing proteins.
  • said one or more isolated and purified iron-containing proteins is selected from the group consisting of hemoglobin, myoglobin, leghemoglobin, non-symbiotic hemoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • said one or more isolated and purified iron-containing proteins comprises an amino acid sequence with at least 70% homology to SEQ ID NO 1.
  • SEQ ID NO 1 MVAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEK LFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDKWSDELS RAWEVAYDELAAAIKKA.
  • said one or more isolated and purified iron-containing proteins comprises an amino acid sequence with at least 80% homology to SEQ ID NO 1.
  • said one or more isolated and purified iron-containing proteins comprises an amino acid sequence with at least 90% homology to SEQ ID NO 1. In a particular embodiment, said one or more isolated and purified iron-containing proteins comprises an amino acid sequence with at least 95% homology to SEQ ID NO 1. In a particular embodiment, said one or more isolated and purified iron-containing proteins comprises an amino acid sequence with at least 98% homology to SEQ ID NO 1.
  • the muscle tissue replica comprises a protein content, wherein (i) one isolated and purified protein that is not an iron-containing protein accounts for 40-95% of said protein content, (ii) one or more isolated and purified iron-containing proteins accounts for 1-20% of said protein content, and (iii) one or more cross-linking reagents accounts for 0.1-35% of said protein content.
  • said protein content accounts for 5-50% of said replica by weight or by weight/volume.
  • said one isolated and purified protein is moong bean 8S protein.
  • said one or more isolated and purified iron-containing proteins is leghemoglobin.
  • said one or more cross-linking reagents is transglutaminase.
  • the muscle tissue replica contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the muscle tissue replica additionally contains less than 1% wheat gluten. In particular embodiments, the muscle tissue replica additionally contains less than 5% wheat gluten. In particular embodiments, the muscle tissue replica additionally contains less than 10% wheat gluten. In particular embodiments, the muscle tissue replica additionally contains less than 0.1% wheat gluten.
  • said muscle tissue replica contains no wheat gluten.
  • said muscle tissue replica contains no soy protein isolate.
  • said muscle tissue replica contains no soy protein concentrate.
  • said muscle tissue replica contains no soy protein.
  • said muscle tissue replica contains less than 5% carbohydrates.
  • said muscle tissue replica contains no tofu.
  • said muscle tissue replica contains no tofu, and no wheat gluten.
  • said muscle tissue replica contains no soy protein, and no wheat gluten.
  • said muscle tissue replica contains no animal products and less than 5% carbohydrates.
  • said muscle tissue replica contains less than 1% cellulose.
  • said muscle tissue replica contains less than 5% insoluble carbohydrates.
  • said muscle tissue replica contains no soy protein, and less than 1% cellulose.
  • said muscle tissue replica contains no soy protein, and less than 5% insoluble carbohydrates.
  • said muscle tissue replica contains no wheat gluten, and less than 1% cellulose.
  • said muscle tissue replica contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the muscle tissue replica contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the meat replica contains less than 1% wheat gluten. In particular embodiments, the meat replica contains less than 5% wheat gluten. In particular embodiments, the meat replica contains less than 10% wheat gluten. In particular embodiments, the meat replica contains less than 0.1% wheat gluten.
  • the meat replica contains no wheat gluten.
  • the meat replica contains no soy protein isolate.
  • the meat replica contains no soy protein concentrate.
  • the meat replica contains no soy protein.
  • the meat replica contains less than 5% carbohydrates.
  • the meat replica contains no tofu.
  • the meat replica contains no tofu, and no wheat gluten.
  • the meat replica contains no soy protein, and no wheat gluten.
  • the meat replica contains no animal products and less than 5% carbohydrates.
  • the meat replica contains less than 1% cellulose. In some embodiments, the meat replica contains less than 0.1% cellulose. In some embodiments, the meat replica contains less than 10% cellulose. In some embodiments, the meat replica contains less than 5% cellulose.
  • the meat replica contains less than 5% insoluble carbohydrates.
  • the meat replica contains no soy protein, and less than 1% cellulose.
  • the meat replica contains no soy protein, and less than 5% insoluble carbohydrates.
  • the meat replica contains no wheat gluten, and less than 1% cellulose.
  • the meat replica contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the invention provides a fat tissue replica comprising a gelled emulsion, said gelled emulsion comprising a protein solution with fat droplets suspended therein.
  • said fat droplets are derived from a non-animal source.
  • said fat droplets are comprised of one or more plant oils.
  • said one or more plant oils is selected from the group consisting of corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, oils produced by bacteria, algae, archaea or fungi or genetically engineered bacteria, algae, archaea or fungi, triglycerides, monoglycerides, diglycerides, sphingosides, glycolipids, lecithin, lysolecithin, phophatidic acids, lysophosphatidic acids, oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid,
  • said one or more plant oils is rice bran oil or canola oil.
  • said protein solution comprises one or more isolated, purified proteins.
  • said one or more isolated, purified proteins accounts for 75% or more of the protein in said protein solution.
  • said one or more isolated, purified proteins are derived from a non-animal source.
  • said non-animal source is a plant source.
  • said non-animal source is a genetically modified yeast or bacteria.
  • each of said one or more isolated proteins is isolated and purified separately.
  • said one or more isolated proteins are selected from the group consisting of hemoglobin, myoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, triose phosphate isomerases, phosphoglycerate kinases, phosphoglycerate mutases, enolases, pyruvate kinases, glyceraldehyde-3-phosphate dehydrogenases, pyruvate decarboxylases, actins,
  • said one or more isolated, purified proteins is an albumin protein, a seed storage protein, or pea globulin protein.
  • said albumin protein is isolated pea albumin protein.
  • said seed storage protein is moong bean 8S protein.
  • said gelled emulsion comprises a protein solution comprising 1-3 isolated and purified proteins, wherein said solution accounts for 30-70% of the volume of said emulsion; a plant oil, wherein said plant oil accounts for 30-70% of the volume of said emulsion; and an isolated, purified cross-linking enzyme, wherein said cross-linking enzyme accounts for 0.5-5% of said emulsion by wt/volume; wherein said plant oil is emulsified in said protein solution, wherein said emulsion is formed into a gel by said cross-linking enzyme.
  • said gelled emulsion comprises a protein solution comprising 1-3 isolated and purified proteins, wherein said solution accounts for 1-30% of the volume of said emulsion; a plant oil, wherein said plant oil accounts for 70-99% of the volume of said emulsion; and an isolated, purified cross-linking enzyme, wherein said cross-linking enzyme accounts for 0.5-5% of said emulsion by wt/volume; wherein said plant oil is emulsified in said protein solution, wherein said emulsion is formed into a gel by said cross-linking enzyme.
  • the fat replica further comprises a cross-linking enzyme.
  • said cross-linking enzyme is transglutaminase.
  • one of said 1-3 isolated and purified proteins is moong bean 8S protein, pea albumin protein, or pea globulin protein.
  • said plant oil is rice bran oil or canola oil.
  • the fat tissue replica contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the fat tissue replica additionally contains less than 1% wheat gluten.
  • said fat tissue replica contains no wheat gluten.
  • said fat tissue replica contains no soy protein isolate.
  • said fat tissue replica contains no soy protein concentrate.
  • said fat tissue replica contains no soy protein.
  • said fat tissue replica contains less than 5% carbohydrates.
  • said fat tissue replica contains no tofu.
  • said fat tissue replica contains no tofu, and no wheat gluten.
  • said fat tissue replica contains no soy protein, and no wheat gluten.
  • said fat tissue replica contains no animal products and less than 5% carbohydrates.
  • said fat tissue replica contains less than 1% cellulose.
  • said fat tissue replica contains less than 5% insoluble carbohydrates.
  • said fat tissue replica contains no soy protein, and less than 1% cellulose.
  • said fat tissue replica contains no soy protein, and less than 5% insoluble carbohydrates.
  • said fat tissue replica contains no wheat gluten, and less than 1% cellulose.
  • said fat tissue replica contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the invention provides a connective tissue replica, comprising a protein content comprising one or more isolated, purified proteins, wherein said protein content has been assembled into structures approximating the texture and visual appearance of connective tissue or skin.
  • said protein content is derived from non-animal source.
  • said non-animal source is a plant source.
  • said non-animal source is a genetically modified yeast or bacteria.
  • said one or more isolated proteins account for 50% or more of said protein content by weight.
  • said one isolated and purified protein accounts for 90% or more of said protein content by weight.
  • each of said one or more isolated proteins is isolated and purified separately.
  • said one or more isolated proteins are selected from the group consisting of hemoglobin, myoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, triose phosphate isomerases, phosphoglycerate kinases, phosphoglycerate mutases, enolases, pyruvate kinases, glyceraldehyde-3-phosphate dehydrogenases, pyruvate decarboxylases, actins,
  • said one or more isolated and purified proteins is a prolamin family protein.
  • said one or more isolated and purified proteins is zein.
  • said protein content is suspended in a gel.
  • said gel comprises an isolated, purified cross-linking enzyme.
  • said isolated, purified cross-linking enzyme is selected from the group consisting of transglutaminase, lysyl oxidases, and amine oxidases.
  • said isolated, purified cross-linking enzyme is transglutaminase.
  • said protein content is formed into a fiber.
  • said fiber is produced by an extrusion process.
  • said fiber is stabilized by protein crosslinks.
  • fiber contains an isolated, purified cross-linking enzyme.
  • said isolated, purified cross-linking enzyme is selected from the group consisting of transglutaminase, lysyl oxidases, and amine oxidases.
  • said isolated, purified cross-linking enzyme is transglutaminase.
  • the invention provides a meat substitute product, comprising a muscle replica; a fat tissue replica; and a connective tissue replica; wherein said muscle replica, fat tissue replica, and/or connective tissue replica are assembled in a manner that approximates the physical organization of meat.
  • the meat substitute product comprises two or more of said muscle replica, fat tissue replica, and connective tissue replica.
  • said muscle replica accounts for 40-90% of said product by weight
  • said fat tissue replica accounts for 1-60% of said product by weight
  • said connective tissue replica accounts for 1-30% of said product by weight.
  • the meat substitute product comprises 60-90% water; 5-30% protein content; and 1-20% of a fat or fat replica; wherein said protein content comprises one or more isolated, purified plant proteins.
  • said protein content is derived from non-animal source.
  • non-animal source is a plant source.
  • said non-animal source is a genetically modified yeast or bacteria.
  • 50% or more of said protein content by weight are one or more isolated purified proteins.
  • each of said one or more isolated proteins is isolated and purified separately from different plant species.
  • one or more of said isolated proteins is selected from the group consisting of: hemoglobin, myoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, triose phosphate isomerases, phosphoglycerate kinases, phosphoglycerate mutases, enolases, pyruvate kinases, glyceraldehyde-3-phosphate dehydrogenases, pyruvate decarboxylases, actin
  • the meat substitute product further comprises one or more isolated and purified iron-containing proteins.
  • said one or more isolated and purified iron-containing proteins is selected from the group consisting of hemoglobin, myoglobin, leghemoglobin, non-symbiotic hemoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 1. [SEQ ID NO 1:
  • the meat substitute product contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the meat substitute product additionally contains less than 1% wheat gluten.
  • said meat substitute product contains no wheat gluten.
  • said meat substitute product contains no soy protein isolate.
  • said meat substitute product contains no soy protein concentrate.
  • said meat substitute product contains no soy protein.
  • said meat substitute product contains less than 5% carbohydrates.
  • said meat substitute product contains no tofu.
  • said meat substitute product contains no tofu, and no wheat gluten.
  • said meat substitute product contains no soy protein, and no wheat gluten.
  • said meat substitute product contains no animal products and less than 5% carbohydrates.
  • said meat substitute product contains less than 1% cellulose.
  • said meat substitute product contains less than 5% insoluble carbohydrates.
  • said meat substitute product contains no soy protein, and less than 1% cellulose.
  • said meat substitute product contains no soy protein, and less than 5% insoluble carbohydrates.
  • said meat substitute product contains no wheat gluten, and less than 1% cellulose.
  • said meat substitute product contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the invention provides a food product comprising one or more isolated, purified iron-containing proteins, wherein said food product is configured for consumption by an animal.
  • said one or more isolated, purified iron-containing proteins is derived from a non-animal source.
  • said non-animal source is a plant source.
  • said plant source comprises one or more plants of the legume family.
  • said one or more plants of the legume family is a soy or pea plant.
  • said non-animal source is a genetically modified yeast or bacteria.
  • said iron-containing protein is selected from the group consisting of hemoglobin, myoglobin, leghemoglobin, non-symbiotic hemoglobin, chlorocruorin, erythrocruorin, neuroglobin, cytoglobin, protoglobin, truncated 2/2 globin, HbN, cyanoglobin, HbO, Glb3, and cytochromes, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • said iron-containing protein comprises an amino acid sequence with at least 70% homology to SEQ ID NO 1. [SEQ ID NO 1:
  • the food product contains no methylcellulose, no carrageenan, no caramel color, no konjac flour, no gum arabic, and no acacia gum.
  • the food product additionally contains less than 1% wheat gluten.
  • said food product contains no wheat gluten.
  • said food product contains no soy protein isolate.
  • said food product contains no soy protein concentrate.
  • said food product contains no soy protein.
  • said food product contains less than 5% carbohydrates.
  • said food product contains no tofu.
  • said food product contains no tofu, and no wheat gluten.
  • said food product contains no soy protein, and no wheat gluten.
  • said food product contains no animal products and less than 5% carbohydrates.
  • said food product contains less than 1% cellulose.
  • said food product contains less than 5% insoluble carbohydrates.
  • said food product contains no soy protein, and less than 1% cellulose.
  • said food product contains no soy protein, and less than 5% insoluble carbohydrates.
  • said food product contains no wheat gluten, and less than 1% cellulose.
  • said food product contains no wheat gluten, and less than 5% insoluble carbohydrates.
  • the invention provides a method of making a meat substitute composition, comprising isolating and purifying one or more proteins; and assembling said one or more proteins into a physical organization that approximates the physical organization of meat.
  • the invention provides a method of making a muscle tissue replica, comprising isolating and purifying one or more proteins; and assembling said one or more proteins into a physical organization that approximates the physical organization of skeletal muscle.
  • the invention provides a method of making a fat tissue replica, comprising isolating and purifying one or more proteins; preparing a solution comprising one or more proteins; emulsifying one or more fats in said solution; and stabilizing said solution into a gelled emulsification with one or more cross-linking reagents.
  • the invention provides a method of making a connective tissue replica, comprising isolating and purifying one or more proteins; and precipitating said one or more proteins, wherein said precipitating results in said one or more proteins forming physical structures approximating the physical organization of connective tissue.
  • said precipitating comprises solubilizing said one or more proteins in a first solution; and extruding said first solution into a second solution, wherein said one or more proteins is insoluble in said second solution, wherein said extruding induces precipitation of said one or more proteins.
  • the invention provides a food product comprising one or more isolated, purified iron-containing proteins, wherein said food product is configured for consumption by an animal.
  • the invention provides a food product comprising one or more isolated, purified iron-containing proteins, wherein said food product is configured for consumption by humans.
  • the invention provides a food product comprising one or more isolated, purified iron-containing proteins, wherein said food product is configured for consumption by an animal. In another aspect, the invention provides a food product comprising one or more isolated, purified iron-containing proteins, wherein said food product is configured for consumption by humans.
  • FIG. 1 depicts a portion of the root of a pea plant ( Pisum sativum ) with the root nodules sliced open to demonstrate the red color conferred by leghemoglobin contained therein. The sliced open rood nodule appears red.
  • FIG. 2 depicts leghemoglobin isolated from 1 oz of pea roots. The red color commonly attributed to meat is evident in the color photo.
  • FIG. 3 shows that leghemoglobins from different species are homologs and have similar color properties.
  • panel A shows an SDS_PAGE gels of lysed root-nodules of three legume plant species (1) Fava bean (2) English Pea (3) Soybean. Arrows mark respective leghemoglobins.
  • Panel B shows the similarity of UV-VIS spectral profile of leghemoglobins from two different plant species (Favabean and Soybean).
  • FIG. 4 shows a comparison of reduced (heme iron 2+) and oxidized (heme iron 3+) soybean leghemoglobin ( FIG. 4 panel A) and equine heart muscle myoglobin ( FIG. 4 panel B) showing similarity of UV-VIS absorption profiles of two proteins.
  • soybean leghemoglobin from soybean root-nodules using here described protocol.
  • Purified equine myoglobin was purchased from SigmaAldrich. Soybean leghemoglobin ( FIG. 4 panel A) and equine myoglobin ( FIG. 4 panel B) were reduced with 1 mm sodium hydrosulfite. Shown are UV-VIS absorption spectra of heme Fe3+ (blue line—the higher peak in FIGS.
  • FIG. 4 panel A Images of 10 ul liquid droplet of a 40 mg/ml solution of soybean leghemoglobin in the heme-Fe3+ state (left droplet) showing characteristic rusty red color and a 40 mg/ml solution of soybean leghemoglobin solution in the heme-Fe2+ state (right droplet) showing characteristic red color of and (right image) corresponding samples of equine myoglobin.
  • FIG. 5 depicts examples of successful reduction of leghemoglobin heme iron with sodium hydrosulfite and titanium citrate.
  • the UV-VIS spectrogram of purified soybean leghemoglobin in which the heme iron is in the oxidized (+3) state is represented by the blue curves in each panel (the blue curves have the higher peaks on the main graphs).
  • the red curves in each panel represent the UV-VIS spectra of the same leghemoglobin species after reduction to the (+2) state (red lines) by addition of (Panel A) 1 mM sodium hydrosulfite or (Panel B) 0.24% (wt/v) titanium citrate in 20 mM potassium phosphate pH 7.3, 100 mM sodium chloride buffer.
  • leghemoglobin was purified from soybean root nodules using 60/90% ammonium sulfate fractionation and exchanged into 20 mM potassium phosphate pH 7.4, 100 mM sodium chloride buffer.
  • Sodium hydrosulfite stock solution was prepared by dissolving 100 mM sodium hydrosulfite in 1 mM sodium hydroxide in water.
  • Titanium citrate stock solution was prepared from 20% (wt/v) Ti-chloride in hydrochloric acid by mixing it with 0.2M sodium citrate (1:10 v/v). pH was adjusted using sodium carbonate to pH 7.0.
  • FIG. 6 depicts an example of the leghemoglobin purification flow from soybean root nodules.
  • the figure shows SDS-PAGE fractionation of different soybean leghemoglobin purification steps (Lane 1) Soybean root-nodule lysate; (Lane 2) Soybean root-nodule lysate purified by 60/90% (wt/v) ammonium sulfate fractionation.
  • leghemoglobin content at different purification steps was determined by determining the fraction of leghemoglobin band on SDS-PAGE gel in a respective sample using ImageDoc analysis software (BioRad). Purity (partial abundance) of leghemoglobin at respective steps in the purification steps was: lysate: 32.7% (lane 1), 60/90% (wt/v) ammonium sulfate fractionation 78% (lane 2), anion-exchange chromatography ⁇ 83% (lane 3), and size-exclusion chromatography to 95% (lane 4).
  • FIG. 7 shows stained SDS-PAGE gel analysis of (A) soybean leghemoglobin expressed and purified using recombinant protein technology and (B) soybean leghemoglobin purified from soybean root nodules.
  • A Recombinant Soybean leghemoglobin A carrying His-tag and TEV protease His-tag removal site was expressed in E. coli BL21 strain and purified using His-tag affinity chromatography (Talon resin, CloneTech). The left lane contains molecular weight standards, the right lane contains purified recombinant soybean leghemoglobin A (arrow). Expected molecular weight of the recombinant soybean leghemoglobin A is 17.1 kDa.
  • FIG. 8 shows an example of 6 cubes of a commercial meat analog (Quorn chicken analog), about 1 cm on a side, 4 of which (Left and lower right) have been soaked in a solution of about 10 mg/ml soybean leghemoglobin in 20 mM Potassium phosphate pH 7.4 and 100 mM NaCl; the remaining two (Upper right) were soaked in the same buffer without leghemoglobin.
  • a deep pink color of the leghemoglobin-infused cubes is apparent in color photos contrasting the pale tan color of the un-infused cubes.
  • FIG. 9 shows the 4 leghemoglobin-infused cubes of Quorn chicken analog in the process of cooking in a pan at 350° C.
  • the two lower cubes have been turned over to expose the grilled surface, which has turned brown.
  • the heated portion has turned grey-brown, while the cooler top surface retains its pink color.
  • the consumable is injected with a heme containing solution, for instance a leghemoglobin solution, until the consumable is the color of uncooked meat.
  • FIG. 10 depicts 43 ml of moong bean protein solution (150 mg/ml in dialysis buffer) were mixed with 37 ml of leghemoglobin solution (46.5 mg/ml leghemoglobin and 20 mg/ml of other soybean root nodule protein) in 20 mM potassium phosphate, 100 mM NaCl, pH 7.3). 20 ml of transglutaminase solution (20% w/w) were added, solutions thoroughly mixed, divided into two 50 ml Falcon tubes and incubated overnight at room temperature. Final protein concentrations were 65 mg/ml for moong bean protein, 18 mg/ml of leghemoglobin, 91 mg/ml total protein.
  • FIG. 11 depicts “White” muscle analog prepared by mixing 43 ml moong bean protein solution (150 mg/ml) with 45 ml of 11.7 mg/ml solution of leghemoglobin and 0.8% (wt/v) of transglutaminase solution. Final protein concentrations were 63 mg/ml for moong bean protein, 5.2 mg/ml of leghemoglobin, 68 mg/ml total protein.
  • FIG. 12 depicts a fat tissue analog based on moong beans and prepared in eppendorf tubes formed an opaque gel of off-white color, smooth uniform texture, with no visible discernible liquid that was not incorporated into the gel.
  • the gel was freely standing, elastic and springy.
  • the gel has a slight, pleasant aroma and a mild and pleasant flavor.
  • the taste is mildly salty.
  • FIG. 13 depicts at tissue analog based on pea globulin and prepared in eppendorf tubes very similar to moong bean-based fat analog, except that it gave up a little of oil upon compression.
  • FIG. 14 shows connective-tissue analog strands that were created using a 1:3 ratio in 70% ethanol, loaded into a syringe with a 23 gauge needle (ID 0.337 mm)
  • the solution was slowly extruded from the bottom of a 5 inch-high vessel into an excess of 5 M NaCl solution.
  • the ethanol-zein solution being less dense than the NaCl solution, floated upward, drawing out a fibrous stand of solidifying zein.
  • the NaCl was constantly stirred as the strands began to develop to assist in the strand lengthening. The strands bunch together and become a hard, dense mass.
  • FIG. 15 depicts a ground beef prototype patty was made by combining 62% (wt/wt) muscle analog (62% (wt/wt) “dark muscle analog” and 38% (wt/wt) “white muscle analog”), 29% (wt/wt) fat tissue analog (from pea globulin and canola oil), 5% (wt/wt) connective tissue analog ( FIG. 15 panel A).
  • a ground beef prototype patty was made by combining 62% muscle analog (62% “dark muscle analog” and 38% “white muscle analog), 29% fat tissue analog (from moong bean seed 8S protein and rice bran oil), 5% connective tissue analog ( FIG. 15 panel B).
  • a ground beef prototype patty was made by combining 71% (wt/wt) muscle tissue analog (composed of 60% “white” muscle analog, 40% “dark” muscle analog), 23% fat tissue (from pea seed globulin proteins and canola oil) ( FIG. 15 panel C).
  • a ground beef prototype patty was made by combining 67% “White” muscle analog, with 28% fat tissue analog (from pea globulins and rice bran oil), ( FIG. 15 , panel D)
  • FIG. 16 depicts a ground beef patty analog was made by combining 62% (wt/wt) muscle tissue analog (62% (wt/wt) “dark muscle analog” and 38% (wt/wt) “muscle analog”), 29% (wt/wt) fat tissue analog (from pea globulin and canola oil), 5% (wt/wt) connective tissue analog.
  • the panel on the left shows the patty before cooking and the panel on the right shows the same patty after cooking for about 2 minutes. Observers described the aroma of the cooking ground beef replica as distinctly “beefy”.
  • the consumables can be for animal consumption.
  • the consumable can be food fit for human consumption.
  • the consumable can be approved by suitable regulatory authorities.
  • the consumables can be sold in grocery stores or prepared in restaurants, schools, hospitals, military facilities, prisons, shelters, long-term care facilities, similar to already existing human foods.
  • the consumables could also be food for domestic animals.
  • dog food could be produced according to the present inventions.
  • the consumables may also be food for wild animals.
  • the consumables could be provided to non-domesticated predatory animals.
  • the consumables of the present invention can compete with, supplement or replace animal based foods.
  • the consumables can be meat replicas made entirely from plant sources.
  • the consumables can be made to mimic the cut or appearance of meat as it is currently sold.
  • a consumable may be visually similar to or indistinguishable from ground beef or a particular cut of beef.
  • the consumables can be made with a unique look or appearance.
  • the consumable could contain patterns or lettering that is based upon the structure of the consumable.
  • the consumables look like traditional meat products after they are prepared. For example a consumable may be produced which is larger than a traditional cut of beef but which, after the consumable is sliced and cooked appears the same as a traditional cooked meet.
  • the consumable may resemble a traditional meat shape in two dimensions, but not in a third.
  • the consumable may resemble a cut of meat in two dimensions (for example when viewed from the top), but may be much longer (or thinker) than the traditional cut. So in some embodiments a composition that can be cut repeatedly into traditionally meat shaped products is provided.
  • the consumable may be made entirely from plant based sources. In some instances the consumable can be made from organic sources. The consumables may also be made from a combination of plant based sources and animal based sources. For instance, the consumable may be a ground beef product supplemented with plant based products of the invention.
  • the consumables can be made from local products.
  • the consumables can be made from plants grown within a certain radius of the eventual consumer. That radius could be 1, 10, 100, or 1000 miles for example. So, in some embodiments, the invention provides a method for producing a meat replica which does not contain products which have been shipped over 1, 10, 100, or 1000 miles prior to producing the meat replica.
  • the present invention provides methods for producing consistent properties from the consumables when they are produced from various sources. So, for example, a plant based meat replica produced from local plants in Iowa, USA, will have substantially similar taste, odor, and texture as a plant based meat replica produced from local plants in Lorraine, France.
  • This consistency allows for methods for advertising locally grown foods with consistent properties.
  • the consistency can arise from the concentration or purification of similar components at different locations. These components can be combined in predetermined ratios to insure consistency.
  • a high degree of characteristic consistency is possible using components (e.g. isolated or concentrated proteins and fats) which come from the same plant species.
  • a high degree of characteristic consistency is possible using components (e.g. isolated or concentrated proteins and fats) which come from the different plant species.
  • the same proteins can be isolated from different plant species.
  • the invention provides for a method comprising isolating similar plant constituents from plant sources in different locations, assembling in both locations compositions provided herein, and selling the compositions, wherein the compositions assembled and sold at different the geographic locations have consistent physical and chemical properties.
  • the isolated constituents are from different plant populations in different locations. In some embodiments one or more of the isolated constituents are shipped to the separate geographic locations.
  • the consumables may require fewer resources to produce than consumables produced from domesticated animals. Accordingly, the present invention provides for meat replicates which require less water or energy to produce than meat.
  • a consumable can require less than about 10, 50, 100, 200, 300, 500, or 1000 gallons of water per pound of consumable.
  • beef can require over 2000 gallons of water per pound of meat.
  • the consumable may require less land are to produce than a meat product with similar protein content.
  • the consumable may require 30% or less of the land area required to produce a meat product with similar protein content.
  • the consumable may have health benefits compared to an animal product it replaces in the diet. For example it may have less cholesterol or lower levels of saturated fats than comparable meat products.
  • the consumable may have animal welfare benefits compared to an animal product it replaces in the diet. For instance it may be produced without requiring confinement, forced feeding, premature weaning, disruption of maternal-offspring interactions, or slaughter of animals for their meat.
  • the consumable may have a smaller “carbon footprint” than the meat products they replace.
  • the consumable may result in net greenhouse gas emissions of 1%, 5%, 10%, 25%, 50% or 75% of the greenhouse gas emissions attributable to the animal product it replaces.
  • the consumable may provide alternatives to animal products or combinations of animal products whose consumption is forbidden by religious beliefs.
  • the consumable may be a kosher pork chop.
  • the consumable can also be shipped in components and produced or assembled at a different location.
  • local components can be used for production of the consumable. These can be supplemented with components which are not locally available. This allows for methods of producing consumables, for instance meat replicates, using less energy in shipment than is required for meat.
  • local water can be used in combination with a kit which provides other components of the consumable. Using local water will reduce shipping weight thereby reducing cost and environmental impact.
  • the consumables can be produced or assembled wholly or in part in areas where animal farming is not practical or is not allowed.
  • the consumable can be produced or assembled within an urban environment.
  • a kit may be provided to a user to enable the user to produce the consumable.
  • the user could use local water or use plants from a rooftop garden, for instance in Shanghai.
  • the consumables could be produced aboard a space craft, space station, or lunar base.
  • the present invention provides methods and systems for the production of meat replicas for use in space travel or for training for the same.
  • the present invention could be used in earth based training for space travel.
  • the consumables could also be produced on an island or upon a manmade platform at sea where the keeping of livestock is difficult or prohibited.
  • the consumables are, in some embodiments, designed to replicate the experience of eating meat.
  • the look, texture, and taste of the consumable can be such that it is similar or indistinguishable from meat.
  • the invention therefore provides in certain embodiments methods for determining whether an animal or human can distinguish the consumable from meat.
  • One method to determine whether the consumable is comparable to meat is to a) define the properties of meat and b) determine whether the consumable has similar properties.
  • Properties of meat that can be tested include mechanical properties such as hardness, cohesiveness, brittleness, chewiness, gumminess, viscosity, elasticity, and adhesiveness.
  • Properties of meat that can be tested also include geometric properties such as particle size and shape, and particle shape and orientation. Additional properties can include moisture content and fat content.
  • a group of people can be asked to rate a certain meat, for instance ground beef, according to properties which describe the meat. These ratings can be used as an indication of the properties of the meat.
  • the consumables of the present invention can then be compared to the meat to determine how similar the consumable is to the meat. In some instances the properties of the consumables are then altered to make the consumable more similar to the meat. So, in some embodiments, the consumable is rated similar to meat according to human evaluation. In some embodiments the consumable is indistinguishable from real meat to a human.
  • subjects asked to identify the consumable identify it as a form of meat.
  • one property of the compositions of the invention is that an animal, for example a human, will identify the composition as a meat.
  • the human identifies the composition of the invention as having properties equivalent to meat.
  • one or more properties of meat are equivalent according to a human's perception. Such properties include the properties that can be tested.
  • a human identifies a consumable of the present invention as more meat like than meat substitutes found in the art.
  • an experiment can demonstrate that consumable s acceptable to consumers.
  • a panel can be used to screen a variety of consumables described herein.
  • a number of human panelists can tested multiple consumable samples, namely, natural meats vs. the consumable compositions described herein.
  • Variables such as fat content can be standardized for example to 20% fat using lean and fat meat mixes. Fat content can be determined using the Babcock for meat method (S. S, Nielson, Introduction to the Chemical Analysis of Foods (Jones & Bartlett Publishers, Boston, 1994)).
  • Mixtures of ground beef and consumables of the invention prepared according to the procedure described herein can be formulated.
  • compositions of the invention are judged as acceptably equivalent to real meat products. Additionally these results can demonstrate that compositions of the invention are preferred by panelist over other commercially available meat substitutes. So, in some embodiments the present invention provides for consumables that are significantly similar to traditional meats.
  • Consumables of the invention can also have similar physical characteristics as traditional meat.
  • the force required to pierce a 1 inch thick structure (e.g. a patty) made of a consumable of the invention with a fixed diameter steel rod is not significantly different than the force required to pierce a 1 inch thick similar meat structure (e.g. a ground beef patty) with a similar fixed diameter steel rod. Accordingly, the invention provides for consumables with similar physical strength characteristics to meat.
  • composition of the invention have a similar cook loss characteristic as meat.
  • a consumable of the invention with a similar fat and protein content as ground beef has the same reduction in size when cooked as real ground beef. Similar similarities in size loss profiles can be achieved for various compositions of consumables described herein matched to various meats.
  • the consumable is compared to real meat based upon olfactometer readings.
  • the olfactometer can be used to assess odor concentration and odor thresholds, odor suprathresholds with comparison to a reference gas, hedonic scale scores to determine the degree of appreciation, or relative intensity of odors.
  • the olfactometer allows the training and automatic evaluation of expert panels. So in some embodiments the consumable is a product that causes similar or identical olfactometer readings. In some embodiments the similarity is sufficient to be beyond the detection threshold of human perception.
  • Gas chromatography-mass spectrometry is a method that combines the features of gas-liquid chromatography and mass spectrometry to separate and identify different substances within a test sample.
  • GCMS can, in some embodiments, be used to evaluate the properties of a consumable. For example volatile chemicals can be isolated from the head space around meat. These chemicals can be identified using GCMS. A profile of the volatile chemicals in the headspace around meat is thereby created.
  • each peak of the GCMS can be further evaluated. For instance, a human could rate the experience of smelling the chemical responsible for a certain peak. This information could be used to further refine the profile. GCMS could then be used to evaluate the properties of the consumable. The GCMS profile could be used to refine the consumable.
  • Characteristic flavor and fragrance components are mostly produced during the cooking process by chemical reactions molecules including amino acids, fats and sugars which are found in plants as well as meat. Therefore in some embodiments the consumable is tested for similarity to meat during or after cooking.
  • human ratings, human evaluation, olfactometer readings, or GCMS measurements, or combinations thereof are used to create an olfactory map of cooked meat.
  • an olfactory map of the consumable for instance a meat replica, can be created. These maps can be compared to assess how similar the cooked consumable it so meat.
  • the olfactory map of the consumable during or after cooking is similar to or indistinguishable from that of cooked or cooking meat.
  • the similarity is sufficient to be beyond the detection threshold of human perception.
  • the invention provides a meat substitute product (alternatively referred to herein as “consumable”) that is substantially or entirely composed of ingredients derived from non-animal sources, yet recapitulates key features associated with the cooking and consumption of an equivalent meat product derived from animals.
  • the equivalent meat product can be a white meat or a dark meat.
  • the equivalent meat product can be derived from any animal.
  • Non-limiting examples of animals used to derive the equivalent meat product include farmed animals such as, e.g., cattle, sheep, pig, chicken, turkey, goose, duck, horse, dog or game animals (whether wild or farmed) such as, e.g., rabbit, deer, bison, buffalo, boar, snake, pheasant, quail, bear, elk, antelope, pigeon, dove, grouse, fox, wild pig, goat, kangaroo, emu, alligator, crocodile, turtle, groundhog, marmot, possum, partridge, squirrel, raccoon, whale, seal, ostrich, capybara, nutria, guinea pig, rat, mice, vole, any variety of insect or other arthropod, seafood such as, e.g, fish, crab, lobster, oyster, muscle, scallop, abalone, squid, octopus, sea urchin, tunicate and others.
  • the equivalent meat product is a cut of meat derived from skeletal muscle.
  • the equivalent meat product is an organ such as, e.g., a kidney, heart, liver, gallbladder, intestine, stomach, bone marrow, brain, thymus, lung, tongue. Accordingly, in some embodiments the compositions of the present invention are consumables similar to skeletal muscle or organs.
  • the present invention provides meat substitute products comprising one or more of a first composition comprising a muscle tissue replica, a second composition comprising an adipose tissue replica, and/or a third composition comprising a connective tissue replica, wherein the one or more compositions are combined in a manner that recapitulates the physical organization of meat.
  • the present invention provides compositions for a muscle tissue replica (herein referred to as “muscle replica”), an adipose tissue replica (herein referred to as “fat replica”), and a connective tissue replica (herein referred to as “connective tissue replica”).
  • the compositions and meat substitute products are principally or entirely composed of ingredients derived from non-animal sources.
  • the muscle, fat, and/or connective tissue replica, or the meat substitute products comprising one or more of said replicas are partially derived from animal sources but supplemented with ingredients derived from non-animal sources.
  • the invention provides meat products substantially derived from animal sources but which are supplemented with one or more of a muscle tissue replica, a fat replica, and/or a connective tissue replica, wherein said replicas are derived substantially or entirely from non-animal sources.
  • a non-limiting example of such a meat product is an ultra-lean ground beef product supplemented with a non-animal derived fat replica which improves texture and mouthfeel while preserving the health benefits of a consumable low in animal fat.
  • the physical organization of the meat substitute product can be manipulated by controlling the localization, organization, assembly, or orientation of the muscle, fat, and/or connective tissue replicas described herein.
  • the product is designed in such a way that the replicas described herein are associated with one another as in meat.
  • the consumable is designed so that after cooking the replicas described herein are associated with one another as in cooked meat.
  • one or more of the muscle, fat, and/or connective tissue replicas are combined in a manner that recapitulate the physical organization of different cuts or preparations of meat.
  • the replicas are combined in a manner that approximates the physical organization of natural ground meat.
  • the replicas are combined in a manner that approximates different cuts of beef, such as, e.g., ribeye, filet mignon, London broil, among others.
  • any of the meat substitute products, muscle tissue replica, fat replica, or connective tissue replica comprise one or more isolated, purified proteins.
  • the meat substitute products are comprised of one or more of a muscle replica, a fat replica, and/or connective tissue replica which comprise one or more isolated, purified proteins.
  • the muscle replica, fat replica, and/or connective tissue replica comprises one or more isolated, purified proteins.
  • about 0.1%, 0.2%, 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99% or more of the protein component is comprised of one or more isolated, purified proteins.
  • purified protein will refer to a preparation in which the cumulative abundance by mass of protein components other than the specified protein, which can be a single monomeric or multimeric protein species, is reduced by a factor of 2 or more, 3 or more, 5 or more, 10 or more, 20 or more, 50 or more, 100 or more or 1000 or more relative to the source material from which the specified protein was isolated.
  • the one or more isolated, purified proteins are derived from non-animal sources.
  • non-animal sources include plants, funghi, bacteria, archaea, genetically modified organisms such as genetically modified bacteria or yeast, chemical or in vitro synthesis.
  • the one or more isolated, purified proteins are derived from plant sources.
  • Non-limiting examples of plant sources include grains such as, e.g., corn, maize, rice, wheat, barley, rye, triticale, teff, oilseeds including cottonseed, sunflower seed, safflower seed, rapeseed, leafy greens such as, e.g., lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, cabbage, green matter not ordinarily consumed by humans, including biomass crops, including switchgrass, miscanthus, sorghum, other grasses, alfalfa, corn stover, green matter ordinarily discarded from harvested plants, sugar cane leaves, leaves of trees, root crops such as cassava, sweet potato, potato, carrots, beets, turnips, plants from the legume family, such as, e.g., clover, peas such as cowpeas, english peas, yellow peas, green peas, beans such as,
  • the one or more isolated proteins comprises an abundant protein found in high levels in a plant and capable of being isolated and purified in large quantities.
  • the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70% of the total protein content of the source plant.
  • the abundant protein comprises about 0.5-10%, about 5-40%, about 10-50%, about 20-60%, or about 30-70% of the total protein content of the source plant. In some embodiments, the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50% of the total weight of the dry matter of the source plant. In some embodiments, the abundant protein comprises about 0.5-5%, about 1-10%, about 5-20%, about 10-30%, about 15-40%, about 20-50% of the total weight of the dry matter of the source plant.
  • the one or more isolated proteins comprises an abundant protein that is found in high levels in the leaves of plants.
  • the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80% of the total protein content of the leaves of the source plant.
  • the abundant protein comprises about 0.5-10%, about 5%-40%, about 10%-60%, about 20%-60%, or about 30-70% of the total protein content of the leaves of the source plant.
  • the one or more isolated proteins comprise ribulose-1,5-bisphosphate carboxylase oxygenase (rubisco activase). Rubisco is a particularly useful protein for meat replicas because of its high solubility and an amino acid composition with close to the optimum proportions of essential amino acids for human nutrition.
  • the one or more isolated proteins comprise ribulose-1,5-bisphosphate carboxylase oxygenase activase (rubisco activase).
  • the one or more isolated proteins comprise a vegetative storage protein (VSP).
  • the one or more isolated proteins include an abundant protein that is found in high levels in the seeds of plants.
  • the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85% or 90% or more of the total protein content of the seeds of the source plant.
  • the abundant protein comprises about 0.5-10%, about 5%-40%, about 10%-60%, about 20%-60%, or about 30-70% or >70% of the total protein content of the seeds of the source plant.
  • Non-limiting examples of proteins found in high levels in the seeds of plants are seed storage proteins, e.g., albumins, glycinins, conglycinins, globulins, vicilins, conalbumin, gliadin, glutelin, gluten, glutenin, hordein, prolamin, phaseolin (protein), proteinoplast, secalin, triticeae gluten, zein, any seed storage protein, oleosins, caloleosins, steroleosins or other oil body proteins
  • seed storage proteins e.g., albumins, glycinins, conglycinins, globulins, vicilins, conalbumin, gliadin, glutelin, gluten, glutenin, hordein, prolamin, phaseolin (protein), proteinoplast, secalin, triticeae gluten, zein, any seed storage protein, oleosins, calo
  • the one or more isolated proteins include proteins that interact with lipids and help stabilize lipids in a structure. Without wishing to be bound by a particular theory, such proteins may improve the integration of lipids and/or fat replicas with other components of the meat substitute product, resulting in improved mouthfeel and texture of the final product.
  • a non-limiting example of a lipid-interacting plant protein is the oleosin family of proteins. Oleosins are lipid-interacting proteins that are found in oil bodies of plants.
  • the present invention provides a composition derived from non-animal sources which replicates or approximates key features of animal skeletal muscle.
  • the present invention provides a meat substitute product that comprises a composition derived from non-animal sources which replicates or approximates animal skeletal muscle.
  • Such a composition will be labeled herein as “muscle replica”.
  • the muscle replica and/or meat substitute product comprising the muscle replica are partially derived from animal sources.
  • the muscle replica and/or meat substitute product comprising the muscle replica are entirely derived from non-animal sources.
  • the muscle replica comprises fibers that are to some extent organized isotropically.
  • the fibers comprise a protein component.
  • the fibers comprise about 1%, about 2%, about 5%, about 10%, about 15%, about 20%, about 30%, about 40%, about 50%, about 60%, about 70%, about 80%, about 90%, about 95%, about 99% or more of a protein component.
  • the protein component comprises one or more isolated, purified proteins.
  • the one or more isolated, purified protein can comprise the 8S globulin from Moong bean seeds, or the albumin or globulin fraction of pea seeds.
  • These proteins provide examples of proteins with favorable properties for constructing meat replicas because of their ability to form gels with textures similar to animal muscle or fat tissue.
  • Examples and embodiments of the one or more isolated, purified proteins are described herein.
  • the list of potential candidates here is essentially open and may include Rubisco, any major seed storage proteins, proteins isolated from fungi, bacteria, archaea, viruses, or genetically engineered microorganisms, or synthesized in vitro.
  • the proteins may be artificially designed to emulate physical properties of animal muscle tissue.
  • the proteins may be artificially designed to emulate physical properties of animal muscle tissue.
  • one or more isolated, purified proteins accounts for about 0.1%, 0.2%, 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99% or more of the protein component by weight.
  • Glycogen is a branched polymer of glucose linked together by alpha (1->4) glycosidic bonds in linear chains, with branch points comprising alpha (1->6) glycosidic bonds.
  • Starches from plants, particularly amylopectins are also branched polymers of glucose linked together by alpha (1->4) glycosidic bonds in linear chains, with branch points comprising alpha (1->6) glycosidic bonds and can therefore be used as an analog of glycogen in constructing meat replicas.
  • the muscle or meat replica includes a starch or pectin.
  • animal muscle tissue includes sodium, potassium, calcium, magnesium, other metal ions, lactic acid, other organic acids, free amino acids, peptides, nucleotides and sulfur compounds.
  • the muscle replica can include sodium, potassium, calcium, magnesium, other metal ions, lactic acid, other organic acids, free amino acids, peptides, nucleotides and sulfur compounds.
  • the concentration of sodium, potassium, calcium, magnesium, other metal ions, lactic acid, other organic acids, free amino acids, peptides, nucleotides and/or sulfur compounds in the muscle replica or consumable are within 10% of the concentrations found in a muscle or meat being replicated.
  • the invention provides methods for making a muscle replica.
  • the composition is formed into asymmetric fibers prior to incorporation into the consumable. In some embodiments these fibers replicate muscle fibers.
  • the fibers are spun fibers. In other embodiments the fibers are extruded fibers. Accordingly, the present invention provides for methods for producing asymmetric or spun protein fibers.
  • the fibers are formed by extrusion of the protein component through an extruder. Methods of extrusion are well known in the art, and are described in U.S. Pat. No. 6,379,738, U.S. Pat. No. 3,693,533, US20120093994, which are herein incorporated by reference.
  • extrusion can be conducted using an MPF19 twin-screw extruder (APV Baker, Grand Rapids, Mich.) with a cooling die.
  • the cooling die can cool the extrudate prior to return of the extrudate to atmospheric pressure, thus substantially inhibiting expansion or puffing of the final product.
  • dry feed and liquid can be added separately and mixed in the barrel.
  • Extrusion parameters can be, for example: screw speed of 200 rpm, product temperature at the die of 150 C., feed rate of 23 g/min, and water-flow rate of 11 g/min.
  • Product temperature can be measured during extrusion by a thermocouple at the end of the extrusion barrel.
  • Observations can be made on color, opacity, structure, and texture for each collected sample. Collected samples can be optionally dried at room temperature overnight, then ground to a fine powder ( ⁇ 60 mesh) using a Braun food grinder. The pH of samples can be measured in duplicate using 10% (w/v) slurries of powdered sample in distilled water.
  • the present invention provides a composition derived from non-animal sources which recapitulates key features of animal fat.
  • the present invention provides a meat substitute product that comprises a composition derived from non-animal sources which recapitulates animal fat.
  • a composition will be labeled herein as a “fat replica”.
  • the fat replica and/or meat substitute product comprising the fat replica are partially derived from animal sources.
  • the meat substitute product has a fat component.
  • the fat content of the consumable is 1%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, or 60% fat.
  • the fat replica comprises a gel with droplets of fat suspended therein.
  • the gel is a soft, elastic gel comprising proteins and optionally carbohydrates.
  • the proteins used in the gel are plant or microbial proteins.
  • the proteins used in the fat replica might include Rubisco, any major seed storage proteins, proteins isolated from fungi, bacteria, archaea, viruses, or genetically engineered microorganisms, or synthesized in vitro.
  • the proteins may be artificially designed to emulate physical properties of animal fat.
  • the proteins may be artificially designed to emulate physical properties of animal fat.
  • the fat droplets used in some embodiments of the present invention can be from a variety of sources.
  • the sources are non-animal sources.
  • the sources are plant sources.
  • oils include corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, oils produced by bacteria, algae, archaea or fungi or genetically engineered bacteria, algae, archaea or fungi, triglycerides, monoglycerides, diglycerides, sphingosides, glycolipids, lecithin, lysolecithin, phophatidic acids, lysophosphatidic acids, oleic acid, palmitoleic acid, palm
  • fat droplets are derived from pulp or seed oil.
  • the source may be yeast or mold.
  • the fat droplets comprise triglycerides derived from Mortierella isabellina.
  • plant oils are modified to resemble animal fats.
  • the plant oils can be modified with flavoring or other agents to recapitulate the taste and smell of meat during and after cooking. Accordingly, some aspects of the invention involve methods for testing the qualitative similarity between the cooking properties of animal fat and the cooking properties of plant oils in the consumable.
  • the fat replica comprises a protein component comprising one or more isolated, purified proteins.
  • the purified proteins contribute to the taste and texture of the meat replica.
  • purified proteins can stabilize emulsified fats.
  • the purified proteins can form gels upon denaturation or enzymatic crosslinking, which replicate the appearance and texture of animal fat. Examples and embodiments of the one or more isolated, purified proteins are described herein.
  • the one or more isolated proteins comprise a protein isolated from the legume family of plants. Non-limiting examples of legume plants are described herein, although variations with other legumes are possible.
  • the legume plant is a pea plant.
  • the isolated purified proteins stabilize emulsions.
  • the isolated purified proteins form gels upon crosslinking or enzymatic crosslinking.
  • the isolated, purified proteins comprise seed storage proteins.
  • the isolated, purified proteins comprise albumin.
  • the isolated, purified proteins comprise globulin.
  • the isolated, purified protein is a purified pea albumin protein.
  • the isolated, purified protein is a purified pea globulin protein.
  • the isolate purified protein is a Moong bean 8S globulin.
  • the isolated, purified protein is an oleosin.
  • the isolated, purified protein is a caloleosin.
  • the isolated, purified protein is Rubisco.
  • the protein component comprises about 0.1%, 0.5%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90% or more of the fat replica by dry weight or total weight.
  • the protein component comprises about 0.1-5%, about 0.5-10%, about 1-20%, about 5-30%, about 10-50%, about 20-70%, or about 30-90% or more of the fat replica by dry weight or total weight.
  • the protein component comprises a solution containing one or more isolated, purified proteins.
  • the fat replica comprises cross-linking enzymes that catalyze reactions leading to covalent crosslinks between proteins.
  • Cross-linking enzymes can be used to create or stabilize the desired structure and texture of the adipose tissue replica, to mimic the desired texture of an equivalent desired animal fat.
  • Non-limiting examples of cross-linking enzymes include, e.g., transglutaminase, lysyl oxidases, or other amine oxidases (e.g. Pichia pastoris lysyl oxidase).
  • the cross-linking enzymes are isolated and purified from a non-animal source, examples and embodiments of which are described herein.
  • the fat replica comprises at least 0.0001%, or at least 0.001%, or at least 0.01%, or at least 0.1%, or at leastl % (wt/vol) of a cross-linking enzyme.
  • the cross-linking enzyme is transglutaminase.
  • the invention provides methods for making a fat replica.
  • the fat droplets are suspended in a gel.
  • the present invention provides for methods for producing droplets of fat suspended in the gel.
  • the fat can isolated and homogenized.
  • an organic solvent mixture can be used to help mix a lipid.
  • the solvent can then be removed.
  • the lipid can be frozen, lyophilized, or stored.
  • the invention provides for a method for isolating and storing a lipid which has been selected to have characteristics similar to animal fat.
  • the lipid film or cake can then be hydrated.
  • the hydration can utilize agitation or temperature changes.
  • the hydration can occur in a precursor solution to a gel. After hydration the lipid suspension can be sonicated or extruded to further alter the properties of the lipid in the solution.
  • the fat replica is assembled to approximate the organization adipose tissue in meat.
  • some or all of the components of the fat replica are suspended in a gel.
  • the gel can be a proteinaceous gel, a hydrogel, an organogel, or a xerogel.
  • the gel can be thickened to a desired consistency using an agent based on polysaccharides or proteins.
  • the fat replica is an emulsion comprising a solution of one or more proteins and one or more fats suspended therein as droplets.
  • the emulsion is stabilized by one or more cross-linking enzymes into a gel.
  • the one or more proteins in solution are isolated, purified proteins.
  • the isolated, purified proteins comprise a purified pea albumin enriched fraction.
  • the isolated, purified proteins comprise a purified pea globulin enriched fraction.
  • the isolated, purified proteins comprise a purified Moong bean 8S globulin enriched fraction.
  • the isolated, purified proteins comprise a Rubisco enriched fraction.
  • the one or more fats are derived from plant-based oils.
  • the one or more fats are derived from one or more of: corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, oils produced by bacteria, algae, archaea or fungi or genetically engineered bacteria, algae, archaea or fungi, triglycerides, monoglycerides, diglycerides, sphingosides, glycolipids, lecithin, lysolecithin, phophatidic acids, lysophosphatidic acids, ole
  • the one or more fats is a rice bran oil. In another particular embodiment, the one or more fats is a canola oil.
  • the cross-linking enzyme is transglutaminase, lysyl oxidase, or other amine oxidase. In yet even more particular embodiments, the cross-linking enzyme is transglutaminase.
  • the fat replica is a high fat emulsion comprising a protein solution of purified pea albumin emulsified with 40-80% rice bran oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel.
  • the fat replica is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% rice bran oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel.
  • the fat replica is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% canola oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel.
  • the fat replica is a high fat emulsion comprising a protein solution of purified pea albumin emulsified with 40-80% rice bran oil, stabilized with 0.0001-1% (wt/vol) transglutaminase into a gel.
  • the fat replica is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% rice bran oil, stabilized with 0.0001-1% (wt/vol) transglutaminase into a gel.
  • the fat replica is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% canola oil, stabilized with 0.0001-1% (wt/vol) transglutaminase into a gel.
  • Animal connective tissue provides key textural features that are an important component of the experience of eating meat. Accordingly, the present invention provides a composition derived from non-animal sources which recapitulates key features of animal connective tissue.
  • the present invention provides a meat substitute product that comprises a composition derived from non-animal sources which recapitulates important textural and visual features of animal connective tissue.
  • Such a composition will be labeled herein as “connective tissue replica”.
  • the connective tissue replica and/or meat substitute product comprising the connective tissue replica are partially derived from animal sources.
  • Fascia-type tissue is highly fibrous, resistant against extension (has high elastic modulus), and has a high protein content, a moderate water content (ca. 50%), and low-to-none fat and polysaccharide content. Accordingly, the present invention provides a connective tissue replica that recapitulates key features of fascia type tissue.
  • the connective tissue replica comprises about 50% protein by total weight, about 50% by liquid weight, and has a low fat and polysaccharide component.
  • the protein content of most fascia-type connective tissue is comprised mainly of collagen.
  • Collagen is characterized by a high fraction of proline and alanine, and also is assembled into characteristic elongated fibrils or rod-like, flexible structures.
  • Prolamins are one family of proteins found in non-animal sources, such as plant sources. Prolamins are highly abundant in plants and are similar in amino acid composition to collagen. Among proteins we tested for this purpose, prolamins were particularly favorable because of their low cost and their ability to readily form fibers or sheets when spun or extruded.
  • prolamin family proteins include, e.g., zein (found in corn), these include hordein from barley, gliadin from wheat, secalin, extensins from rye, kafirin from sorghum, avenin from oats.
  • zein found in corn
  • the prolamin family of proteins individually or combinations thereof, demonstrates suitability for the protein component because they are highly abundant, similar in global amino acid composition to collagen (high fraction of proline and alanine), and amenable to processing into films and fibers.
  • zein found in corn
  • these include hordein from barley, gliadin from wheat, secalin, extensins from rye, kafirin from sorghum, avenin from oats.
  • Other proteins may be necessary to supplement prolamins in order to achieve targets specifications for physicochemical and nutritional properties.
  • the list of potential candidates here is essentially open and may include Rubisco, any major seed storage proteins, proteins isolated from fungi, bacteria, archaea, viruses, or genetically engineered microorganisms, or synthesized in vitro.
  • the proteins may be artificially designed to emulate physical properties of animal connective tissue.
  • fascia-type connective tissue Methods for forming fascia-type connective tissue will be as those practiced in the art with a bias towards methods producing fibrous or fibrous-like structures by biological, chemical, or physical means, individually or in combination, serially or in parallel, before final forming These methods may include extrusion or spinning.
  • Cartilage-type tissue is macroscopically homogenous, resistant against compression, has higher water content (up to 80%), lower protein (collagen) content, and higher polysaccharide (proteoglycans) contents (ca. 10% each).
  • cartilage-type connective tissue will be very similar to fascia-type tissue with the relative ratios of each adjusted to more closely mimic ‘meat’ connective tissue.
  • cartilage-type connective tissue will be similar to those for fascia-type connective tissue, but with a bias towards methods producing isotropically homogenous structures.
  • the fat can be suspended in a gel.
  • the present invention provides for methods for producing droplets of fat suspended in the proteinaceous gel.
  • the fat can be isolated from plant tissues and emulsified.
  • the emulsification can utilize high-speed blending, homogenization, agitation or temperature changes.
  • the lipid suspension can be sonicated or extruded to further alter the properties of the lipid in the solution.
  • other components of the consumable are added to the solution followed by a gelling agent.
  • crosslinking agents e.g. transglutaminase or lysyl oxidase
  • the gelling agent is added and the lipid/gel suspension is later combined with additional components of the consumable.
  • the prolamin family of proteins demonstrates suitability for the protein component because they are highly abundant, similar in global amino acid composition to collagen (high fraction of proline and alanine), and amenable to processing into films.
  • zein found in corn
  • these include hordein from barley, gliadin from wheat, secalin, extensions from rye, kafirin from sorghum, avenin from oats.
  • Other proteins may be necessary to supplement prolamins in order to achieve targets specifications for physicochemical and nutritional properties.
  • the list of potential candidates here is essentially open and may include any major seed storage proteins, animal-derived or recombinant collagen, extensins (hydroxyproline-rich glycoproteins abundant in cell walls e.g. Arabidopsis thaliana , monomers of which are “collagen-like” rod-like flexible molecules).
  • the components of the consumable are suspended in a gel.
  • the gel can be a hydrogel, an organogel, or a xerogel,
  • the gel can be made thick using an agent based on polysaccharides or proteins.
  • Enzymes that catalyze reactions leading to covalent crosslinks between proteins can also be used alone or in combination to form an architecture or structure for the consumable.
  • transclutaminase, lysyl oxidases, or other amine oxidases e.g. Pichia pastoris lysyl oxidase (PPLO)
  • PPLO Pichia pastoris lysyl oxidase
  • multiple gels with different components are combined to form the consumable.
  • a gel containing a plant-based protein can be associated with a gel containing a plant-based fat.
  • fibers or stings of proteins are oriented parallel to one another and then held in place by the application of a gel containing plant based fats.
  • compositions of the invention can be puffed or expanded by heating, such as frying, baking, microwave heating, heating in a forced air system, heating in an air tunnel, and the like, according to methods well known in the art.
  • multiple gels with different components are combined to form the consumable.
  • a gel containing a plant-based protein can be associated with a gel containing a plant-based fat.
  • fibers or strings of proteins are oriented parallel to one another and then held in place by the application of a gel containing plant based fats.
  • the meat replica contains no animal products, less than 1% wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no soy protein isolate, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no soy protein concentrate, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no soy protein, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no tofu, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products, no tofu, and no wheat gluten.
  • the meat replica contains no animal products, no soy protein, and no wheat gluten.
  • the meat replica contains no methylcellulose, no carrageenan, no caramel color, no Konjac flour, no gum Arabic, and no acacia gum.
  • the meat replica contains no animal products and less than 5% carbohydrates.
  • the meat replica contains no animal products, no soy protein, no wheat gluten, no methylcellulose, no carrageenan, no caramel color and no Konjac flour, no gum Arabic, and no acacia gum and less than 5% carbohydrates.
  • the meat replica contains no animal products, and less than 1% cellulose.
  • the meat replica contains no animal products, and less than 5% insoluble carbohydrates.
  • the meat replica contains no animal products, no soy protein, and less than 1% cellulose.
  • the meat replica contains no animal products, no soy protein, and less than 5% insoluble carbohydrates.
  • the meat replica contains no animal products, no wheat gluten, and less than 1% cellulose.
  • the meat replica contains no animal products, no wheat gluten, and less than 5% insoluble carbohydrates.
  • the percentage of different components may also be controlled.
  • non-animal-based substitutes for muscle, fat tissue, connective tissue, and blood components can be combined in different ratios and physical organizations to best approximate the look and feel of meat.
  • the various can also components can be arranged to insure consistency between bites of the consumable.
  • the components can be arranged to insure that no waste is generated from the consumable.
  • a traditional cut of meat may have portions that are not typically eaten, a meat replicate can improve upon meat by not including these inedible portions. Such an improvement allows for all of the product made or shipped to be consumed, which cuts down on waste and shipping costs.
  • a meat replica may include inedible portions to mimic the experience of meat consumption.
  • Such portions can include bone, cartilage, connective tissue, or other materials commonly referred to as gristle, or materials included simulating these components.
  • the consumable may contain simulated inedible portions of meat products which are designed to serve secondary functions.
  • a simulated bone can be designed to disperse heat during cooking, making the cooking of the consumable faster or more uniform than meat.
  • a simulated bone may also serve to keep the consumable at a constant temperature during shipping.
  • the simulated inedible portions may be biodegradable.
  • the meat substitute compositions contains no animal protein, comprising between 10-30% protein, between 5-80% water, between 5-70% fat, comprising one or more isolated purified proteins.
  • the meat substitute compositions comprise transglutaminase.
  • the consumable contains components to replicate the components of meat.
  • the main component of meat is typically skeletal muscle. Skeletal muscle typically consists of roughly 75 percent water, 19 percent protein, 2.5 percent intramuscular fat, 1.2 percent carbohydrates and 2.3 percent other soluble non-protein substances. These include organic acids, sulfur compounds, nitrogenous compounds, such as amino acids and nucleotides, and inorganic substances such as minerals. Accordingly, some embodiments of the present invention provide for replicating approximations of this composition for the consumable.
  • the consumable is a plant-based meat replica can comprise roughly 75% water, 19% protein, 2.5% fat, 1.2% carbohydrates; and 2.3 percent other soluble non-protein substances.
  • the consumable is a plant-based meat replica comprising between 60-90% water, 10-30% protein, 1-20% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments the consumable is a plant-based meat replica comprising between 60-90% water, 5-10% protein, 1-20% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments the consumable is a plant-based meat replica comprising between 0-50% water, 5-30% protein, 20-80%% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments, the replica contains between 0.01% and 5% by weight of a heme protein.
  • the replica contains between 0.01% and 5% by weight of leghemoglobin.
  • Some meat also contains myoglobin, a heme protein, which accounts for most of the red color and iron content of some meat.
  • the replica contains between 0.01% and 5% by weight of a heme protein.
  • the replica contains between 0.01% and 5% by weight of leghemoglobin. It is understood that these percentages can vary in meat and the meat replicas can be produced to approximate the natural variation in meat. Additionally, in some instances, the present invention provides for improved meat replicas, which comprise these components in typically unnatural percentages. For example a meat replica can be produced with a higher than typical average fat content. The percentages of these components may also be altered to increase other desirable properties.
  • a meat replica is designed so that, when cooked, the percentages of components are similar to cooked meat. So, in some embodiments, the uncooked consumable has different percentages of components than uncooked meat, but when cooked the consumable is similar to cooked meat. For example, a meat replica may be made with a higher than typical water content for raw meat, but when cooked in a microwave the resulting product has percentages of components similar to meat cooked over a fire.
  • the consumable is a meat replica with a lower that typical water content for meat.
  • the inventions provides for methods for hydrating a meat replica to cause the meat replica to have a content similar to meat. For example a meat replica with a water content that would be low for meat, for example 1%, 10%, 20%, 30%, 40% or 50% water, is hydrated to roughly 75% water. Once hydrated, in some embodiments, the meat replica is then cooked for human consumption.
  • the consumable can have a protein component.
  • the protein content of the consumable is 10%, 20%, 30%, or 40%.
  • the protein content of the consumable is similar to meat.
  • the protein content in the consumable is greater than that of meat.
  • the consumable has less protein than meat.
  • the protein in the consumable can come from a variety or combination of sources.
  • Non-animal sources can provide some or all of the protein in the consumable.
  • Non-animal sources can include vegetables, fruits, nuts, grains, algae, bacteria, or fungi.
  • the protein can be isolated or concentrated from one or more of these sources.
  • the consumable is a meat replica comprising protein only obtained from non-animal sources.
  • protein is formed into asymmetric fibers for incorporation into the consumable. In some embodiments these fibers replicate muscle fibers. In some embodiments the protein are spun fibers. Accordingly, the present invention provides for methods for producing asymmetric or spun protein fibers.
  • the consumable contains a protein or proteins that have all of the amino acids found in proteins that are essential for human nutrition. In some embodiments the proteins added to the consumable are supplemented with amino acids.
  • the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking beef. In some embodiments, the consumable when cooked generates an aroma recognizable by humans as typical of cooking pork. In some embodiments, the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking bacon. In some embodiments, the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking chicken. In some embodiments, the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking lamb.
  • the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking fish. In some embodiments, the consumable is a meat replica entirely composed of non-animal products that when cooked generates an aroma recognizable by humans as typical of cooking turkey. In some embodiments the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, with an odorant that is released upon cooking. In some embodiments the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, with an odorant that is produced by chemical reactions that take place upon cooking.
  • the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, containing mixtures of proteins, peptides, amino acids, nucleotides, sugars and polysaccharides and fats in combinations and spatial arrangements that enable these compounds to undergo chemical reactions during cooking to produce odorants and flavor-producing compounds.
  • the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, with a volatile or labile odorant that is released upon cooking.
  • the consumable is a method for preparing a meat replica where meat replicas principally or entirely composed of ingredients derived from non-animal sources are heated to release a volatile or labile odorant.
  • Odorants released during cooking of meat are generated by reactions that can involve as reactants fats, protein, amino acids, peptides, nucleotides, organic acids, sulfur compounds, sugars and other carbohydrates.
  • the odorants that combine during the cooking of meat are identified and located near one another in the consumable, such that upon cooking of the consumable the odorants combine.
  • the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions involving amino acids, fats and sugars found in plants as well as meat.
  • the characteristic flavor and fragrance components are mostly produced during the cooking process by chemical reactions involving one or more amino acids, fats, peptides, nucleotides, organic acids, sulfur compounds, sugars and other carbohydrates found in plants as well as meat.
  • Some reactions that generate odorants released during cooking of meat can be catalyzed by iron, in particular the heme iron of myoglobin.
  • iron in particular the heme iron of myoglobin.
  • some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by iron.
  • some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by heme.
  • some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by the heme iron in leghemoglobin.
  • some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by the heme iron in a heme protein.
  • leghemoglobin contributes favorably to aroma of meat replicas
  • a muscle replica comprising pea flour, sunflower oil, and glucose was heated for 10 minutes at 140 C in the presence of either reduced leghemoglobin (LHb) or a mixture of iron (Fe3+), sodium and EDTA (EFS) in sealed containers carrying solid phase microextraction (SPME) fibers.
  • LHb reduced leghemoglobin
  • FES sodium and EDTA
  • SPME solid phase microextraction
  • PDMS polydimethylsiloxane
  • Analysis of GC-MS data from multiple replicas reveal consistent differences between the LHb and EFS samples.
  • Non-limiting examples of compounds found exclusively or more abundantly in the LHb samples are: 2-octanone, 2-methyl furan, which are often associated with the aroma of cooked meat, and many other unidentified compounds.
  • the color of meat is an important part the experience of cooking and eating meat. For instance, cuts of beef are of a characteristic red color in a raw state and gradually transition to a brown color during cooking. As another example, white meats such as chicken or pork have a characteristic pink color in their raw state and gradually transition to a white or brownish color during cooking. The amount of the color transition is used to indicate the cooking progression of beef and titrate the cooking time and temperature to produce the desired state of done-ness.
  • the invention provides a non-meat based meat substitute product that provides a visual indicator of cooking progression.
  • the visual indicator is a color indicator that undergoes a color transition during cooking.
  • the color indicator recapitulates the color transition of a cut of meat as the meat progresses from a raw to a cooked state.
  • the color indicator colors the meat substitute product a red color before cooking to indicate a raw state and causes the meat substitute product to transition to a brown color during cooking progression.
  • the color indicator colors the meat substitute product a pink color before cooking to indicate a raw state and causes the meat substitute product to transition to a white or brown color during cooking progression.
  • the main determinant of the nutritional definition of the color of meat is the concentration of iron carrying proteins in the meat.
  • one of the main iron-carrying proteins is myoglobin. It is estimated that the white meat of chicken has under 0.05%; pork and veal have 0.1-0.3%; young beef has 0.4-1.0%; and old beef has 1.5-2.0%. So, in some embodiments, the consumable is a meat replica which comprises an iron-carrying protein.
  • the meat replica comprises about 0.05%, about 0.1%, about 0.2%, about 0.3%, about 0.4%, about 0.5%, about 0.6%, about 0.7%, about 0.8%, about 0.9%, about 1%, about 1.1%, about 1.2%, about 1.3%, about 1.4%, about 1.5%, about 1.6%, about 1.7%, about 1.8%, about 1.9%, about 2%, or more than about 2% of an iron-carrying protein by dry weight or total weight.
  • the iron carrying protein has been isolated and purified from a source. In other cases, the iron carrying protein has not been isolated and purified.
  • the source of the iron-carrying protein is an animal source, or a non-animal source such as a plant, fungus, or genetically modified organisms such as, e.g., bacteria or yeast.
  • the iron-carrying protein is myoglobin.
  • the consumable is a plant based meat replica that has animal myoglobin added. So, for example a replica of young beef can have about 0.4-1% myoglobin.
  • the iron-carrying protein is leghemoglobin.
  • the consumable is a plant based meat replica that has leghemoglobin added. So, for example a replica of young beef can have about 0.4-1% leghemoglobin.
  • the iron-carrying protein is a cytochrome.
  • the consumable is a plant based meat replica that has a cytochrome added. So, for example a replica of young beef can have about 0.4-1% of a cytochrome.
  • hemoglobin the iron-containing oxygen-binding protein in the red blood cells of vertebrates. Hemoglobin is similar in color to myoglobin.
  • the invention provides methods of saving and recycling blood from animal farming to supplement the color of a consumable. For example blood is saved from a slaughter house, hemoglobin from the blood is used to enhance the color of a consumable.
  • the consumable is a plant-based meat replica containing hemoglobin.
  • the consumable comprises an iron containing protein that is not myoglobin. In some embodiments the consumable does not contain myoglobin. In some embodiments the consumable does not contain hemoglobin. In some embodiments the consumable is a meat replica that comprises an iron containing protein other than myoglobin or hemoglobin.
  • iron containing proteins examples include hemoglobin, myoglobin, neuroglobin, cytoglobin, leghemoglobin, non-symbiotic hemoglobin, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins.
  • these iron containing proteins are added to the consumable to alter the visual characteristics or iron content of the consumable.
  • the consumable comprises a hemoprotein (e.g. hemoglobin, myoglobin, neuroglobin, cytoglobin, leghemoglobin, non-symbiotic hemoglobin, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins).
  • the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, including a muscle tissue replica, an adipose tissue replica, a connective tissue replica, and leghemoglobin.
  • the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, containing a heme protein.
  • the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, containing a leghemoglobin. In some embodiments the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, containing a member of the globin protein family. In some embodiments the consumable is a meat replica principally or entirely composed of ingredients derived from non-animal sources, with a high iron content from a heme protein. In some embodiments the iron content is similar to meat. In some embodiments the consumable has the distinctive red color of meat, such color provided by leghemoglobin.
  • Leghemoglobin is, in some embodiments, used as an indicator that the consumable is finished cooking. So, one embodiment of the invention is a method for cooking a consumable comprising detecting leghemoglobin which has migrated from the interior of the consumable to the surface when the product is cooked. Another embodiment of the invention is a method for cooking a consumable comprising detecting the change in color of from red to brown when the product is cooked.
  • a heme protein is, in some embodiments, used as an indicator that the consumable is finished cooking. So, one embodiment of the invention is a method for cooking a consumable comprising detecting leghemoglobin which has migrated from the interior of the consumable to the surface when the product is cooked. Another embodiment of the invention is a method for cooking a consumable comprising detecting the change in color of from red to brown when the product is cooked.
  • a heme protein from the group of: Hemoglobin, myoglobin, neuroglobin, cytoglobin, leghemoglobin, non-symbiotic hemoglobin, Hell's gate globin I, bacterial hemoglobins, ciliate myoglobins, flavohemoglobins, is, in some embodiments, used as an indicator that the consumable is finished cooking. So, one embodiment of the invention is a method for cooking a consumable comprising detecting leghemoglobin which has migrated from the interior of the consumable to the surface when the product is cooked. Another embodiment of the invention is a method for cooking a consumable comprising detecting the change in color of from red to brown when the product is cooked.
  • leghemoglobin is added to meat to enhance the properties of meat.
  • a leghemglobin containing solution can be injected into raw or cooked meat.
  • a leghemoglobin solution is dripped over meat or a consumable of the invention to enhance appearance.
  • advertising, photography, or videography of food products such as meat or a meat substitute is enhanced with leghemoglobin.
  • the present invention provides methods for obtaining leghemoglobin from plants.
  • Leghemoglobin can be obtained from a variety of plants.
  • Various legumes species and their varieties for example, Soybean, Fava bean, Lima bean, Cowpeas, English peas, Yellow peas, Lupine, Kidney bean, Garbanzo beans, Peanut, Alfalfa, Vetch hay, Clover, Lespedeza and Pinto bean, contain nitrogen-fixing root nodules in which leghemoglobin has a key role in controlling oxygen concentrations (for example root nodules from a pea plant, FIG. 1 ).
  • FIG. 2 shows 100 mls of leghemoglobin solution isolated from 30 grams of pea root nodules.
  • FIG. 3 Leghemoglobins from different species are homologs and have similar color properties ( FIG. 3 ).
  • panel A shows an SDS_PAGE gels of lysed root-nodules of three legume plant species (1) Fava bean (2) English Pea (3) Soybean. Arrows mark respective leghemoglobins. Note that leghemoglobin is the most abundant soluble protein in each lysate.
  • Panel B shows the similarity of UV-VIS spectral profile of leghemoglobins from two different plant species (Favabean and Soybean). We purified leghemoglobin from fava bean (green curve) and Soybean (red curve) root nodules using the protocol described elsewhere in the specification.
  • UV-VIS spectra of both proteins shows that the heme iron is in the reduced (+2) state. Note that they are almost perfectly superimposed, consistent with their visually identical red color.
  • the heme iron in the respective leghemoglobins was reduced to the +2 oxidation state by incubating Fava bean and Soybean leghemoglobin with 10 mM sodium hydrosulfite in 20 mM potassium-phosphate pH 7.4, 100 mM sodium chloride buffer. Sodium hydrosulfite was then removed from the leghemoglobin solution using gel-exclusion chromatography. Inset shows a zoom-in of UV-VIS spectra in 450 nm to 700 nm region.
  • leghemoglobin isoforms express several leghemoglobin isoforms (for example soybean has four leghemoglobin isoforms). Minor variations in precise amino acid sequence can modify overall charge of the protein at a particular pH and can modify precise structural conformation of iron containing heme group in leghemoglobin. Differences in structural conformation of heme group of different leghemoglobins can influence oxidation and reduction rates of the heme iron. These differences may contribute to color and flavor generation properties of different leghemoglobins.
  • FIG. 4 shows a comparison of reduced (heme iron 2+) and oxidized (heme iron 3+) soybean leghemoglobin ( FIG. 4 panel A) and equine heart muscle myoglobin ( FIG. 4 panel B) showing similarity of UV-VIS absorption profiles of two proteins.
  • soybean leghemoglobin from soybean root-nodules using here described protocol.
  • Purified equine myoglobin was purchased from SigmaAldrich. Soybean leghemoglobin ( FIG. 4 panel A) and equine myoglobin ( FIG. 4 panel B) were reduced with 1 mm sodium hydrosulfite.
  • FIG. 4 panel A Shown are UV-VIS absorption spectra of heme Fe3+ (blue line) and heme Fe2+ (red line) of soybean leghemoglobin ( FIG. 4 panel A) and equine myoglobin ( FIG. 4 panel B). Insets show a zoom-in of UV-VIS spectra in 450 nm to 700 nm region.
  • leghemoglobin can be sourced from non-plant sources, such as from organisms such as bacteria or yeast which have been genetically modified to express high levels of leghemoglobin.
  • leghemoglobin The oxidation state of the iron ion in leghemoglobin is important for its color. Leghemoglobin with the heme iron in the +2 oxidation state appears vivid red in color, while leghemoglobin with the heme iron in the +3 oxidation state appears brownish red. Thus, in using leghemoglobin as a source of red color in a meat replica, it is desirable to reduce the heme iron from the +3 state to the +2 state. Heme iron in leghemoglobin can be switched from oxidized (+3) state to reduced (+2) state with reducing reagents. Examples of successful reduction of leghemoglobin heme iron with sodium hydrosulfite and titanium citrate are illustrated in FIG. 5 . In FIG.
  • the UV-VIS spectrogram of purified soybean leghemoglobin in which the heme iron is in the oxidized (+3) state is represented by the blue curves in each panel.
  • the red curves in each panel represent the UV-VIS spectra of the same leghemoglobin species after reduction to the (+2) state (red lines) by addition of (Panel A) 1 mM sodium hydrosulfite or (Panel B) 0.24% (wt/v) titanium citrate in 20 mM potassium phosphate pH 7.3, 100 mM sodium chloride buffer.
  • the Insets show a zoom-in of UV-VIS spectra in 450-700 nm region.
  • leghemoglobin was purified from soybean root nodules using 60/90% ammonium sulfate fractionation and exchanged into 20 mM potassium phosphate pH 7.4, 100 mM sodium chloride buffer.
  • Sodium hydrosulfite stock solution was prepared by dissolving 100 mM sodium hydrosulfite inlmM sodium hydroxide in water.
  • Titanium citrate stock solution was prepared from 20% (wt/v) Ti-chloride in hydrochloric acid by mixing it with 0.2M sodium citrate (1:10 v/v). pH was adjusted using sodium carbonate to pH 7.0.
  • Leghemoglobin can be purified from legume root nodules, such as the root nodules of peas or soybeans ( FIG. 1 shows Leghemoglobin isolated from pea root nodules). Root nodules from soy beans were thoroughly cleaned to remove soil and extraneous root tissues prior to root nodule lysis in 20 mM potassium phosphate pH 7.4, 100 mM sodium chloride, 1 mm EDTA and 1 mM ascorbic acid. Root nodules were lysed by grinding root-nodules using a Vitamix blender. For some samples Polyvinylpyrrolidone polymer was added at 30% wt/v to aid in removal of plant phenolic small molecules that mediate oxidation of leghemoglobin heme-iron.
  • Root nodule lysate was fractionated using ammonium sulfate in two steps, first ammonium sulfate was added to 60% wt/v. Pellet was discarded and supernatant brought to 90% wt/v. ammonium sulfate. Leghemoglobin was collected as a precipitated pellet in 90% ammonium sulfate fraction Ammonium sulfate precipitated leghemoglobin was resuspended in 20 mM potassium phosphate, 1 mM EDTA, 50 mM sodium chloride and ammonium sulfate was removed using dialysis or size-exclusion chromatography in the same buffer.
  • leghemoglobin was further purified using anion-exchange chromatography (FFQ GE Healthcare), which was sometimes followed by size-exclusion chromatography (Sephacryl S-100, GE Healthcare).
  • Soybean leghemoglobin from 90% ammonium sulfate pellet was loaded on anion exchange columns (FFQ or DEAE, GE Healthcare) in different buffers (20 mM potassium phosphate pH 7.4, containing 0 to 100 mM sodium chloride, 20 mM Tris pH 8 containing 0 to 100 mM sodium chloride, 20 mM sodium borax pH 9.8, 20 mM sodium chloride, 20 mM sodium carbonate pH 9, 20 mM sodium chloride) and purified either in flow-through or using sodium chloride (0-1M salt gradient).
  • An example of the leghemoglobin purification flow from soybean root nodules is represented in FIG. 6 .
  • the figure shows SDS-PAGE fractionation of different soybean leghemoglobin purification steps (Lane 1) Soybean root-nodule lysate; (Lane 2) Soybean root-nodule lysate purified by 60/90% (wt/v) ammonium sulfate fractionation.
  • leghemoglobin content at different purification steps was determined by determining the fraction of leghemoglobin band on SDS-PAGE gel in a respective sample using ImageDoc analysis software (BioRad). Purity (partial abundance) of leghemoglobin at respective steps in the purification steps was: lysate: 32.7% (lane 1), 60/90% (wt/v) ammonium sulfate fractionation 78% (lane 2), anion-exchange chromatography ⁇ 83% (lane 3), and size-exclusion chromatography to ⁇ 95% (lane 4).
  • FIG. 7 shows stained SDS-PAGE gel analysis of (A) soybean leghemoglobin expressed and purified using recombinant protein technology and (B) soybean leghemoglobin purified from soybean root nodules.
  • A Recombinant Soybean leghemoglobin A carrying His-tag and TEV protease His-tag removal site was expressed in E. coli BL21 strain and purified using His-tag affinity chromatography (Talon resin, CloneTech). The left lane contains molecular weight standards, the right lane contains purified recombinant soybean leghemoglobin A (arrow).
  • Expected molecular weight of the recombinant soybean leghemoglobin A is 17.1 kDa.
  • B SDS-PAGE gel of purified Soybean leghemoglobin from root nodules. The left lane contains molecular weight standards, the right lane contains purified soybean leghemoglobin A (arrow). Mass spectrometry analysis of purified material determined that all four soybean leghemoglobin isoforms are present, and are full length (data not shown). Expected molecular weights (MW) of soybean leghemoglobin isoforms range from MW15.4 to 15.8 kDa.
  • Leghemoglobin can be isolated from the roots nodules of legumes such as soy beans, fava beans, cow peas, lima beans, garbanzo beans, peas, lupine, lotus japonicum or other legumes.
  • the root nodule for example root nodules from a pea plant
  • the root nodule is obtained and homogenized in an aqueous solution, soluble proteins including leghemoglobin are recovered after insoluble matter is removed by precipitation or filtration.
  • Leghemoglobin can be purified by selective precipitation and/or chromatography and/or the use of molecules with specific affinity for leghemoglobin. ( FIG. 1 , showing 100 mls of solution of leghemoglobin isolated from 30 grams of pea root nodules).
  • Heme proteins for example leghemoglobin
  • the heme proteins can be combined with other plant based meat replica components.
  • the heme proteins are captured in a gel which contains other components, for example lipids and or proteins.
  • a multiple gels are combined with non-gel based heme proteins.
  • the combination of the heme proteins and the other compounds of the consumable are done to insure that the heme proteins are able to diffuse through the consumable.
  • the consumable is ed in a heme-protein containing solution, for instance a leghemoglobin solution.
  • the consumable is soaked in a heme protein containing solution, for instance a leghemoglobin solution for 1, 5, 10, 15, 20 or 30 hours.
  • the consumable is soaked in a heme containing solution, for instance a leghemoglobin solution for 1, 5, 10, 15, 30, or 45 minutes.
  • FIG. 8 shows an example of 6 cubes of a commercial meat analog (Quorn chicken analog), about 1 cm on a side, 4 of which (Left and lower right) have been soaked in a solution of about 10 mg/ml soybean leghemoglobin in 20 mM Potassium phosphate pH 7.4 and 100 mM NaCl; the remaining two (Upper right) were soaked in the same buffer without leghemoglobin. Note the deep pink color of the leghemoglobin-infused cubes in contrast to the pale tan color of the un-infused cubes.
  • a commercial meat analog Quorn chicken analog
  • FIG. 9 shows the 4 leghemoglobin-infused cubes of Quorn chicken analog in the process of cooking in a pan at 350° C.
  • the two lower cubes have been turned over to expose the grilled surface, which has turned brown. Note in the upper two cubes that the heated portion has turned grey-brown, while the cooler top surface retains its pink color.
  • the consumable is injected with a heme containing solution, for instance a leghemoglobin solution, until the consumable is the color of uncooked meat.
  • the present invention includes in some embodiments methods to determine whether a product contains a heme protein.
  • Methods for detecting proteins are well known in the art. For example an ELISA or proximity-ligation assoacy or luninex assay or western blot analysis can be performed to determine whether leghemoglobin is present in a food product such as meat or a meat replica. In one embodiment the detection methods are performed to determine whether meat has been altered with leghemoglobin.
  • An exemplary muscle replica composition comprising one or more isolated, purified plant proteins is described herein.
  • Moong bean 8S globulins Moong bean flour was resuspended in in 50 mM potassium phosphate buffer pH 7 and 0.5M NaCl at 1:4 (wt/v) ratio, and mixture was incubated for 1 hr. Unsoluble material was separated by centrifugation and proteins in the supernatant were fractionated by addition of ammonium sulfate in 2 steps: 50% (wt/v) followed by 90% (wt/v). Protein precipitated in 90% fraction contained the moong bean 8S globulins and was stored at ⁇ 20 C until further use.
  • Pea-albumins Green pea dry seed flour was resuspended at 1:10 (wt/v) ratio in 50 mM sodium acetate buffer pH 5 and incubated for 1 hr. Unsoluble material was separated by centrifugation and proteins in the supernatant were fractionated by ammonium sulfate precipitation in two steps: 50% (wt/v) followed by 90% (wt/v) Ammonium sulfate solutions were stirred for 1 hour and ammonium sulfate precipitated proteins removed by centrifugation. Proteins of interest precipitated in 90% (wt/v) ammonium sulfate. Pellet was stored at ⁇ 20 C until further use.
  • Pea-globulins Green pea dry seed flour was resuspended at 1:10 (wt/v) ratio in 20 mM potassium phosphate buffer pH 8, 0.4M sodium chloride and stirred for 1 hr. After centrifugation, the supernatant was subjected to ammonium sulfate fractionation. First, supernatant was brought to 50% (wt/v) ammonium sulfate, and precipitated proteins removed. Second, 50% (wt/v) ammonium sulfate supernatant was brought to 80% (wt/v) ammonium sulfate saturation. The 80% (wt/v) ammonium sulfate pelleted protein contained globulins of interest. Pellet was stored at ⁇ 20′C until further use.
  • RuBisCO was fractionated from alfalfa greens (or other green plants eg soybean plants, spinach etc) by first grinding leaves with 4 volumes of cold 50 mM KPhosphate buffer pH 7.4 buffer (with (in lab) or without (in field) 0.5M NaCl+2 mM DTT+1 mM EDTA) in a blender. The resulting slurry was centrifuged to remove debris, and the supernatant (crude lysate) was used in further purification steps. Proteins in the crude lysate were fractionated by addition of ammonium sulfate to 30% (wt/v) saturation. The solution was stirred for 1 hr and then centrifuged.
  • the pellet from this step was discarded and additional ammonium sulfate was added to the supernatant to 50% (wt/v) ammonium sulfate saturation.
  • the solution was centrifuged again after stirring for 1 hr.
  • the pellet from this step contains RuBisCO, and was kept at ⁇ 20 C until used.
  • Moong bean seed 8S protein was purified by ammonium sulfate fractionation as described. Pellet was resuspended in 20 mM potassium phosphate pH 7.4 and 0.5M sodium chloride and ammonium sulfate removed by dialysis against the same buffer. Any precipitate was removed by centrifugation at 16 000 g, 10 min and protein concentrated to desired concentration. Pea globulins purified by ammonium sulfate fractionation as described. Protein pellet was resuspended in 20 mM potassium phosphate pH pH 7.4 and 0.4M sodium chloride and ammonium sulfate removed by dialysis against the same buffer. Any precipitate was removed by centrifugation at 16 000 g, 10 min and protein concentrated to desired concentration.
  • Moong bean seed 8S protein was purified by ammonium sulfate fractionation as described above, For preparation of gels, 200 g of pellet was dissolved in 400 ml of dialysis buffer (20 mM potassium phosphate, 400 mM NaCl, pH 7.3) and the resulting solution dialyzed for 6 hours against 5 l of dialysis buffer, replaced twice with fresh buffer. Protein solution was centrifuged at 12,000 g for 15 min to remove debris. Protein was concentrated by dialyzing for 36 hours against 5 l of 30% w/w solution of PEG 8000 (polyethylene glycol, molecular weight 8000) in dialysis buffer. Final protein concentration was 150 mg/ml.
  • PEG 8000 polyethylene glycol, molecular weight 8000
  • Root nodules were cleaned to remove soil and extraneous root tissues prior to root nodule lysis in 20 mM potassium phosphate pH 7.4, 100 mM sodium chloride, 1 mm EDTA and 1 mM ascorbic acid. Root nodules were lysed by grinding root-nodules using juicer blender. Unsoluble material was separated by centrifugation. Root nodule lysate was fractionated using ammonium sulfate in two steps, first ammonium sulfate was added to 60% wt/v and solution incubated for 1 hr, 4′C.
  • Pellet was discarded and supernatant brought to 90% wt/v ammonium sulfate and incubated for 12 hr, 4′C.
  • Leghemoglobin was collected as a precipitated pellet in 90% ammonium sulfate fraction and resuspended in 20 mM potassium phosphate, 1 mM EDTA, 100 mM sodium chloride.
  • SDS-PAGE gel analysis determined that protein solution contains 70% leghemoglobin and 30% other root nodule proteins Ammonium sulfate was removed using size-exclusion chromatography in the same buffer.
  • leghemoglobin was concentrated by dialyzing for 48 hr against 30% PEG 8000 (polyethylene glycol, molecular weight 8000) in 20 mM potassium phosphate pH 7.3, 100 mM sodium chloride. Total protein concentration was 57 mg/ml.
  • UV-VIS spectra suggested that leghemoglobin was in heme-iron oxidized state.
  • leghemoglobin was incubated with 5 mM sodium hydrosulfite for 5 min and sodium hydrosulfite was removed using size-exclusion chromatography in 20 mM potassium phosphate, 100 mM sodium chloride buffer.
  • Leghemoglobin was further concentrated to 35.4 mg/ml. UV-VIS spectra analysis confirmed that leghemoglobin is in heme-iron reduced state.
  • Transglutaminase was obtained commercially from (Activa TI, Ajimoto). Stock solution (20% wt/v) was made in 20 mM potassium phosphate pH 7.3, 100 mM sodium chloride buffer.
  • “White” muscle analog ( FIG. 11 ) was prepared by mixing 43 ml moong bean protein solution (150 mg/ml) with 45 ml of 11.7 mg/ml solution of leghemoglobin and 0.8% (wt/v) of transglutaminase solution. Final protein concentrations were 63 mg/ml for moong bean protein, 5.2 mg/ml of leghemoglobin, 68 mg/ml total protein.
  • the “dark” muscle tissue analog formed an opaque gel of dark chocolate color, smooth uniform texture, with glistening surface, and a small amount ( ⁇ 1 ml) of dark red, venous blood colored liquid on top.
  • the gel was freely standing, elastic but fragile, similar in appearance to thin Jell-O.
  • the gel has a medium aroma with notes of beans and blood clearly discernible.
  • the flavor is dominated by notes of beans and iron/blood, with weaker grassy and medicinal/chemical flavors.
  • the taste is salty, with a long aftertaste of blood.
  • the “white” muscle tissue analog was very similar, but with much lighter, cappuccino-like, color. It was also more fragile, 2-3-fold less strong against compression.
  • Fat tissue analog using moong bean 8S globulin fraction was prepared as follows: 15 ml of moong bean protein solution (150 mg/ml in dialysis buffer) were mixed with 15 ml of rice bran oil. 6 ml of transglutaminase solution (20% w/w) were added, solutions thoroughly emulsified using a homogenizer (VWR) at speed #2. Emulsion was aliquoted into 1.6 eppendorf tubes and incubated overnight at room temperature. After that, tubes were heated at 95° C. for 5 min in a heat block, and allowed to cool down to room temperature on a bench. Final concentrations were 75 mg/ml for moong bean protein, 50% w/w oil.
  • Fat tissue analog using pea globulin was prepared by the same method. Additionally, fat tissue analog was prepared from pea globulin, and either rice bran or canola oil, in bulk by the same method, but without aliquoting emulsions into eppendorf tubes. Instead, emulsions in 50 ml Falcon tubes were rotated overnight on a nutator, and were subsequently incubated at 90° C. for 30 min.
  • Fat tissue analog based on moong beans ( FIG. 12 ) and prepared in eppendorf tubes formed an opaque gel of off-white color, smooth uniform texture, with no visible discernible liquid that was not incorporated into the gel.
  • the gel was freely standing, elastic and springy.
  • the gel has a slight, pleasant aroma and a mild and pleasant flavor.
  • the taste is mildly salty.
  • Fat tissue analog based on pea globulin ( FIG. 13 ) and prepared in eppendorf tubes was very similar to moong bean-based fat analog, except that it gave up a little of oil upon compression.
  • Fat tissue analog prepared in 50 ml Falcon tubes were similar in appearance, texture and aromas, but substantially softer (2-fold softer for canola oil, and 3-fold softer for rice bran oil, according to compressibility measurements).
  • Connective tissue analog prototypes were developed using zein protein sourced from 100% yellow corn gluten meal, or from commercial sources, such as Amazein (Prairie Gold, Bloomington, Ill.). Zein proteins were solubilized in 70-90% ethanol with desired ratios at 1:3 to 1:5 (solids:solution). By precipitating zein proteins, for example by a change in pH, in a controlled manner, large zein structures result with physicochemical properties that can be manipulated as desired. For example, FIG.
  • FIG. 14 shows connective-tissue analog strands that were created using a 1:3 ratio in 70% ethanol, loaded into a syringe with a 23 gauge needle (ID 0.337 mm)
  • the solution was slowly extruded from the bottom of a 5 inch-high vessel into an excess of 5 M NaCl solution.
  • the ethanol-zein solution being less dense than the NaCl solution, floated upward, drawing out a fibrous stand of solidifying zein.
  • the NaCl was constantly stirred as the strands began to develop to assist in the strand lengthening. The strands bunch together and become a hard, dense mass.
  • a ground beef prototype patty was made by combining 62% (wt/wt) muscle analog (62% (wt/wt) “dark muscle analog” and 38% (wt/wt) “white muscle analog”), 29% (wt/wt) fat tissue analog (from pea globulin and canola oil), 5% (wt/wt) connective tissue analog ( FIG. 15 panel A).
  • a ground beef prototype patty was made by combining 62% muscle analog (62% “dark muscle analog” and 38% “white muscle analog), 29% fat tissue analog (from moong bean seed 8S protein and rice bran oil), 5% connective tissue analog ( FIG. 15 panel B).
  • a ground beef prototype patty was made by combining 71% (wt/wt) muscle tissue analog (composed of 60% “white” muscle analog, 40% “dark” muscle analog), 23% fat tissue (from pea seed globulin proteins and canola oil) ( FIG. 15 panel C).
  • a ground beef prototype patty was made by combining 67% “White” muscle analog, with 28% fat tissue analog (from pea globulins and rice bran oil), ( FIG. 15 , panel D)
  • a ground beef patty analog was made by combining 62% (wt/wt) muscle tissue analog (62% (wt/wt) “dark muscle analog” and 38% (wt/wt) “muscle analog”), 29% (wt/wt) fat tissue analog (from pea globulin and canola oil), 5% (wt/wt) connective tissue analog ( FIG. 16 ).
  • the panel on the left shows the patty before cooking and the panel on the right shows the same patty after cooking for about 2 minutes. Observers described the aroma of the cooking ground beef replica as distinctly “beefy”.

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Nutrition Science (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Molecular Biology (AREA)
  • Animal Husbandry (AREA)
  • Zoology (AREA)
  • Mycology (AREA)
  • Physiology (AREA)
  • Biotechnology (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Microbiology (AREA)
  • Biomedical Technology (AREA)
  • Botany (AREA)
  • Peptides Or Proteins (AREA)
  • Meat, Egg Or Seafood Products (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Seasonings (AREA)
  • Detergent Compositions (AREA)
  • Sanitary Thin Papers (AREA)
  • Beans For Foods Or Fodder (AREA)
  • Fodder In General (AREA)
  • Management, Administration, Business Operations System, And Electronic Commerce (AREA)
US14/152,499 2011-07-12 2014-01-10 Methods and compositions for consumables Abandoned US20140193547A1 (en)

Priority Applications (4)

Application Number Priority Date Filing Date Title
US14/152,499 US20140193547A1 (en) 2011-07-12 2014-01-10 Methods and compositions for consumables
US14/752,540 US20150289541A1 (en) 2011-07-12 2015-06-26 Methods and compositions for consumables
US15/985,694 US20190008192A1 (en) 2011-07-12 2018-05-21 Methods and compositions for consumables
US17/531,491 US20220071250A1 (en) 2011-07-12 2021-11-19 Methods and compositions for consumables

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US201161572205P 2011-07-12 2011-07-12
PCT/US2012/046560 WO2013010042A1 (fr) 2011-07-12 2012-07-12 Procédés et compositions pour produits consommables
US14/152,499 US20140193547A1 (en) 2011-07-12 2014-01-10 Methods and compositions for consumables

Related Parent Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2012/046560 Continuation WO2013010042A1 (fr) 2011-07-12 2012-07-12 Procédés et compositions pour produits consommables

Related Child Applications (2)

Application Number Title Priority Date Filing Date
US14/752,540 Continuation US20150289541A1 (en) 2011-07-12 2015-06-26 Methods and compositions for consumables
US15/985,694 Continuation US20190008192A1 (en) 2011-07-12 2018-05-21 Methods and compositions for consumables

Publications (1)

Publication Number Publication Date
US20140193547A1 true US20140193547A1 (en) 2014-07-10

Family

ID=47506556

Family Applications (5)

Application Number Title Priority Date Filing Date
US14/152,499 Abandoned US20140193547A1 (en) 2011-07-12 2014-01-10 Methods and compositions for consumables
US14/752,540 Abandoned US20150289541A1 (en) 2011-07-12 2015-06-26 Methods and compositions for consumables
US15/624,505 Active US9808029B2 (en) 2011-07-12 2017-06-15 Methods and compositions for affecting the flavor and aroma profile of consumables
US15/985,694 Abandoned US20190008192A1 (en) 2011-07-12 2018-05-21 Methods and compositions for consumables
US17/531,491 Pending US20220071250A1 (en) 2011-07-12 2021-11-19 Methods and compositions for consumables

Family Applications After (4)

Application Number Title Priority Date Filing Date
US14/752,540 Abandoned US20150289541A1 (en) 2011-07-12 2015-06-26 Methods and compositions for consumables
US15/624,505 Active US9808029B2 (en) 2011-07-12 2017-06-15 Methods and compositions for affecting the flavor and aroma profile of consumables
US15/985,694 Abandoned US20190008192A1 (en) 2011-07-12 2018-05-21 Methods and compositions for consumables
US17/531,491 Pending US20220071250A1 (en) 2011-07-12 2021-11-19 Methods and compositions for consumables

Country Status (11)

Country Link
US (5) US20140193547A1 (fr)
EP (1) EP2731446A4 (fr)
JP (4) JP6650671B2 (fr)
KR (5) KR20230022455A (fr)
CN (3) CN105724726A (fr)
AU (5) AU2012281069B2 (fr)
BR (1) BR112014000614A2 (fr)
CA (2) CA2841473C (fr)
MX (5) MX2014000469A (fr)
RU (1) RU2653751C2 (fr)
WO (1) WO2013010042A1 (fr)

Cited By (22)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US9526267B2 (en) 2014-04-17 2016-12-27 Savage River, Inc. Nutrient-dense meat structured protein products
WO2017165756A1 (fr) * 2016-03-24 2017-09-28 Cargill, Incorporated Concentré de protéine de maïs et ses procédés de fabrication
USD805728S1 (en) 2016-09-06 2017-12-26 Mars, Incorporated Food product
USD806351S1 (en) 2016-09-06 2018-01-02 Mars, Incorporated Food product
WO2018097887A1 (fr) 2016-11-22 2018-05-31 Sisney Gary Procédé de traitement de la viande
EP3628173A1 (fr) 2014-03-31 2020-04-01 Impossible Foods Inc. Répliques de viande hachée
CN112839522A (zh) * 2018-08-07 2021-05-25 诺瓦曼特技术有限公司 包含蛋白质的可食用微挤出产品的制造方法、由此获得的组合物及其用途
US11019836B2 (en) 2015-08-03 2021-06-01 Savage River, Inc. Food products comprising cell wall material
WO2022072833A2 (fr) 2020-10-02 2022-04-07 Impossible Foods Inc. Constructions d'expression et méthodes de modification génétique de cellules
WO2022072846A2 (fr) 2020-10-02 2022-04-07 Impossible Foods Inc. Plantes transgéniques ayant des profils d'acides gras modifiés et une biosynthèse d'hème régulée à la hausse
US11375736B2 (en) 2016-03-24 2022-07-05 Cargill, Incorporated Corn protein product having decreased free sulfite levels and method for manufacturing same
WO2022165164A1 (fr) 2021-01-28 2022-08-04 Epogee, Llc Viandes d'imitation à base de plantes avec des liants pour produits alimentaires à base de plantes
WO2022187736A1 (fr) * 2021-03-05 2022-09-09 Motif Foodworks, Inc. Formulation de substitut de viande
WO2022251166A3 (fr) * 2021-05-25 2023-01-05 Evelo Biosciences, Inc. Compositions bactériennes comprenant de l'hémoglobine de soja
US11561201B2 (en) * 2017-10-31 2023-01-24 Universidad De La Republica Device and method for determining the elasticity of soft-solids
US11667670B2 (en) 2017-09-21 2023-06-06 Cargill, Incorporated Corn protein retention during extraction
US11771112B2 (en) 2021-10-19 2023-10-03 Eat Scifi Inc. Plant base/animal cell hybrid meat substitute
WO2024026348A1 (fr) * 2022-07-28 2024-02-01 Pioneer Hi-Bred International, Inc. Production de leghémoglobine végétale
US11980217B2 (en) 2017-08-02 2024-05-14 Cargill, Incorporated Extruded corn protein material
US11985990B2 (en) 2016-09-23 2024-05-21 Cargill, Incorporated Corn protein retention during extraction
US11992033B2 (en) 2017-01-27 2024-05-28 Mars, Incorporated Pet food
US12054515B2 (en) 2015-03-24 2024-08-06 Cargill, Incorporated Corn protein isolate and methods of manufacturing same

Families Citing this family (63)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US10039306B2 (en) 2012-03-16 2018-08-07 Impossible Foods Inc. Methods and compositions for consumables
CN110742128A (zh) 2011-07-12 2020-02-04 非凡食品有限公司 用于消费品的方法和组合物
US20140220217A1 (en) 2011-07-12 2014-08-07 Maraxi, Inc. Method and compositions for consumables
KR20230022455A (ko) 2011-07-12 2023-02-15 임파서블 푸즈 인크. 소비재를 위한 방법 및 조성물
EP3513664A1 (fr) 2013-01-11 2019-07-24 Impossible Foods Inc. Procédé de production d'un produit non-laitier fermenté et aromatisé
PL2943078T3 (pl) * 2013-01-11 2021-09-20 Impossible Foods Inc. Sposoby wytwarzania i kompozycje produktów konsumpcyjnych
RS60259B1 (sr) * 2013-09-11 2020-06-30 Impossible Foods Inc Izlučivanje polipeptida koji obuhvataju hem
WO2015041235A1 (fr) * 2013-09-17 2015-03-26 不二製油株式会社 Utilisation d'aliment pour traiter des maladies liées au mode de vie
ES2782380T5 (es) 2013-10-30 2023-05-08 Univ Missouri Método de especificación y cultivo de linaje del músculo esquelético escalable
JP6676874B2 (ja) * 2014-12-26 2020-04-08 不二製油株式会社 非アルコール性脂肪性肝疾患の発症リスクを低減する機能を有する食品
CN104855526B (zh) * 2015-04-28 2018-02-06 福州大学 一种基于豆粕的仿牛肉制品
EP3294762B1 (fr) 2015-05-11 2022-01-19 Impossible Foods Inc. Constructions d'expression et procédés de modification génétique de la levure méthylotrophique
US11849741B2 (en) * 2015-10-20 2023-12-26 Savage River, Inc. Meat-like food products
US11266163B2 (en) 2016-02-19 2022-03-08 Eat Just, Inc. Functional mung bean-derived compositions
JP2018131414A (ja) * 2017-02-16 2018-08-23 株式会社植物ハイテック研究所 未利用作物組織から高栄養価機能を持つルビスコを調製する方法
WO2018189738A1 (fr) 2017-04-09 2018-10-18 Supermeat The Essence Of Meat Ltd. Aliment hybride contenant de la viande de culture
WO2018208628A1 (fr) 2017-05-06 2018-11-15 Memphis Meats, Inc. Compositions et procédés permettant d'augmenter la densité de culture d'une biomasse cellulaire dans une infrastructure de culture
US10745682B2 (en) * 2017-06-14 2020-08-18 R.J. Reynolds Tobacco Company Method of producing RuBisCO protein fibers
WO2019014652A1 (fr) 2017-07-13 2019-01-17 Memphis Meats, Inc. Compositions et procédés pour augmenter l'efficacité de cultures cellulaires utilisées pour la production d'aliments
WO2019060759A1 (fr) 2017-09-21 2019-03-28 Dana-Farber Cancer Institute, Inc. Isolement, conservation, compositions et utilisations d'extraits de plantes justicia
US11051532B2 (en) 2017-09-22 2021-07-06 Impossible Foods Inc. Methods for purifying protein
GB201720900D0 (en) * 2017-12-14 2018-01-31 Mars Inc Pet food product
WO2020035268A1 (fr) * 2018-08-13 2020-02-20 Chr. Hansen A/S Production d'un jus de légumes fermenté exempt d'alcool à l'aide d'une levure pichia kluyveri
KR20210052458A (ko) 2018-08-21 2021-05-10 브이2 푸드 피티와이 엘티디 식품 성분
GB201901092D0 (en) * 2019-01-26 2019-03-13 Jet Eat Printed Food Ltd Multi-layered meat substitute and methods of production thereof
BR112021020727A2 (pt) 2019-04-17 2021-12-14 Impossible Foods Inc Materiais e métodos para produção de proteína
CA3137581A1 (fr) 2019-04-25 2020-10-29 Impossible Foods Inc. Compositions et procedes pour la production de proteines contenant de l'heme
WO2021098966A1 (fr) 2019-11-21 2021-05-27 Bunge Loders Croklaan B.V. Produit analogue à la viande et procédé
BR112022011460A2 (pt) * 2019-12-12 2022-08-23 Glanbia Nutritionals Ltd Produto de proteína vegetal texturizado e método
US20230095432A1 (en) 2020-01-31 2023-03-30 Spiber Inc. Meat Substitute Composition
KR20220162129A (ko) 2020-02-28 2022-12-07 임파서블 푸즈 인크. 단백질 생산을 위한 물질 및 방법
IL295703A (en) 2020-03-02 2022-10-01 Air Protein Inc Structured analog compositions of protein-rich meat
WO2021191913A1 (fr) * 2020-03-23 2021-09-30 Dr. Eyal Bressler Ltd. Substituts de viande produits dans des systèmes végétaux et procédé associé
EP4161281A1 (fr) 2020-06-07 2023-04-12 Comestaag LLC Compositions de revêtement protecteur pour denrées périssables et procédés, systèmes, kits et articles revêtus associés
BR112023001548A2 (pt) 2020-07-30 2023-04-04 Cooeperatie Koninklijke Avebe U A Patatina como aglutinante em substitutos de carne
WO2022043059A1 (fr) 2020-08-26 2022-03-03 Société des Produits Nestlé S.A. Produit du type succédané de viande
AU2020467230A1 (en) 2020-09-14 2023-03-09 Impossible Foods Inc. Protein purification methods at alkaline pH
US12011016B2 (en) 2020-09-14 2024-06-18 Impossible Foods Inc. Protein methods and compositions
US10947552B1 (en) 2020-09-30 2021-03-16 Alpine Roads, Inc. Recombinant fusion proteins for producing milk proteins in plants
US10894812B1 (en) 2020-09-30 2021-01-19 Alpine Roads, Inc. Recombinant milk proteins
WO2022072718A1 (fr) 2020-09-30 2022-04-07 Nobell Foods, Inc. Protéines de lait recombinantes et compositions les comprenant
JP2023548301A (ja) 2020-10-28 2023-11-16 パイオニア ハイ－ブレッド インターナショナル， インコーポレイテッド ダイズにおけるレグヘモグリン
EP4250952A2 (fr) * 2020-11-24 2023-10-04 Cargill, Incorporated Produit de substitution à la viande
CA3199531A1 (fr) * 2020-11-24 2022-06-02 Beatrice Ines FELKE Produit de succedane de viande
EP4250948A1 (fr) 2020-11-25 2023-10-04 Thrilling Foods, Inc. Composition et procédé de fabrication de produits alimentaires à base de plantes
WO2022159204A1 (fr) * 2021-01-22 2022-07-28 AuraPea LLC Produits alimentaires gélifiés à base de plantes imitant les caractéristiques du gras de viande
CA3212363A1 (fr) 2021-03-01 2022-09-09 Impossible Foods Inc. Substances et procedes pour la production de proteines
EP4362694A1 (fr) * 2021-07-01 2024-05-08 Cargill, Incorporated Pigment pour compositions de substituts de viande
WO2023014849A1 (fr) * 2021-08-06 2023-02-09 Back of the Yards Algae Sciences LLC Analogue d'hème algal
WO2023046914A1 (fr) 2021-09-27 2023-03-30 Firmenich Sa Compositions d'arôme contenant des composés de fer et leur utilisation
MX2024003781A (es) 2021-09-30 2024-04-19 Unilever Ip Holdings B V Mimetico de tejido graso.
WO2023052563A2 (fr) * 2021-10-01 2023-04-06 Société des Produits Nestlé S.A. Produit analogue de graisse
IL288258B2 (en) * 2021-11-21 2023-08-01 More Alternative Foods Ltd Meat substitute products that include oilseed solids
WO2023126248A1 (fr) 2021-12-29 2023-07-06 Unilever Ip Holdings B.V. Mimétique de tissu gras
US12004539B2 (en) 2022-01-31 2024-06-11 The Livekindly Company Switzerland GmbH Methods for creating of high fibrousness, high moisture extrudates
WO2023161507A1 (fr) * 2022-02-28 2023-08-31 Société des Produits Nestlé S.A. Procédé d'éclaircissement d'un produit protéique texturé
WO2023199757A1 (fr) * 2022-04-15 2023-10-19 株式会社ニッスイ Gel émulsifié, procédé de production de gel émulsifié, aliment transformé de type viande et procédé de production d'aliment transformé de type viande
JP7355967B1 (ja) * 2022-04-15 2023-10-03 株式会社ニッスイ 加工肉様食品の製造方法、加工肉様食品のジューシー感の向上方法、乳化ゲルの破断抑制方法、および凍結乳化ゲル
WO2023199758A1 (fr) * 2022-04-15 2023-10-19 株式会社ニッスイ Procédé de production d'aliment transformé de type viande, procédé pour améliorer la sensation juteuse d'un aliment transformé de type viande, procédé pour prévenir la rupture d'un gel émulsifié, et gel émulsifié congelé
GB202208198D0 (en) 2022-06-03 2022-07-20 Givaudan Sa Colouring compositions
EP4278900B1 (fr) * 2022-06-29 2024-07-24 Paleo B.V. Procédé de préparation d'aliments pour animaux
WO2024002708A1 (fr) 2022-07-01 2024-01-04 Givaudan Sa Perfectionnements apportés aux composés organiques ou en relation avec ceux-ci
WO2024167695A1 (fr) 2023-02-08 2024-08-15 Danisco Us Inc. Compositions et procédés de production de globines hétérologues dans des cellules fongiques filamenteuses

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20060035006A1 (en) * 2004-08-16 2006-02-16 Mcmindes Matthew K Restructured meat product and process for preparing same
EP1759593A1 (fr) * 2005-09-06 2007-03-07 Nug Nahrungs-Und Genussmittel Vertriebsgesellschaft Mbh Analogue de viande hachée et procédé de fabrication
US20100074998A1 (en) * 2006-11-01 2010-03-25 Alicia Espeleta Vega Meat Substitute Food Product And Process For Preparing The Same

Family Cites Families (154)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3870801A (en) 1968-08-09 1975-03-11 Lever Brothers Ltd Fluid aqueous protein compositions and food products prepared therefrom
US3658550A (en) 1969-10-16 1972-04-25 Ralston Purina Co Method for producing an artificial adipose tissue
BE760075A (fr) 1970-01-13 1971-06-09 Int Flavors & Fragrances Inc Methodes et compositions pour aromatiser les denrees alimentaires
US3693533A (en) 1970-12-28 1972-09-26 Procter & Gamble Meat analog apparatus
US3829582A (en) 1972-09-21 1974-08-13 Us Agriculture Method of imparting fatty-fried flavor to foods and composition
US3966985A (en) 1974-02-18 1976-06-29 Pfizer Inc. Flavoring agent obtained by reacting a monosaccharide and a supplemented plastein
US3973043A (en) 1975-07-31 1976-08-03 Lynn Howard D Feedlot animal wastes into useful materials
JPS52110875A (en) 1976-03-12 1977-09-17 Kikkoman Shoyu Co Ltd Production of beef like flavor substance and said flavor imparting agent
JPS52156962A (en) 1976-06-21 1977-12-27 Hiroatsu Matsuoka Method of producing cheesee like food from soybean melk
JPS53115846A (en) 1977-03-18 1978-10-09 Jiyunsaku Nonaka Color developing agent for protein food
US4218487A (en) 1977-05-31 1980-08-19 Givaudan Corporation Processes for preparing flavoring compositions
US4141999A (en) * 1977-10-07 1979-02-27 Miles Laboratories, Inc. Bacon-like meat analog
CA1108003A (fr) 1978-03-06 1981-09-01 Radcliffe F. Robinson Procede de preparation d'analogues du fromage
US4435438A (en) 1980-12-29 1984-03-06 A. E. Staley Manufacturing Company Soy isolate suitable for use in imitation cheese
JPS5959151A (ja) 1982-09-29 1984-04-04 Ajinomoto Co Inc 新規なゲル状食品の製造法
US4604290A (en) 1983-09-01 1986-08-05 Nestec S.A. Meat flavoring agents and process for preparing same
JPH0611216B2 (ja) 1983-10-04 1994-02-16 太陽油脂株式会社 チーズ様乳化食品の製造法
WO1988002991A1 (fr) 1986-10-22 1988-05-05 Asahi Kasei Kogyo Kabushiki Kaisha Substance comestible et procede de production
JP2536086B2 (ja) 1988-09-02 1996-09-18 味の素株式会社 長期常温保存可能な豆腐の製造法
US5021248A (en) * 1988-09-19 1991-06-04 Enzytech, Inc. Hydrophobic protein microparticles and preparation thereof
US5264239A (en) 1989-10-12 1993-11-23 Nestec S.A. Preparation of dried flavored meats
US5213829A (en) * 1990-02-23 1993-05-25 Lipidyne Corporation Meat products containing artificial edible adipose and methods of making
US5230915A (en) 1990-10-24 1993-07-27 Fereidoon Shahidi Process for preparing a powdered cooked cured-meat pigment
US5650554A (en) 1991-02-22 1997-07-22 Sembiosys Genetics Inc. Oil-body proteins as carriers of high-value peptides in plants
US6753167B2 (en) 1991-02-22 2004-06-22 Sembiosys Genetics Inc. Preparation of heterologous proteins on oil bodies
ATE142082T1 (de) 1991-02-22 1996-09-15 Herrmann Martin Verfahren zur herstellung eines quarkähnlichen produktes aus sojamilch
WO1993025697A1 (fr) 1992-06-15 1993-12-23 California Institute Of Technology Renforcement de la croissance des cellules par expression de proteines clonees fixatrices d'oxygene
US5366740A (en) 1993-02-04 1994-11-22 Warner-Lambert Company Chewing gum containing wheat gluten
JP3081101B2 (ja) 1994-03-03 2000-08-28 キッコーマン株式会社 チーズ様食品の製造法
US5753295A (en) 1994-04-05 1998-05-19 Goldman; Marc S. Non-dairy composition containing fiber and method for making same
FR2719222B1 (fr) 1994-05-02 1996-06-21 Rocher Yves Biolog Vegetale Vésicules lipidiques, leur procédé de fabrication et leurs applications.
MX9602035A (es) 1994-10-07 1997-06-28 Firmenich & Cie Composiciones y metodo para proporcionar sabor.
JP2883823B2 (ja) 1994-11-28 1999-04-19 ハウス食品株式会社 ヘム鉄含有食品の製造方法
US5580499A (en) 1994-12-08 1996-12-03 E. I. Du Pont De Nemours And Company Process for producing zein fibers
GB9509015D0 (en) 1995-05-03 1995-06-21 Dalgety Plc Textured proteins
NZ310975A (en) 1995-06-30 1998-12-23 Novo Nordisk As A cheese making process
US5766657A (en) 1996-06-21 1998-06-16 California Polytechnic State University Melt-controlled cheese and process of making
US5807601A (en) 1996-09-09 1998-09-15 Schreiber Foods, Inc. Imitation cheese composition and products containing starch
US5959187A (en) 1996-09-26 1999-09-28 Bailey; James E. Expression of oxygen-binding proteins in plants
US5856452A (en) 1996-12-16 1999-01-05 Sembiosys Genetics Inc. Oil bodies and associated proteins as affinity matrices
GB9706235D0 (en) 1997-03-26 1997-05-14 Dalgety Plc Flavouring agents
US6171640B1 (en) * 1997-04-04 2001-01-09 Monsanto Company High beta-conglycinin products and their use
ATE386439T1 (de) 1997-05-27 2008-03-15 Sembiosys Genetics Inc Verwendungen von ölkörpern
US6599513B2 (en) 1997-05-27 2003-07-29 Sembiosys Genetics Inc. Products for topical applications comprising oil bodies
US6761914B2 (en) 1997-05-27 2004-07-13 Sembiosys Genetics Inc. Immunogenic formulations comprising oil bodies
US6183762B1 (en) 1997-05-27 2001-02-06 Sembiosys Genetics Inc. Oil body based personal care products
US7585645B2 (en) 1997-05-27 2009-09-08 Sembiosys Genetics Inc. Thioredoxin and thioredoxin reductase containing oil body based products
US6372234B1 (en) 1997-05-27 2002-04-16 Sembiosys Genetics Inc. Products for topical applications comprising oil bodies
JP4137224B2 (ja) 1998-03-31 2008-08-20 天野エンザイム株式会社 酵素による蛋白質の架橋法
CA2331772C (fr) 1998-06-26 2009-08-04 The University Of Manitoba Hemoglobines servant au maintien de la vitalite cellulaire
US6372961B1 (en) 1998-08-20 2002-04-16 Pioneer Hi-Bred International, Inc. Hemoglobin genes and their use
CA2346989A1 (fr) 1998-10-19 2000-04-27 The Board Of Trustees Of The Leland Stanford Junior University Bibliotheque de chimie combinatoire a matrice d'adn
US6399121B1 (en) 1999-03-16 2002-06-04 Novozymes A/S Process for producing cheese
US6228418B1 (en) 1999-04-07 2001-05-08 Cyvex Nutrition Vegetarian pet treat
US6093424A (en) 1999-04-27 2000-07-25 Kraft Foods, Inc. Process for making cheese using transglutaminase and a non-rennet protease
US6399135B2 (en) 1999-09-29 2002-06-04 Archer-Daniels-Midland Company Use of soy isolated protein for making fresh cheese
US6413569B1 (en) 1999-09-29 2002-07-02 Archer-Daniels-Midland Company Use of isolated soy protein for making fresh, unripened cheese analogs
CN1252231A (zh) * 1999-10-14 2000-05-10 余国华 血红蛋白系列食品及其制造方法
US6379738B1 (en) 1999-11-16 2002-04-30 Nestec S.A. Meat emulsion product
CN1301811A (zh) * 1999-12-29 2001-07-04 吴光耀 一种可用于人体补铁的转基因铁蛋白酵母及其生产方法
US20010049132A1 (en) 2000-03-21 2001-12-06 Borge Kringelum Method for supply of starter cultures having a consistent quality
DE10028225A1 (de) 2000-06-07 2001-12-20 Haarmann & Reimer Gmbh Käsearoma
JP5155502B2 (ja) * 2000-06-20 2013-03-06 雪印メグミルク株式会社 鉄含有タンパク質組成物
US6858422B2 (en) 2000-07-13 2005-02-22 Codexis, Inc. Lipase genes
US20040161513A1 (en) * 2000-11-30 2004-08-19 Kraft Foods Holdings, Inc. Method of preparation of high quality soy-containing meat and meat analog products
US6416797B1 (en) 2001-02-14 2002-07-09 Kraft Foods Holdings, Inc. Process for making a wheyless cream cheese using transglutaminase
AU2002233639B2 (en) 2001-02-15 2007-03-01 Adeka Corporation Products containing $G(b)-glucan
US6579992B2 (en) 2001-03-23 2003-06-17 Council Of Scientific & Industrial Research Method for producing chiral dihydrotagetone, and its conversion to chiral 5-isobutyl-3-methyl-4,5-dihydro-2(3H)-furanone
US6572901B2 (en) 2001-05-02 2003-06-03 Kraft Foods Holdings, Inc. Process for making a cheese product using transglutaminase
FR2824756B1 (fr) 2001-05-16 2005-07-08 Mainelab Microcapsules a base de proteines vegetales
AU2002331272A1 (en) * 2001-07-18 2003-03-03 Dsm Ip Assets B.V. Vegetarian protein foodstuff
US7052879B2 (en) 2001-08-31 2006-05-30 Academia Sinica Recombinant Candida rugosa lipases
CN1407108A (zh) * 2001-09-06 2003-04-02 胡放 表达乳铁蛋白的基因工程重组菌株及其应用
US6495184B1 (en) 2001-10-12 2002-12-17 Kraft Foods Holdings, Inc. Grilled meat flavoring composition and method of preparation
US8021695B2 (en) 2002-02-15 2011-09-20 Arch Personal Care Products, L.P. Personal care composition containing leghemoglobin
US20030224476A1 (en) 2002-03-01 2003-12-04 Szu-Yi Chou Method of producing transglutaminase reactive compound
CN1466903A (zh) 2002-07-11 2004-01-14 余国民 花生水晶豆腐
ATE536747T1 (de) 2002-08-28 2011-12-15 Fuji Oil Co Ltd Saure sojaproteingel-nahrungsmittel und verfahren zu ihrer herstellung
US20060233721A1 (en) 2002-10-25 2006-10-19 Foamix Ltd. Foam containing unique oil globules
AU2003296714A1 (en) 2002-12-23 2004-07-22 Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften Ev Method for altering the content of reserve substances in plants
JP3824082B2 (ja) * 2003-03-13 2006-09-20 孝明 武部 豆乳カードの製造方法
US6908634B2 (en) 2003-03-20 2005-06-21 Solae, Llc Transglutaminase soy fish and meat products and analogs thereof
WO2004087755A2 (fr) 2003-04-01 2004-10-14 Cropdesign N.V. Hemoglobine vegetale
WO2004113543A1 (fr) 2003-06-18 2004-12-29 The University Of York Lipase vegetale
US7070827B2 (en) 2003-07-03 2006-07-04 Solae, Llc Vegetable protein meat analog
WO2005013713A1 (fr) 2003-08-12 2005-02-17 Unilever Plc Confiserie glacee et son procede de production
FR2861549B1 (fr) 2003-10-31 2006-07-07 Rhodia Chimie Sa Aromatisation d'un produit laitier a partir d'au moins une bactrerie produisant une bacteriocine et appartenant au genre pediococcus
FR2861955B1 (fr) 2003-11-07 2006-02-10 Protial Sa Produit alimentaire de type fromage, matrice fromagere et caille a base de lait vegetal fermente et procede de fabrication d'un tel caille
TW201119585A (en) 2003-11-12 2011-06-16 J Oil Mills Inc Body taste improver comprising long-chain highly unsaturated fatty acid and/or its ester
TW200526778A (en) 2003-11-14 2005-08-16 Sembiosys Genetics Inc Methods for the production of apolipoproteins in transgenic plants
CN1250109C (zh) 2004-01-20 2006-04-12 浙江省农业科学院 无废水豆腐制品生产方法
GB0405637D0 (en) 2004-03-12 2004-04-21 Danisco Protein
DK1765279T3 (da) 2004-04-05 2011-01-10 Sembiosys Genetics Inc Fremgangsmåde til fremstilling af kosmetiske emulsioner
CN100563465C (zh) * 2004-05-26 2009-12-02 王健柏 一种活性阿胶营养保健口服液浆
WO2006008508A1 (fr) 2004-07-16 2006-01-26 Danisco A/S Procede de demucilagination enzymatique
US20060073261A1 (en) * 2004-10-06 2006-04-06 Mcmindes Matthew K Soy protein containing food product and process for preparing same
US20060035003A1 (en) * 2004-08-16 2006-02-16 Mcmindes Matthew K Soy protein containing food product and process for preparing same
WO2006042608A1 (fr) 2004-10-18 2006-04-27 Unilever Plc Confiserie glacee
CN1284571C (zh) * 2004-10-31 2006-11-15 青海石油管理局 改善营养性贫血保健食品
US20070269571A1 (en) * 2005-07-27 2007-11-22 Stc System Japan Co., Ltd. Composition for Soybean Protein-Processed Food, Paste for Meat-Containing or Meat-Not-Containing Processed Food, Dried Meat-Like Food
FR2889416B1 (fr) 2005-08-05 2007-10-26 Roquette Freres Composition de proteines de pois
FI121525B (fi) 2005-11-22 2010-12-31 Valio Oy Menetelmä maitoperäisen hapatetun tuoretuotteen valmistamiseksi
WO2007115899A1 (fr) 2006-04-07 2007-10-18 Unilever N.V. Produits alimentaires augmentant la satiété
US20100064384A1 (en) 2006-04-13 2010-03-11 Max Planck Institut fur molekulare Method for modifying the atp/adp ratio in cells
BRPI0711212A2 (pt) * 2006-05-19 2011-10-18 Solae Llc processo para produção de uma composição de carne reestruturada e composição de carne reestruturada
US8685485B2 (en) 2006-05-19 2014-04-01 Solae, Llc Protein composition and its use in restructured meat and food products
WO2008017499A1 (fr) 2006-08-11 2008-02-14 Technische Universität München Préparation d'un produit alimentaire à partir d'un substrat enrichi en protéines par l'utilisation simultanée de la transglutaminase et de la protéase
CN101138405A (zh) 2006-09-08 2008-03-12 周伯根 懒豆腐营养方便菜及其制做方法
EP2061334B1 (fr) 2006-09-08 2013-04-10 CSK Food Enrichment B.V. Utilisation de levure et de bactéries pour fabriquer des fromages qui présentent des caractéristiques de saveur et/ou de texture améliorées
US20080268112A1 (en) * 2006-12-28 2008-10-30 Solae, Llc Ground Meat and Meat Analog Compositions Having Improved Nutritional Properties
EP2124905B1 (fr) 2007-01-10 2016-09-07 DSM Nutritional Products AG Microcapsules comprenant de la proteine de pois
EP1952695A1 (fr) 2007-01-31 2008-08-06 Unilever N.V. Vésicules lipidiques et procédé de production de telles huiles
US8293297B2 (en) 2007-04-05 2012-10-23 Solae, Llc Colored structured protein products
US20080254168A1 (en) 2007-04-10 2008-10-16 Solae, Llc Dried Food Compositions
KR100888623B1 (ko) 2007-05-29 2009-03-11 주식회사 엔유씨전자 프로바이오틱 유산균을 이용한 기능성 발효두부의 제조방법및 그 두부
US20110008502A1 (en) * 2007-07-02 2011-01-13 San-Ei Gen F.F.I., Inc. Processed food composition containing dextrin
EP2011404A1 (fr) 2007-07-04 2009-01-07 Nestec S.A. Produits alimentaires extrudés et procédé de fabrication de produits alimentaires extrudés
CN101156632B (zh) 2007-10-19 2010-04-21 扬州大学 再制大豆干酪制品的加工方法
US8304522B2 (en) * 2007-11-08 2012-11-06 Fuji Oil Company, Limited Soy protein gel and method of producing the same
DE102007061256A1 (de) 2007-12-19 2009-06-25 Katrin Von Oppenkowski Verfahren zur Herstellung einer pflanzlichen Substanz sowie derartige Substanz und deren Verwendung
JP2009171877A (ja) 2008-01-23 2009-08-06 Toshio Sasaki 純植物性チーズ様食品の製造法
EP2274015A2 (fr) 2008-04-11 2011-01-19 SemBioSys Genetics Inc. Libération contrôlée d agents actifs à partir d oléosomes
MX2010011104A (es) 2008-04-11 2011-02-15 Sembiosys Genetics Inc Preparaciones estabilizadas de oleosoma y metodos para elaborarlas.
US20090264520A1 (en) 2008-04-21 2009-10-22 Asha Lipid Sciences, Inc. Lipid-containing compositions and methods of use thereof
EP2277932B1 (fr) 2008-05-14 2018-01-10 Nippon Shokubai Co., Ltd. Procédé pour la fabrication d'un copolymère d'acide polycarboxylique et composition de copolymère pour adjuvant de ciment
ES2534888T3 (es) 2008-06-26 2015-04-29 Emsland-Stärke GmbH Imitación de queso
US8188415B2 (en) 2008-10-24 2012-05-29 Emcore Solar Power, Inc. Terrestrial solar tracking photovoltaic array
US20100196575A1 (en) 2009-01-30 2010-08-05 Solae, Llc Melting Vegetable Protein Based Substitute Cheese
US20110288389A9 (en) 2009-03-02 2011-11-24 Seventh Sense Biosystems, Inc. Oxygen sensor
US20100233347A1 (en) 2009-03-13 2010-09-16 Uhrhan Richard B Food compositions having a realistic meat-like appearance, feel, and texture
WO2010129724A2 (fr) * 2009-05-05 2010-11-11 Anne Schwartz Système de fractionnement de biomasse efficace pour des cultures de légumes secs énergétiques
US20100310738A1 (en) 2009-06-04 2010-12-09 Wti, Inc. Method of processing meat
JP5271827B2 (ja) 2009-06-19 2013-08-21 ハウス食品株式会社 チーズ様食品組成物及びその製造方法
CN101606574B (zh) * 2009-07-14 2011-09-07 中国农业大学 天然高铁蛋白粉及其制备方法
US20110064862A1 (en) 2009-09-11 2011-03-17 Dean Intellectual Property Services, Inc. Non-Dairy, Nut-Based Milk and Method of Production
CN101861895B (zh) 2010-04-06 2012-05-30 扬州大学 一种发酵豆乳制品的制备方法
JP2012016336A (ja) 2010-07-09 2012-01-26 Ekoopasu Laboratories:Kk ヘム鉄含有食品素材およびその製造方法
US20120093994A1 (en) 2010-10-13 2012-04-19 The Curators Of The University Of Missouri Meat Analog Compositions and Process
DE202011002097U1 (de) 2011-01-28 2011-03-24 Tofutown.Com Gmbh pflanzliche Frischcreme
BR112013020001A2 (pt) 2011-02-07 2016-08-09 Commw Scient Ind Res Org corpo de óleo artificial, uso de um ou mais corpos de óleo artificiais, método para produzir corpos de óleo artificiais e método de parcialmente purificar oleosina à partir de um extrato de planta
GB201102557D0 (en) 2011-02-14 2011-03-30 Univ Nottingham Oil bodies
US9491958B2 (en) 2011-03-01 2016-11-15 Kobenhavns Universitet Process for the manufacture of a product from a plant material
WO2013013292A1 (fr) 2011-05-12 2013-01-31 University Of Guelph Produits de type fromage et de type yaourt à base de soja/lait et procédé de fabrication
CN102835460B (zh) 2011-06-21 2014-06-04 光明乳业股份有限公司 一种涂抹干酪模拟物及其制备方法
US20130004617A1 (en) 2011-07-01 2013-01-03 Pepsico, Inc. Coacervate complexes, methods and food products
CN110742128A (zh) 2011-07-12 2020-02-04 非凡食品有限公司 用于消费品的方法和组合物
KR20230022455A (ko) 2011-07-12 2023-02-15 임파서블 푸즈 인크. 소비재를 위한 방법 및 조성물
CN102440302B (zh) 2011-11-11 2013-03-20 华东理工大学 一种涂抹型大豆干酪及其制作方法
CN102578544A (zh) 2012-03-06 2012-07-18 李连成 一种调味品及其制备方法和使用方法
EP2825694A4 (fr) 2012-03-16 2016-04-20 Impossible Foods Inc Réactifs d'affinité pour la purification de protéines
EP3513664A1 (fr) 2013-01-11 2019-07-24 Impossible Foods Inc. Procédé de production d'un produit non-laitier fermenté et aromatisé
WO2015127388A1 (fr) 2014-02-21 2015-08-27 Impossible Foods Inc. Fromage à base de soja
US20150296834A1 (en) 2014-04-17 2015-10-22 Savage River, Inc. dba Beyond Meat, Inc. Plant based meat structured protein products
US9526267B2 (en) 2014-04-17 2016-12-27 Savage River, Inc. Nutrient-dense meat structured protein products

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20060035006A1 (en) * 2004-08-16 2006-02-16 Mcmindes Matthew K Restructured meat product and process for preparing same
EP1759593A1 (fr) * 2005-09-06 2007-03-07 Nug Nahrungs-Und Genussmittel Vertriebsgesellschaft Mbh Analogue de viande hachée et procédé de fabrication
US20100074998A1 (en) * 2006-11-01 2010-03-25 Alicia Espeleta Vega Meat Substitute Food Product And Process For Preparing The Same

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
Asgar et al., "Nonmeat Protein Alternatives as Meat Extenders and Meat Analogs". Comprehensive Reviews in Food Science and Food Safety. Vol. 9 (2010). *
Brewer., "Chemistry of Beef Flavor - Excutive Summary". Available online at www.beefresearch.org in 2006. *
Lombardi et al., "Total Heme and NOn-Heme Iron in Raw adn Cooked Meats". Journal of Food Science, Vol. 67, Nr. 5, pp. 1738-1741. (2002) *
Proulx et al., "Iron Bioavailability of Hemoglobin from Soy Root Nodules Using a Caco-2 Cell Culture Model'. Journal Agricultural Food Chem, 54, 1518-1522 (2006). *

Cited By (25)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3628173A1 (fr) 2014-03-31 2020-04-01 Impossible Foods Inc. Répliques de viande hachée
US11819041B2 (en) 2014-03-31 2023-11-21 Impossible Foods Inc. Ground meat replicas
US9526267B2 (en) 2014-04-17 2016-12-27 Savage River, Inc. Nutrient-dense meat structured protein products
US12054515B2 (en) 2015-03-24 2024-08-06 Cargill, Incorporated Corn protein isolate and methods of manufacturing same
US11019836B2 (en) 2015-08-03 2021-06-01 Savage River, Inc. Food products comprising cell wall material
WO2017165756A1 (fr) * 2016-03-24 2017-09-28 Cargill, Incorporated Concentré de protéine de maïs et ses procédés de fabrication
US11375736B2 (en) 2016-03-24 2022-07-05 Cargill, Incorporated Corn protein product having decreased free sulfite levels and method for manufacturing same
USD805728S1 (en) 2016-09-06 2017-12-26 Mars, Incorporated Food product
USD806351S1 (en) 2016-09-06 2018-01-02 Mars, Incorporated Food product
US11985990B2 (en) 2016-09-23 2024-05-21 Cargill, Incorporated Corn protein retention during extraction
WO2018097887A1 (fr) 2016-11-22 2018-05-31 Sisney Gary Procédé de traitement de la viande
EP3544439A4 (fr) * 2016-11-22 2020-06-17 Avure Technologies Incorporated Procédé de traitement de la viande
US11992033B2 (en) 2017-01-27 2024-05-28 Mars, Incorporated Pet food
US11980217B2 (en) 2017-08-02 2024-05-14 Cargill, Incorporated Extruded corn protein material
US11667670B2 (en) 2017-09-21 2023-06-06 Cargill, Incorporated Corn protein retention during extraction
US11561201B2 (en) * 2017-10-31 2023-01-24 Universidad De La Republica Device and method for determining the elasticity of soft-solids
US11779033B2 (en) 2018-08-07 2023-10-10 Novameat Tech, S.L. Process of manufacturing edible microextruded product comprising protein,composition thereby obtained and the use thereof
CN112839522A (zh) * 2018-08-07 2021-05-25 诺瓦曼特技术有限公司 包含蛋白质的可食用微挤出产品的制造方法、由此获得的组合物及其用途
WO2022072846A2 (fr) 2020-10-02 2022-04-07 Impossible Foods Inc. Plantes transgéniques ayant des profils d'acides gras modifiés et une biosynthèse d'hème régulée à la hausse
WO2022072833A2 (fr) 2020-10-02 2022-04-07 Impossible Foods Inc. Constructions d'expression et méthodes de modification génétique de cellules
WO2022165164A1 (fr) 2021-01-28 2022-08-04 Epogee, Llc Viandes d'imitation à base de plantes avec des liants pour produits alimentaires à base de plantes
WO2022187736A1 (fr) * 2021-03-05 2022-09-09 Motif Foodworks, Inc. Formulation de substitut de viande
WO2022251166A3 (fr) * 2021-05-25 2023-01-05 Evelo Biosciences, Inc. Compositions bactériennes comprenant de l'hémoglobine de soja
US11771112B2 (en) 2021-10-19 2023-10-03 Eat Scifi Inc. Plant base/animal cell hybrid meat substitute
WO2024026348A1 (fr) * 2022-07-28 2024-02-01 Pioneer Hi-Bred International, Inc. Production de leghémoglobine végétale

Also Published As

Publication number Publication date
AU2023203720A1 (en) 2023-07-13
EP2731446A1 (fr) 2014-05-21
AU2021200365A1 (en) 2021-03-18
CA3083009A1 (fr) 2013-01-17
RU2014104812A (ru) 2015-08-27
WO2013010042A1 (fr) 2013-01-17
MX2019002513A (es) 2019-06-17
AU2016231499B2 (en) 2018-08-02
EP2731446A4 (fr) 2015-04-15
JP2023116683A (ja) 2023-08-22
US20220071250A1 (en) 2022-03-10
KR20210095240A (ko) 2021-07-30
JP6930951B2 (ja) 2021-09-01
MX2021013278A (es) 2021-11-17
AU2018256629A1 (en) 2018-11-22
CN103889243A (zh) 2014-06-25
AU2012281069A1 (en) 2014-02-13
RU2018112565A3 (fr) 2021-08-05
MX2014000469A (es) 2014-10-17
CA2841473C (fr) 2020-08-11
RU2018112565A (ru) 2019-02-28
US20170290363A1 (en) 2017-10-12
JP2019010105A (ja) 2019-01-24
AU2012281069A2 (en) 2014-04-24
KR20190143492A (ko) 2019-12-30
BR112014000614A2 (pt) 2017-07-11
US9808029B2 (en) 2017-11-07
KR20140047125A (ko) 2014-04-21
AU2021200365B2 (en) 2023-03-16
RU2653751C2 (ru) 2018-05-14
AU2018256629B2 (en) 2020-10-22
KR20230022455A (ko) 2023-02-15
CN105724726A (zh) 2016-07-06
CA2841473A1 (fr) 2013-01-17
MX2022008149A (es) 2022-08-11
CN112471322A (zh) 2021-03-12
JP7297825B2 (ja) 2023-06-26
KR102254531B1 (ko) 2021-05-20
KR102024952B1 (ko) 2019-09-26
US20150289541A1 (en) 2015-10-15
JP2014520554A (ja) 2014-08-25
MX2021000079A (es) 2021-04-12
KR20190059986A (ko) 2019-05-31
AU2016231499A1 (en) 2016-10-06
JP2021184737A (ja) 2021-12-09
KR102283514B1 (ko) 2021-07-29
US20190008192A1 (en) 2019-01-10
JP6650671B2 (ja) 2020-02-19
AU2012281069B2 (en) 2016-10-13

Similar Documents

Publication Publication Date Title
US20220071250A1 (en) Methods and compositions for consumables
US20210289824A1 (en) Methods and compositions for consumables
AU2018200726B2 (en) Methods and compositions for consumables
RU2772991C2 (ru) Копирующие мясо пищевые продукты

Legal Events

Date Code Title Description
AS Assignment

Owner name: MARAXI, INC., CALIFORNIA

Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNORS:BROWN, PATRICK O'REILLY;VRLJIC, MARIJA;VARADAN, RANJANI;AND OTHERS;REEL/FRAME:032734/0598

Effective date: 20140109

Owner name: IMPOSSIBLE FOODS INC., CALIFORNIA

Free format text: CHANGE OF NAME;ASSIGNOR:MARAXI, INC.;REEL/FRAME:032742/0795

Effective date: 20140416

STCB Information on status: application discontinuation

Free format text: ABANDONED -- FAILURE TO RESPOND TO AN OFFICE ACTION