METHODS AND COMPOSITIONS FOR CONSUMABLES

Abstract

This paper describes methods and compositions for the production of non-meat consumable products. It describes a meat substitute constructed from a muscle analogue, a fat analogue, and a connective tissue analogue.

Description

This application claims priority to United States Patent Application Serial Number 13 / 941,211, filed July 12, 2013, to United States Patent Application Serial Number 61 / 908,634, filed on November 25, 2013, and for United States Patent Application with Serial Number 61 / 751,816, filed on January 11, 2013; and relates to the following co-pending patent applications: Application Serial Number PCT / US12 / 46560; Application with Serial Number PCT / US12 / 46552; Application with Serial Number 61,876,676, filed on September 11, 2013; Application with Serial Number 61 / 751,818, filed on January 11, 2013, and Application with Serial Number 61 / 61 1,999, filed on March 16, 2012, all of which are incorporated herein by reference. TECHNICAL FIELD This invention relates to consumable products and more particularly, to non-animal-based replicas of food products of animal origin, which can be produced, in some embodiments, by breaking down non-animal materials into their constituent parts and reassembling said parts. parts to form the consumables. QQCI BACKGROUND OF THE INVENTION Animal farming has a profound negative environmental impact. It is currently estimated that 30 percent of the Earth's land surface is dedicated to animal husbandry and that these livestock account for 20 percent of the total biomass of terrestrial animals. Because of this massive scale, livestock farming accounts for more than 18 percent 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 biggest threat to biodiversity. It has been estimated that if the world's human population switched from a diet containing meat to a diet free of animal products, 26 percent of the Earth's land surface would be freed up for other uses. Additionally, switching to a vegetarian diet would massively reduce water and energy consumption. Meat consumption has a profound negative impact on human health. The health benefits of a vegetarian diet are well established. If the human population shifted to a more vegetarian diet, there would be a decrease in health costs. Hunger is a problem throughout the world; However, the world's 4 major commodity crops (soybean, corn, wheat and rice) provide more than 100 percent of the calorie and protein needs of the human population, including all essential amino acids. QQCI I n / l 7Π7 / Κ / ΥΙΛΙ Plant-based meat substitutes have largely failed to spark a shift to a vegetarian diet. The current state of the art of meat substitute compositions involves extrusion of the soy / wheat mixture, resulting in products that largely fail to replicate the experience of cooking and eating meat. Common limitations of these products are a texture and mouthfeel that are more homogeneous than those of equivalent meat products. Additionally, because products must largely be sold pre-cooked, with artificial flavors and aromas included, they fail to replicate the aromas, flavors, and other key characteristics associated with cooking meat. As a result, these products primarily appeal to a limited consumer base already committed to vegetarianism / veganism, but have failed to appeal to the larger consumer segment accustomed to eating meat. Food is any substance that is either eaten or drunk by any animal, including humans, for nutrition or pleasure. It is usually of plant or animal origin, and contains essential nutrients, such as carbohydrates, fats, proteins, vitamins or minerals. The substance is ingested by an organism and assimilated by the organism's cells, in an effort to produce energy, sustain life, or stimulate growth. Food typically originates from a photosynthetic organism, typically from plants. Some foods are obtained directly from plants; But even animals that are used as food sources are raised by feeding foods derived from plants. Edible fungi and bacteria are used to transform plant or animal materials into other food products, mushrooms, bread, yogurt and the like. In most cases, the plant or animal is divided into a variety of different portions, depending on the purpose of the meal. Often, certain parts of the plant, such as seeds or fruits, are highly valued more than others by humans and these are selected for human consumption, while other less desirable parts, such as the stems of herbs, are They are typically used for animal feed. Animals are typically divided into smaller cuts of meat with specific flavor and handling properties before consumption. While many foods can be eaten raw, many also go through some form of preparation for reasons of safety, palatability, texture or flavor. At the simplest level, this may involve washing, cutting, trimming, or adding other foods or ingredients. It may also involve mixing, heating or cooling, or fermentation, and individual foods may be combined with other food products to achieve the desired combination of properties. In recent years, attempts have been made to bring scientific rigor to the food preparation process, under the fields of food science and molecular gastronomy. Food science broadly studies the safety, microbiology, preservation, chemistry, engineering and physics of food preparation, while molecular gastronomy focuses on the use of scientific tools such as liquid nitrogen, emulsifying agents such as lecithin soy, and gelling agents such as calcium alginates, to transform food products into unexpected shapes. However, the raw material is typically a complete organism (plant or animal) or an isolated tissue such as a steak, the fruiting body of a mushroom, or the seed of a plant. In some cases, the isolated tissue is modified before food preparation, such as by making flour or isolating oils and bulk proteins from seeds. Despite the fact that all of these elements comprise a mixture of proteins, carbohydrates, fats, vitamins and minerals, the physical arrangement of these elements in the original plant or animal determines the use to which the plant or animal tissue will be put. . Improved methods and compositions for the production of consumables are disclosed herein. BRIEF DESCRIPTION OF THE INVENTION Consumable products and methods for their production are provided herein. Consumables can be non-animal-based consumer goods, for example, that QQCI I n / l Znz / R / ΥΙΛΙ contain proteins and / or fats based mainly on plants or entirely on plants, and may be in the form of a beverage (for example, an alcoholic beverage, such as cream liqueur, or protein), a protein supplement, a baked product (e.g., a bread or cookie), a condiment (e.g., mayonnaise, mustard), a meat product, or a meat substitute product (e.g. , a ground beef product). For example, the protein drink may be a meal replacement drink, a beer supplemental with the protein, or a distilled alcoholic beverage (e.g., vodka or rum) supplemental with the protein. The condiment can be mayonnaise. The meat product may be a pate, a sausage, or a meat substitute that may include a replica of muscle, plant-based fat and / or connective tissue. Coacervates that include one or more proteins can be used to help ingredients bond together in consumable products (for example, a ground beef product). Accordingly, provided herein is a consumable product comprising an isolated and purified plant protein, wherein the isolated and purified plant protein has (i) a solubility in solution of at least 25 grams / liter at a temperature between about 2°C and about 32°C, where the solution has a pH between 3 and 8, and has a sodium chloride content of 0 to 300 mM, or (ii) a solubility in a solution of at least 1 m i I i g ram o / m i I i I i t ro to a QQCI I n / l 7Π7 / Ε / ΥΙΛΙ temperature between 90°C and 110°C, where the solution has a pH between 5 and 8 and has a sodium chloride content of 0 to 300 mM. In some embodiments, the consumable product is a beverage, protein supplement, baked product, condiment, meat product, or meat substitute product. In some embodiments, the beverage is an alcoholic beverage or a protein drink. In some embodiments, the alcoholic beverage is a cream liqueur. The cream liquor may further include a non-dairy lipid emulsion, wherein the cream liquor is free of animal products. In some embodiments, the protein drink is a meal replacement drink, a protein-supplemented beer, or a protein-supplemented distilled alcoholic beverage. A condiment can be a replica of mayonnaise. In some embodiments, the meat product may be a pâté, a sausage replica, or a meat substitute. In some embodiments, the isolated and purified plant protein is at least 10 kDa in size. In some embodiments, the isolated and purified plant protein is not completely denatured. In some cases, the isolated and purified plant protein is not derived from soybeans. In some embodiments, the isolated and purified plant protein comprises one or more of RuBisCo, Mung Globulin 8S, a pea globulin, a pea albumin, a lentil protein, zein, or an oleosin. In some embodiments, the isolated plant protein and Purified QQCI I n / l 7Π7 / Β / ΥΙΛΙ comprises a dehydrin, a hydrophilin, an intrinsically disordered protein, or a protein identified on the basis of its ability to remain soluble after boiling at a pH and salt concentration comparable to those of a food In some embodiments, the consumable product further comprises a plant-derived lipid or a microbial-derived lipid. In some embodiments, the consumable product further includes a second isolated and purified protein, and / or a seasoning agent, flavoring agent, emulsifier, gelling agent, sugar, or fiber. The disclosure also provides a consumable product comprising a coacervate comprising one or more isolated and purified proteins. In some embodiments, the consumable product is a replica of meat. In some embodiments, the consumable product further includes a plant-derived lipid or a microbial-derived lipid. The plant-derived lipid or the microbial-derived lipid may comprise lecithin and / or an oil. The product may include up to about 1 percent lecithin by weight. The product may include lecithin and oil. In some embodiments, the oil is cannon oil, palm oil, or cocoa butter. The product may include from about 1 percent to about 9 percent oil. The isolated and purified protein(s) may comprise plant proteins. The proteins from one or more plants may comprise one or more pea proteins, QQCI I n / l 7Π7 / Ε / ΥΙΛΙ chickpea, lentil proteins, lupine proteins, other legume proteins, or mixtures thereof. In some embodiments, the pea protein(s) are casein, vicilin, convicilin, or a mixture thereof. The disclosure also provides a meat replica comprising a muscle replica, a connective tissue replica, an adipose tissue replica, and a coacervate comprising one or more isolated and purified proteins. The coacervate can further comprise a lipid derived from plants or a lipid derived from microbes. The plant-derived lipid or a microbial-derived lipid may be lecithin and / or an oil. The meat replica may be a ground meat replica. Also provided is a consumable product comprising a cold-fixing gel comprising one or more proteins isolated and purified from a non-animal source and a salt. In some embodiments, the isolated and purified plant protein comprises one or more of RuBisCo, 8S mung globulin, a pea globulin, a pea albumin, a lentil protein, zein, or an oleosin. In some embodiments, the isolated and purified plant protein comprises a dehydrin, a hydrophilin, or an intrinsically disordered protein. In some embodiments, the cold-set gel further comprises a plant-derived lipid or a microbial-derived lipid. In some embodiments, the plant-derived lipid or microbial-derived lipid is lecithin and / or oil. QQCI I n / l 7Π7 / Β / ΥΙΛΙ The disclosure further provides an adipose tissue replica comprising one or more isolated plant proteins, one or more oils derived from plants or algae, and optionally a phospholipid. In some embodiments, the phospholipid is lecithin. In some embodiments, the vegetable oils are selected from the group consisting of corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil. , rapeseed oil, canola oil, saffron oil, sunflower oil, linseed oil, palm oil, palm seed oil, coconut oil, babassu oil, shea butter, mango butter, ghee cocoa, wheat germ oil, rice bran oil, and combinations thereof. In some embodiments, the fat release temperature of the adipose tissue replica is 23°C to 33°C, 34°C to 44°C, 45°C to 55°C, 56°C to 66 °C, from 67°C to 77°C, from 78°C to 88°C, from 89°C to 99°C, from 100°C to 110°C, from 111°C to 121°C, from 122 °C to 132°C, from 133°C to 143°C, from 144°C to 154°C, from 155°C to 165°C, from 166°C to 167°C, from 168°C to 169 °C, from 170°C to 180°C, from 181°C to 191°C, from 192°C to 202°C, from 203°C to 213°C, from 214°C to 224°C, from 225 °C to 235°C, from 236°C to 246°C, from 247°C to 257°C, from 258°C to 268°C, from 269°C to 279°C, from 280°C to 290° C, or from 291°C to 301°C. In some embodiments, the percentage of fat release from the adipose tissue replica is 0 to 10 percent, 10 percent to 20 percent, 20 percent to 30 percent, 30 percent to 40 percent , from 40 percent to 50 percent, from 50 percent to 60 percent, from 60 percent to 70 percent, from 70 percent to 80 percent, from 80 percent to 90 percent, or from 90 percent percent to 100 percent at the time of cooking. In some embodiments, the isolated and purified plant protein comprises one or more of RuBisCo, 8S mung globulin, a pea globulin, a pea albumin, a lentil protein, zein, or an oleosin. In some embodiments, the adipose tissue replica comprises from about 40 percent to about 90 percent of the oil. In some embodiments, the adipose tissue replica comprises from about 1 percent to about 6 percent of the isolated and purified plant protein. In some embodiments, the adipose tissue replica comprises from about 0.05 to about 2 percent of the phospholipid. In some embodiments, the firmness of the adipose tissue replica is similar to that of beef adipose tissue. Also provided is a consumable product comprising a heme-containing protein and (i) carbon monoxide and / or (i) a nitrite, wherein the consumable product does not comprise meat. In some embodiments, the heme-containing protein represents at least 0.01 percent of the composition. In some embodiments, the consumable product further comprises one or more ammonium, sodium, potassium, or calcium salts. In some embodiments, the isolated and purified proteins are cross-linked. Further provided is a consumable product comprising a gelled emulsion, wherein the gelled emulsion comprises: a) an isolated and purified protein; b) a first lipid that when not in the consumable product is solid in a selected temperature range; and c) a second lipid that when not in the consumable product is liquid in a selected temperature range; wherein the melting temperature of the mixture of the first and second lipids is similar to the melting temperature of the lipids present in meat, and wherein the first and second lipids are lipids derived from plants or lipids derived from microbes. The disclosure also provides a method for manufacturing a consumable product comprising: a) preparing a solution comprising an isolated and purified plant protein, wherein the isolated and purified plant protein has (i) a solubility in the solution of at least 25 at a temperature of between about 2°C and 32° C, wherein the solution has a pH of between 3 and 8, and has a sodium chloride content of 0 to 300 mM, or (i) a solubility in the solution of at least 1 milligram / milliliter at a temperature between 90°C and 110°C, where the solution has a pH of between 5 and 8, and has a sodium chloride content of 0 to 300 mM; and b) add the solution to a drink. QQCI I n / l 7Π7 / Κ / ΥΙΛΙ In some embodiments, the solution comprises two or more isolated and purified plant proteins. In some embodiments, the beverage is transparent. In some embodiments, the isolated and purified plant protein is at a concentration of at least 1 weight percent in the solution. In some embodiments, the isolated and purified plant protein is selected from the group consisting of RuBisCo, an 8S mung globulin, a soy globulin, a pea globulin, a pea albumin, a prolamin, a lentil protein , a dehydrin, a hydrophilin, and an intrinsically disordered protein. In some embodiments, the isolated and purified plant protein is lyophilized before making said solution. In some embodiments, the beverage has an improved mouthfeel compared to a corresponding beverage without the isolated and purified protein. Also provided is a method of extending the shelf life of a meat-free consumable product, the method comprising adding a heme-containing protein to the consumable product, wherein the heme-containing protein is oxidized more slowly than myoglobin under conditions of equivalent storage. In some embodiments, the heme-containing protein comprises an amino acid sequence with at least 70 percent homology to an amino acid sequence set forth in any of SEQ ID NOs: 1-27. Additionally, a method is provided to make a replica of QQCI I n / l 7Π7 / Β / ΥΙΛΙ meat comprising a cold fixation gel, wherein the method includes: a) denaturation of a solution comprising at least one protein isolated and purified from a non-animal source under conditions where the isolated and purified protein does not precipitate out of the solution; b) optionally adding any of the heat labile components to the denatured protein solution; c) gelling the denatured protein solution from about 4°C to about 25°C by increasing the ionic strength of the solution to form a cold fixation gel; and d) incorporate the cold fixation gel into a meat replica. In some embodiments, gelation is induced using 5 to 100 mM sodium or calcium chloride. In some embodiments, the thermolabile components are proteins or lipids, or mixtures thereof. In some embodiments, the protein is a heme-containing protein. In some embodiments, the cold-fix gel is formed in a matrix comprising a freeze-aligned plant protein. In some embodiments, the protein isolated and purified from a non-animal source is a plant protein. In some embodiments, the plant protein is selected from the group consisting of RuBisCo, a mung globulin, a QQCI I n / l 7Π7 / Κ / ΥΙΛΙ soy, a pea globulin, a pea albumin, a prolamin, a lentil protein, a dehydrin, a hydrophilin, and an intrinsically disordered protein. A replica of adipose tissue is also provided, which comprises a) an isolated and purified non-animal protein; b) a non-animal lipid; and c) a three-dimensional matrix comprising fibers obtained from non-animal sources, where the lipid and protein are dispersed in the three-dimensional matrix, and where the three-dimensional matrix stabilizes the structure of the adipose tissue replica. Also provided is a connective tissue replica comprising one or more isolated and purified proteins assembled into fibrous structures by a solution centrifugation process. In some embodiments, the fibrous structures are stabilized by a cross-linking agent. Provided herein is a method of imparting a beef flavor to a consumable product, which comprises adding a heme-containing protein to the consumable composition, wherein, after cooking, a beef flavor is imparted. of beef to the consumable composition. Also provided is a method for making a beef-flavored poultry or fish composition, the method comprising adding a heme protein to the poultry or fish composition, respectively. QQCI I n / l Znz / R / YIAI In some embodiments, the heme-containing protein has an amino acid sequence with at least 70 percent homology to any one of the amino acid sequences set forth in SEQ ID NOs: 1-27. Additionally, a method is provided for the preparation of a coacervate, the method comprising: a) acidifying a solution of one or more plant proteins to a pH of between 3.5 and 5.5, wherein the solution comprises 100 mM or less of sodium chloride; and b) isolate the coacervate from the solution. In some embodiments, the pH is between 4 and 5. In some embodiments, the plant proteins comprise one or more pea proteins, chickpea proteins, lentil proteins, lupine proteins, other legume proteins, or mixtures thereof. In some embodiments, pea proteins comprise isolated and purified casein, isolated and purified vicilins, isolated and purified convicilins, or combinations thereof. In some embodiments, the isolated and purified pea proteins comprise isolated and purified vicilins and isolated and purified convicilins. In some embodiments, the acidification step is carried out in the presence of a plant-derived lipid or a microbial-derived lipid. In some embodiments, the plant-derived lipid or the microbial-derived lipid comprises oils and / or phospholipids. Provided herein is a method for making a QQCI I n / l 7Π7 / Ε / ΥΙΛΙ adipose tissue replica, the method comprising the formation of an emulsion comprising one or more isolated plant proteins, one or more oils derived from plants or algae, and, optionally, a phospholipid . In some embodiments, when the phospholipid is included, it is lecithin. In some embodiments, the vegetable oils are selected from the group consisting of corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil. , rapeseed oil, canola oil, saffron oil, sunflower oil, linseed oil, palm oil, palm seed oil, coconut oil, babassu oil, shea butter, mango butter, ghee cocoa, wheat germ oil, rice bran oil, and combinations thereof. In some embodiments, the fat release temperature of the adipose tissue replica is 23°C to 33°C, 34°C to 44°C, 45°C to 55°C, 56°C to 66°C. °C, from 67°C to 77°C, from 78°C to 88°C, from 89°C to 99°C, from 100°C to 110°C, from 111°C to 121°C, from 122 °C to 132°C, from 133°C to 143°C, from 144°C to 154°C, from 155°C to 165°C, from 166°C to 167°C, from 168°C to 169 °C, from 170°C to 180°C, from 181°C to 191°C, from 192°C to 202°C, from 203°C to 213°C, from 214°C to 224°C, from 225 °C to 235°C, from 236°C to 246°C, from 247°C to 257°C, from 258°C to 268°C, from 269°C to 279°C, from 280°C to 290° C, or from 291°C to 301°C. In some embodiments, the percentage of fat release from the adipose tissue replica is 0 to 10 percent, 10 percent to 20 percent, 20 percent to 30 percent. QQCI I n / l Znz / R / ΥΙΛΙ percent, 30 percent to 40 percent, 40 percent to 50 percent, 50 percent to 60 percent, 60 percent to 70 percent, 70 percent percent to 80 percent, 80 percent to 90 percent, or 90 percent to 100 percent cooking. In some embodiments, the isolated and purified plant protein comprises one or more of RuBisCo, 8S mung globulin, a pea globulin, a pea albumin, a lentil protein, zein, or an oleosin. In some embodiments, the emulsion comprises from about 40 percent to about 90 percent of the oil. In some embodiments, the emulsion comprises from about 1 percent to about 4 percent of the isolated and purified plant protein. In some embodiments, the adipose tissue replica comprises from about 0.05 to about 1 percent of the phospholipid. In some embodiments, the emulsion is formed by high pressure homogenization, sonication, or manual homogenization. Additionally provided is a method for minimizing undesirable odors or flavors in a composition comprising plant proteins, the method comprising contacting the composition with a ligand having affinity for one or more lipoxygenases. Also provided is a method for minimizing undesirable odors or flavors in a composition comprising plant proteins, the method comprising contacting the composition with activated carbon and then removing the activated carbon from the composition. Also provided is a method for minimizing undesirable odors or flavors in a composition comprising plant proteins, the method comprising adding to the composition a lipoxygenase inhibitor and / or an antioxidant. The disclosure further provides a chocolate flavored spread comprising: a) sugar, b) a chocolate flavoring, and c) a plant-based milk cream fraction. Provided herein is a method for altering the texture of a consumable during or after cooking, which comprises incorporating into the consumable one or more plant proteins at a low denaturation temperature. In some embodiments, at least one of the one or more plant proteins is isolated and purified. In some embodiments, the one or more plant proteins are selected from the group consisting of RuBisCo, pea proteins, lentil proteins, or other legume proteins. In some embodiments, the pea proteins comprise pea albumin proteins. In some embodiments, the consumable becomes firmer during or after cooking. A tissue replica is also provided, which comprises a freeze-aligned non-animal protein. In QQCI I n / l 7Π7 / Ε / ΥΙΛΙ In some embodiments, the non-animal protein is a plant protein. In some embodiments, the non-animal protein is isolated and purified. In some embodiments, the tissue replica is a muscle tissue replica. The disclosure also provides a meat replica that includes a tissue replica comprising a freeze aligned non-animal protein. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. Although methods and materials similar or equivalent to those described herein may be used to practice the invention, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, it will be controlled with this specification, including the definitions. Furthermore, the materials, methods, and examples are illustrative only and are not intended to be limiting. Details of one or more embodiments of the invention are set forth in the accompanying drawings and in the following description. Other features, objects and advantages of the invention will be apparent from the description and drawings, and from the claims. The word included in the claims may be replaced by "consisting essentially of" or with "consisting of", in accordance with conventional practice in patent law. DESCRIPTION OF THE DRAWINGS Figure 1 contains amino acid sequences of example heme-containing proteins. Figure 2 A is a bar graph representing the percentage of fat release based on the amount of lecithin. Figure 2B is a bar graph representing the temperature of fat release based on the amount of lecithin. Figure 2C is a bar graph representing the firmness of adipose tissue replicas based on the amount of lecithin. Figure 3 is a bar graph representing the percentage of fat release from adipose tissue replicas containing different oils (canola oil, cocoa butter, coconut oil, or rice bran oil). Figure 4 is a bar graph representing the fat release temperature of adipose tissue replicas containing different oils (canola oil, cocoa butter, coconut oil, or rice bran oil). DETAILED DESCRIPTION OF THE INVENTION I. Consumables Methods and compositions for QQCI I n / l 7Π7 / Ε / ΥΙΛΙ produce consumables. In some cases, consumables are non-animal based replicas of animal-derived food products that can be produced by breaking down non-animal materials into their constituent parts and reassembling those parts to form consumables. In certain cases, consumables are not intended to replicate a food of animal origin and instead have their own unique characteristics desirable as a food. Additionally, consumables can, in some cases, act as nutraceuticals or carriers for pharmaceutical compositions rather than serving a primary function as food. Advantages of the consumables described herein may include, for example, using less energy or water in the production of the consumable compared to similar food products, using no animals in the production of the consumable, making for a healthier product. , using raw materials that would otherwise go to waste, or allowing the removal (or lack of incorporation) of certain components (eg allergens) from consumables. Consumables can also have a higher degree of consistent production, allowing for better quality control of products. Another advantage is that consumables can be intentionally designed to have desirable characteristics for food preparation that are superior to traditional food products. The consumables may be for animal consumption, including human consumption. The consumables can be food for domestic animals (for example, dog food could be produced in accordance with the present invention) or for wild animals (for example, food for non-domesticated predatory animals). Consumables can be sold similar to existing human foods in grocery stores, convenience stores, wholesalers, and club stores, or can be prepared in restaurants, including fast food restaurants, schools, event venues, hospitals, military installations, prisons, shelters, or long-term care facilities. The consumable may be approved by the appropriate regulatory authorities. For example, the consumable could be prepared to be suitable for the U.S. Food and Drug Administration. The methods of the invention may include measures necessary to satisfy regulatory agencies. The consumables of the present invention can replicate, compete with, complement or replace conventional food products (referred to herein as food products). Food products can be any food that currently exists. The consumables of the invention can be made to replicate food products, for example, an equivalent meat product. The equivalent meat product may 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 make the equivalent meat product include animals such as, for example, beef, sheep, pork, chicken, turkey, goose, duck, horse, dog, or game (whether wild or farm-raised). ), such as, for example, rabbit, deer, bison, buffalo, wild boar, snake, pheasant, quail, bear, moose, antelope, pigeon, turtle dove, wild bird, fox, wild boar, goat, kangaroo, emu, crocodile, turtle , prairie dog, marmot, opossum, partridge, squirrel, raccoon, whale, seal, ostrich, capybara, otter, guinea pig, rat, mouse, field mouse, any variety of insects or other arthropods, or fish and shellfish such as, for example, fish, crab, lobster, oysters, mussels, scallops, abalone, squid, octopus, sea urchin, tunicates and others. Many meat products are typically derived from the skeletal muscle of an animal, but it is understood that meat can also come from other muscles or organs of the animal. In some embodiments, the equivalent meat product is a cut of meat derived from skeletal muscle. In other embodiments, the equivalent meat product is an organ such as, for example, kidney, heart, liver, gallbladder, intestine, stomach, bone marrow, brain, thymus, lung, or tongue. Accordingly, in some embodiments, the compositions of the present invention are similar to skeletal muscle or organ consumables. A consumable (e.g., a meat substitute) may comprise one or more of a first composition comprising a replica of muscle tissue, a second composition comprising a replica of adipose tissue, and / or a third composition comprising a replica of connective tissue, where one or more compositions are combined in a way that recapitulates the physical organization of meat. The present invention also provides distinct compositions for a muscle tissue replica (herein referred to as a muscle replica), an adipose tissue replica (herein referred to as an adipose tissue replica or fat replica), and a connective tissue (herein referred to as connective tissue replica). In some embodiments, these compositions are composed primarily or entirely of ingredients derived from non-animal sources (e.g., 10 percent or less of the ingredients are from animal sources). In alternative embodiments, the muscle, fat and / or connective tissue replica, or meat substitute products comprising one or more of the replicas, are partially derived from animal sources, but supplemented with ingredients derived from non-animal sources. In some embodiments, as much as 90 percent of the food product is derived from animal sources. In some embodiments approximately 75 percent of the food product is derived from animal sources. In some embodiments, approximately 50 percent of the food product is derived from animal sources. In some embodiments approximately 10 percent of the food product is derived from animal sources. In still other alternative embodiments, the invention provides meat products substantially derived from animal sources (e.g., a beef, chicken, turkey, or pork product) that are complemented by one or more than one muscle tissue replica, a fat replica, and / or a connective tissue replica, wherein the 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 fat replica that improves texture and mouthfeel, while retaining the health benefits of a low consumption of animal fat. Such alternative modalities may result in products with properties that more closely recapitulate key characteristics associated with meat preparation and consumption, but are less expensive and associated with less environmental impact, less impact on animal welfare, or better health benefits for the consumer. Examples of other food products that the consumable can replicate or replace include: beverages (for example, cream or milk liqueur), protein drinks (for example, RuBisCo can be used as a protein supplement in beer, distilled spirits such as vodka, fruit juice, meal replacement drinks, or water), pasta (for example, Nutella™ replicas, cream, nacho cheese, or mayonnaise), pate, blood sausage, meat preservers, eggs, fish, sausage , chicken strips, canned ham, or refrigerated foods (for example, ice cream replicas, yogurt, kefir, sour cream, or butter). Consumables can be a replica of meat. Consumables can be made to mimic the cut or appearance of meat. For example, a consumer product may be visually similar to or indistinguishable from ground beef or a particular cut of beef. In an exemplary embodiment, the replicas are combined in a manner that approximates the physical organization of natural ground meat (e.g., ground beef, ground chicken, or ground turkey). In other embodiments, the replicas are combined in a manner that approximates different cuts of beef, such as, for example, rib-eye, filet mignon, London roast, among others. Alternatively, the consumables can be a made with a unique look and feel. For example, the consumable could contain patterns (for example, letters or images) that are formed from the structure of the consumable. In some cases, consumables resemble traditional food products after they are prepared. For example, a consumer product that can be produced, which is larger than a traditional cut of beef, but which, after the consumable is cut and cooked, resembles the same traditional cooked meat. In some embodiments the consumable may resemble a traditional form of a food product in two dimensions, but not in three. For example, the consumable may resemble a cut of meat in two dimensions (for example, when viewed from the top), but may be much longer (or thicker) than the traditional cut. In this example, the composition can be repeatedly cut into traditional meat-shaped products. Consumables can be made from local products. For example, consumables can be made from plants grown within a certain radius of the eventual consumer. That radius could be 1, 10, 100, or 1,000 kilometers for example. Therefore, in some embodiments, the invention provides a method for producing a consumable that does not contain products that have been shipped more than 1, 10, 100, or 1,000 kilometers. The present invention provides methods for producing consistent properties of consumables when produced from various sources. For example, a replica plant-based meat produced from local plants in Iowa, United States, will have substantially similar taste, odor, and texture as a replica plant-based meat produced from local plants in Lorraine. , France. This consistency allows for methods of advertising locally grown foods with consistent properties. Consistency may arise from the concentration or purification of similar components in different locations. These components can be combined in predetermined ratios to ensure consistency. In some embodiments, a high degree of characteristic consistency is possible using components (e.g., isolated or concentrated proteins and fats) that come from the same plant species. In some embodiments, a high degree of characteristic consistency is possible using components (e.g., isolated or concentrated proteins and fats) that come from different plant species. In some embodiments, the same proteins can be isolated from different plant species (i.e., homologous proteins). In some embodiments, the invention provides a method comprising isolating similar plant components from plant sources at different locations, assembling at both locations the compositions provided herein, and selling the compositions, wherein the compositions assembled and sold in different geographic locations have consistent physical and chemical properties. In some embodiments, the isolated constituents are from different plant populations in different locations. In some embodiments one or more of the isolated constituents are shipped to separate geographic locations. Consumables may require fewer resources to produce than consumables produced from domesticated animals. Accordingly, the present invention provides meat replicas that require less water or energy to produce than meat. For example, a consumable described herein may require less than about 10, 50, 100, 200, 300, 500 or 1,000 liters of water per kilogram of consumable. By comparison, beef production can require more than 2,000 gallons of water per kilogram of meat. The consumable may require less area to produce than a meat product of similar protein content. For example, a consumable described herein may require 30 percent 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 fat than comparable meat products. The American Heart Association and the National Cholesterol Education Program recommend limiting cholesterol intake from foods to 300 milligrams per day, which is equivalent to consuming 12 ounces of beef or two egg yolks. The consumables described herein that are indistinguishable from animal products such as ground meat, and that have a reduced or no cholesterol content, can help maintain a low cholesterol diet. In another example, a consumable described herein may contain no cholesterol, or higher levels of polyunsaturated fatty acids compared to the animal product it replaces. The consumable may have animal welfare benefits compared to an animal product it replaces in the diet. For example, it can occur without the need for confinement, force-feeding, early weaning, interruption of mother-infant interactions, or slaughter of animals for their meat. The consumable may have a smaller carbon footprint than the meat products it replaces. For example, consumption may result in net greenhouse gas emissions of 1 percent, 5 percent, 10 percent, 25 percent, 50 percent, or 75 percent of the attributable greenhouse gas emissions. to the product of animal origin that it replaces. As an example, according to the Environmental Working Group (2011), meat consumers lead to Climate and Health Change, meat production causes the emission of 27 kg carbon dioxide equivalent per kilogram of beef that is produced. consumes, and lamb production causes the emission of 39 kg carbon dioxide equivalent per kilogram of beef consumed. The consumable described herein may provide alternatives to animal products or combinations of animal products whose consumption is prohibited by religious beliefs. For example, the consumable might be a replica kosher pork chop. The consumable can also be shipped in components and produced or assembled at a different location. When this QQCI I n / l 7Π7 / Κ / ΥΙΛΙ available, local components can be used for the production of the consumable. Local components can be supplemented with components that are not available locally. This allows methods to produce consumables, for example meat replicas, using less energy in shipping than is required for the meat. For example, local water can be used in combination with a kit that provides other consumable components. Using local water reduces shipping weight, which reduces cost and environmental impact. The consumables described herein may be produced or assembled in whole or in part in areas where animal husbandry is not practical or permitted. The consumable can be produced or assembled within an urban environment. For example, a kit may be provided to a user to allow the user to produce the consumable. The user can use local water or use plants from a rooftop garden, for example in Shanghai. In another example, consumables could be produced aboard a spacecraft, space station, or a lunar base. Accordingly, the present invention provides methods and systems for the production of meat replicas for use in space travel or for the formation of meat. For example, the present invention could be used in ground-based training for space travel. Consumables could also be produced on an island or on an artificial platform in the sea, where livestock farming is difficult or prohibited. II. Consumable properties The consumables described herein are typically designed to replicate the experience of eating a food product, for example, meat. The appearance, texture and flavor of the consumable may be such that it is similar to, or indistinguishable from, a food product, for example, meat. The consumable can also be produced to have the desirable characteristics of the food products without incorporating other undesirable characteristics. For example, a consumer product may be a replica steak that does not have cartilage or other components that are not typically consumed in a predicate food product. The invention provides, in certain embodiments, methods for determining the suitability for a consumable to qualify as a replica of a food product, for example, by determining whether an animal or human can distinguish the consumable from a predicate food product, e.g. example, in particular, meat. One method of determining whether the consumable is comparable to a food product (e.g., meat) is to a) define the properties of the meat and b) determine if the consumable has similar properties. Properties that may be tested or used to compare or describe a food product or consumable include mechanical properties such as hardness, cohesiveness, brittleness, chewiness, gumminess, viscosity, elasticity, and adhesiveness. The properties of food products QQCI I n / l 7Π7 / Β / ΥΙΛΙ can also test include geometric properties such as the size and shape of the particles and the shape and orientation of the particles. The three-dimensional organization of the particles can also be tested. Additional properties may include moisture content and fat content. These properties can be described with terms such as soft, firm, or hard to describe hardness; crumbly, crunchy, brittle, chewy, tender, hard, short, mealy, doughy or rubbery, to describe cohesion; thin or slimy to describe viscosity; plastic or elastic to describe elasticity; sticky, tasteless or sticky to describe stickiness; sandy, granular or course to describe the shape and size of the particles; fibrous, cellular or crystalline to describe the shape and orientation of the particles, dry, moist, wet, or aqueous to describe the moisture content; or oily or greasy to describe the fat content. Accordingly, in one embodiment, a group of people may be asked to evaluate a certain food product, for example ground beef, according to properties that describe the food product. A consumable described herein may be qualified by the same people to determine equivalence. The taste of the food product can also be evaluated. Flavors can be classified according to the similarity of food products, for example, egg, fish, butter, chocolate, fruit, pepper, bacon, cream, milk, or meat. The QQCI I n / l 7Π7 / Β / ΥΙΛΙ flavors can be classified according to the seven basic flavors, that is, sweet, sour, bitter, salty, umami (salty), pungent (or spicy) and metallic. Flavors can be described according to the similarity to an experience caused by a chemical substance, for example, diacetyl (butter), 3-hydroxyl-2-butanone (butter), nona-2E-enal (fatty), 1-octene -3-ol (mushroom), hexanoic acid (sweaty), 4-hydroxy-5-methyl furanone (HMF, meaty), pyrazines (nutty), bis(2-methyl-3-f uryl) disulfide (roast ), decanone (moist / fruity), isoamyl acetate (banana), benzaldehyde (bitter almond), cinnamic aldehyde (cinnamon), ethyl propionate (fruity), methyl anthranilate (grape), limonene (orange), ethyl decadienoate (pear), allyl hexanoate (pineapple), ethyl maltol (sugar, cotton candy), ethiIvain11in (vanilla), butanoic acid (rancid), 1 2-methyltridecanal (round), or methyl salicylate (wintergreen). These ratings can be used as an indication of the properties of the food product. The consumables of the present invention can then be compared to the food product to determine how similar the consumable is to the food product. In some cases the properties of the consumables are then altered to make the consumable more similar to that of the food product. Accordingly, in some embodiments, the consumable has a classification similar to a food product according to human evaluation. In some embodiments the consumable is indistinguishable to a human from real meat. QQCI I n / l 7Π7 / Β / ΥΙΛΙ Consumables can be made to remove properties associated with the source of the consumable components. For example, a consumable can be made from components obtained from beans, but can be made to lack a bean flavor or texture. One way this can be accomplished is by breaking down the source materials of the components into isolated and purified components and not using the components that cause undesirable characteristic properties of the source. In addition, as described herein, off-flavors or aromas (eg, off-flavors or aromas) in isolated and / or purified components can be minimized by deodorization with activated carbon or by removal of enzymes such as lipoxygenases (LOX). , which may be present in trace amounts and which can convert unsaturated tri aci I g I i cerides (such as linoleic acid or linolenic acid) into smaller, more volatile molecules. LOX are naturally present in legumes such as peas, soy and peanuts, as well as rice, potatoes and olives. When legume flours are fractionated into separate protein fractions, LOX can act as undesirable time bombs that can cause off-flavors or aromas with aging or storage. As shown in Example 34, compositions containing plant proteins (for example, from soil plant seeds) can be subjected to purification to remove LOX using, for example, an affinity resin that binds to LOX. the LOX and removes them from the protein sample. The affinity resin can be linoleic acid, linolenic acid, stearic acid, oleic acid, propyl gallate, epigallocatechin gallate bound to a solid support such as a bead or resin. See, for example, Patent Application Number WO201 31 38793. In addition, depending on the protein component, certain combinations of antioxidants and / or LOX inhibitors may be used as effective agents to minimize off-taste or off-flavor generation. bad odor in protein solutions, especially in the presence of fats and oils. Such compounds may include, for example, one or more of β-carotene, o-tocopherol, caffeic acid, propyl gallate, or epigallocatechin gallate. These can be included during purification of the proteins or during subsequent food processing steps to mitigate the generation of off-flavors or off-odors in protein-based foods. In some compositions, subjects were asked to identify the identity of the consumable as a form of a food product, or as a particular food product, for example, a subject will identify the consumable as meat. For example, in some compositions a human will identify the consumable as having properties equivalent to meat. In some embodiments one or more properties of the consumable are equivalent to the corresponding properties of the meat according to the perception of a human being. Such properties QQCI I n / l 7Π7 / Ε / ΥΙΛΙ include the properties that can be tested. In some embodiments a human identifies a consumable of the present invention as more similar to meat than any meat substitute found in the art. Experiments can show that a consumable is acceptable to consumers. A panel can be used to detect a variety of consumables described herein. Multiple samples of consumables may be tested by various human panelists, namely, natural meats against the consumable compositions described herein, or a meat substitute against a consumable composition described herein. Variables such as fat content can be standardized, for example, to 20 percent fat using mixtures of lean and fat meat. Fat content can be determined by the Babcock method for meat (SS Nielson, Introduction to the Chemical Analysis of Foods (Jones & Bartlett Publishers, Boston, 1994)). Ground beef and consumable mixtures of the invention prepared in accordance with the procedure described herein can be formulated. Samples may be served to panelists (for example, in booths), under red lights or under white light, in an open consumer panel. Random three-digit numbers can be assigned to samples and rotated in voting position to avoid bias. Panelists may be asked to evaluate samples for tenderness, juiciness, texture, flavor, and overall acceptability using a hedonic scale from 1=extremely dislike, to 9=extremely like, with a mean of 5=neither like nor dislike. . Panelists may be encouraged to rinse their mouths with water between samples, and they may be given the opportunity to comment on each sample. The results of this experiment may indicate significant differences or similarities between traditional meats and the compositions of the invention. These results may demonstrate that the compositions described herein are judged to be acceptably equivalent to actual meat products. Furthermore, these results may demonstrate that the compositions described herein are preferred by panelists over other commercially available meat substitutes. Thus, in some embodiments, the present invention provides consumables that are similar to traditional meats and are more meat-like than previously known meat alternatives. The consumables of the invention may also have similar physical characteristics as food products, for example, traditional meat. In one embodiment, the force required to pierce a 1-inch thick structure (e.g., a hamburger) made of a consumable of the invention with a fixed diameter steel rod is not significantly different than the force required to pierce a structure of a similar food product with a thickness of 1 inch (for example, a QQCI I n / l 7Π7 / Ε / ΥΙΛΙ ground beef patty) with a similar fixed diameter steel rod. Accordingly, the invention provides consumables with characteristics similar to physical strength for meat. In another embodiment, the force necessary to tear a sample of the invention with a cross-sectional area of ​​100 mm2 is not significantly different from the force necessary to tear a sample of animal tissue (muscle, fat or connective tissue) with a cross section of 100 mm2measure in the same way. Force can be measured using, for example, TA.XT Plus Texture Analyzer (Texture Technologies Corp.). Accordingly, the invention provides consumables with similar physical strength characteristics to meat. The consumables described herein may have a cook loss characteristic similar to a food product, eg, meat. For example, a consumable may have a similar fat and protein content to ground beef and have the same reduction in size when cooked as actual ground beef. Similarities in size loss profiles can be achieved for various consumable compositions described herein tailored to different types of meats. The cooking loss characteristics of the consumable can also be designed to be superior to food products. For example a consumable can be produced to have less loss during cooking, but achieve similar tastes and texture qualities to cooked products. Form QQCI I n / l 7Π7 / Ε / ΥΙΛΙ where this is achieved is by altering the proportions of lipids based on melting temperatures in the consumable composition. Another way this is achieved is by altering the protein composition of the consumable by controlling the protein concentration or by the mechanism by which the tissue replica is formed. In some embodiments, the consumable is compared to an animal-based food product (e.g., meat) based on olfactometer readings. In various embodiments, the olfactometer can be used to evaluate odor concentration and odor thresholds, or odor over-threshold with respect to a reference gas, hedonic scale scores to determine the degree of appreciation, or the relative intensity of the smells. In some embodiments, the olfactometer allows for the automatic training and evaluation of panels of experts. Thus, in some embodiments, the consumable is a product that causes similar or identical olfactometer readings. In some modalities, the differences are small enough to be below the detection threshold of human perception. Gas chromatography mass spectrometry (GCMS) is a method that combines the features of gas 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 headspace around the meat. These chemicals can be identified using GCMS. This creates a profile of the volatile chemicals in the headspace around the meat. In some cases each GCMS peak can be evaluated. For example, a human might evaluate the experience of smelling the chemical responsible for a certain spike. This information could be used to refine the profile. The GCMS could then be used to evaluate the properties of the consumable. The GCMS profile can be used to refine the consumable. The characteristic flavor and fragrance components are produced primarily during the cooking process by the reactions of chemical molecules including amino acids, fats and sugars found in plants as well as meat. Therefore, in some embodiments, the consumable tested for similarity to meat during or after cooking. In some embodiments human grading, human evaluation, olfactometer readings, or GCMS measurements, or combinations thereof, are used to create an olfactory map of cooked meat. Similarly, an olfactory map of the consumable, eg a replica of meat, can be created. These maps can be compared to assess the similarity of consumables to cooked meat. In some embodiments the olfactory map of the consumable during or after cooking is similar or indistinguishable from that of cooked or cooking meat. In some modalities, the similarity is sufficient to be beyond the detection threshold of human perception. The consumable may be created so that its characteristics are similar to a food product after cooking, but the uncooked consumable may have properties that are different from the predicated food product before cooking. Shelf life is the period of time that a consumable is given before it is considered unfit for sale, use or consumption. In general, it is important to keep a meat product at approximately 2°C since shelf life decreases with exposure to higher temperatures. The shelf life of meat is determined through investigation of the sensory cues of meat products over time (odor, visual appearance of the package, color, flavor, and texture), and through laboratory analysis under controlled conditions to determine how long a product remains safe, healthy and enjoyable. Ground beef is being used as an example, but similar conditions would apply to steaks, chops, and roasts of other types of meat. Beef in its natural state is dark bluish-purple. However, oxygen can penetrate the meat and cause a chemical reaction with the myoglobin in the meat, leading to a red color. Continuous exposure to oxygen causes the oxidation of myoglobin and causes red meat to turn brown and develop unpleasant flavors. To control this oxidation, significant research has been done into different methods of storing and displaying meat products to increase the shelf life of meat products. These include the use of vacuum packaging, modified atmosphere packaging (high oxygen), modified atmosphere packaging (low oxygen with carbon monoxide), and / or high pressure pasteurization (HPP). The main determinant of meat color is the concentration of iron carried by proteins in the meat. In the skeletal muscle component of meat products, one of the main iron proteins is myoglobin. White chicken meat is estimated to have less than 0.05 percent myoglobin; pork and beef have 0.1 to 0.3 percent myoglobin; young beef has 0.4 to 1.0 percent myoglobin; and old beef has 1.5 to 2.0 percent myoglobin. Typically, meat myoglobin exists in three states: oxymyoglobin (Fe2+) (oxygenated = bright red); myoglobin (Fe2+) (non-oxygenated = purple / magenta); and metmyoglobin (Fe3+) (oxidized = brown). The transition from oxymyoglobin to metmyoglobin in the presence of oxygen is thought to be the cause of the color change of ground meat from red to brown, meat shelf life preservatives have been developed to extend the red color time in meat products. meat, including, but not limited to, carbon monoxide, nitrites, sodium metabisulfite, Bombal, vitamin E, rosemary extract, green tea extract, catechins and other antioxidants. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ However, an intrinsically more stable heme protein such as a hemoglobin isolated from Aquifex aeolicus (SEQ ID NO: 3) or Methylacidiphilum infernorum (SEQ ID NO: 2) is oxidized more slowly than a mesophilic hemoglobin such as myoglobin. The heme proteins described herein (see, for example, Figure 1) may also have the shelf life of the reduced heme-Fe2+ state extended by meat shelf life extenders, such as carbon monoxide and sodium nitrite. Heme proteins can be selected for the desired color retention properties. For example for low temperature sous vide cooking, a relatively unstable heme protein such as Hordeum vulgare can provide a brown product that appears cooked under conditions where the myoglobin would maintain its red appearance uncooked. In some embodiments, the heme protein may be selected to have greater stability where for example the meat replica may retain an attractive medium-rare appearance despite being well cooked for food safety. The primary determinant of rancidity and the production of off-flavors or odors is the oxidation of consumable components, including, but not limited to, fats. For example, the oxidation of unsaturated fatty acids is a known cause of musty odors. In some embodiments, replica meats have extended shelf life because the chemical composition of the replica meat is controlled in such a way that the flavor, texture, odor, and chemical properties do not react with oxygen to create strange flavors or odors. In some embodiments the meat replicas are less sensitive to oxidation due to the presence of a higher degree of unsaturated fatty acids than those present in beef. In some embodiments, the meat replica does not contain unsaturated fatty acids. In other embodiments, the meat replica contains higher levels of antioxidants such as glutathione, vitamin C, vitamin A, and vitamin E, as well as enzymes such as catalase, superoxide dismutase and various peroxidases that are present in the meat. meat. In other embodiments, foreign flavor or odor generating components such as lipoxygenase are not present. In some embodiments, a consumable described herein exhibits greater stability under commercial packaging conditions. In some embodiments, improved shelf life is improved by the use of components with greater oxidative stability such as lipids with reduced levels of unsaturated fatty acids, and / or by the use of a more stable heme protein such as hemoglobin isolated from Aquifex aeolicus. (SEQ ID NO: 3) or Methylacidiphilum infernorum (SEQ ID NO: 2). In some embodiments, the improved shelf life is due to the combination of components used in the consumable. In some embodiments, the consumable is specifically designed for the desired packaging method. III. Composition of consumables A consumable described herein includes one or more isolated and purified proteins. Isolated and purified protein refers to a preparation in which the cumulative mass abundance of protein components other than the specified protein, which may be a single species of monomeric or multimeric proteins, 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 1,000 or more relative to the source material from which the specified protein was isolated. For clarity, isolated and purified protein is described as isolated and purified with respect to its starting material (e.g., plants or other non-animal sources). In some embodiments, the term isolated and purified may indicate that the protein preparation is at least 60 percent pure, e.g., greater than 65 percent, 70 percent, 75 percent, 80 percent, 85 percent , 90 percent, 95 percent, or 99 percent pure. The fact that a consumable may comprise materials other than the isolated and purified protein does not change the isolated and purified nature of the protein as this definition typically applies to the protein prior to addition to the composition. In some embodiments, the isolated and purified protein(s) represent at least 1 percent, at least 5 percent, at least 10 percent, at least 20 percent, at least 30 percent, minus 40 percent, or so QQCI I n / l 7Π7 / Β / ΥΙΛΙ minus 50 percent of the protein content of the consumable by weight. In some embodiments, each of the isolated protein(s) is isolated and purified separately. A consumable described herein may be composed substantially or entirely of ingredients derived from non-animal sources, e.g., plants, fungi, microbial-based sources. Plant sources can be organically grown sources. Proteins can be extracted from the source material (for example, extracted from animal tissues, or plants, fungi, algae, or from bacterial biomass, or from culture supernatant for secreted proteins) or from a combination of materials. of origin (for example, multiple plant species). Consumables can also be made from a combination of animal and plant based sources. For example, the consumable may be a ground meat product supplemented with plant-based products of the invention. A. SOURCES OF CONSUMABLE COMPONENTS As described above, isolated and purified proteins may be derived from non-animal sources such as plants, algae, fungi (e.g., yeast or filamentous fungi), bacteria or archaea. In some embodiments, the isolated and purified proteins can be obtained from genetically modified organisms, such as genetically modified bacteria or yeast. In some embodiments, isolated and purified proteins are synthesized or obtained through in vitro chemical synthesis. In some embodiments, the isolated and purified protein(s) are derived from plant sources. Isolated and purified proteins can be isolated from a single plant source or, alternatively, multiple plant sources can serve as starting material for protein isolation and purification. As described herein, isolated and purified plant proteins are soluble in solution. The solution may comprise EDTA (0 to 0.1 M), NaCl (0 to 1), KC1 (0 to 1M), NaSO4 (0 to 0.2 M), potassium phosphate (0 to 1M), sodium citrate (0 to 1 ), sodium carbonate (0 to 1M), sucrose (0 to 50 percent), Urea (0 to 2M), or any combination thereof. The solution may have a pH of 3 to 11. In some embodiments, the plant proteins may have a solubility in a solution of > 25 grams / liter (e.g., at least 25, 30, 35, 40, 45, 50 , 75, 100, 125, 150, 175, 200, or 225 g / L) at a temperature between about 2°C and about 32°C (for example, between 3°C and 8°C, 10°C and 25°C, or 18°C ​​and 25°C), where the solution has a pH between 3 and 8 (for example, pH 3 to 6, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, or 8), and has a sodium chloride content of 0 to 300 mM (eg, 50, 100, 150, 200, 250, or 300 mM). In some embodiments, the isolated and purified proteins are soluble in a solution greater than 10, 15, 20, 25, 50, 100, 150, 200, or 250 g / L. One skilled in the art will understand that proteins that can be isolated from any organism in the plant kingdom can be used to produce the consumables described herein. Examples of non-limiting plant sources include cereal crops such as, for example, corn, oats, rice, wheat, barley, rye, millet, sorghum, buckwheat, amaranth, quinoa, triticale (rye wheat hybrid), teff (Eragrostis tef); oilseeds, including cotton, sunflower seed, safflower seed, Crambe, Camelina, mustard, rapeseed (Brassica napus); Acacia, or plants of the legume family, such as, for example, clover, Stylosanthes, Sesbania, vetch (Vicia), Arachis, Indigofera, Leucaena, Cyamopsis, peas, such as cowpeas, English peas, yellow peas, or peas , or beans such as, for example, soybeans, fava beans, lima beans, kidney beans, chickpeas, mung beans, pinto beans, lentils, lupins, mesquite, carob, soybeans and peanuts (Arachis hypogaea); leafy greens, such as lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, or collard greens; or green matter not typically consumed by humans, including biomass crops such as switchgrass (Panicum virgatum), Miscanthus, Arundo donax, power cane, sorghum or other grasses, alfalfa, corn stover, kelp or other algae, green matter typically discarded from harvested plants, sugar cane leaves, tree leaves, root crops such as cassava, sweet potato, potato, carrot, beet, or turnips; or coconut. The protein can be isolated from any part of the plant, including roots, stems, leaves, flowers or seeds. For example, ribulose-1,5-bisphosphate-carboxylase / oxygenase (RuBisCo) can be isolated from, for example, alfalfa, carrot leaves, corn stover, sugar cane leaves, soybean leaves, switchgrass, Miscanthus, power reed, Arundo donax, seagrass, kelp, seaweed or mustard greens. Proteins that are abundant in plants can be isolated in large quantities from one or more plant sources and are therefore an economical option for use in any of the compositions provided herein (e.g., muscle, fat, or replicas of connective tissue, meat substitute products or others). Accordingly, in some embodiments, the isolated and purified protein(s) comprise an abundant protein that is found at high levels in a plant and is capable of being isolated and purified in large quantities. In some embodiments, the abundant protein comprises about 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent, 60 percent, 65 percent, or 70 percent of the total protein content of the source plant material. In some embodiments, the abundant protein comprises about 0.5 to 10 percent, about 5 to 40 percent, about 10 to 50 percent, about 20 to 60 percent, or about 30 to 70 percent of the total protein content. of the plant material of origin. In some embodiments, the abundant protein comprises about 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, or 50 percent of the total dry matter weight of the source plant material . In some embodiments, the abundant protein comprises about 0.5 to 5 percent, about 1 to 10 percent, about 5 to 20 percent, about 10 to 30 percent, about 15 to 40 percent, or approximately 20 to 50 percent of the total dry matter weight of the source plant material. The isolated and purified protein(s) may comprise an abundant protein found at high levels in plant leaves. In some embodiments, the abundant protein comprises about 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent, 60 percent, 65 percent, 70 percent percent, 75 percent, or 80 percent of the total protein content of the leaves of the plant of origin. In some QQCI I n / l 7Π7 / Β / ΥΙΛΙ modalities, the abundant protein comprises about 0.5 to 10 percent, about 5 to 40 percent, about 10 to 60 percent, about 20 to 60 percent, or about 30 to 70 percent of the total protein content of the leaves of the plant of origin. In some embodiments, the isolated protein(s) comprise RuBisCo, which is a particularly useful protein for meat replicas due to its high solubility and an amino acid composition that is close to optimal proportions of essential amino acids for human nutrition. In particular embodiments, the isolated protein(s) comprise ribulose-1,5-bisphosphate-carboxylaseoxygenase activase (RuBisCo activase). In some embodiments, the isolated and purified protein(s) comprise a vegetative storage protein (VSP). The isolated protein(s) may comprise an abundant protein found at high levels in plant seeds. In some embodiments, the abundant protein comprises about 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent, 60 percent, 65 percent, 70 percent percent, 75 percent, 80 percent, 85 percent or 90 percent or more of the total protein content of the seeds of the plant of origin. In some embodiments, the abundant protein comprises about 0.5 to 10 percent, about 5 to 40 percent, about 10 to 60 percent, about 20 to 60 percent, or about 30 to 70 percent of the total protein content. protein from the seeds of the plant of origin. Non-limiting examples of proteins found at high levels in plant seeds include seed storage proteins, e.g., albumins, glycinins, conglycinins, casein, globulins, vicilins, conalbumin, gliadin, glutelin, gluten, glutenin, hordein , prolamins, phaseolin (proteins), proteinoplast, secalin, Triticae gluten, or zein, or oil body proteins such as oleosins, caloleosins or steroleosins. The isolated and purified protein(s) may include highly soluble proteins, such as dehydrins, hydrophilins, native unfolded proteins (also referred to as intrinsically disordered proteins), or other families of late embryogenesis abundant (LEA) proteins. LEA proteins have been found in animals, plants and microorganisms and are believed to act as osmoprotectors and stress response proteins. See, for example, Battaglia, et al., Plant Physiol, 148: 6-24 (2008). Such proteins are also heat stable. Such LEA proteins may have a solubility in a solution of at least 1 gram / liter (e.g., 2, 4, 6, 8, 10, 15, 20, 25, 50, 100, 150, 200, or 250 g / liter). L) at a temperature between 90°C and 110°C (for example, between 95°C and 105°C, 95°C, or 100°C), where the solution has a pH between 5 and 8 ( for example, pH of 5, 5.5, 6, 6.5, 7, 7.5, or 8) and has a sodium chloride content of 0 to 300 mM (for example, 50, 100, 150, 200, 250, or 300 mM). In some cases, LEA proteins can be isolated by heating a protein extract between 90°C to 110°C (e.g., 95°C or 100°) and, after centrifugation or filtration of insoluble material, concentrating the LEA protein fraction by, for example, uItrafiItration. In some cases, ionic pH precipitation steps, trichloroacetic acid precipitation, and / or ammonium sulfate can be done before or after the heating step to further remove non-LEA proteins. Heating the solution from 90°C to 110°C denatures most of the proteins, allowing most of the proteins to be removed from the solution. B. PROTEINS Without being bound by theory, it is believed that by isolating and purifying non-animal proteins (e.g., plant proteins), consumables can be made with greater consistency and greater control over the properties of the consumable. In some embodiments, approximately 0.1 percent, 0.2 percent, 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent, 60 percent, 65 percent , 70 percent, 75 percent, 80 percent, 85 percent, 90 percent, 95 percent, 99 percent or more of the protein component of the consumable is composed of one or more isolated and purified proteins. The isolated and purified protein may be greater than 60 percent, 70 percent, 80 percent, 85 percent, 90 percent, 95 percent, 99 percent or 100 percent pure. Isolated and purified proteins can be isolated from one or more other components of a non-animal source. For example, a protein fraction may be isolated from a plant isolate. Isolated proteins can in some cases be purified, where a certain type of protein is separated from other components found in the non-animal source. Proteins can be separated based on their molecular weight, for example, by size exclusion chromatography, ultrafiltration through membranes, or density centrifugation. In some embodiments, proteins can be separated based on their surface charge, for example, by isoelectric precipitation, anion exchange chromatography, or cation exchange chromatography. Proteins can also be separated based on their solubility, for example, by ammonium sulfate precipitation, isoelectric precipitation, surfactants, detergents, or solvent extraction. Proteins can also be separated by their affinity to another molecule, using, for example, hydrophobic interaction chromatography, reactive dyes, or hydroxyapatite. Affinity chromatography may also include the use of antibodies that have specific binding affinity for the protein of interest, nickel NTA for labeling recombinant proteins, lectins to bind to sugar moieties on a glycoprotein, or other molecules that specifically bind. to the protein of interest. Protein isolation allows removal of unwanted material. In some embodiments, an isolated and purified protein is a protein that has been substantially separated from unwanted material (for example, nucleic acids such as RNA and DNA, lipid membranes, phospholipids, fats, oils, carbohydrates, such as starch, cellulose , and glucans, phenolic compounds, polyphenolic compounds, aromatic compounds, or pigments) in the seeds, leaves, stems, or other part of the plant. Isolated and purified proteins can also be produced recombinantly using polypeptide expression techniques (for example, heterologous expression techniques using bacterial cells, insect cells, fungal cells such as yeast cells, plant cells, or mammalian cells). . In some cases, standard polypeptide synthesis techniques (eg, liquid phase polypeptide synthesis techniques or solid phase polypeptide synthesis techniques) can be used to produce proteins synthetically. In some cases, cell free transfer techniques can be used to produce proteins synthetically. The protein or proteins incorporated into the consumable may serve a nutritional function. In some case, the protein also serves to alter the properties of the consumable, for example, the taste, color, odor and / or texture of the consumable. For example, a meat substitute product may comprise a protein indicator that indicates the progression of cooking from a raw state to a cooked state, where the meat substitute product is obtained from non-animal sources. Examples of proteins that can be isolated and purified, and used in the consumables described herein include ribosomal proteins, actin, hexokinase, lactate dehydrogenase, fructose bisphosphate aldolase, phosphofructokinases, isomerases, triose-phosphate-phosphoglycerate kinases, phosphoglycerate, enolases, pyruvate kinases, proteases, lipases, amylases, glycoproteins, lectins, mucins, glyceraldehyde-3-phosphate dehydrogenases, pyruvate decarboxylases, actins, elongation translation factors, histones, oxygenase-ribulose-1,5-bisphosphate- carboxylase (RuBisCo), oxygenase-ribulose 1,5-bisphosphate-carboxylase activase (RuBisCo activase), albumins, glycinins, conglycinins, globulins, vicilins, conalbumin, gliadin, glutelin, gluten, glutenin, hordein, prolamin, phaseolin (proteins) , proteinoplast, secalin, extensins, Triticae gluten, collagens, zein, kapphirin, oats, dehydrins, hydrins, abundant late embryogenesis proteins, natively unfolded proteins, any seed storage protein, oleosins, caloleosins , steroleosins or other oil body proteins, vegetative storage protein A, vegetative storage protein B, mung seed storage globulin 8S, globulin, pea globulins, and pea albumins. In some embodiments, an isolated and purified protein may be a protein that interacts with lipids and helps stabilize lipids in a structure, a protein that binds lipids and helps cross-link lipid structures, or a protein that binds lipids. to lipids and assists in the cross-linking interaction of lipid and non-lipid protein structures. Without wishing to be bound by any particular theory, the use of such proteins in a consumable described herein may enhance the integration of lipids and / or fat replicas with other components of the meat substitute product, resulting in a better mouthfeel and texture of the final product. A non-limiting example of a lipid-interacting plant protein includes proteins in the oleosin family. Oleosins are lipid-interacting proteins found in the oil bodies of plants. Other non-limiting examples of plant proteins that can interact with lipids and stabilize emulsions include Great Northern bean storage seed proteins, pea albumins, pea globulins, mung bean 8S globulins, bean protein 8S globulins, prolamins and lipids In some embodiments, one or more of the isolated proteins and Purified QQCI I n / l 7Π7 / Ε / ΥΙΛΙ may be an iron transport protein such as a heme-containing protein. As used herein, the term heme-containing protein can be used interchangeably with heme-containing polypeptide or heme protein or heme polypeptide and includes any polypeptide that can bind covalently or non-covalently to a heme moiety. In some embodiments, the hemoglobin-containing polypeptide is a and may include a globin fold, comprising a series of seven to nine alpha helices. Globin-like proteins can be of any class (e.g., class I, class II, or class III), and in some embodiments, can transport or store oxygen. For example, a heme-containing protein may be a non-symbiotic type of hemoglobin or a leghemoglobin. A heme-containing polypeptide may be a monomer, that is, a single polypeptide chain, or may be a dimer, trimer, tetramer, and / or higher order oligomers. The lifetime of the oxygenated Fe2+ state of a heme-containing protein may be similar to that of myoglobin or may exceed it by 10 percent, 20 percent, 30 percent, 50 percent, 100 percent or more in conditions under which the heme protein-containing consumable is manufactured, stored, handled or prepared for consumption. The lifetime of the non-oxygenated Fe2+ state of a heme-containing protein may be similar to that of myoglobin or may exceed by 10 percent, 20 percent, 30 percent, 50 percent, 100 percent or more under conditions in which the consumable is manufactured, stored, handled or prepared. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ contains heme protein for consumption. Non-limiting examples of heme-containing polypeptides may include an androglobin, a cytoglobin, an E globin, an hemoglobin beta, an alpha hemoglobin, a protoglobin, a cyanoglobin, a cytoglobin, a histoglobin, a neuroglobin, a chloroquorin, a truncated hemoglobin (e.g. HbN or HbO), a 2 / 2 truncated globin, a hemoglobin 3 (e.g. , Glb3), a cytochrome, or a peroxidase. Heme-containing proteins that can be used in the consumables described herein can be from mammals (for example, farm animals, such as cattle, goats, sheep, horses, pigs, oxen, or rabbits), birds, plants, algae, fungi (for example, yeast or filamentous fungi), ciliates, or bacteria. For example, a heme-containing protein may be from a mammal such as a farm animal (e.g., a cow, goat, sheep, pig, ox, or rabbit) or a bird such as a turkey or chicken. Heme-containing proteins can be from a plant such as Nicotiana tabacum or Nicotiana sylvestris (tobacco); Zea mays (corn), Arabidopsis thaliana, a legume such as Glycine max (Soybean), Cicer arietinum (chickpea), Pisum sativum (pea) varieties such as peas or sweet peas, common bean varieties Phaseolus vulgaris such as green beans, black beans , navy beans, northern beans, or pinto beans, Vigna varieties QQCI I n / l Znz / R / YIAI unguiculata (cowpea), Vigna radiata (mung bean), Lupinas albus (lupine), or Medicago sativa (alfalfa); Brassica napus (canola); Triticum sps. (Wheat, including wheat and spelled grains); Gossypium hirsutum (cotton); Oryza sativa (rice); Zizania sps (Wild rice); Helianthus annuus (sunflower); Beta vulgaris (sugar beet); Pennisetum glaucum (pearl millet); Chenopodium sp. (Quinoa); Sesamum sp. (Sesame); Linum usitatissimum (flax); u Hordeum vulgare (barley). Heme-containing proteins can be isolated from fungi such as Saccharomyces cerevisiae, Pichia pastoris, Magnaporthe oryzae, Fusarium graminearum or Fusarium oxysporum. Heme-containing proteins can be isolated from bacteria such as Escherichia coli, Bacillus subtilis, Bacillus megaterium, Synechocistis sp., Aquifex aeolicus, Methylacidiphilum infernorum, or thermophilic bacteria (e.g., growing at temperatures greater than 45°C). , such as Thermophilus. Heme-containing proteins can be isolated from algae such as Chlamydomonas eugametes. Heme-containing proteins can be isolated from protozoa such as Paramecium caudatum or Tetrahymena piriformis. In some embodiments, the bacterial hemoglobins are selected from the group consisting of Aquifex aeolicus, Thermobifida fusca, Methylacidiphilum infernorum (Hell's Gate), Synechocystis SP, or Bacillus subtilis. The sequences and structure of numerous heme-containing proteins are known. See, for example, Reedy, et al., Nucleic Acids Research, 2008, vol. 36, database topic D307-D313 and the Heme Protein Database available on the World Wide Web at http: / / hemeprotein.info / heme.php. For example, a non-symbiotic hemoglobin may be from a plant selected from the group consisting of soybeans, soybean sprouts, alfalfa, golden flax, black beans, black-eyed peas, northern chickpeas, mung beans, cowpeas, pinto beans, peas. of pods, dried peas, quinoa, sesame, sunflower, wheat grains, spelt, barley, wild rice, or rice. Any of the heme-containing proteins described herein may be used for the production of consumables may have at least 70 percent (e.g., at least 75 percent, 80 percent, 85 percent, 90 percent , 95 percent, 97 percent, 98 percent, 99 percent, or 100 percent) of sequence identity with the amino acid sequence of the corresponding protein or fragments thereof that contain a heme-containing heme binding motif wild type. For example, a heme-containing protein may have at least 70 percent sequence identity with an amino acid sequence set forth in Figure 1, including a non-symbiotic hemoglobin such as from Vigna radiata (SEQ ID NO: 1 ), Hordeum vulgare (SEQ ID NO: 5), Zea mays (SEQ ID NO: 13), Oryza sativa subsp. japonica (rice) (SEQ ID NO: 14), or Arabidopsis thaliana (SEQ ID NO: 15), a Hell's Gate I globin such as from Methylacidiphilum infernorum (SEQ ID NO: 2), a flavohemoprotein such as from Aquifex aeolicus (SEQ ID NO: 3), a leghemoglobin such as from Glycine max (SEQ ID NO: 4), Pisum sativum (SEQ ID NO: 16), or Vigna unguiculata (SEQ ID NO: 17), a heme-dependent peroxidase such as from Magnaporthe oryzae, (SEQ ID NO: 6) or Fusarium oxysporum (SEQ ID NO: 7), a cytochrome c peroxidase from Fusarium graminearum ( SEQ ID NO: 8), a truncated hemoglobin from Chlamydomonas moewusii (SEQ ID NO: 9), Tetrahymena piriformis (SEQ ID NO: 10, group I truncated), Paramecium caudatum (SEQ ID NO: I 1, Group I truncated) , a hemoglobin from Aspergillus niger (SEQ ID NO: 12), or a mammalian myoglobin protein such as Bos taurus (SEQ ID NO: 18) myoglobin, Sus scrofa (SEQ ID NO: 19) myoglobin, or Equus caballus (SEQ ID NO: 20) myoglobin, a heme protein from Nicotiana benthamiana (SEQ ID NO: 21), Bacillus subtilis (SEQ ID NO: 22), Corynebacterium glutamicum (SEQ ID NO: 23), Synechocystis PCC6803 (SEQ ID NO: 24) , Synechococcus sp. PCC 7335 (SEQ ID NO: 25), Nostoc commune (SEQ ID NO: 26), or Bacillus megaterium (SEQ ID NO: 27). See Figure 1. The percentage of identity between two amino acid sequences can be determined as follows. First, the amino acid sequences are aligned using the BLAST 2 Sequences (B12seq) program from the standalone version of BLASTZ containing BLASTP version 2.0.14. This standalone version of BLASTZ can be obtained from the Fish & Richardson website (for example, www.fr.com / blast / ) or from the US government's National Center for Biotechnology Information website (www.ncbi. nlm.nih.gov). Instructions explaining how to use the B12seq program can be found in the readme file accompanying BLASTZ. B12seq performs a comparison between two amino acid sequences using the BLASTP algorithm. To compare two amino acid sequences, the B12seq options are set as follows: -i sets to a file containing the first amino acid sequence to be compared (for example, C:\seq1.txt); -j sets to a file containing the second amino acid sequence to be compared (for example, C:\ seq2.txt); -p fits blastp; -o is set to any desired file name (for example, C:\output.txt); and all other options are left at their default settings. For example, the following command can be used to generate an output file containing a comparison between two amino acid sequences: C:\B12seq -i c:\ seq1.txt -j c:\seq2.txt -p blastp -o C: \output.txt. If the two compared sequences share homology, then the designated output file will present those regions of homology as aligned sequences. If the two compared sequences do not share homology, then the designated output file will not present aligned sequences. Similar procedures can be followed for nucleic acid sequences except that BLASTN is used. Once aligned, the number of matches is determined by counting the number of positions at which an identical amino acid residue occurs in both sequences. The percent identity is determined by dividing the number of matches by the length of the amino acid sequence of the full-length polypeptide followed by multiplying the resulting value by 100. Note that the percent identity value is rounded to the nearest tenth. For example, 78.1 1, 78.12, 78.13, and 78.14 are rounded down to 78.1, while 78.15, 78.16, 78.17, 78.18, and 78.19 are rounded down to 78.2. It is also noted that the length value will always be an integer. It will be appreciated that a number of nucleic acids may encode a polypeptide having a particular amino acid sequence. The degeneration of the genetic code is well known in the art; That is, for many amino acids, there is more than one nucleotide triplet that serves as the codon for the amino acid. For example, the codons in the coding sequence for a given enzyme can be modified in such a way that optimal expression is obtained in a particular species (e.g., bacteria or fungi), using codon bias tables appropriate for that species. Heme-containing proteins can be extracted from the source material (for example, extracted from animal tissues, or plants, fungi, algae, or bacterial biomass, or from culture supernatant for secreted proteins) or from a combination of base materials (e.g. multiple species QQCI I n / l 7Π7 / Ε / ΥΙΛΙ of plants). Leghemoglobin is readily available as an unused byproduct of raw material legume crops (e.g., soybeans, alfalfa, or peas). The amount of leghemoglobin in the roots of these crops in the United States exceeds the myoglobin content of all the red meat consumed in the United States. In some embodiments, heme-containing protein extracts include one or more proteins from the source material (e.g., another animal, plant, fungus, algae, or bacterial proteins) that do not contain heme or from a combination of materials. base (for example, different animals, plants, fungi, algae or bacteria). In some embodiments, heme-containing proteins are isolated and purified from other components of the source material (e.g., another animal, plant, fungus, algae, or bacterial proteins) using techniques described above. As used herein, the term isolated and purified indicates that the heme-containing protein preparation is at least 60 percent pure, e.g., greater than 65 percent, 70 percent, 75 percent, 80 percent. percent, 85 percent, 90 percent, 95 percent, or 99 percent pure. Heme-containing proteins can also be produced recombinantly using polypeptide expression techniques (for example, heterologous expression techniques using bacterial cells, insect cells, algal cells, QQCI I n / l Znz / R / YIAI fungal cells such as yeast cells, plant cells, or mammalian cells). For example, heme-containing protein can be expressed in E. coli cells. Heme-containing proteins can be tagged with a heterologous amino acid sequence, such as FLAG, polyhistidine (e.g., hexahistidine, HIS tag), hemagglutinin (HA), glutathione-Stransferase (GST), or maltose-binding protein ( MBP) to aid in protein purification. In some embodiments, a recombinant heme-containing protein that includes a HIS tag and a protease site (e.g., TEV) to allow dissociation of the HIS tag, can be expressed in E. coli and purified using affinity chromatography. HIS label (Heel resin, CloneTech). In some cases, standard polypeptide synthesis techniques (e.g., liquid phase polypeptide synthesis techniques or solid phase polypeptide synthesis techniques) can be used to produce heme-containing proteins synthetically. In some cases, cell-free translation techniques can be used to produce heme-containing proteins synthetically. In some embodiments, the isolated and purified protein is substantially in its native fold and water soluble. In some embodiments, the isolated and purified protein is more than 50, 60, 70, 80, or 90 percent in its native fold. In some embodiments, the isolated and purified protein is greater than 50, 60, 70, 80, or 90 percent water soluble. The proteins used in the consumable may be altered (e.g., hydrolyzed, chopped, cross-linked, denatured, polymerized, extruded, electrospun, spray dried or iophylized, or derivatively or chemically modified). For example, proteins can be covalently modified by attaching sugars, lipids, cofactors, peptides, or other chemical groups including phosphate, acetate, methyl, and other natural or non-natural molecules. For example, the peptide backbones of proteins can be cleaved by exposure to acid or proteases or other means. For example, proteins can be denatured, that is, their secondary, tertiary or quaternary structure can be altered, by exposure to heat or cold, changes in pH, exposure to denaturing agents such as detergents, urea, or others. chaotropic agents, or mechanical stress including shear. The alignment of proteins in a solution, colloid, or solid assembly can be controlled to affect mechanical properties, including tensile strength, elasticity, deformability, hardness, or hydrophobicity. Proteins can also be assembled into fibers that can form a matrix for a structure for the compositions. A three-dimensional matrix of protein fibers may, for example, contain chemicals that promote the formation of intermolecular disulfide cross-links (mixed glutathione, dithioerythritol (DTT), beta-mercaptoethanol (BME)). In some embodiments, the chemicals are proteins (thioredoxin, glutaredoxin). In QQCI I n / l 7Π7 / Β / ΥΙΛΙ In some embodiments, proteins are enzymes (disulfide isomerase). In some embodiments, the fibers are cross-linked by cross-linking chemicals with two reactive groups selected from the group consisting of N-hydroxysuccinimide (NHS) esters, imidoesters, aryl fluorides, aldehydes, maleimides, pyrididithiols, haloacetyls, aryl azides, diazirines, carbodiimides. , hydrazides and isocyanates. In some embodiments, coacervates comprising one or more plant proteins may be formed and used, for example, as binding agents in meat or other replicas. Coacervation is the process in which a homogeneous solution of charged polymers undergoes phase separation to give rise to a dense polymer-rich phase (the 'coacervate') and a solvent-rich phase (supernatant). Protein polysaccharide coacervates have been used in the development of biomaterials. See, for example, Boral and Bohidar (2010) Journal of Physical Chemistry B. Vol 1 14 (37): 12027-35; and Liu et al., (2010) Journal of Agriculture / and Food Chemistry, Vol 58: 552-556. The formation of such coacervates is driven by associative interactions between oppositely charged polymers. However, as described herein, coacervates can be formed using proteins (for example, plant proteins comprising one or more pea proteins, chickpea proteins, lentil proteins, lupine proteins, other legume proteins, or mixtures thereof). In general, a coacervate can be formed by acidifying a low ionic strength solution (e.g., a solution buffered at or below 100 mM sodium chloride) comprising one or more isolated and purified plant proteins such as legumes or vicilins. pea (for example, a vicilin fraction comprising convicilins), a combination of both vicilins and legume, or unfractionated pea proteins at a pH of 3.5 to 5.5. (For example, pH 4 to 5). Under these conditions, the proteins are separated from the solution and the mixture can be centrifuged to cleanly separate the coacervate. This coacervate, unlike a precipitate, is a viscous material that can be stretched by traction and melts with heat. The process can be carried out in the presence of oils (up to 70 percent, for example, palm or other oil), to form a creamy material. By varying the composition of the solution (vicilin:legume ratio, type and amount of oil used), the binding properties of the coacervate can be tuned as desired. In some embodiments, one or more gums (e.g., acacia gum or xanthan gum) may be used to form a coacervate. Coacervates can be used as binding agents in beef burger replicas and keep adipose tissue, muscle tissue, and connective tissue replicas linked. Bonding materials with different adhesive and baking characteristics can be prepared by combining wheat gluten (0 to 20 percent) and pea protein fractions (0 to 50 percent) in the presence of such a plasticizer. QQCI I n / l 7Π7 / Β / ΥΙΛΙ as glycerol (0 to 30 percent) or polyethylene glycol. Leghemoglobin or another heme-containing protein can be added to the mixture if necessary. After mixing to eliminate lumps, the material can be incorporated into replica beef burgers. In some embodiments, proteins can be subjected to freeze alignment to texturize the proteins without extrusion. The method involves slow freezing of protein comprising materials to allow the formation of ice crystals. When cooled from one side, ice crystals preferentially form in a direction perpendicular to the cooled side. After freezing, the ice can be removed from the material in an Ioophilizer, leaving behind the multi-layered material. The structure can then be stabilized by heating under pressure, humid conditions to produce a material that can be used in meat replicas. Freeze alignment of soy proteins has been described by Lugay and Kim (1981) (see Freeze alignment: A novel method for protein texturization Page 177-187, chapter 8, in: DW Stanley, ED Murray and DH Lees eds. 1981. Utilization of Protein Resources. Westport, CT: Food & Nutrition Press, Inc). Freeze aligned proteins may be subjected to further processing (by immersion in solutions comprising beef flavors and / or leghemoglobin) and used in combination with adipose and connective tissue replicas to form meat replicas. The replicas can also be used as structures around QQCI I n / l 7Π7 / Ε / ΥΙΛΙ which cold-fixing gels (comprising, for example, pea proteins and myoglobin) or cross-linked gels (comprising, for example, pea proteins and leghemoglobin) can be formed before its combination with adipose and connective tissues. C. LIPIDS The consumables described herein may include a lipid component. Lipids can be isolated and / or purified and can be in the form of triglycerides, monoglycerides, diglycerides, free fatty acids, sphingosines, glycolipids, phospholipids, or oils, or assemblies of such lipids (e.g., membranes, lecithin, IisoIecithin, or fat droplets containing a small amount of lipid in a bulk water phase). In some embodiments, the lipid sources are oils obtained from non-animal sources (for example, oils obtained from plants, algae, fungi such as yeast or filamentous fungi, algae, bacteria, or archaebacteria), including genetically modified bacteria, algae. , archaebacteria or fungi. Examples of vegetable oils include, but are not limited to, corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, saffron oil, sunflower oil, linseed oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil , either QQCI I n / l 7Π7 / Ε / ΥΙΛΙ rice bran oil; or margarine. The oils can be hydrogenated (for example, a hydrogenated vegetable oil) or non-hydrogenated. In some embodiments, the lipids may be triglycerides, monoglycerides, diglycerides, free fatty acids, sphingosines, glycolipids, lecithin, isolecithin, phospholipids such as phosphatidic acids, lysophosphatidic acids, f osf at id i I col i n as, phosphatidyl inositols, phosphatidylethanolamines, phosphatidyl serines; sphingolipids such as sphingomyelins or ceramides; sterols such as stigmasterol, sitosterol, campesterol, brassicasterol, sitostanol, campestanol, ergosterol, zymosterol, fecosterol, dinosterol, lanosterol, cholesterol, or episterol; lipid amides, such as N-palmitoyl-proline, N-stearoyl-glycine, N-palmitoyl-g I i c i n a, Narachidonoyl-glycine, N-palmitoyl-taurine, N-arachidonoyl-histidine, or anandamide; free fatty acids, such as palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid (C18:2), eicosanoic acid (C22:0 ), arachidonic acid (C20:4), eicosapentaenoic acid (C20:5), docosapentanoic acid (022:5), docosahexanoic acid (C22:6), erucic acid (C22: I), conjugated linoleic acid, linolenic acid (C18 :3), oleic acid (018:1), elaidic acid (trans isomer of oleic acid), trans-vaccenic acid (018:1 trans 11), or conjugated oleic acid; or esters of such fatty acids, including monoacyl glyceride esters, diacyl glyceride esters, and triacyl glyceride esters of such fatty acids. Lipids may comprise phospholipids, lipid amides, sterols or neutral lipids. Phospholipids may comprise a plurality of antipathogenic molecules comprising fatty acids (for example, see above), glycerol and polar groups. In some embodiments, the polar groups are, for example, choline, ethanolamine, serine, phosphate, glycerol-3-phosphate, inositol or inositol phosphates. In some embodiments, the lipids are, for example, sphingolipids, ceramides, sphingomyelins, cerebrosides, gangliosides, ether lipids, plasmalogens or pegylated lipids. In some embodiments, the lipids used in the consumable are the creamy fraction created from seeds, nuts and legumes, including, but not limited to, sunflower seeds, safflower seeds, sesame seeds, rapeseed, almonds. , macadamia, grapefruit, lemon, orange, watermelon, pumpkin, cocoa, coconut, mango, pumpkin, cashews, Brazil nuts, chestnuts, hazelnuts, peanuts, pecans, walnuts and pistachios. As used herein, the term cream fraction can refer to an isolated emulsion comprising lipids, proteins and water. To obtain a creamy fraction from seeds, nuts, legumes, one or more of the following steps can be performed. Seeds, nuts or legumes can be mixed for between 1 minute and 30 minutes. For example, seeds, nuts, or legumes can be mixed by gradually increasing the speed to maximum speed for 4 minutes, then mixing at maximum speed for 1 minute. Seeds, nuts or legumes can be mixed in water or in solutions containing all or some of the following: EDTA (0 to 0.1 M), NaCl (0 to 1 M), KC1 (0 to 1M), NaSÜ4 (0 to 0.2 M), potassium phosphate (0 to 1 M), sodium citrate (0 to 1 M), sodium carbonate (0 to 1 M), and / or sucrose (0 to 50 percent), from a pH of 3 to 11 to obtain a suspension. The suspension can be heated to 20°C to 50°C and centrifuged to obtain the cream fraction (the top layer, also known as the cream). Further purification of the cream fraction can be achieved by washing the cream fraction with 0.1 M to 2 M urea solution before re-isolating the cream fraction by centrifugation. The residual liquid (referred to as the skim layer) which is a solution comprising proteins in water can also be used. The cream can be used as is, or undergo further purification steps. For example, washing and heating can remove color and flavor molecules (e.g., unwanted molecules), or unwanted granulated particles to improve mouthfeel and creaminess. In particular, washing with a high pH buffer (pH>9) can remove bitter-tasting compounds and improve mouthfeel, washing with urea can remove storage proteins, washing below pH 9, followed by washing with a pH above pH 9 can remove unwanted color molecules, and / or washing with QQCI I n / l 7Π7 / Ε / ΥΙΛΙ Salts can decrease flavor compounds. Heating can increase the removal of grainy particles, color and flavor compounds. For example, the creamy fraction can be heated from 0 to 24 hours, at temperatures ranging from 25°C to 80°C. In some embodiments, the resulting creamy fraction comprises storage seed proteins. In some embodiments, the storage seed proteins are substantially removed from the resulting creamy fraction. D. FIBER The fiber can be isolated and / or purified for inclusion in the consumables described herein. Fiber can refer to non-starch polysaccharides such as arabinoxylans, cellulose, and other plant components such as resistant starch, resistant dextrins, inulin, lignin, waxes, chitins, pectins, beta-glucans, and oligosaccharides from any plant source. Fibers can refer to proteins extruded and centrifuged in solution as described herein. E. SUGARS In some embodiments, the consumable may also comprise sugars. For example, the consumable may comprise: monosaccharides, including, but not limited to, glucose (dextrose), fructose (levulose), galactose, mannose, arabinose, xylose (D- or L-xylose), and ribose, disaccharides, including, but not limited to, sucrose, lactose, melibiose, trehalose, cellobiose, or maltose, sugar alcohols such as arabitol, mannitol, dulcitol, or sorbitol, sugar acids such as galacturonate, glucuronate, or gluconate, oligosaccharides and polysaccharides such as glucans , starches such as corn starch, potato starch, pectins such as apple pectin or orange pectin, raffinose, stachyose, or dextrans; the cell wall of plant degradation products such as salicin, and / or sugar derivatives such as N-acetyl-glucosamine. F. GEL FORMATION The components of the composition can be formed into a gel. In some embodiments, the gels comprise protein, wherein the protein is derived from a non-animal source (e.g., a plant source or other non-animal source such as a genetically modified yeast or bacteria). Gels can be formed using a variety of methods. The concentration of the protein, the concentration of the enzyme, the pH and / or temperature of the process will affect the rate of gel formation and the quality of the final tissue replica. Gels can be fully stabilized by physical cross-linking between the components. In some embodiments, gels can be produced by heat / cold cycles, in which case the gel is stabilized by physical interactions (entanglements, hydrophobic interactions) between the protein molecules. For example, a gel can be formed by heating a protein solution to a temperature of at least 40°C, 45°C, 50°C, 60°C, 70°C, 80°C, 90°C, or 100°C and then cool to room temperature, or to a QQCI I n / l Znz / R / YIAI temperature below 40°C. In some embodiments, a gel can be formed by subjecting the composition containing the protein and any other component (e.g., a lipid) to high pressure processing. In some embodiments, gels can be produced by adjusting the pH of the solution. For example, the pH of a concentrated protein solution can be adjusted to near the isoelectric pH of the main protein component by the addition of hydrochloric acid or other acid, or sodium hydroxide or other base. In some embodiments, gels can be produced by immersion in protein powder solutions. For example, protein powder can be immersed in a concentrated sodium hydroxide solution of at least 1 percent, 5 percent, 10 percent, 20 percent (by weight / volume) or more. In other examples, protein powder may be soaked in mixed water / ethanol solutions. In some embodiments, a cold-setting gel is formed to prevent denaturation or decomposition of heat-labile components (eg, oxidation of iron in a heme fraction or generation of off-flavors). See, Ju and Kilara A. (1998) J. Food Science, Vol 63 (2): 288-292; and Maltais et al., (2005) J. Food Science, Vol 70 (1): C67-C73) for general methodologies for the formation of cold-set gels. In general, cold setting gels are first formed QQCI I n / l 7Π7 / Κ / ΥΙΛΙ heat denaturing a protein solution below its minimum gelling concentration (pH and protein type dependent, typically <8 percent (w / v) at pH 6 to 9 for globular plant proteins such as pea proteins). The protein solution can be heated to a temperature above the protein denaturation temperature under conditions in which it will not precipitate out of solution (eg, 0 to 500 mM sodium chloride, pH 6 to 9). The solution can be cooled back to room temperature or below, and any heat-labile components (for example, heme-containing proteins and / or oils) mixed in when the solution is cool enough, but before gelation. . Gelation can be induced by the addition of sodium chloride or calcium chloride (eg, 5 to 100 mM), and the solution incubated at or below room temperature to allow gel formation (typically minutes to hours). The resulting gel can be used as is in the meat replicas or further processed (eg, stabilized) prior to incorporation into the meat replicas. In some embodiments, the gels may comprise or be produced (eg, stabilized by) at least in part by a cross-linked enzyme. The cross-linked enzyme can be, for example, a transglutaminase, a tyrosinase, a lipoxygenase, a protein disulfide reductase, a protein disulfide isomerase, a sulfhydryl oxidase, a peroxidase, a hexose oxidase, a QQCI I n / l 7Π7 / Ε / ΥΙΛΙ I i s i I - oxid as a, an oxidase or amine. In some cases, the gels may contain chemicals that promote the formation of intermolecular disulfide cross-links between proteins. In some embodiments, the chemicals are proteins (e.g., thioredoxin, glutaredoxin). In some embodiments, the proteins are enzymes (disulfide isomerase). Gels can be stabilized by chemical crosslinking using crosslinking chemicals with two reactive groups selected from the group consisting of N-hydroxysuccinimide (NHS) esters, imidoesters, aryl fluorides, aldehydes, maleimides, pyridyldithiols, haloacetyls, aryl azides, diazirines, carbodiimides , hydrazides and isocyanates. In some embodiments, the gels can be stabilized by the addition of starches and gums. In some embodiments, more than one of these approaches are used in combination. For example, a transglutaminase cross-link can be further stabilized by a heat / cold treatment. G. MUSCLE REPLICAS A large number of meat products comprise a high proportion of skeletal muscle. Accordingly, the present invention provides a composition, which can be derived from non-animal sources, that replicates or approximates the key characteristics of animal skeletal muscle. A composition derived from QQCI I n / l 7Π7 / Β / ΥΙΛΙ non-animal sources, which replicate or approximate animal skeletal muscle may be used as a component of a consumable, for example, a meat replica. Such composition will be marked herein as muscle replica. In some embodiments, the muscle replica and / or meat substitute product comprising the muscle replica is partially derived from animal sources. In some embodiments, the muscle replica product and / or meat substitute comprising the muscle replica are wholly derived from non-animal sources. The muscle tissue replica may comprise a protein content, wherein the protein content comprises one or more isolated and purified proteins, wherein the muscle tissue replica approximates the flavor, texture, or color of an equivalent muscle tissue derived from a animal source. Many meat products comprise a high proportion of striated skeletal muscle where individual muscle fibers are organized primarily in an anisotropic fashion. Accordingly, in some embodiments, the muscle replica comprises fibers that are to some extent anisotropically organized. The fibers may comprise a protein component. In some embodiments, the fibers comprise a protein component of about 1 percent (w / w), about 2 percent, about 5 percent, about 10 percent, about 15 percent, about 20 percent, cent, about 30 QQCI I n / l 7Π7 / Κ / ΥΙΛΙ percent, about 40 percent, about 50 percent, about 60 percent, about 70 percent, about 80 percent, about 90 percent, about 95 percent, approximately 99 percent (w / w) or more. The connective tissue component of skeletal muscle contributes substantially to the texture, mouthfeel, and cooking behavior of meat products. Connective tissue is composed of protein fibers (collagen, elastin) in the range of 0.1 to 20 microns. In some embodiments, a mixture of fibers of diameters from <1 to 10 microns, and 10 to 300 microns are produced to replicate the composition in animal connective tissue fibers. In some embodiments, the three-dimensional matrix of fibers is stabilized by cross-linked proteins to replicate the tensile strength of animal connective tissue. In some embodiments, the three-dimensional fiber matrix contains an isolated and purified cross-linked enzyme. The cross-linked enzyme can be, for example, a transglutaminase, a tyrosinase, a lipoxygenase, a protein disulfide reductase, a protein disulfide isomerase, a sulfhydryl oxidase, a peroxidase, a hexose oxidase, a lysyl oxidase, an oxidase or an amine. Some proteins (for example, mung bean seed globulin 8S, or the albumin or globulin fraction of pea seeds) have favorable properties for the construction of meat replicas due to their ability to form gels with QQCI I n / l 7Π7 / Ε / ΥΙΛΙ textures similar to animal muscle or adipose tissue. See also the proteins identified in Section III A and B. Proteins can be artificially engineered to emulate the physical properties of animal muscle tissue. In some embodiments, one or more isolated and purified proteins represent about 0.1 percent, 0.2 percent, 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent percent, 60 percent, 65 percent, 70 percent, 75 percent, 80 percent, 85 percent, 90 percent, 95 percent, 99 percent or more of the protein component by weight of the replica meat . In some embodiments, one or more isolated and purified proteins represent about 0.1 percent, 0.2 percent, 0.5 percent, 1 percent, 2 percent, 3 percent, 4 percent, 5 percent, 6 percent, 7 percent, 8 percent, 9 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent, 50 percent, 55 percent percent, 60 percent, 65 percent, 70 percent, 75 percent, 80 percent, 85 percent, 90 percent, 95 percent, 99 percent or more of the protein content of a consumable. The skeletal muscles of animals such as cattle typically contain substantial amounts of glycogen, which may comprise on the order of 1 percent of the mass of the muscle. QQCI I n / l 7Π7 / Κ / ΥΙΛΙ muscle tissue at the time of slaughter. After slaughter, a fraction of this glycogen continues to be metabolized, yielding products that include lactic acid, which contributes to lowering the pH of muscle tissue, a desirable quality in meat. Glycogen is a branched polymer of glucose linked by alpha (l->4) glycosidic bonds in linear chains, with branch points comprising alpha (l->6) glycosidic bonds. Plant starches, particularly amylopectins, are also branched polymers of glucose linked together by alpha (l->4) glycosidic bonds in linear chains, with branching points comprising alpha (l->6) glycosidic bonds and They can therefore be used as a glycogen analogue in the construction of meat replicas. Therefore, in some embodiments, the muscle or meat replica includes a starch or pectin. Additional components of animal muscle tissue include sodium, potassium, calcium, magnesium and other metal ions, lactic acid and other organic acids, free amino acids, peptides, nucleotides, and sulfur compounds. Therefore, in some embodiments, a muscle replica may include sodium, potassium, calcium, magnesium, other metal ions such as iron, zinc, copper, nickel, lithium, or selenium, lactic acid, and other organic acids such as acids. fatty, free of amino acids, peptides, nucleotides and sulfur compounds of glutathione, beta mercaptoethanol, or dithioerythritol. In some embodiments, 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 percent. percent of the concentrations found in a muscle or meat be replicated. The invention also provides methods for making a muscle replica. In some embodiments, the method includes forming the composition into asymmetric fibers prior to incorporation into the consumable. In some embodiments, these fibers replicate muscle fibers. In some embodiments, the centrifuged fibers. In other embodiments, the fibers are extruded fibers. Accordingly, the present invention provides methods for producing asymmetric or spun protein fibers. In some embodiments, the fibers are formed by extrusion of the protein component through an extruder. Extrusion methods are well known in the art, and are described, for example, in United States Patent Number 6,379,738, United States Patent Number 3,693,533, and United States Patent Publication Number 20120093994, which are incorporated herein by reference. These methods can be applied to manufacture the compositions provided herein. Extrusion can be carried out using, for example, a Leistritz Nano-16 twin-screw co-rotating extruder (American QQCI I n / l 7Π7 / Β / ΥΙΛΙ Leistritz Extruder Corp. United States, Sommerville, NJ). Active cooling of the barrel section can be used to limit protein denaturation. Active cooling of the die section can be used to limit expansion of the extruded product and excessive moisture loss. The protein feed and liquid are added separately: the protein is fed by a volumetric plunger feeder or a continuous auger feeder, and the liquid can be added into the barrel through a high-pressure liquid injection system. pressure. Die nozzles with different inner diameters and channel lengths can be used for precise control of extrusion pressure, cooling rate and product expansion. In some examples, the extrusion parameters were: screw speed 100-200 rpm, die diameter 3 mm, die length 15 centimeters, product temperature at the end of the die 50°C, feed speed 2 g / min, and the water flow at a speed of 3 grams / minute. The temperature of the product in the nozzle during extrusion is measured by a thermocouple. Centrifuged fibers can be produced by preparing a high-viscosity protein additive by adding sodium hydroxide to concentrated protein solutions or to the precipitated proteins, and forcing the solution with a plunger-type device (in some examples, a syringe). with a syringe pump) through a small steel capillary (in some examples, a 27-gauge hypodermic needle) into a coagulation bath. In some examples, the bath is filled with a concentrated acid solution (e.g. 3 M hydrochloric acid). In some examples, the bath is filled with a buffer solution with a pH approximately equal to the ionic point of the protein. The propellant from the coagulant protein solution forms a fiber that accumulates at the bottom of the tub. Bundles of spun fibers can be produced by forcing the protein additive through spinnerets with many small holes. In some examples, the spinnerets are stainless steel plates with approximately 25,000 holes per centimeter2, with a diameter at each hole of approximately 200 microns. In some embodiments, muscle tissue replication occurs by immersing the three-dimensional fiber matrix (connective tissue replication) in protein solutions and creating protein gels that incorporate the three-dimensional fiber matrix. H. FAT REPLICAS Animal fats are important to the experience of eating cooked meat and are important to some of the nutritional values ​​of meat. Accordingly, the present invention provides compositions derived from non-animal sources, which recapitulate the key characteristics of animal fat, including texture and / or flavor, through the use of components that mimic the chemical composition and physical properties of, for example, meat. ground beef. In another aspect, the present invention provides a meat substitute product comprising a composition QQCI I n / l 7Π7 / Ε / ΥΙΛΙ derived from non-animal sources, which recapitulates animal fat. Such a composition will be referred to herein as an adipose tissue replica or a fat replica. In some embodiments, the adipose tissue replica and / or meat substitute product comprising the adipose tissue replica is partially derived from animal sources. The consumable may also include adipose tissue replicas that recapitulate key characteristics of non-animal fats, including texture, flavor, firmness, percentage of fat release, and / or temperature of fat release. The fat content of the consumable may be at least 1 percent, 5 percent, 10 percent, 15 percent, 20 percent, 25 percent, 30 percent, 35 percent, 40 percent, 45 percent. percent, 50 percent, 55 percent, 60 percent, 70 percent, 80 percent, 90 percent, or 95 percent fat. Ground beef is typically prepared by blending lean beef with adipose tissue (fat) that is cut from steaks, with the adipose tissue added at 16 to 30 percent (Cox 1993). Without fatty tissue, meat passed through a grinder is tough and brittle, and dries out quickly. Fat is added to lean beef in such a way that the fat released during cooking provides a liquid surface that aids in cooking, and to generate key beef flavors, which are largely products of fatty acids. . Engineering a replica of adipose tissue that plays the same key roles in texture and flavor as plant-based ground beef QQCI I n / l 7Π7 / Β / ΥΙΛΙ is an important driver for texture and flavor. The adipose tissue replicas described here have a great health benefit over meat adipose tissue since the fatty acid composition can be controlled such that the amount of saturated fat can be decreased. In addition, plant-based adipose tissue replicas are free of cholesterol. Plant-based adipose tissue replicas can contain a lower percentage of total fat, and still have the same amount of fat to be released or retained for the properties of desired cooking, flavor and texture. As described herein, adipose tissue replicas comprising emulsions of plant-derived lipids and one or more isolated and purified proteins can be produced in which the composition (e.g., fatty acid composition), cooking characteristics ( e.g., fat release percentage or fat release temperature), and physical properties (e.g., firmness) can be controlled, allowing the plant-based composition to mimic adipose tissue of animal origin. The adipose tissue replica includes (1) a vegetable oil containing three fatty acids; (2) one or more proteins isolated and purified from non-animal sources (e.g., a plant protein); and (3) a phospholipid such as lecithin. The proteins may be plant or microbial proteins as described above (for example, RuBisCo, an oleosin, an albumin, a globulin, or another seed protein). QQCI I n / l 7Π7 / Ε / ΥΙΛΙ storage). See also proteins described in sections III A and B. Vegetable oils can be any of the oils described herein. See, for example, section III C. The fat replica may be a gelled emulsion. In some embodiments, the gel is a soft, elastic gel comprising proteins and optionally carbohydrates. The gelled emulsion may comprise a protein solution comprising multiple proteins, for example, 1 to 5 or 1 to 3 isolated and purified proteins, wherein the protein solution represents 1 to 30 percent of the volume of the emulsion. The gelled emulsion may comprise a fat droplet, where the fat droplet accounts for 70 to 99 percent of the volume of the emulsion. The gelled emulsion may comprise an isolated and purified cross-linked enzyme, wherein the cross-linked enzyme represents 0.0005 percent to 0.5 percent of the emulsion weight by volume, 0.5 to 2.5 percent of the emulsion weight by volume, or 0.001 percent or less than the weight per volume emulsion. The emulsion of fat droplets in the protein solution can be stabilized by forming the emulsion into a gel by cross-linked enzyme, for example, a transglutaminase, by gelation of proteins through heating and cooling of the solutions. proteins, by forming a cold-fixing gel, by forming a coacervate, or combinations of these techniques as described for coacervates in section C, and gel formation in section F. In some embodiments, the fat replica comprises cross-linked enzymes that catalyze reactions that lead to covalent cross-links between proteins. Cross-linked enzymes can be used to create or stabilize the desired structure and texture of the adipose tissue replica, to mimic the desired texture of a desired equivalent animal fat. In some embodiments, cross-linked enzymes are isolated and purified from a non-animal source, examples and embodiments of which are described herein. In some embodiments, the fat replica comprises at least 0.0001 percent, at least 0.001 percent, at least 0.01 percent, at least 0.1 percent, or at least 1 percent (by weight / volume). of a cross-linked enzyme. The cross-linked enzyme can be selected from, for example, transglutaminases, tyrosinases, lipoxygenases, protein disulfide reductases, protein disulfide isomerases, sulfhydryl oxidases, peroxidases, hexose oxidases, lysyl oxidases, and amine oxidases. In some embodiments, the cross-linked enzyme is transglutaminase, a lysyl oxidase (e.g., Pichia pastoris lysyl oxidase), or another amine oxidase. The fat replica may comprise a gel with fat droplets suspended therein. The fat droplets used in some embodiments of the present invention can be from a variety of sources. In some embodiments, the sources are non-animal sources (eg, plant sources). See, for QQCI I n / l 7Π7 / Β / ΥΙΛΙ for example, the examples provided in Section III C. In some embodiments, the fat droplets are derived from animal products (for example, butter, cream, lard, and / or or tallow). In some embodiments, the fat beads are derived from pulp or seed oil. In other embodiments, the sources may be algae, yeast, oily yeast such as Yarrowia lipolytica, or mold. For example, in one embodiment, trig I i cerides derived from Mortierella isabellina can be used. In some modalities, the fat droplets contain synthetic or partially synthetic lipids. In some embodiments, the fat droplets are stabilized by the addition of surfactants, including but not limited to phospholipids, lecithins, and lipid membranes. Lipid membranes can be derived from algae, fungi, or plants. In some embodiments the surfactants comprise less than 5 percent of the fat replica. Fat droplets can in some examples range from 100 nanometers to 150 microns in diameter. The diameter of these stabilized droplets can be obtained by homogenization, high pressure homogenization, extrusion or sonication. In some embodiments, plant oils are modified to resemble animal fats. Plant oils can be modified with flavorings or other agents such as heme proteins, amino acids, organic acids, lipids, alcohols, aldehydes, ketones, lactones, furans, sugars, or other QQCI I n / l 7Π7 / Ε / ΥΙΛΙ aroma precursor, to recapitulate the flavor 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. In some embodiments, additional polysaccharides may be added to a fat replica, including flax seed polysaccharides and xanthan gum. The creation of a plant-based adipose tissue replica requires the stabilization of oil-in-water emulsions. Typically the adipose tissue of animals contains about 95 percent fat, and is stabilized by the bilayer of phospholipids and associated proteins. The adipose tissue replicas described herein can be created with up to 95 percent fat in some cases, with 80 percent fat under many conditions, or with lower amounts of fat (for example, 50 percent or less), while mimicking the properties of animal fat. The achievement of a high percent fat is controlled by the stabilization of the emulsion. The composition (e.g., fatty acid composition), cooking characteristics (e.g., fat release temperature or percentage of fat release), and physical properties (e.g., firmness) can be manipulated by controlling the type and the amount of fat, the amount of protein, the type and amount of lecithin, the presence of additives, and the gelation method. In some embodiments, the protein component comprises about 0.1 percent, 0.5 percent, 1 percent, 2 percent, 5 percent, 10 percent, 15 percent, or 20 percent, 25 percent, or more of fat replica in dry weight or total weight. In some embodiments, the protein component comprises about 0.1 to 5 percent or about 0.5 to 10 percent or more of the fat replica on a dry weight basis or total weight. In some embodiments, the protein component is 0.5 to 3.5 percent or 1 to 3 percent of the fat replica on a dry weight basis or total weight. In some embodiments, the protein component comprises a solution containing one or more isolated and purified proteins. The type of protein can affect the stability of the emulsion, RuBisCo and pea albumins allow fat replicas with a percentage greater than 90 percent fat. The addition of polysaccharides including flax seeds and xanthan gum help to emulsify the mixture, allowing for an increase in fat content. The type and amount of fat can be controlled by the choice of the source of the fat and its lipid composition. In general, oils with higher amounts of saturated fatty acids are more capable of being emulsified at lower protein concentrations, while oils with more unsaturated fatty acids require higher protein concentrations to be emulsified. Protein is necessary to stabilize the emulsion, and an increase in protein content increases stability. If the amount of protein added is too little to emulsify the amount of fat, the mixture will separate into layers. Lecithin is also an emulsion modulator, and emulation can be stabilized or disrupted depending on the amount of protein present and the type of oil used. For example, lecithin can alter the protein / fat matrix to make a less stable emulsion, but can be added at low levels to modulate other physical properties. Emulsions made from oils with higher amounts of unsaturated fats can be destabilized by a high amount of lecithin (1 percent), so that the emulsion does not solidify. Emulsions made from oils with higher amounts of saturated fat can solidify to high amounts of lecithin (1 percent), but are very soft. As described herein the adipose tissue replicas that can be prepared can range from very soft to very firm. The composition and quantity of the fat controls the firmness of the replica. Firmer oils, which contain more long-chain saturated fats, make firmer gels. Oils that produce softer gels typically contain more unsaturated fatty acids or short-chain saturated fatty acids. In general, the firmness of the gel increases as the total fat percent increases, as long as the emulsification takes place and does not separate. The amount of QQCI I n / l 7Π7 / Ε / ΥΙΛΙ protein also contributes to the firmness of the replica. In general, an increase in protein concentration increases the firmness of the replica. The amount of lecithin is a modulator of the firmness of the replica. Larger amounts of lecithin (1 percent) are much softer than smaller amounts of lecithin (0.05 percent) when forming gels with a high percentage of protein (3 percent). When protein is decreased (1.8 percent), all gels are softer, and there is little difference in firmness between low (0.05 percent) and high (1 percent) lecithin if emulsification is carried out. . The addition of polysaccharides to the replicas including, but not limited to, xanthan gum and flax seed paste can increase the firmness of the adipose tissue replica gels. When a replica of adipose tissue is cooked, fat is released from the structured replica as it is cooked. There is often fat that remains in the cooked product; It is important to assist in cooking to achieve balance between released fat and retained fat for texture and flavor. The percentage of fat released (per total fat) can be determined by measuring the amount of fat released during cooking to completion. The percentage of fat released is reported as the weight of fat released times the total fat of the replicate. For example, the percentage of fat release from an adipose tissue replica described herein may be 0 to 10 percent, 10 percent to 20 percent, 20 percent to 30 percent, 30 percent to 40 percent. cent, 40 percent to 50 QQCI I n / l 7Π7 / Κ / ΥΙΛΙ percent, 50 percent to 60 percent, 60 percent to 70 percent, 70 percent to 80 percent, 80 percent to 90 percent, or 90 percent to 100 percent at the time of cooking. Adipose tissue replicas typically release 0 to 90 percent fat under standard cooking conditions. By comparison, beef adipose tissue typically releases 40 to 55 percent fat under equivalent conditions. While plant oils have fixed melting temperatures, the range of temperatures over which adipose tissue replicas can be made to release fat is wide. Fat release temperature is the temperature at which fat is visibly released from the replica on the cooking surface. As described herein, the fat release temperature of the adipose tissue replica can be tailored based on the type and amount of fat, the amount of protein, the type and amount of lecithin, the presence of additives, the emulsion method, and the g e I i f i ca i on method. The resulting adipose tissue replicas may have a fat release temperature of 23°C to 33°C, 34°C to 44°C, 45°C to 55°C, 56°C to 66°C, from 67°C to 77°C, from 78°C to 88°C, from 89°C to 99°C, from 100°C to 110°C, from 111°C to 121°C, from 122°C to 132°C, from 133°C to 143°C, from 144°C to 154°C, from 1 55°C to 165°C, from 166°C to 167°C, from 168°C to 169°C, from 170°C to 180°C, from 181°C to 191°C, from 192°C to 202°C, from 203°C to 213°C, from 214°C to 224°C, from 225°C to 235°C, 236°C to 246°C, 247°C to 257°C, 258°C to 268°C, 269°C to 279°C, 280°C to 290°C, or from 291°C to 301°C. The release of beef fat was measured between 100 to 1 50°C. Emulsification is also a factor in controlling the temperature of fat release: Once fats are incorporated into a replica with protein, or protein and lecithin, the temperature at which fat is released increases significantly above the temperature at which fat melts on its own. Fatty acid composition is also a factor in fat release temperature and fat release percentage. Plant oils containing a higher proportion of unsaturated fatty acids have low melting temperatures and many are liquid at room temperature. Plant oils that contain a higher proportion of saturated fatty acids have a higher melting temperature, and are solid at room temperature. Replicas with a higher amount of unsaturated fats have a higher fat release temperature than the same replica with more saturated fatty acids. Gels made from 75 percent oils with higher amounts of unsaturated fatty acids, a high protein content (3 percent), and minimal lecithin content (0.05 percent), where the mixture was emulsified using a homogenizer By hand and gelled using the hot / cold method, they can be heated to 200°C with little or no fat release. Replicas containing oils with more saturated long-chain fats typically have greater fat release at higher contents. 100 in protein, but release a lower percentage of total fat compared to replicas containing oils with shorter chain fats and a low percentage of protein. Oil-based gels with a higher proportion of saturated short-chain fatty acids, high protein content (3 percent), and minimal lecithin content (0.05 percent), can be heated to 200°C with little release. of fat. The percentage of fat release from a replica of adipose tissue when cooked is also a function of the amount of protein and the amount of lecithin. Typically, the adipose tissue replica contains 1 to 3 percent protein by mass. Increasing protein content leads to increased fat release temperatures, and reduces the fraction of fat released. Increasing the lecithin content to 1 percent can decrease the fat release temperature from 60 to 115°C, and increase the fraction of fat released (e.g., 25 to 30 percent). The source or composition of lecithin used can modulate the amount of fat release and the temperature threshold for fat release. Without being linked to a particular mechanism, lecithin is thought to destabilize the emulsion by disrupting protein-protein interactions. In one embodiment, at a high protein concentration of 3 percent, increasing the lecithin content to 1 percent decreased the fat release temperature from 55 to 60°C, and increased the percentage of fat released to 60 to 65 percent. hundred. QQCI I n / l 7Π7 / Β / ΥΙΛΙ 101 The method of making the emulsion is also a factor in determining the amount of fat release. The emulsion consists of a homogeneous mixture of fat retained in a matrix of proteins and lecithin. Emulsification methods may include high pressure homogenization, sonication, hand homogenization. Alternative methods result in characteristic differences in the size of oil droplets in the emulsion, which influence the stability of the resulting emulsions and the maximum fat concentration at which stable emulsions can form. The method of replica gelation is also a factor in determining the amount of fat release. While replicas of adipose tissue can form without gel formation, gelation results in a firmer and more stable emulsion. Gelation methods are described above, and may include, for example, adding a cross-linked enzyme such as a transglutaminase (TG), or subjecting the emulsion to a hot / cold cycle. For example, either TG treatment or the hot / cold method can convert an emulsion, as described above, to a gel. Furthermore, gelled emulsions formed by TG-catalyzed cross-linking typically release fat at a higher temperature than that at which the emulsions gel by the hot / cold technique. Gels formed by cross-linking with a TG also tend to release less fat than gels formed by the cold techniqueQQCI I n / l 7Π7 / Ε / ΥΙΛΙ > ί 102νc c heat. In some embodiments, a fat replica may be made with a protein content of <1.5 percent and a minimum lecithin content (0.05 percent) and have a fat release temperature of 45 to 65°C, and a high amount of fat released (e.g., 70 to 90 percent). These gels are on the higher end of percentage of fat released. In some embodiments, a fat replica can be made with a lower protein content (<1.5 percent) and a higher lecithin content (>1 percent), and have a lower fat release temperature (e.g., 30 to 50°C, for example, 30 to 45°C), and with an intermediate percentage of fat release (45 to 65 percent). Thus, in gels formed from oils with short chain fatty acids or long chain fatty acids at low protein concentrations, lecithin can play a role in stabilizing the emulsion. In some embodiments, greater than 2 percent RuBisCo or pea albumin may be used to produce adipose tissue replicas with greater than 70 percent fat. In some embodiments, gels formed with more than 3 percent isolated and purified protein can result in adipose tissue replicas with more than 70 percent fat. In some embodiments, adipose tissue replicas made from oils with a higher proportion of long-chain saturated fatty acids, a protein content of 3 percent, and a QQCI 103 minimum lecithin content (0.05 percent), fat can be released at a temperature similar to that at which beef fat does (50 to 100°C), and a low to intermediate fat level (15 to 45 percent). In some embodiments, an adipose tissue replica with a higher protein concentration (>3 percent), and a lecithin content >1 percent may have a fat release temperature of 50 to 70 ° C, and a higher amount of fat release (50 to 80 percent). At high protein, low lecithin concentrations, gels with high saturated fatty acids typically release about 10 percent more fat than gels made up of corresponding unsaturated fats. In some embodiments, protease treatment of protein constituents prior to gel formation can lead to an increase in fat release. In some embodiments, an adipose tissue replica matrix stabilized by cross-linked enzymes releases more fat than an adipose tissue replica matrix stabilized by heat / cold protein denaturation. In one embodiment, an adipose tissue matrix composed of 8S mung bean protein and canola oil, or an equal mixture of coconut, cocoa, olive oil, and palm oils, retains more mass when formed upon heat denaturation / colder than when they are formed by cross-linking with an enzyme. In one embodiment, an adipose tissue matrix formed by denaturation by 104 heat / cold of a preformed oil-protein emulsion containing RuBisCo and cocoa butter, has a higher melting temperature than an adipose tissue replica of similar composition stabilized by a cross-linked enzyme. In some embodiments, adipose tissue replicas constructed from 1.4 w / v percent 8S mung bean protein with 90 w / v percent canola oil and 0.45 w / v percent lecithin soybean, can be homogenized in the presence of varying concentrations of sunflower oleosins. The concentrations of oleosins can vary from a molar ratio of 1:10 to 1:106 of oleosin:triglyceride. An increase in mass retention is observed after cooking by increasing the concentration of oleosins in the adipose tissue replica. The firmness of an adipose tissue replica constructed as a stabilized fat-protein emulsion can be modified by varying the concentration of the protein within the adipose tissue replica matrix. For example, a series of adipose tissue replicas formed with varying concentrations of RuBisCo with 70 to 80 percent vol / vol sunflower oil varied in firmness. Adipose tissue replicas with 0 percent and 0.18 percent (w / v) RuBisCo were very soft, while replicas formed with 1.6 percent (w / v) RuBisCo were soft, and replicas formed with 1.9 percent (w / v) of RuBisCo were medium firm. 105 In one embodiment, the firmness of the adipose tissue replica formed can be modified by stabilizing the oil and protein emulsion by varying the amount of protein in the adipose tissue replica. In one embodiment, adipose tissue replicas made of RuBisCo and 70 percent sunflower oil are softer at lower concentrations, such as 1 percent RuBisCo than at higher concentrations of RuBisCo, such as 3 percent, in adipose tissue replicas. In another aspect, the invention provides methods for making a fat replica. The fat can be isolated and homogenized. For example, an organic solvent mixture can be used to help solubilize a lipid in a gel and then removed to provide the final gel. At this point, the lipid can be frozen, I i of i I i z ated, or stored. Thus, in one aspect, the invention provides 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 be hydrated. Hydration can use agitation or temperature changes. Hydration can occur in a precursor solution to a gel. After hydration, the lipid suspension can be sonicated, homogenized, high-pressure homogenized, or extruded to further alter the properties of the lipids in the solution. In some embodiments, the fat replica is assembled to approximate the organization of adipose tissue in meat. In QQCI I n / l 7Π7 / Β / ΥΙΛΙ In some embodiments, some or all of the components of the fat replica are suspended in a gel (for example, protein gel). In other embodiments, the gel may be a hydrogel, an organogel, or a xerogel. In some embodiments, the gel can be thickened to a desired consistency using a polysaccharide or protein-based agent. For example, you can use starch, arrowroot, corn starch, Katakuri starch, potato starch, sago, tapioca, alginin, guar gum, carob gum, xanthan gum, collagen, egg whites, furcellaran, gelatin, agar, carrageenan, cellulose, methylcellulose, hydroxymethylcellulose, acadia gum, konjac, starch, pectin, amylopectin or proteins derived from legumes, grains, nuts, other seeds, leaves, algae, bacteria, or fungi alone or in combination to thicken the gel, forming an architecture or structure for the consumable. In some embodiments, the tensile strength of the fat replica mimics the tensile strength of adipose tissue. The tensile strength of gelled emulsions can be increased by incorporating fibers. Fibers may be derived from non-animal sources, including, but not limited to, watermelon, jackfruit, chayote, coconut, filamentous green algae, corn and / or cotton. In some embodiments, the fibers are derived from the self-polymerization of proteins, for example, oleosins and prolamins. In some embodiments the fibers are derived from electrospun or extruded proteins. The fibers can form a mesh or three-dimensional strands where each fiber can be of QQCI I n / l 7Π7 / Β / ΥΙΛΙ 107 less than 1 mm in diameter. The adipose tissue replica may be an emulsion comprising a solution of one or more proteins and one or more fats suspended therein in the form of droplets. A more robust emulsion can be provided by slowly adding the oil phase to the aqueous phase and avoid occasional failures for the emulsion. The addition of lecithin can, in some circumstances, destabilize a stabilized protein emulsion, allowing greater fat release when the replica is cooked. In some embodiments, the emulsion is stabilized by one or more enzymes cross-linked in a gel. In some embodiments, the emulsion is stabilized by a matrix formed by proteins induced in a gel by a hot / cold technique or a cold-fixed gel technique. Heating a stabilized protein emulsion can heat denature the proteins leading to an increase in the firmness of the adipose tissue replica. Heating to a sufficient temperature can also reduce the viability of natural microflora by at least 100x. In some embodiments, the emulsion is stabilized by a gelled protein matrix formed by a combination of one or more cross-linked protein enzymes and a heat / cold technique or a cold-set gel technique. After the emulsion has sufficiently cooled, but before gelation is complete, one or more optional ingredients may be added, such as a heme-containing protein (for example, up to about 0.4 percent, such as 0.15, QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 108 0.2., 0.25, 0.3, or 0.4 percent) to give the adipose tissue a more natural-looking pink color and / or one or more flavor compounds such as amino acids, sugars, thiamine, or phospholipids to provide improved flavor to the product final. The protein(s) in solution may comprise isolated and purified proteins, for example, an enriched fraction of purified pea albumin, an enriched fraction of purified pea globulin, an enriched fraction of mung bean 8 globulin, and / or an enriched fraction. by RuBisCo. In other embodiments, the fat(s) are derived from plant-derived oils (a canola oil or rice bran oil). See, for example, Section III C. In some cases, the composition comprises a cross-linked enzyme such as a transglutaminase, lysyl oxidase, or other amine oxidase. Therefore, in some embodiments, a replica of adipose tissue can be made by isolation and purification of one or more proteins; preparing a solution comprising one or more proteins; emulsify one or more fats in the solution; and stabilizing the solution into a gelled emulsion with one or more cross-linking reagents. In some embodiments, the fat replica is a high-fat emulsion comprising a purified pea albumin protein solution emulsified with 40 to 80 percent rice bran oil, stabilized with 0.5 to 5 percent ( in weight / volume) of transglutaminase in a gel. 109 In some embodiments, the fat replica is a high-fat emulsion comprising a solution of isolated protein mung bean globulin 8S emulsified with 40 to 80 percent rice bran oil or 40 to 80 percent rice bran oil. canola, stabilized with 0.5 to 5 percent (w / v) transglutaminase in a gel. Fat can be isolated from plant tissues and emulsified. The emulsion can use high-speed mixing, homogenization, high-pressure homogenization, sonication, shearing, stirring or changes. The lipid suspension can be sonicated or extruded to further alter the properties of the lipids in the solution. At this point, in some embodiments other components of the consumable are added to the solution followed by a gelling agent. In some embodiments cross-linking agents (e.g., transglutaminase or I isi l-oxidase) are added to bind to consumable components. In other embodiments, the gelling agent is added and the lipid / gel suspension is then combined with additional components of the consumable. CONTROL OF THE MELTING POINT BY CONTROLLING THE FAT COMPOSITION The process of cooking meat is an integral part of the experience of using and enjoying meat. An important property of meat is that as the meat is heated, fats are released from the meat, which lubricates the cooking surface and QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 110 increases heat transfer and is a component of the visual, auditory and olfactory experience of cooking meat. The amount of fat that is released rather than retained during cooking varies with cooking temperature and contributes to the visual, auditory, and olfactory experience of cooking meat. The composition and ratio of fatty acids in triglycerides and phospholipids, together with the ratio of phospholipid head groups, contribute to the generation of different flavor profiles of cooked meat. For example, increased levels of phosphatidyl choline and phosphatidylethanolamine in fat provide a more intense meat flavor. As discussed above, the flavor of meat replicas can be modified by varying the proportions and type of different oils, and phospholipids that comprise the meat replica. For example, the flavor of cooked replica meat can be controlled by varying the amount of phospholipids, sterols and lipids (e.g., 0.2 to 1 percent w / w). In one embodiment, the flavor of the cooked meat replica can be controlled by varying the ratio of the different phospholipid head groups. In some embodiments, the phospholipids comprise a plurality of antipathetic molecules comprising fatty acids, glycerol, and polar groups. See, eg, Section III C for examples of fatty acids, phospholipids, polar groups, and sterols associated with phospholipids. See also section III C for examples of useful plant oils. 111 In different cuts of meat, fat has different properties, ranging from the structurally important nature of fat in bacon to the smooth melting behavior of marbled fat in Wagyu beef. By controlling the melting point of the adipose tissue replicas in the consumables, it is possible to reproduce the cooking experience of different types of meat. For example, adipose tissue replicas created from fats with a melting point of 23°C to 27°C may have melting points analogous to Wagyu beef adipose tissue; adipose tissue replicas created from fats with a melting point of 35°C to 40°C may have melting points analogous to adipose tissue in regular ground beef; and adipose tissue replicas created from fats with a melting point of 36°C to 45°C may have melting points analogous to bacon adipose tissue. Adipose tissue replicas can be created and incorporated into consumables such that a proportion of fat that is released and the proportion of fat that is retained by the adipose tissue replica during cooking is similar to the fat properties of meat, for example, from ground beef. In some embodiments, the fat release temperature of a fat replica can be controlled by mixing different proportions of plant oils containing triacylglycerides and phospholipids (eg, lecithin). The melting point of fats is governed by the chemical composition of the acids QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 112 fatty. In general, fats comprising saturated fatty acids (for example, 010:0, C12:0, C14:0, C16:0, C18:0, 020:0, 022:0) are solid at refrigeration temperatures (for For example, about 1°C to about 5°C and at room temperature (for example, about 20°C to 25°C). By controlling the temperature of fat release when cooking a replica of adipose tissue, you can control the firmness of an adipose tissue replica during refrigeration (e.g., about 1.5°C to about 4°C) and at room temperature (e.g., about 20°C to 25°C) Fats comprising monounsaturated fatty acids (e.g. , 016:1 or C18:1) are generally solid at refrigeration temperatures and liquid at room temperature. Fats comprising polyunsaturated fatty acids (e.g., 018:2, 018:3, 020:5, or 022:6) They are generally liquid at refrigeration temperatures and at room temperature. For example, virgin coconut oil melts at around 24°C, while hydrogenated coconut oil melts at 36 to 40°C. For example, adipose tissue replicas containing triglycerides and phospholipids that are liquid at room temperature (approximately 20°C to 25°C) will be softer than adipose tissue replicas containing triglycerides and phospholipids that are solid at refrigeration temperatures. . Adipose tissue replicas may contain oils from one or more sources that are liquid at both storage temperatures. QQCI I n / l Znz / R / YIAI 113 refrigeration and ambient (for example, canola oil, sunflower oil, and / or hazelnut oil). In one embodiment, an adipose tissue replica contains oils from single or multiple sources that are solid at refrigeration temperature, but liquid at room temperature (e.g., olive oil, palm oil, and / or rice bran oil). ). In one embodiment, an adipose tissue replica contains oils from single or multiple sources that are solid at room temperature but liquid at oral temperature (about 37°C) (e.g., palm kernel oil, coconut oil, and / or cocoa butter). In one embodiment, an adipose tissue replica contains oils from single or multiple sources that are solid at oral temperature (approximately 37°C) (e.g., mango butter oil). In one embodiment, an adipose tissue replica includes triglycerides and phospholipids with a high proportion of saturated fatty acids, and is firmer than an adipose tissue replica that contains a higher proportion of triglycerides and monounsaturated and polyunsaturated lipids. For example, an adipose tissue replica containing sunflower oil is softer than an adipose tissue replica containing cocoa butter. Adipose tissue replicas can be formed with 0 percent, 0.18 percent, 1.6 percent, or 2.4 percent w / v RuBisCo with 70 percent, 80 percent, or 90 percent w / v sunflower oil or cocoa butter. Each QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 114 adipose tissue replica containing cocoa butter was firmer than replicas formed with sunflower oil. In one embodiment, an adipose tissue replica made as a stable emulsion of 8S mung bean protein with sunflower oil is smoother than an adipose tissue replica made as a stable emulsion of 8S mung bean protein and cocoa butter. Adipose tissue replicas were formed with 2 percent, 1 percent, or 0.5 percent w / v 8S mung bean protein with 70 percent, 80 percent, or 90 percent w / v oil. sunflower or cocoa butter. Each adipose tissue replica containing cocoa butter was firmer than the replicas formed with sunflower oil. In one embodiment, a replica of adipose tissue made as a stable emulsion of 8S mung bean protein with canola oil is smoother than a replica of adipose tissue made as a stable emulsion of 8S mung bean protein with an equal mixture of coconut, cocoa, olive oil, and palm oils. Adipose tissue replicas can be formed with 1.4 percent w / v 8S mung bean protein with 50 percent, 70 percent, or 90 percent w / v sunflower oil or a mixture of oils. Each adipose tissue replica containing a mixture of oils was firmer than the replicas formed with sunflower oil. In one embodiment, a replica of adipose tissue made as a stable emulsion of soy proteins with sunflower oil is QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 115 softer than a replica of adipose tissue made as a stable emulsion of soy proteins and cocoa butter. Adipose tissue replicas were formed with 0.6 percent, 1.6 percent, or 2.6 percent w / v soy with 50 percent, 70 percent, 80 percent, or 90 percent w / v oil sunflower or oil mixture. Each adipose tissue replica containing a mixture of oils was firmer than the replicas formed with sunflower oil. In some embodiments, adipose tissue replicas comprising 0 percent, 0.18 percent, 1.6 percent, and 2.4 weight / volume percent RuBisCo with 70 percent, 80 percent, and 90 volume percent volume of cocoa butter are solid at room temperature but melt at approximately mouth temperature. In some embodiments, adipose tissue replicas comprising 0.6 percent, 1.6 percent, and 2.6 percent by weight / volume of soybeans with 50 percent, 70 percent, 80 percent, and 90 percent by volume / volume of cocoa butter are solid at room temperature but melt at around mouth temperature. In some embodiments, adipose tissue replicas comprising 8S mung bean protein at 1.4 w / v percent with 50 percent, 70 percent, and 90 v / v percent of an equal mixture of coconut, Cocoa, olive oil, and palm oil are solid at room temperature but fuse at approximately mouth temperature. In one embodiment, the melting temperature of 116 replicas of adipose tissue will be similar to meat fat. In some embodiments the fat replicas comprise oils with a 1:1 ratio of saturated fatty acids to unsaturated fatty acids. In some embodiments, the adipose tissue replica contains equal amounts of cocoa and mango butters. In some embodiments, the adipose tissue replica contains equal amounts of coconut oil, cocoa butter, olive oil and palm oil. In one embodiment, an adipose tissue replica comprising triglycerides and phospholipids will contain a ratio of fatty acids similar to that found in beef (C14:0 at 5 percent w / w, C16:0 at 25 percent). cent, C18:0 0 to 20 percent, C18:1 0 to 60 percent, C18:2 0 to 25 percent, C18:3, 0 to 5 percent, C20:4 0 to 2 percent, and C20 :6 0 to 2 percent). For example, the adipose tissue replica may comprise equal proportions of olive oil, cocoa butter, coconut oil and mango butter. In another example, the adipose tissue replica may comprise equal proportions of olive oil and rice bran oil. In one embodiment, the melting temperature of the adipose tissue replicas will be similar to Wagyu beef fat. In some embodiments the fat replicas comprise oils with a 1:2 ratio of saturated fatty acids to unsaturated fatty acids (for example, 1 part coconut oil to 2 parts sunflower oil). In some embodiments, the tissue replica 117 adipose contains equal amounts of olive oil, rice bran oil, cocoa butter and mango butter. I. CONNECTIVE TISSUE REPLICA Animal connective tissue provides key textural characteristics that are an important component of the meat-eating experience. Accordingly, the present invention provides a composition derived from non-animal sources that recapitulates the key characteristics of animal connective tissue. The present invention further provides a meat substitute product comprising a composition derived from non-animal sources, which recapitulates important textural and visual characteristics of animal connective tissue. Such compositions will be referred to herein as connective tissue replicas. In some embodiments, the connective tissue replica and / or meat substitute product comprising the connective tissue replica are partially derived from animal sources. Animal connective tissue can generally be divided into fascia type and cartilage type tissue. Fascia-type tissue is highly fibrous, resistant against extension (has high elastic modulus), and has a high protein content, a moderate water content (about 50 percent), and low to no fat and polysaccharide content. . Accordingly, the present invention provides a connective tissue replica that recapitulates the key characteristics of fascia-like tissue. In some embodiments, the connective tissue replica comprises approximately 50 percent 118 percent protein by total weight, about 50 percent by liquid weight, and has a low fat and polysaccharide component. The fibrous nature of fascia-type connective tissue is largely composed of collagen fibers. It is observed that the collagen fibers are cable or ribbon-shaped species, from 1 to 20 microns wide. These fibers consist of tightly packed thin collagen fibrils 30 to 100 nanometers thick. These fibrils are also associated into elastic and reticular fibrous networks with individual fibers that can be 200 nanometers thick. In one embodiment, the fascia-like connective tissue replica is composed of a fibrous or fibrous-like structure that may consist of proteins. In some embodiments, the protein content is derived from non-animal sources (for example, a plant source, algae, bacteria or fungi, see, for example, sections IIIA and B). In some embodiments, the isolated proteins represent 50 percent, 60 percent, 70 percent, 80 percent, or 90 percent or more of the protein content by weight. In some embodiments, multiple isolated proteins are isolated and purified separately and represent the total protein content. In fascia-type connective tissue, the prolamin family of proteins, individually or in combinations thereof, demonstrate suitability for the protein component, as they are highly abundant, similar in overall amino acid composition to QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 119 collagen (high fraction of proline and alanine), and susceptible to transformation into films. In some embodiments, prolamin family proteins are selected from the group consisting of zein (found in corn), barley hordein, wheat gliadin, secalin, rye extensins, sorghum caphyrin, or oatmeal avenin. In some embodiments, the isolated and purified protein(s) are zeins. In some embodiments, other proteins can be used to complement prolamins to achieve target specifications for physicochemical and nutritional properties. See list in Sections III A and B, including any major storage seed proteins, animal-derived or recombinant collagen, or extensins (hydroxyproline-rich glycoproteins abundant in cell walls e.g. Arabidopsis thaliana, monomers of which are d flexible rod-like collagen-like molecules). The proteins can be freeze-dried and ground and combined with one or more other ingredients (for example, wheat gluten, fiber such as bamboo fiber, or soy protein isolate). Fibrous or fibrous-like structures can be formed by extrusion. In some embodiments the extrusion is carried out using a Leistritz Nano-16 dual co-rotating axis extruder (American Leistritz Extruder Corp. United States, Sommerville, NJ). Active heating and cooling of the barrel section is used to optimize the mechanical properties, degree of swelling and 120 water content of the fibers. For example, the water content can be adjusted to about 50 percent to make a tough connective tissue replica. The protein feed and liquid are added separately: the protein is fed by a volumetric plunger feeder or a continuous auger feeder, and the liquid can be added into the barrel through a high-pressure liquid injection system. pressure. In some examples, the extrusion parameters were: screw speed of 200 rpm, product temperature at the die of 120°C, feed rate of 2.3 g / min, and water flow rate of 0.7 grams / minute. The temperature of the product in the nozzle during extrusion is measured by a thermocouple. Fibrous or fibrous-like structures can be formed by extrusion through a filament matrix and multiple filaments to produce fibrous structures. In some embodiments, matrices incorporating multiple different sizes of holes in the range of 10 to 300 microns can be used to create replicas of mixed fibrous tissues with precise control over fiber dimensions and compositions. Fibers of different sizes can be incorporated into the compositions to control the properties of the compositions. Electrospinning can be used to create fibers in the range of <1 to 10 microns. In some embodiments, electrospinning is used to create fibers in the diameter range of <1 to 10 microns. For example, a concentrated globulin solution 121 Mung bean (140 milligrams / milliliter) containing 400 mM sodium chloride can be mixed with poly(vinyl alcohol) or poly(ethylene oxide) solution (9 percent weight / volume) to obtain mixed solutions with 22 .5 milligrams / milliliter of mung bean globulin and 6.75 percent weight / volume of the respective polymer. The resulting solution is slowly pumped (for example, at 3 microliters / minute), by a syringe pump, from a 5 milliliter syringe through a Teflon tube and a blunt 21 gauge needle. The needle is connected to a positive terminal of a high voltage supply (e.g. Spellman CZE 30 kV) and fixed 20 to 30 centimeters from a collection electrode. The collection electrode is an aluminum drum (about 12 centimeters long, 5 centimeters in diameter) that is wrapped in aluminum foil. The drum is attached to a shaft which is rotated by an IKA RW20 motor at approximately 600 rpm. The shaft is connected to a ground terminal of the high voltage supply. The protein / polymer fibers are accumulated on aluminum foil and, once electrospinning is completed, they are removed from the foil and added to the tissue replicas. The dimension and composition of the fibers produced by the methods of the invention have an effect on the flavor, texture and mechanical properties of the fabric replicas. Tissues comprising between 1 and 50 percent of fibers in the range of <1 to 10 microns, and between 10 and 50 percent of fibers in the range of 10 to 300 microns most closely approximate connective tissues. 122 of the animals in terms of taste, mouthfeel and mechanical properties. Cartilage-type tissue is macroscopically homogeneous, resistant to compression, has higher water content (up to 80 percent), lower protein (collagen) content, and higher polysaccharide (proteoglycan) contents (about 10 percent each). ). Compositionally, cartilage-type connective tissue replicas are similar to fascia-type ejido replicas with the relative proportions of each adjusted to more closely mimic meat connective tissue. During extrusion, the water content can be adjusted to about 60 percent to make a soft connective tissue replica. Methods for the formation of cartilage-type connective tissue are similar to those for fascia-type connective tissue, but methods that produce isotropic non-fibrous gels are preferred. A connective tissue replica can be made by isolating and purifying one or more proteins; and precipitating the protein(s), wherein the precipitate results in the protein(s) forming physical structures that approximate the physical organization of connective tissue. The precipitate may comprise the solubilization of the protein(s) in a first solution; and extruding the first solution into a second solution, wherein the protein(s) are insoluble in the second solution, wherein extrusion induces precipitation of the protein(s). 123 In some embodiments some or all of the components of the consumable are suspended in a gel (e.g., a protein gel). In various embodiments, the gel may be a hydrogel, an organogel, or a xerogel. The gel can be thickened using a polysaccharide or protein based agent. For example, starch, arrowroot, corn starch, Katakuri starch, potato starch, sago, tapioca, alginin, guar gum, locust bean gum, xanthan gum, collagen, egg whites, furcellaran, gelatin, agar, can be used. carrageenan, cellulose, methylcellulose, hydroxymethylcellulose, acadia gum, konjac, starch, pectin, amylopectin or proteins derived from legumes, grains, nuts, other seeds, leaves, algae, bacteria, or fungi alone or in combination to thicken the gel, forming an architecture or structure for the consumable. Enzymes that catalyze reactions leading to covalent cross-links between proteins can also be used alone or in combination to form an architecture or structure for the consumable. For example, transglutaminase, tyrosinases, lysyl oxidases, or other amino oxidases (e.g., Pichia pastoris lysyl oxidase (PPLO)) can be used alone or in combination to form an architecture or structure for the consumable by cross-linking the component proteins. In some embodiments, multiple gels with different components are combined to form the consumable. For example, a gel containing a protein of plant origin can be associated with a gel containing a fat of plant origin. In some embodiments, the protein fibers or ropes QQCI I n / l 7Π7 / Β / ΥΙΛΙ 124 are oriented parallel to each other and are then held in place by applying a gel containing plant-based fats. The compositions of the invention may be swollen 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. technique. In some embodiments, multiple gels with different components are combined to form the consumable. For example, a gel containing a protein of plant origin can be associated with a gel containing a fat of plant origin. In some embodiments the protein fibers or ropes are oriented parallel to each other and then held in place by the application of a gel containing plant-based fats. J. OMISSIONS FROM THE COMPOSITIONS Because the consumable can be created from defined ingredients, which can in turn be isolated and purified, it is possible to produce consumables that do not contain certain components. This, in some cases, allows the production of consumables lacking ingredients that may be undesirable to consumers (for example, proteins to which some humans are allergic may be omitted or added). In some embodiments, the consumable does not contain 125 no animal products. In some embodiments the consumable contains no or less than 1 percent wheat gluten. In some embodiments the consumable does not contain methylcellulose. In some embodiments the consumable does not contain carrageenan. In some embodiments the consumable does not contain any candy color. In some embodiments the consumable does not contain konjac flour. In some embodiments the consumable does not contain gum arabic (also known as acacia gum). In some embodiments, the consumable does not contain wheat gluten. In some embodiments the consumable does not contain isolated soy protein. In some embodiments the consumable does not contain tofu. In some embodiments the consumable contains less than 5 percent carbohydrates. In some embodiments, the consumable contains less than 1 percent cellulose. In some embodiments the consumable contains less than 5 percent cellulose. In some embodiments the consumable contains less than 5 percent insoluble carbohydrates. In some embodiments the consumable contains less than 1 percent insoluble carbohydrates. In some embodiments the consumable does not contain any artificial colors. In some embodiments, the consumable does not contain artificial flavorings. In some embodiments, the consumable contains one or more of the following characteristics: no animal products; without methylcellulose; without carrageenan; no konjac flour; without Arabic gum; less than 1 percent wheat gluten; wheat gluten free; without QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 126 tofu; about 5 percent carbohydrates; less than 5 percent cellulose; less than 5 percent insoluble carbohydrates; less than 1 percent insoluble carbohydrates; non-edible colorants such as caramel color, paprika, cinnamon, beet color, carrot oil, tomato lycopene extract, raspberry powder, carmine, cochineal extract, annatto, turmeric, saffron, FD&C Red number 3, yellow number 5, Yellow number 6., Green number 3, Blue number.2, Blue number 1, Violet number 1, FD & C Red number 40 - allura red AC, and / or E129 (red tone); and / or no artificial scent. In some embodiments the consumable does not contain isolated soy protein. In other embodiments, the consumable does not contain soy protein or protein concentrate. In some embodiments, the muscle tissue replica further contains less than 10 percent, less than 5 percent, less than 1 percent, or less than 0.1 percent wheat gluten. In some embodiments, the muscle tissue replica does not contain wheat gluten. IV. Combinations of components A. MEAT REPLICAS A meat substitute product (alternatively a meat replica) may comprise the compositions described herein. For example, a meat replica may comprise a muscle replica; a replica of fatty tissue; and a replica of connective tissue (or a sub-combination thereof). The replica QQCI I Π / I 7Π7 / Ε / ΥΙΛΙ 127 muscle, adipose tissue replica, and / or connective tissue replica can be assembled in a way that approximates the physical organization of meat. In some embodiments, a binding agent such as a coacervate is used to assist in binding the replicas to each other. The percentage of the different components can also be controlled. For example, non-animal substitutes for muscle, adipose tissue, connective tissue, and blood components can be combined in different proportions and physical organizations to better approximate the appearance of meat. The various components can be arranged to ensure consistency between bites of consumables. The components may be arranged to ensure that no consumable waste is generated. For example, while a traditional cut of meat may have parts that are not typically eaten, a replica meat may improve upon meat by not including these inedible parts (e.g., bone, cartilage, connective tissue, or other materials). commonly known as cartilage). Such an improvement allows all product made or shipped to be consumed, reducing waste and shipping costs. Alternatively, a meat replica may include inedible parts to mimic the experience of eating meat. Such parts may include bone, cartilage, connective tissue, or other materials commonly known as cartilage, or materials included simulating these components. In some embodiments, the 128 consumable may contain simulated inedible parts of meat products that are designed to serve secondary functions. For example, a simulated bone can be designed to disperse heat during cooking, making the consumable cook faster or more uniformly than meat. In other embodiments, a simulated bone can also serve to keep the consumable at a constant temperature during shipping. In other embodiments, the simulated inedible portions may be biodegradable (e.g., a biodegradable plastic). In some embodiments, a meat substitute composition comprises between 10 to 30 percent protein, between 5 to 80 percent water, and between 5 to 70 percent fat, wherein the composition includes one or more proteins. isolated and purified. Such a meat substitute may not include any animal protein. In some embodiments, meat substitute compositions comprise transglutaminase. In some embodiments, a meat substitute product includes a muscle replica, an adipose tissue replica, and a connective tissue replica, where the muscle replicas count for 40 to 90 percent of the product by weight, the replicas Adipose tissue counts for 1 to 60 percent of the product by weight, and connective tissue replicas count for 1 to 30 percent of the product by weight. In some embodiments, the meat substitute product comprises 60 to 90 percent water; 5 to 30 percent of QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 129 protein content; and 1 to 20 percent of a fat; wherein the protein content comprises one or more proteins isolated and purified from the plant. In some embodiments the consumable contains components to replicate the components of meat. The main component of meat is typically skeletal muscle. Skeletal muscle typically consists of approximately 75 percent water, 19 percent protein, 2.5 percent intramuscular fat, 1.2 percent carbohydrates, and 2.3 percent other soluble nonprotein 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 a replication of approximations of this composition for the consumable. For example, in some embodiments, the consumable is a plant-based meat replica comprising approximately 75 percent water, 19 percent protein, 2.5 percent fat, 1.2 percent carbohydrates; and 2.3 percent other soluble non-protein substances. In some embodiments the consumable is a plant-based meat replica comprising 60 to 90 percent water, 10 to 30 percent protein, 1 to 20 percent fat, 0.1 to 5 percent carbohydrates; and 1 to 10 percent other soluble nonprotein substances. In some embodiments the consumable is a plant-based meat replica that QQCI I n / l 7Π7 / Β / ΥΙΛΙ 130 comprises between 60 to 90 percent water, 5 to 10 percent protein, 1 to 20 percent fat, 0.1 to 5 percent carbohydrates; and 1 to 10 percent other soluble non-protein substances. In some embodiments the consumable is a plant-based meat replica comprising 0 to 50 percent water, 5 to 30 percent protein, 20 to 80 percent fat, 0.1 to 5 percent of carbohydrates; and 1 to 10 percent of other soluble nonprotein substances. In some embodiments, a meat replica contains between 0.01 percent and 5 percent by weight of a heme-containing protein. In some embodiments, the replica contains between 0.01 percent and 5 weight percent leghemoglobin. Some meat also contains myoglobin, a heme-containing protein, which accounts for most of the red color and iron contained in some meat. It is understood that these percentages can vary in meat and meat replicas can be produced to approximate the natural variation in meat. In embodiments that include a heme-containing protein and optional flavors, k-carrageenan can be used to absorb some of the contributed liquid from the flavor and heme solution so that the ground tissue is not excessively wet. During the addition of the heme and flavor mixture solution the k-carrageenan powder is evenly distributed over the tissue mixture to ensure homogeneity in the final ground product. It will be appreciated that when proteins are supplied as QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 131 a solution, water removal techniques, such as I i of i I i zation or spray drying, can optionally be used to concentrate the protein. The proteins can then be reconstituted in an amount of liquid that prevents the ground tissue from being too wet. Furthermore, in some cases, the present invention provides improvements to meat replicas, which comprise these components in unnatural percentages. The concentration of heme-containing protein is an important determinant of meat flavor and aroma. So, for example, a replica meat could have a higher heme protein content than typical meat. For example, a replica meat can be produced with a higher fat content than the typical average. The percentages of these components can also be altered to increase other desirable properties. In some cases a replica meat is designed so that when cooked, the component percentages are similar to cooked meat. Thus, in some embodiments, the uncooked consumable has different percentages of the components than uncooked meat, but when cooked, the consumable is similar to cooked meat. For example, a meat replica can be made with a higher water content than is typical for raw meat, but when cooked in a microwave oven, the resulting product has non-starch polysaccharides such as arabinoxylans, cellulose, and many others. components of 132 plant, such as resistant starch, resistant dextrins, inulin, lignin, waxes, chitins, pectins, beta-glucans, and oligosaccharide percentages of fire-cooked meat-like components. In some embodiments, the consumable is a replica of meat with a lower water content than typical for meat. In some embodiments the inventions provide methods for hydrating a meat replica to make the meat replica have a similar water content to meat. For example, a meat replica with a water content that would be low for meat, for example 1 percent, 10 percent, 20 percent, 30 percent, 40 percent, or 50 percent water, can be hydrated. to about 75 percent water. Once hydrated, in some embodiments, the meat replica is cooked for human consumption. The consumable may have a protein component. In some embodiments, the protein content of the consumable is 10 percent, 20 percent, 30 percent, or 40 percent. In some embodiments, the protein content of the consumable is similar to meat. In some embodiments, the protein content in the consumable is greater than that of the meat. In some embodiments, the consumable has less protein than meat. The protein in the consumable can come from a variety or combination of sources. Non-animal sources may provide some or all of the protein in the consumable. The 133 Non-animal sources may include vegetables, non-food biomass such as carrot and Miscanthus leaves, sea grasses, fruits, nuts, grains, algae, bacteria or fungi. See, for example, Sections III A and B. The protein may be isolated or concentrated from one or more of these sources. In some embodiments, the consumable is a meat replica comprising only proteins obtained from non-animal sources. In some embodiments the protein is formed into asymmetric fibers for incorporation into the consumable. In some embodiments these fibers replicate muscle fibers. In some embodiments, the proteins are centrifuged fibers. Accordingly, the present invention provides methods for producing spun or asymmetric protein fibers. In some embodiments the consumable contains a protein or proteins that have all of the amino acids found in the proteins that are essential for human nutrition. In some embodiments, the proteins added to the consumable are complemented with amino acids. Physical organization may be a determinant of the meat substitute's response to cooking. For example, the flavor of meat is modified by the size of the particles. Ground beef that has been reduced to a paste offers different flavors than more raw ground beef during cooking. The ability to control the relative size and orientation of individual tissue replicas allows the flavor and aroma profile of the consumables to be modified during cooking. For example, the 134 muscle tissue replicas and adipose tissue replicas provide different flavor profiles when cooked independently or when mixed. It was also observed that the changes in the flavor profile are based on the method by which the different tissue replicas are mixed. The physical organization of the meat substitute product can be manipulated by controlling the location, organization, assembly, or orientation of the muscles, fat and / or connective tissue replicas described herein. In some embodiments, the product is designed such that the replicas described herein are associated with each other as in meat. In some embodiments, the consumable is designed so that after cooking the replicas described herein are associated with each other as in cooked meat. The characteristic flavor and fragrance components of meat are mainly produced during the cooking process by chemical reactions, the substrates for which are amino acids, fats and sugars found in plants, as well as meat. Therefore, in some embodiments, similarity of the consumable to meat is proven during or after cooking. In some embodiments, human ratings, human evaluations, olfactometer readings or GCMS measurements, or combinations thereof, are used to create an olfactory map of cooked meat. Similarly, an olfactory map of the consumable, for example a meat replica, can be created. These maps qqci i η / ι ζηζ / Ε / γ 135 can be compared to evaluate the similarity of the consumable with cooked meat. In some embodiments the olfactory map of the consumable during or after cooking is similar or indistinguishable from that of cooked or cooking meat. In some modalities, the differences are small enough to be below the detection threshold of human perception. In some embodiments the individual tissue replicas are assembled into layers, sheets, blocks and ropes in defined positions and orientations. In some embodiments, the replicas are combined in the process of passing through the plates of a meat grinder with the holes set to less than 1 / 2 inch (e.g., % inch). The mill offers multiple functions for particle size reduction, providing additional mixing or working and forming the material into cylindrical portions as is typically done for ground beef. During assembly, milling, and forming, it is important to keep replica tissues cold (e.g., 4 to 15°C) to control microbial growth, limit flavor reactions, and also to maintain adipose tissue in a solid state. in such a way that discrete pieces of adipose tissue are maintained throughout the grinding process. Before milling, replica tissues are usually divided in some way to a defined particle size. QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 136 For example, in some embodiments, individual tissue replicas may be formed into small pieces of less than 1 centimeter in diameter or less than 5 mm in diameter prior to combination with the other tissue replicas. Adipose tissue can be broken down into particles of about 3 to 7 millimeters. This is important both for the appearance of the final material and the fat release behavior during cooking. This size range allows for a natural appearance of flecks of adipose tissue in the final raw product. If the fatty tissues are too small (for example, less than 2 mm), there will be an insufficient amount of fat will be released from the product when it is cooked. Soft replicas of connective tissue can be divided into pieces about 1 to 3 mm long with irregular edges. If the pieces are too large (for example, larger than about 4 mm), the texture of the final product may be too small and round. Sticky tissue or noodle replicas, composed of pieces of amorphous or long noodle-like tissue replicas, respectively, and raw tissue replicas can be manually divided into pieces about 1 to 3 centimeters in diameter. Achieving particles in this size range allows for proper mixing and proper homogeneity in the final ground material. In some embodiments, the hard connective tissue replicas qqci i η / ι ζηζ / Ε / γ can be cut at three levels, (e.g., thick, 137 intermediate, and fine). Cutting on three levels provides a greater amount of heterogeneity than a single-step cutting process, and makes the mouthfeel of the final product more similar to ground beef. In formulations that contain gluten, an additional function to grinding foods is to work the gluten and develop a gluten network of aligned gluten molecules. For gluten-containing formulations it is important to minimize the interaction of adipose tissue with the gluten network. This is done by cold layering the adipose tissue replicates and the ground tissue replicates prior to combining and also minimizing the amount of handling after the adipose tissue is added. Over working the adipose tissue replicates in the gluten breaks down or shortens the gluten network. Finally, for gluten-containing formulations, the patties are allowed to rest at room temperature for 30 minutes or overnight at 4°C before cooking. This allows time for the gluten network to relax, giving a better overall texture. In some embodiments, the connective tissue replica is incorporated into the protein solution prior to formation of the muscle tissue replica. In some modalities, the connective tissue replica is QQCI I n / l 7Π7 / Β / ΥΙΛΙ incorporates directly into the emulsion prior to the formation of the adipose tissue replica. 138 In some embodiments, the adipose tissue replica is added to the muscle tissue replica in strands and sheets to replicate the marbling or bacon effect. Mixed meat tissue replicas can enhance the sense of flavors, such flavors including, but not limited to, various flavoring compounds associated with fruity / green bean / metallic, nutty / green, peanut butter / musty, raw / roasted potato / earthy, vinegary, spicy / caramel / almond, creamy, sweet, fruity / stale beer, moist / nutty / coumarin / licorice / walnut / bread, coconut / woody / sweet, pungent / icky, minty, or toasted caramel aromas . In some modalities, the mixed meat replicas increase the presence of volatile odorous substances, such as 2-pentylfuran; 4-methylthiazole; ethyl-pyrazine, 2,3-dimethyl-pyrazine, acetic acid; 5-methyl-2-furan-carboxaldehyde; butyrolactone; 2,5-dimethyl-3-(3-methylb u t i I) - p i raz i na; 2-cyclopenten-1-one, 2-hydroxy-3-methyl; 3-acetyl-1Hpyrrole; pantolactone; 1-methy 1-1(H)-pyrrole-2,2-carboxaldehyde; caprolactam; 2,3-dihydro-3,5-dihydroxi-6-methyl-4-(H)-pyran-4-one. In some embodiments, off-flavors, including, but not limited to, gasoline-like, petroleum, sour / putrid / fishy, ​​bland / woody / yogurt, fatty / honey / citrus, spicy / sweet / caramel, and green walnut / burned, they form only in individual tissue replicates, but do not accumulate in mixed meat replicates. In some embodiments, individual tissue replicas increase the presence of volatile odors, including, but not QQCI I n / l 7Π7 / Β / Υ 139 limited to, nonane, 2,6-dimethyl, 3-methyl-3-hexene; pyridine; acetoin; octanal; 1-hydroxy-2-propanone; and / or ethenyl-pyrazine. In some embodiments, the levels to which all of the above compounds accumulate during cooking depend on the sizes of the tissue replica units and the way they are mixed (coarse, fine, or mixed). In some embodiments, the mixed meat tissue replicas enhance the sensation of flavors, including, but not limited to, multiple aroma compounds associated with fruity / green bean / metallic, nutty / green, peanut butter / moist, raw potato flavor. / roasted / earthy, vinegary / caramel / almond, creamy, sweet, fruity / stale beer, dank / nutty / coumarin / licorice / walnut / bready, coconut / woody / sweet, penetrating / icky, minty, or toasted caramel aromas . In some embodiments, mixed meat replicas increase the presence of volatile odors, including, but not limited to, phenylacetaldehyde, 1-octen-3-one, 2-n-heptyl-furan, 2-thiophen-carboxaldehyde, 3-thiophen -carboxaldehyde, butyrolactone, 2-undecenal, methyl-pyrazine, furfural, 2-decanone, pyrrole, 1-octen-3-ol, 2-acetyl-thiazole, (E)-2-octenal, decanal, benzaldehyde, (E) -2-nonenal, pyrazine, 1-hexanol, 1-heptanol, dimethyl trisulfide, 2-nonanone, 2-pentanone, 2-heptanone, 2,3butanedione, heptanal, nonanal, 2-octanone, 1-octanol, 3-ethylcyclopentanone , 3-octen-2-one, (E,E)-2,4-heptadienal, (Z)-2-heptenal, 2-heptanone, 6-methyl-(Z)-4-heptenal, (E,Z) -2,6-nonadienal, 3-methyl-2butenal, 2-pentyl-furan, thiazole, (E,E)-2,4-decadienal, acid QQCI I n / l 7Π7 / Β / ΥΙΛΙ 140 hexanoic, 1 -ethyl-5-methyl-cyclopentene, (E,E)-2,4-nonadíenal, (Z)-2decenal, dihydro-5-pentyl-2(3H)-furanone, trans-3- nonen-2-one, (E,E)3,5-octadien-2-one, (Z)-2-octen-1 -ol, 5-ethyl-dihydro-2(3H)-furanone, 2butenal, 1 -penten-3-ol, (E)-2-hexenal, formic acid, heptyl ester, 2pentylthiophene, (Z) -2-nonenal, 2-hexylthiophene, (E)-2-decenal, 2 -ethyl-5methyl-pyrazine, 3-ethyl-2,5-dimethyl-pyrazine, 2-ethyl-1-hexanol, thiophene, 2-methylfuran, pyridine, butanal, 2-ethylfuran, 3-methyl -butanal, trichloromethane, 2-methyl-butanal, methacrolein, 2-methyl-propanal, propanal, acetaldehyde, 2-propyl-furan, dihydro-5-propyl-2(3H)-furanone, 1,3hexadiene, 4- decino, 1-propanol, pentanal, heptanoic acid, trimethylethanethiol, 1-butanol, 1-penten-3-one, dimethyl sulfide, 2-ethylfuran, 2-pentylthiophene, 2-propenal, 2-tridecen-1-ol , 4-octene, thiazol2-methyl, methyl-pyrazine, 2-butanone, 2-pentyl-furan, 2-methylpropanal, butyrolactone, 3-methyl-butanal, methyl-thiirane, 2-hexyl-furan, butanal, 2-methyl -butanal, 2-methyl-furan, furan, octanal, 2-heptenal, 1-octene, heptyl ester of formic acid, 3-pentyl-furan, and 4-penten-2ene. In some embodiments, the levels to which all of the above compounds accumulate during cooking depend on the sizes of the tissue units and the manner in which they are mixed (coarse, fine, or mixed). The production of volatile odorous substances can be enhanced when adipose, muscle and connective tissue replicas are in contact with each other. In some embodiments, the production of volatile odorous substances is enhanced when replicas of adipose tissue, muscle and connective tissues are QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 141 mixed intimately with an average size of individual tissue replicas of 5 millimeters. In some embodiments, the production of volatile odorants is enhanced when replicates of fat, muscle, and connective tissues are intimately mixed with an average size of individual tissue replicates of 2 millimeters. In some embodiments, such volatile odorant production is enhanced when the fat, muscle, and connective tissue replicates are intimately mixed with an average size of individual tissue replicates of 1 millimeter. In some embodiments, the meat substitute is optimized for the particular cooking methods (optimized for cooking in a microwave oven, or optimized for cooking in a stew). In some embodiments, the meat substitute is optimized for dehydration. In some embodiments, said meat substitute is optimized for rapid rehydration upon exposure of the jerky meat replica to water. In some embodiments, said meat substitute is optimized for use as pop-up, camping or astronaut food. The methods described herein can be used to provide replica meat with defined cooking characteristics to enable the production of replica meats that are optimized for particular cooking techniques. For example, QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 142 casseroles that require slow cooking to gelatinize the connective tissue of the meat, while replica meats can be designed where the connective tissue replica gelatinizes more easily thus allowing casseroles to be prepared quickly. B. MEAT COOKING INDICATORS The consumable may include compositions that may indicate that the consumable is for cooking or that it is cooking. The release of odors in the kitchen is an important aspect of meat consumption. In some embodiments, the consumable is a replica of meat entirely composed of non-animal products that when cooked generates an aroma recognizable to humans as typical of cooking beef. In some embodiments, the consumable when cooked generates an aroma recognizable to humans as typical of cooking pork, bacon, chicken, lamb, fish, or turkey. In some embodiments, the consumable is a replica of meat primarily, or entirely composed of ingredients derived from non-animal sources, with an odorant that is released in cooking or produced by chemical reactions that take place in cooking. In some modalities the consumable is a replica of meat mainly 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 allow these compounds to undergo to chemical reactions that produce odors and carbon compounds during cooking. QQCI I n / l 7Π7 / Β / Υ 143 flavor. In some embodiments, the consumable is a replica of meat primarily, or entirely composed of ingredients derived from non-animal sources, with a volatile or labile odorant released during cooking. In some embodiments, the indicator is a visual indicator that accurately mimics the color transition of a meat product during cooking progression. The color transition can be, for example, from red to brown, from pink to white or brown, or from a translucent to opaque color during the progression of firing. In some embodiments, the indicator is an olfactory indicator that indicates the cooking progression. In one embodiment, the olfactory indicator is one or more volatile odorants released during cooking. In some embodiments, the indicator comprises one or more isolated and purified iron-containing proteins. In some embodiments, the isolated and purified iron-containing protein(s) (eg, a heme-containing protein, see section III B) is in a reduced state prior to cooking. In some embodiments, the isolated and purified iron-containing protein(s) carried in a reduced or oxidized state have a similar UV-VIS profile to a myoglobin protein derived from an animal source which when in an equivalent reduced state or oxidized state. Hemoglobin Aquifex aeolicus has a maximum absorbance wavelength at 413 QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 144 nanometers; Methylacidiphilum infernorum hemoglobin has a maximum absorbance wavelength at 412 nanometers; Glycine max leghemoglobin has a maximum absorbance wavelength at 415 nanometers; The non-symbiotic Hordeum vulgare and Vigna radiata hemoglobins each have a maximum absorbance wavelength at 412 nanometers. Bos taurus myoglobin has a maximum absorbance wavelength at 415 nanometers. In some embodiments, the difference between the maximum absorbency wavelength of the isolated and purified iron-containing protein(s) and the maximum absorbency wavelength of myoglobin derived from an animal source is less than 5 percent. The odorants released during cooking of meat are generated by reactions that may involve fats, proteins, amino acids, peptides, nucleotides, organic acids, sulfur compounds, sugars and other carbohydrates as reactants. In some embodiments, the odorants that combine during cooking of the meat are identified and located near each other in the consumable, so that after cooking of the consumable the odors combine. Thus, in some embodiments, 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. Thus, in some embodiments, the components qqci i η / ι ζηζ / Ε / γ 145 characteristic flavor and fragrance are produced primarily 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 as in meat. Some reactions that generate odors released during cooking of meat can be catalyzed by iron, in particular the heme iron of myoglobin. Thus, in some embodiments, some of the characteristic flavor and fragrance components are produced during the cooking process by iron-catalyzed chemical reactions. In some embodiments, some of the characteristic flavor and fragrance components are produced during the cooking process by heme-catalyzed chemical reactions. In some embodiments, some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by heme iron in leghemoglobin. In some embodiments, some of the characteristic flavor and fragrance components are produced during the cooking process by chemical reactions catalyzed by heme iron in a heme protein. For example, hemoproteins (e.g., from Aquifex aeolicusm, Methylacidiphilum infernorum, Glycine max, Hordeum vulgare, or Vigna radiata) provide a significantly different profile of volatile odorants when heated in the presence of cysteine ​​and glucose than any subset of the three. components when QQCI I n / l 7Π7 / Β / Υ 146 are analyzed by GC-MS. Volatile flavor components that increase under these conditions include, but are not limited to, furan, acetone, thiazole, furfural, benzaldehyde, 2-pyridinecarboxaldehyde, 5-methyl-2-thiophen-carboxaldehyde, 3-methyl-2-thiophencarboxaldehyde, 3-thiophen-methanol and decanol. Under these conditions, cysteine ​​and glucose alone or in the presence of iron salts such as ferrous glucanate produced a sulfurous odor, but the addition of heme proteins reduced the sulfurous odor and replaced it with flavors including, but not limited to, broth. chicken, burnt mushroom, molasses, and bread. Additionally, a hemoprotein (e.g., from Aquifex aeolicus, Methylacidiphilum infernorum, Glycine max, Hordeum vulgare, or Vigna radiata) when heated in the presence of ground chicken increased specific volatile odorants that are elevated compared to chicken meat when analyzed by GC-MS. Volatile flavor components that increase under these conditions include, but are not limited to, propanal, butanal, 2-ethylfuran, heptanal, octanal, trans-2-(2-pentenyl)furan, (Z)-2-heptenal (E )-2-octenal pyrrole, 2,4-dodecadienal, 1-octanal, or (Z)-2-decenal 2undecenal. C. COLOR INDICATORS Meat color is an important part of the experience of cooking and eating meat. For example, cuts of meat are a characteristic red color when raw and gradually transition to a brown color during cooking. As another example, meats qqci i η / ι ζηζ / Ε / γ White vegetables such as chicken or pork have a distinctive pink color when raw and gradually transition to white or brown during cooking. The amount of color transition is used to indicate the progression of beef cooking and to assess cooking time and temperature to produce the desired state of doneness. In some aspects, the invention provides a non-meat based meat substitute product that provides a visual indicator of cooking progression. In some embodiments, the visual indicator is a colored indicator that undergoes a color transition during cooking. In some embodiments, the color indicator recapitulates the color transition of a cut of meat as the meat progresses from a raw state to a cooked state. In further embodiments, the color indicator colors the meat substitute product a red color prior to cooking to indicate a natural state and causes the meat substitute product to transition to a brown color during the cooking progression. In other embodiments, the color indicator colors the meat substitute product a pink color prior to cooking to indicate a natural state and causes the meat substitute product to transition to a white or brown color during the cooking progression. The main determinant of the nutritional definition of meat color is the concentration of iron carrying proteins in the meat. In the skeletal muscle component of meat products, one of the major iron-carrying proteins is qqci i η / ι ζηζ / Ε / γ 148 myoglobin. As described above, myoglobin content varies from below 0.05 percent in white meat chicken to 1.5 to 2.0 percent in old meat. Thus, in some embodiments, the consumable is a meat replica comprising an iron transport protein (e.g., a heme-containing protein). In some embodiments, the meat replica comprises about 0.05 percent, about 0.1 percent, about 0.2 percent, about 0.3 percent, about 0.4 percent, about 0.5 percent, about 0.6 percent, about 0.7 percent, about 0.8 percent, about 0.9 percent, about 1 percent, about 1.1 percent, about 1.2 percent, about 1.3 percent, about 1.4 percent, about 1.5 percent, about 1.6 percent, about 1.7 percent, about 1.8 percent, about 1.9 percent, about 2 percent, or more than about 2 percent of a protein iron transport (e.g., a heme-containing protein) on a dry weight or total weight basis. In some cases, the iron transport protein has been isolated and purified from a source. In other cases, the iron transport protein has not been isolated and purified. In some cases, the source of the iron transport protein is an animal source, or a non-animal source such as a plant, QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 149 fungus, or genetically modified organisms, such as, for example, plants, algae, bacteria or fungi. In some cases, the iron transport protein is myoglobin. In some embodiments the consumable is a plant-based meat replica that has added animal myoglobin. So, for example, a replica of young beef may have about 0.4 to 1 percent myoglobin. In some embodiments the consumable is a plant-based meat replica that has an added leghemoglobin or cytochrome. So, for example, a replica of young beef may have about 0.4 to 1 percent leghemoglobin or cytochrome. Another example of iron-carrying proteins is hemoglobin, the iron-containing oxygen-binding protein in the red blood cells of vertebrates. Hemoglobin is similar in color to myoglobin. In some embodiments, the invention provides methods of saving and recycling blood from animal husbandry to complement the color of a consumable. For example, blood is saved from a slaughterhouse, and the hemoglobin in the blood is used to enhance the color of a consumable. In some respects the consumable is a meat replica made from plants containing hemoglobin. Additionally, there are proteins that contain iron that are found in nature. In some embodiments the consumable comprises an iron-containing protein that is not myoglobin. In some embodiments the consumable does not contain myoglobin. In 150 some modalities the consumable does not contain hemoglobin. In some embodiments the consumable is a meat replica comprising an iron protein containing a protein other than myoglobin or hemoglobin. See, for example, Section III B for examples of heme-containing proteins, as well as Figure 3. For example, in some embodiments, the consumable comprises a hemoprotein (e.g., a hemoglobin, myoglobin, neuroglobin, cytoglobin, leghemoglobin, nonsymbiotic hemoglobin, hell's gate globin 1, bacterial hemoglobin, ciliated myoglobin, or a flavohemoglobin). Leghemoglobin, similar in structure and physical properties to myoglobin, is readily available as an unused byproduct of legume feedstock crops (e.g., soybeans or peas). The leghemoglobin in the roots of these crops in the United States exceeds the myoglobin content of all red meat consumed in the United States. In some embodiments, the consumable is a meat replica primarily, or entirely composed of ingredients derived from non-animal sources, and containing a heme protein (e.g., a leghemoglobin or a member of the globin family of proteins). For example, a meat replica may be primarily or entirely composed of ingredients derived from non-animal sources, including a muscle tissue replica, a QQCI I n / l 7Π7 / Β / ΥΙΛΙ 151 adipose tissue, a replica of connective tissue, and a heme protein. In some embodiments, the consumable is a primarily meat replica, or entirely composed of ingredients derived from non-animal sources, with a high iron content of a heme protein. In some embodiments, the iron content is similar to meat. In some embodiments, the consumable has the characteristic red color of meat, such color being provided by leghemoglobin. A heme protein (e.g., a heme-containing protein described in Section III B) may be used as an indicator that the consumable has completed cooking. Thus, one embodiment of the invention is a method for cooking a consumable that comprises 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 that comprises detecting the color change from red to brown starting when the product is cooked. In some embodiments, increased shelf life is provided by an extension of the shelf life of the desired red color of the food products (e.g., a non-meat-based meat substitute). In one embodiment, this invention provides hemoproteins that provide a desired color to non-meat meat substitutes. In some embodiments, hemoproteins are derived from a non-animal source such as a plant, fungus, or organisms. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 152 genetically modified, such as, for example, plants, algae, bacteria or fungi. See, for example, section III B. In some embodiments, the shelf life of hemoproteins is extended by treatment with meat shelf life extenders. In some embodiments, the meat shelf life extenders are selected from a group consisting of carbon monoxide, nitrites, sodium metabisulfite, Bombal, rosemary extract, green tea extract, catechins and other antioxidants. In one embodiment, this invention provides hemoproteins that provide desired flavor profiles to food products (e.g., non-meat meat substitutes). In some embodiments, the ability of hemoproteins to generate the desired flavor profile is similar to that of myoglobin. In some embodiments, the lifetime of the hemoproteins' ability to generate the desired flavor profile is greater than that of myoglobin by 10 percent, 20 percent, 30 percent, 50 percent, or 100 percent or further. D. FOOD PRODUCTS COMPRISING PURIFIED AND ISOLATED HEME PROTEINS In some embodiments, heme proteins described herein are added to the meat or a consumable described herein to improve the properties of the meat or consumable. For example, a heme protein containing solution can be injected into raw meat (e.g. raw white meat) or cooked meat to improve the organoleptic properties of the meat during cooking. QQCI I n / l 7Π7 / Β / ΥΙΛΙ 153 cooking adding a meaty flavor (for example, for white meats such as chicken). In another example, a heme protein solution may be dripped onto the meat or a consumable of the invention to improve appearance. In one embodiment, advertising, photography or videography of food products such as meat or a meat substitute can be enhanced with a heme protein. In another embodiment, a heme protein is added to the consumable as an iron supplement. In one application of the invention, hemoproteins can be used as food colorants. In one embodiment, heme proteins can be used as a safe digestible replacement for FD&C Red number. 40 - Red Allura AC, E129 (red tone) in a variety of applications. A non-limiting list of such potential uses would include taking photos, especially in forms such as body paint or as theatrical gore. In some embodiments, the present invention provides methods for obtaining hemoproteins (e.g., leghemoglobin) from a plant. Leghemoglobin can be obtained from a variety of plants. Several legume species and their varieties (for example, soybeans, fava beans, lima beans, cowpeas, English peas, yellow peas, lupine, beans, chickpeas, peanuts, alfalfa, hay pea, clover, Lespedeza or pinto beans) contain nitrogen fixers in root nodules in which leghemoglobin plays a key role in controlling 154 oxygen concentrations (for example, root nodules of a pea plant). In one embodiment the leghemoglobin protein is purified from root nodules of leguminous plants (for example, soybeans, beans or peas), using ion exchange chromatography. In one embodiment, leghemoglobin is purified from root nodules of soybeans, peas, fava beans, or sweet beans. Plants can be grown using standard agricultural methods, except that, in some cases, fertilizer is not applied and the soil is enriched in natural nitrogen-fixing bacteria of the genus Rhizobium. Either whole roots or root nodules can be harvested and used, for example in 20 mM potassium phosphate, pH 7.4, 100 mM potassium chloride, 5 mM EDTA using a grinder-mixer. During this process, leghemoglobin is released into the regulator. Used root nodules containing leghemoglobin can be cleaned of cellular debris by filtration through a 5pm filter. In some embodiments, filtration is followed by centrifugation (7000g, 20 minutes). The clarified waste containing leghemoglobin is filtered through the 200 nanometer filter and applied onto the anion exchange chromatography column (High Prep Q; High Prep DEAE, GE Healthtcare) in a fast liquid protein chromatography (GE) machine. Healthcare). Leghemoglobin is collected in the flow-through fraction and concentrated on 3kDa filtration membrane to a desired concentration. The QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 155 purity (partial abundance) of purified leghemoglobin was analyzed by SDS-PAGE gel electrophoresis: in leghemoglobin the lysate is present in 20 to 40 percent, while after anion exchange purification it is present in 70 to 80 percent. In another embodiment, the flow of soy leghemoglobin through anion exchange chromatography is applied over size exclusion chromatography (Sephacryl S100 HR, GE Healthcare). Soybean leghemoglobin was eluted as two fractions corresponding to the dimer and monomeric species. The purity (partial abundance) of leghemoglobin was analyzed by SDS-PAGE and was determined to be approximately 90 to 100 percent. The proteins in used root nodules can be transferred to 10 mM sodium carbonate pH 9.5, 50 mM sodium chloride buffer, filtered through a 200 nanometer filter and applied onto the anion exchange chromatography column of a machine. rapid liquid protein chromatography (GE Healthcare). Leghemoglobin can be linked to an anion exchange chromatography matrix and can be eluted using a sodium chloride gradient. The purity (partial abundance) of leghemoglobin can be analyzed by SDS-PAGE and was determined to be approximately 60 to 80 percent. Unwanted small molecules from legume roots can be removed from the purified leghemoglobin QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 156 passing leghemoglobin in solution over an anion exchange resin. These small molecules imbue different shades of brown to the root nodule lysate, which decreases the color quality of the leghemoglobin solution. In one embodiment, the anion exchange resin is FFQ, DEAE, Amberlite IRA900, Dowex 22, or Dowex 1x4. Leghemoglobin purified either by fractionation with ammonium sulfate (60 percent weight / volume and 90 percent weight / volume ammonium sulfate) or by anion exchange chromatography was exchanged for the buffer into 20 mM potassium phosphate, pH 7.4, 100 mM sodium chloride and a solution passed over one of the aforementioned anion exchange resins. The flux can be collected and is colored in comparison to the color of the solution before passage over anion exchange resins. The color improvement for the purified leghemoglobin solution (from yellow / brown to a more obvious red) can be observed by visual evaluation, however at different degrees of elimination of the yellow-brown dye. Alternatively, the heme-containing protein can be produced recombinantly as described in section III B. For example, a non-symbiotic hemoglobin from mung bean can be expressed recombinantly in E. coli and purified by exchange chromatography. anions or cation exchange chromatography. A cell lysate can be loaded onto a QQCI I n / l 7Π7 / Β / ΥΙΛΙ 157 FF-Q resin on a rapid liquid protein chromatography machine (GE Healthcare). Non-symbiotic mung bean hemoglobin was eluted in the flow-through fractions. The purity (partial abundance) of nonsymbiotic mung bean hemoglobin was analyzed by SDS-PAGE and determined as a fraction of total protein: 12 percent in E. coli lysate, and 31 percent after purification in FFQ. UV-Vis analysis of the purified protein showed characteristic spectra of bound heme proteins. Alternatively, the cellular waste can be loaded through an FF-S resin in a rapid liquid protein chromatography machine (GE Healthcare). Non-symbiotic mung bean hemoglobin may be bound to the FF-S column and was eluted using a sodium chloride gradient (50mM to 1000mM). The purity (partial abundance) of non-symbiotic mung bean hemoglobin can be analyzed by SDS-PAGE and was determined in: E. coli lysate 13 percent, after purification in FFQ 35 percent. UV-Vis analysis of the purified protein can show the characteristic spectra of bound heme proteins. In some embodiments, heme proteins are used as ingredients in food products where the taste of blood is desired. The heme-containing proteins of the invention were tasted by a panel of volunteers and in each case were described as tasting like blood. Heme proteins, for example leghemoglobin, can be combined with other meat-based replica components. 158 plant. In some embodiments the heme proteins are captured in a gel containing other components, for example lipids and proteins or others. In some aspects, multiple gels are combined with non-gel-based heme proteins. In some embodiments, the combination of the heme proteins and the other compounds of the consumable is done to ensure that the heme proteins are capable of diffusing through the consumable. In some embodiments the consumable is soaked in a solution containing heme protein, for example a leghemoglobin solution, for example, for 1, 5, 10, 15, 30, or 45 minutes or for 1, 5, 10, 15, 20 or 30 hours. Given the usefulness of heme proteins for coloring consumables, it is useful to detect whether a product contains a particular heme protein. Accordingly, the present invention includes in some embodiments methods for determining whether a product contains a heme protein. For example, an ELISA, a ligation proximity assay, a Luminex assay, or Western blot analysis can be performed to determine whether leghemoglobin or another heme-containing protein is present in a food product such as meat or a replicate of meat. In one embodiment, detection methods are carried out to determine whether the meat has been altered with leghemoglobin or another heme-containing protein. E. REPLICA OF SPREADABLE MAYONNAISE Mayonnaise is a thick, creamy sauce. Traditional mayonnaise is a stable emulsion of oil and egg yolk. HE QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 159 believes that lecithin and egg yolk proteins stabilize the emulsion. Traditional commercial mayonnaise typically contains 70 to 80 percent (w / w) fat and 5 percent (w / w) egg yolk. Commercial low-fat products may contain ~20 percent w / w fat. The consumable may comprise a composition having properties comparable to mayonnaise. In one embodiment, purified plant proteins can be used as an egg protein substitute to make stable, creamy protein-fat emulsions whose visual appearance and mouthfeel resemble traditional mayonnaise. The fat (~20-80 percent w / w) may be from a single source or from multiple sources, as described herein. Non-traditional mayonnaise products can be used for all culinary applications that use traditional mayonnaise. In one embodiment, vinegar and / or lemon and / or lemon juice are added as flavor additives. In one embodiment, the purified plant proteins are not soy proteins. In one embodiment, the flavor can be modified by adding mustard, spices, herbs, and / or pickles. A replica of mayonnaise may comprise a mixture of non-animal proteins. In one embodiment, a mayonnaise replica is a mixture of 50 percent (w / v) rice bran oil and 7 percent (w / v) 8S mung bean protein. In one embodiment, a mayonnaise replica is a QQCI I n / l Znz / R / YIAI 160 mixture of 70 percent (w / v) sunflower oil or cocoa butter, 2.4 percent (w / v) RuBisCo, 0.29 percent (w / w) soy lecithin, and optionally 8 μΜ of oleosin. The mixture can be emulsified, and the stability of the emulsion can be controlled by modifying the size of the protein-water-oil particles through high-pressure homogenization or sonication. The oil can be added as a liquid. The protein can be added as a solution in the buffer. Soy lecithin can be resuspended in water and sonicated before mixing with an oil-protein solution. A resulting solution of the oil, protein and lecithin can be homogenized, for example, first at 5000 psi (350 kg / cm2) and then at 8000 psi (560 kg / cm2), or can be sonicated in a cycle at 40 percent Work for 2 minutes at maximum setting. The thickness, texture, creaminess and visual appearance of the resulting products are similar to traditional mayonnaise. In some cases (for example, using 8S mung bean proteins and rice bran oil), the product is a slight whitish color. F. LIQUOR CREAM REPLICA Traditionally, cream liqueurs contain heavy cream and liqueur as their base. Examples of liqueur include whiskey, Irish whiskey, Scotch whiskey, rum, vodka, brandy or fermented fruits (for example, cherry schnapps), plum brandy, 161 tequila, or herbal bitters. A cream liqueur replica can be produced by replacing the heavy cream in cream liqueur with a non-dairy cream fraction from plant sources. In one embodiment, the heavy cream in a cream liqueur can be replaced by a stable emulsion of vegetable fats and isolated or purified proteins of a consistency similar to heavy cream. In one embodiment, purified plant proteins and / or vegetable fats may be from single or multiple sources as described herein. For example, a cream liqueur may include a creamy fraction of sunflower, RuBisCo and whiskey, and one or more optional flavorings (for example, vanilla, chocolate, and or coffee). G. PROTEIN ENRICHED ALCOHOLIC BEVERAGES Traditionally, alcoholic beverages contain negligible to low amounts of protein. The addition of plant proteins to various alcoholic beverages would positively modify their flavor, mouthfeel, physical state and increase their nutritional protein content. Furthermore, the presence of protein in various alcoholic beverages used in cocktails would positively modify flavor, mouthfeel, physical state of the cocktail and increase its nutritional protein content. Different kinds of alcoholic beverages contain different amounts of alcohols. For example, refreshing wines contain approximately 4 to 7 percent alcohol, beer contains approximately ~3 to 10 percent alcohol, QQCI I n / l 7Π7 / Β / ΥΙΛΙ 162 wine contains about 8 to 14 percent vol / volume alcohol, dessert wines contain about 17 to 20 percent alcohol, whiskey contains about 40 ~ percent alcohol, and vodka contains about 35 to 50 percent alcohol. Additionally, some traditional alcoholic beverages include sugars (for example, Bacardi Razz at 10 percent weight / volume). Accordingly, alcohol-containing beverages can be supplemented by the addition of purified plant proteins at, for example, 0.1 to 5 percent w / v and optionally sugar (1 to 15 percent w / v). The sugar may be, for example, cane sugar, brown sugar, sucrose, or glucose. For example, RuBisCo purified at 180 milligrams / milliliter in 20 mM potassium phosphate, pH 7.0, 150 mM NaCl can be added to a whiskey. Jameson Whiskey supplemented with 5 percent weight / volume RuBisCo formed a soft gel, with a consistency similar to traditional Jello shots. For example, alcoholic beverages fortified with RuBisCo, mung bean 8S, and pea globulin are made by adding purified RuBisCo, mung bean 8S, and pea globulin proteins to final protein concentrations of 0.5 percent, 1 percent, and 5 percent. percent weight / volume, respectively, to Corona beer, Pinot Grigio wine and Jameson whiskey. Zein was added at 0.5 percent, 1 percent, and 5 percent weight / volume to 60 percent ethanol, 5 percent QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 163 glucose in a solution in water. Pea proteins were extracted from pea flour by resuspending the flour at 5 percent, 20 percent, or 40 QQCI I n / l 7Π7 / Β / Υ percent ethanol, in solutions of 5 percent sucrose in water, followed Any resulting solids at 5000 percent was not centrifuged by incubation at 5000 percent ethanol supernatant was not dissolved at temperature were removed for 10 minutes. clear in appearance. The particularly useful one. The environment. through solution solution A sensory panel evaluated all protein-fortified alcoholic beverages that have different aromas and flavors from non-protein-fortified beverages. In some cases, generated aromas and flavors were judged as neutral, in some cases as more attractive, and in some cases as less attractive than controls. In one particular example, the addition of both 0.5 percent w / v and 1 percent w / v of the Mung Bean 8S protein to Jameson whiskey softened the aroma and mouthfeel of the Jameson. The addition of 0.5 percent weight / volume mung beans to Jameson Whiskey added a slightly creamy flavor to the Jameson, with an aroma similar to a traditional White Russian cocktail. The addition of 5 percent weight / volume zein to Jameson whiskey generates aromas and flavors characterized as moldy grains and raw potatoes. In another example where Corona beer was fortified with 0.5 percent weight / volume pea globulin, aroma 164 changed to hops and resembled an Indian Ale Palé, and the flavor changed to carry pea notes. The addition of 0.5 percent weight / volume and 5 percent weight / volume 8S mung bean protein changed the aroma of Corona's sweet peony flowers with an intensified hop aroma. The flavor was neutral in the case of 0.5 percent weight / volume 8S mung bean and carried notes of nutty plants in the case of 5 percent weight / volume 8S mung bean. In another example where Pinot Grigio wine was fortified with 1 percent weight / volume 8S mung bean protein, additional notes of sweet aroma and citrus were detected, and the flavor changed to that carrying notes of peanut butter. The addition of 1 percent weight / volume pea globulins modified the aroma to that of strong musty oak and wet leaves. The flavor was modified to carry mud notes. The addition of 5 percent weight / volume RuBisCo generated the aroma and flavor of wet hay. An ethanol enriched with 60 percent zein, 5 percent sucrose solution led to burnt tortilla aroma notes compared to a corresponding solution without zein. There was no difference in taste. An ethanol spiked with 5 percent, 20 percent, and 40 percent pea protein, 5 percent sucrose solutions developed an earthy aroma and flavor compared to protein-free controls. In addition, a pea flavor was detected QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 165 and the bitter taste increased with higher alcohol content. H. CHOCOLATE SPREAD Chocolate spread is a chocolate-flavored spread whose traditional main ingredients are cocoa powder, cow's milk, vegetable oil and sugar. Traditional spreadable chocolates solid either firm or soft at room temperature and melt at temperatures lower than that of cocoa butter. The product can be used as a spread on bread, crepes, pancakes, frosting for cakes and cookies, chocolate pastry filling, or non-dairy chocolate cake filling. In one embodiment, dairy milk and dairy products such as ice cream, buttermilk, cream, yogurt, sour cream or shortening are replaced by a non-dairy creamer fraction made as described herein. In one embodiment, a non-dairy creamer fraction comes from a single source or multiple sources described herein. In one embodiment, the milk and dairy products are substituted for any non-dairy milk described herein. In one embodiment, milk and dairy products are replaced by purified plant proteins described herein. In one embodiment, milk and dairy products are replaced by stable soft solid emulsions made of one or multiple plant oils and single or multiple purified plant proteins. I. OTHER APPLICATIONS In one embodiment, the non-dairy plant cream fraction is qqci i η / ι ζηζ / Ε / γ 166 can be used as a substitute for beef milk and dairy products to make non-dairy milk chocolate bars or non-dairy milk chocolate confectionery. In one embodiment, the non-dairy plant cream fraction and purified plant proteins can be used as a substitute for beef milk and dairy products to make non-dairy milk chocolate bars or a non-dairy milk chocolate confection. In one embodiment, the non-dairy plant cream fraction and plant proteins can be used to make chocolate mousse. The main traditional ingredients of chocolate mousse are dark or semisweet chocolate, butter and eggs. In one embodiment, the dairy butter can be replaced with a non-dairy plant cream fraction. In one embodiment, the dairy butter and eggs may be replaced by a non-dairy plant cream fraction and a plant storage seed protein stabilization foam such as pea albumen. In one embodiment, a vegan consumable can be made as a pâté analogue. Vegan analog pâté can be made by finely chopping 10 g of fat replica and heating in a pan with finely chopped onion for 2 to 3 minutes. The muscle replica (20 g) made without connective tissue replica fibers can be chopped into 7-inch cubes and browned in the fat and shallot mixture for another 3 to 5 minutes. The mixture can be forced to QQCI I n / l 7Π7 / Β / Υ 167 through a sieve until homogenized. The pan, while it is still hot, can be rinsed with a tablespoon of madeira without allowing it to completely evaporate. The liquid from the pan is added to the homogenized mixture, spices (salt, pepper) are added to taste, and the mixture is forced through a sieve again. After cooling in the refrigerator (for example, for 15 minutes), the pâté is ready to be served. In some embodiments, other ratios of fat and muscle replicates are used to create leaner or richer pâtés. For example, pâté may contain from 0.5 to 10 percent, from about 5 percent to 40 percent, from about 10 percent to 60 percent, or from about 30 to 70 percent), or more than 70 percent of an adipose tissue replica. In some embodiments, a replica of muscle tissue with a higher iron content can be used for the pâté to make it a closer imitation of pork or poultry liver pâté. For example, the muscle tissue replica may contain about 1 percent, about 1.5 percent, about 2 percent, or more than 2 percent of a heme protein. In some embodiments, replica muscle tissue with a lower iron content can be used for the pâté to be a closer imitation of poultry meat or fish pâté. For example, replica muscle tissue may contain QQCI I n / l 7Π7 / Β / Υ 168 about 1 percent, about 0.5 percent, about 0.2 percent, or more than 0.2 percent of a heme protein. In one embodiment, a vegan consumable can be made as an analogue of black pudding. Vegan black pudding is made from a blood analogue created by mixing heme protein solutions and purified plant protein. For example, 35 milliliters of a mixed solution of leghemoglobin (120 milligrams / milliliter) and pea albumin (100 milligrams / milliliter), which approximates the composition of blood, can be carefully mixed with a suspension of corn flour in Salt water (6:5 weight / volume flour to water ratio). A tablespoon of chopped onion can be fried with 10 g of chopped adipose tissue replica, mixed with some raisins and cooled to room temperature before mixing with the blood / flour mixture. The mixture can be seasoned to taste (for example, the use of salt, pepper, parsley and / or cinnamon), introduced into vegetarian sausages and poached in almost boiling water for about 45 minutes. After cooling, the sausage can be consumed as is or further cooked, for example smoked, roasted in an oven or roasted. In some embodiments, the muscle replica may be included in the recipe to imitate meat / blood sausages. In some embodiments, barley, buckwheat, oats, rice, rye, sorghum, wheat or other cereals can be used in the QQCI I n / l 7Π7 / Β / ΥΙΛΙ 169 black pudding sausage. In some embodiments, bread, chestnuts, potatoes, sweet potatoes, starch or other filling materials may be added to, or substituted for, grains in the blood sausage. qqci i η / ι ζηζ / Ε / γ EXAMPLES EXAMPLE 1: PROTEIN ISOLATION All steps were carried out at 4°C or room temperature, centrifugation steps were at 8000 g for 20 minutes, at 4°C or room temperature. The flour was suspended in a specific buffer, the suspension was centrifuged, and the supernatant was filtered through a PES membrane with a molecular weight cutoff of 0.2 microns, and then concentrated by uItrafiItration on a PES membrane with a cutoff of molecular weight of 3 kDa, 5 kDa, 10 kDa in a Spectrum Labs KrosFlo hollow fiber tangential flow filtration system. Once fractionated, all fractions of the ammonium sulfate precipitate of interest were stored at −20°C until further use. Before use in the experiments, the precipitates were resuspended in 10 volumes of 50 mM potassium phosphate buffer, pH 7.4, + 0.5 M NaCl. The suspensions were centrifuged and the supernatants were microfiltered through a membrane. PES with a molecular weight cutoff of 0.2 microns, and then concentrated by uItrafiltration on a PES membrane with a molecular weight cutoff of 3 kDa, 5 kDa, 10 kDa in a hollow fiber tangential flow filtration system. 170 Spectrum Labs KrosFlo. Protein composition in individual fractionation steps was monitored by SDS-PAGE and protein concentrations were measured by conventional UVVis methods. (i) Pea albumins: Dried green or yellow pea flour was used as a source of pea albumins. The flour was suspended in 10 volumes of 50 mM sodium acetate buffer at pH 5, and stirred for 1 hour. Soluble protein was separated from unextracted protein and pea seed debris either by centrifugation (8000 g, 20 minutes) or by filtration through a 5 micron filter. The supernatant or filtrate was collected, respectively. For this crude protein extract, solid ammonium sulfate was added at 50 percent weight / volume saturation. The solution was stirred for 1 hour and then centrifuged. To the supernatant from this step, ammonium sulfate was added to bring it to 90 percent weight / volume saturation. The solution was stirred for 1 hour, and then centrifuged to collect the pea albumin proteins in the pellet. The chipboard was stored at −20°C until further use. The protein was recovered from the pellet and prepared for use as described above, with the exception that the final buffer may contain 0-500 mM sodium chloride. In some embodiments, the flour was suspended in 10 volumes of 50 mM NaCl, pH 3.8, and stirred for 1 hour. The qqci i η / ι ζηζ / Ε / γ 171 Soluble protein was separated from pea protein and non-extracted seed waste by centrifugation (8000 g, 20 minutes). The supernatant was collected and filtered through a 0.2 micron membrane and concentrated using a PES membrane with a molecular weight cutoff of 10 Kda. (i) Pea globulins: Dried green pea flour was used to extract pea globulin proteins. The flour was suspended in 10 volumes of 50 mM potassium phosphate buffer at pH 8, and 0.4 M sodium chloride, and stirred for 1 hour. Soluble protein was separated from pea seed waste by centrifugation. The supernatant was subjected to ammonium sulfate fractionation in two steps at 50 percent and 80 percent saturation. The 80 percent pellet containing the globulins of interest was stored at −20°C until further use. The protein was recovered from the pellet and prepared for use as described above. iii) 7S and 11 S soybean seed globulins: Globulins were isolated from soybean flour by a first suspension of low-fat / defatted soybean flour in 4 to 15 volumes of 10 (or 20) mM potassium phosphate, pH of 7.4. The suspension was centrifuged at 8,000 relative centrifugal force (ref) for 20 minutes, or clarified by 5 micron filtration and the supernatant was collected. The crude protein extract contained both 7S and 11S globulins. The solution was then filtered to 0.2 microns and QQCI I n / l 7Π7 / Β / ΥΙΛΙ 172 was concentrated using a PES membrane with a molecular weight cutoff of 10 kDa in a Spectrum Labs KrosFlo hollow fiber tangential flow filtration system, or by passing it over anion exchange resin before use in the experiments. The 11S globulins were separated from the 7S proteins by isoelectric precipitation. The pH of the crude protein extract was adjusted to 6.4 with diluted HCl, shaken for 30 minutes to 1 hour, and then centrifuged to collect the 11S precipitate and 7S proteins in the supernatant. The 11S fraction was resuspended with 10 mM potassium phosphate at pH 7.4, and the protein fractions were microfiltered and concentrated before use. Soy proteins can also be extracted by suspending defatted soy flour in 4 to 15 volumes (e.g., 5 volumes) of 20 mM sodium carbonate, pH 9 (or water, pH adjusted to 9 after flour addition) or 20 mM potassium phosphate buffer at pH 7.4 and 100 mM sodium chloride to reduce off-flavors in the purified protein. The suspension was stirred for one hour and centrifuged at 8000 x g for 20 minutes. The extracted proteins were u11rafi11ted and then processed as above or alternatively, the supernatant was collected and filtered through a 0.2 micron membrane and concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (iv) 8S mung bean globulins: qqci i η / ι ζηζ / Ε / γ flour was used 173 mung bean to extract 8S globulins by first suspending the flour in 4 volumes of 50 mM potassium phosphate buffer at a pH of 7 (+ 0.5 M NaCl for laboratory-scale purifications). After centrifugation, proteins in the supernatant were fractionated by adding ammonium sulfate in 2 steps at 50 percent and 90 percent saturation, respectively. The precipitate of the 90 percent fraction contained the 8S globulins and was stored at −20°C until further use. Protein was recovered from the pellet and prepared for use as described above. Mung bean globulins can also be extracted by suspending the flour in 4 volumes of 20 mM sodium carbonate buffer, pH 9 (or water adjusted to a pH of 9 after addition of the mung flour) to reduce off-flavors in purified protein fractions. The suspension was centrifuged (or filtered) to remove solids, subjected to ultrafiltration, and then processed as described above. (v) Proteins abundant in late embryogenesis: Flour (including, but not limited to, mung bean and soybean flour) was suspended in 20 mM Tris-HCl, pH 8.0, 10 mM NaCl, and stirred at room temperature for 1 hour, and then centrifuged. Acid (HCl or acetic acid) was added to the supernatant at a concentration of 5 percent (vol / vol), stirred at room temperature, and then centrifuged. The supernatant is QQCI I n / l 7Π7 / Β / ΥΙΛΙ 174 heated at 95°C for 15 minutes, and then centrifuged. The supernatant was precipitated by adding 25 percent trichloroacetic acid, centrifuged, and then washed with acetone. Heating and acid washing steps can be carried out in the reverse direction as well. (vi) Pea prolamins: Dried green pea flour was suspended in 5 times (w / v) 60 percent ethanol, stirred at room temperature for one hour, then centrifuged (7000 g, 20 minutes) and the supernatant was collected. The ethanol in the supernatant was evaporated by heating the solution to 85°C and then cooled to room temperature. Ice-cold acetone (1:4 vol / vol) was added to precipitate proteins. The solution was then centrifuged (4000 g, 20 min), and the protein was recovered as a light beige agglomerate. (vii) Zein prolamins: A concentration of corn protein or flour was suspended in 5 times (w / v) 60 percent ethanol, stirred at room temperature for one hour, and then centrifuged. The ethanol in the supernatant was evaporated with heat, and then the solution was centrifuged, and the protein was recovered as an agglomerate. (viii) RuBisCo was fractionated from alfalfa leaves by first grinding the leaves with 4 volumes of cold 50 mM potassium phosphate buffer at pH 7.4 (0.5 M NaCl + 2 mM DTT + 1 mM EDTA) in a blender. The resulting aqueous paste is QQCI I n / l 7Π7 / Β / Υ 175 centrifuged to remove debris, and the supernatant (crude lysate) was used in additional purification steps. Proteins from the crude lysate were fractionated by the addition of ammonium sulfate to 30 percent (w / v) saturation. The solution was stirred for 1 hour and then centrifuged. The pellet from this step was discarded and additional ammonium sulfate was added to the supernatant at 50 percent (w / v) saturation. The solution was centrifuged again after stirring for 1 hour. The agglomerate from this stage contained RuBisCo, and was kept at -20°C until use. Protein was recovered from the pellet and prepared for use as described above. RuBisCo can also be purified by adjusting the crude lysate to 0.1 M NaCl, and applying it to an anion exchange resin. Weakly bound protein contaminants were washed with 50 mM potassium phosphate buffer at pH 7.4 + 0.1 M NaCl. The RuBisCo was then eluted with high ionic strength buffer (0.5 M NaCl). RuBisCo solutions were decolorized (pH 7 to 9) by passing them over columns packed with activated carbon. The dyes were bound to the column while RuBisCo was isolated in the filtrate. RuBisCo solutions were also alternately decolorized by incubating the solution with FPX66 resin (Dow Chemicals) packed on a column (or in batch mode). The aqueous paste was incubated for 30 minutes, and then the QQCI I n / l 7Π7 / Β / Υ 176 liquid separated from the resin. The dyes were bound to the resin, and the RuBisCo was collected in the flow-through column. In some embodiments, RuBisCo was isolated from spinach leaves by first grinding the leaves with 4 volumes of 20 mM potassium phosphate buffer, pH 7.4 + 150 mM NaCl + 0.5 mM EDTA) in a blender. The resulting aqueous paste was centrifuged to remove debris, and the supernatant (crude waste) was filtered through a 0.2 micron membrane and concentrated using a RES membrane with a molecular weight cutoff of 10 KDa. In some embodiments, RuBisCo was extracted from alfalfa or wheatgrass juice powder by mixing the powder with 4 volumes of 20 mM potassium phosphate buffer, pH 7.4 + 150 mM NaCl + 0.5 mM EDTA) in a blender. The resulting aqueous paste was centrifuged to remove debris, and the supernatant (crude waste) was filtered through a 0.2 micron membrane and concentrated using a RES membrane with a molecular weight cutoff of 10 KDa. (ix) Leghemoglobin: Soybean root nodules were suspended and used in 20 mM potassium phosphate at a pH of 7.4, 100 mM potassium chloride and 5 mM EDTA using a grinder-blender. During this process, leghemoglobin is released in the regulator. Root nodule waste containing leghemoglobin was cleaned of cellular debris by filtration through a 5 micron filter. In some qqci i η / ι ζηζ / Ε / γ 177 modalities, filtration was followed by centrifugation (7000 g, 20 minutes). The clarified lysate containing leghemoglobin was then filtered through a 0.2 micron filter and applied onto an anion exchange chromatography column (High Prep Q; High Prep DEAE, GE Healthtcare) in a fast liquid protein chromatography instrument ( GE Healthtcare). Leghemoglobin was collected in the flowthrough fraction, and concentrated on a PES membrane with a molecular weight cutoff of 3 kDa, in a Spectrum Labs KrosFlo hollow fiber tangential flow filtration system to a desired concentration. The purity (partial abundance) of purified leghemoglobin was analyzed by SDS-PAGE gel: In lysed leghemoglobin it is present in 20 to 40 percent, while after anion exchange purification it is present in 70 to 80 percent . In another embodiment, a flow through of soybean leghemoglobin was applied from anion exchange chromatography over size exclusion chromatography (Sephacryl S-100 HR, GE Healthcare). Soybean leghemoglobin was eluted as two fractions corresponding to the dimeric and monomeric species. The purity (partial abundance) of leghemoglobin was analyzed by SDS-PAGE and was determined to be approximately 90 to 100 percent. Analysis of UV-VIS spectra (250 to 700 nanometers) revealed a spectral signature consistent with heme-loaded leghemoglobin. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 178 (x) Non-symbiotic mung bean hemoglobin was cloned into the pJexpress401 vector (DNA2.0), and transformed into E. coli BL21. Cells were cultured in LB medium containing soyatone instead of tryptone, kanamycin, 0.1 mM ferric chloride, and 10 micrograms / milliliter of 5-amino-levulinic acid. Expression was induced by 0.2 mM IPTG, and cells were cultured at 30°C for 20 h. E. coli cells expressing non-symbiotic mung bean hemoglobin were harvested and resuspended in 20 mM MES buffer at pH 6.5, 50 mM NaCl, 1 mM MgCU, 1 mM CaCU. Added some DNAsalt and protease inhibitors. The cells were used by sonication. The lysate was cleaned of cellular debris by centrifugation at 16,000 g for 20 minutes, followed by filtration through a 200-nanometer filter. Next, the cellular waste was loaded onto FF-S resin in the rapid liquid protein chromatography instrument (GE Healthtcare). Non-symbiotic mung bean hemoglobin was bound to the FF-S column and eluted using a sodium chloride gradient (50 mM to 1,000 mM). The purity (partial abundance) of mung bean non-symbiotic hemoglobin was analyzed by SDS-PAGE and determined to be: 13 percent E. coli lysate, after purification in 35 percent FFQ. UV–Vis analysis of the purified protein showed the characteristic spectra of heme-bound proteins. (x¡) Hemoproteins were synthesized with an epitope mark QQCI I n / l 7Π7 / Β / ΥΙΛΙ 179 of N-terminal H¡s6 and a TEV dissociation site, were cloned into the pJexpress401 vector (DNA2.0), and transformed into E. coli BL21. Transformed cells were cultured in LB medium containing soyatone instead of tryptone, kanamycin, 0.1 mM ferric chloride, and 10 micrograms / milliliter 5-amino-levulinic acid. Expression was induced by 0.2 mM IPTG and cells were cultured at 30°C for 20 h. E. coli cells expressing heme proteins were harvested and resuspended in 50 mM potassium phosphate, pH 8, 150 mM NaCl, 10 mM imidazole, 1 mM MgCb, 1 mM CaCls, DNAsal, and inhibitors. protease. The cells were used by sonication and clarified by centrifugation at 9000 x g. The lysate was incubated with NiNTA resin (MCLAB), washed with 5 column volumes (CV) of 50 mM potassium phosphate, pH 8, 150 mM NaCl, 10 mM imidazole, and eluted with 50 mM potassium phosphate, pH 8, 150 mM NaCl, 500 mM imidazole. SDS-PAGE and UV-Vis spectra confirmed the expected molecular weights and complete heme loading, respectively. In some embodiments, the transformed cells were cultured in a seeding medium comprised of 10 grams / liter of glucose monohydrate, 8 grams / liter of potassium monophosphate, 2.5 grams / liter of Sensient Amberferm 6400, 2.5 grams / liter of Sensient Tastone 154, 2 grams / liter ammonium di-phosphate, 1 milliliter / liter Trace Metals Mixture (Teknova 1000x Trace Metals Mixture, Cat. No. T1001), 1 gram / liter sulfate QQCI I n / l 7Π7 / Β / Υ 180 magnesium, 0.25 milliliters of a 0.1 M solution of ferric chloride, 0.5 milliliters / liter of Sigma 204 antifoam, 1 milliliter / liter of a 1000x solution of kanamycin sulfate. 250 milliliters of the medium were used in (4)-1L screened shake flasks, inoculated with 0.25 milliliters each from a single glycerol supply culture flask. Shake flasks were cultured for 5.5 hours, with shaking at 250 revolutions per minute (RPM) at 37°C. 40 liters of seeding medium were steam sterilized in a 100 liter bioreactor, cooled to 37°C, pH adjusted to 7.0, and inoculated with 800 milliliters of the shake flask culture once reached a shake flask OD of 2.5. Bioreactor aeration was supplied at 40 liters / m, and agitation was at 250 revolutions per minute (RPM). After 2.2 hours of culture, an OD of 2.20 was reached, and 22 liters of the culture were transferred to the final 4 m3 bio-reactor. The starting medium for the final bio-reactor comprised the following components vaporized in place: 1.775 liters of deionized water, 21.75 kilograms of potassium mono-phosphate, 2.175 kilograms of ammonium di-phosphate, 4.35 kilograms of ferric ammonium citrate , 8.7 kilograms of ammonium sulfate, 10.875 kilograms of Sensient Amberferm 6400, 10.875 kilograms of Sensient Tastone 154. After 30 minutes of vaporization, the medium components were cooled to 37°C, and the following additions were made after sterilization : 2.145 liters of a 0.1 M solution of ferric chloride, 59.32 kilograms of monohydrate QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 181 55 percent w / w glucose, 3.9 liters trace metals mix (Teknova 1000x Trace Metals Mixture, Cat. No. T1001), 10.88 liters 200 grams / liter ammonium di-phosphate, 36.14 liters of 1M magnesium sulfate, and 2,175 liters of Sigma 204 antifoam, 2,175 liters of a 1000x solution of kanamycin sulfate. The pH was controlled at 7.0 by the addition of 30 percent ammonium hydroxide. Aeration was delivered at 2,175 m3 / minute, and dissolved oxygen was controlled at 25 percent by varying agitation between 60 and 150 revolutions per minute (RPM). At two time points (EFT = 4 and EFT8), bolus additions of additional nutrients were provided. Each addition added 5.5 kilograms of Sensient Amberferm 6400, 5.5 kilograms of Sensient Tastone 154, and 4.4 kilograms of ammonium di-phosphate, in autoclaved solutions (100 grams / liter of solution for Amberferm and Tastetone, 200 grams / liter for the ammonium diphosphate). A sterile glucose solution of 55 percent w / w glucose monohydrate was fed to the bio-reactor to maintain a residual glucose level of 2 to 5 grams / liter. Once an OD of 25 was reached, the temperature was reduced to 25°C, and culture was induced with 0.648 liters of 1M isopropyl S-D-1thiogalactopyranoside. The culture was allowed to grow for a total time of 25 hours, at which point, the culture was diluted 1:1 with deionized water, then centrifuged, and the centrifuge was concentrated to a solids content of 50 volume percent. volume. The cell center was frozen at -20°C. He 182 centrote was thawed to 4°C, and diluted in 20 mM potassium phosphate, pH 7.8, 100 mM NaCl, 10 mM imidazole, and homogenized at 15,000 PSI (1,050 kg / cm2). Homogenized cells were filtered through 0.2 microns by tangential flow filtration (TFF), and the filtered lysate was loaded directly onto a zinc-loaded (GE) IMAC column. Bound proteins were washed with 10 column volumes (CV) of 20 mM potassium phosphate, pH 7.4, 100 mM NaCl, 5 mM histidine, and eluted with 10 column volumes (CV) of monobasic potassium phosphate. 500 mM, 100 mM NaCl. Leghemoglobin was concentrated and diafiltered using a PES membrane of a molecular weight cutoff of 3 kDa and tangential flow filtration (TFF). The concentrated sample was reduced with 20 mM sodium dithionite, and desalted using G-20 (GE) resin. Desalted leghemoglobin samples were frozen in liquid nitrogen, and stored at −20°C. The concentration and purity of leghemoglobin were determined by SDS-PAGE and UV-Vis analysis. (xii) Oleosin. Sunflower oil bodies were purified from sunflower seeds. Sunflower seeds were mixed in 100 mM sodium phosphate buffer, pH 7.4, 50 mM sodium chloride, 1 mM EDTA at 1:3 w / v. Oil bodies were collected by centrifugation (5000 g, 20 minutes), and resuspended at 1:5 (w / v) in 50 mM sodium chloride, 2 M urea, and shaken for 30 minutes, at 4 °C. The washing and centrifugation steps with 2M urea were repeated. The QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 183 oil bodies collected by centrifugation were resuspended in 100 mM sodium phosphate buffer, pH 7.4, 50 mM sodium chloride. The centrifugation and washing steps were repeated once more, and the final washed oil body fraction was obtained from a final centrifugation step. The oil bodies were resuspended at 10 percent w / w in 100 mM sodium phosphate buffer, pH 7.4, 50 mM sodium chloride, and 2 percent w / v vegetable oil fatty acid salts. , were homogenized at 5,000 psi (350 kg / cm2) and incubated at 4°C for 12 hours. The solution was centrifuged (8000 g, 30 minutes), removed to the upper layer, and the soluble fraction collected. SDS-PAGE analysis suggested that oleosins are an important protein present in the soluble fraction. The oleosin concentration was 2.8 milligrams / milliliter. (xiii) Pea Total Proteins: Dried green or yellow pea flour was used to extract total pea protein. The flour was suspended in 10 volumes of 20 mM potassium phosphate buffer, pH 8, and 100 mM sodium chloride, and stirred for 1 hour. Soluble protein was separated from pea seed waste by centrifugation. The supernatant was collected and filtered through a 0.2 micron membrane and concentrated using a PES membrane with a molecular weight cutoff of 1 0 KDa. (xiv) Pea vicilin and pea legume: Dried green or yellow pea flour was used to extract the proteins QQCI I n / l 7Π7 / Κ / ΥΙΛΙ 184 pea totals as described above. The crude pea mixture obtained therefrom was fractionated into pea vicilin and pea legumin using ion-exchange chromatography. Material was loaded onto Q Sepharose FastFiow resin and fractions were collected as the salt concentration was varied from 100 mM to 500 mM NaCI. Pea vicilin was collected in 350 mM sodium chloride, while pea legume was collected in 460 mM sodium chloride. The collected fractions were concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (xv) Total Lentil Proteins: Air-sorted lentil flour was used to extract the crude lentil protein mixture. The flour was suspended in 5 volumes of 20 mM potassium phosphate buffer, pH 7.4 and 0.5 M sodium chloride, and stirred for 1 hour. Soluble protein was separated from unextracted protein and lentil seed debris by centrifugation (8000 g, 20 minutes). The supernatant was collected and filtered through a 0.2 micron membrane, and concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (xvi) Lentil albumins: Air-sorted lentil flour was suspended in 5 volumes of 50 mM sodium chloride, pH 3.8, and stirred for 1 hour. Soluble protein was separated from non-extracted protein and lentil seed debris by centrifugation (8000 g, 20 minutes). He QQCI I n / l 7Π7 / Β / Υ 185 supernatant was collected and filtered through a 0.2 micron membrane, and concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (xvii) Total proteins of chickpea seeds: Chickpea seed flour was suspended in 5 volumes of 20 mM potassium phosphate buffer, pH 7.4, and 0.5 M sodium chloride, and stirred for 1 hour. Soluble protein was separated from unextracted protein and chickpea seed debris by centrifugation (8000 g, 20 min). The supernatant was collected and filtered through a 0.2 micron membrane, and concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (xviii) Chickpea seed albumins: Chickpea seed flour was suspended in 5 volumes of 50 mM sodium chloride, pH 3.8, and stirred for 1 hour. Soluble protein was separated from unextracted protein and chickpea seed debris by centrifugation (8000 g, 20 min). The supernatant was collected and filtered through a 0.2 micron membrane, and concentrated using a PES membrane with a molecular weight cutoff of 10 KDa. (xix) Amaranth flour dehydrins: Amaranth flour was suspended in 5 volumes of 0.5 M sodium chloride, pH 4.0, and stirred for 1 hour. Soluble protein was separated from unextracted protein and amaranth seed debris by centrifugation (8000 g, 20 min). He QQCI I n / l 7Π7 / Β / Υ 186 supernatant was collected and filtered through a 0.2 micron membrane, and concentrated using a PES membrane with a molecular weight cutoff of 3 KDa. Additional enrichment of dehydrins was obtained from this fraction by boiling the concentrated protein material, centrifuging at 8000 g for 10 min, and collecting the supernatant. EXAMPLE 2: CONSTRUCTION OF A FABRIC ANALOGUE MUSCULAR To prepare a muscle tissue replica, 8 milliliters of mung bean protein solution (114 milligrams / milliliter in 20 mM phosphate buffer (pH of 7.4) and 400 mM sodium chloride) was mixed with 16 milliliters of leghemoglobin solution ( 6 milligrams / milliliter leghemoglobin in 20 nM potassium phosphate, 400 mM NaCl, pH 7.3). The resulting mixture was concentrated using Amicon centrifugal concentrators (10 kDa cut-off) to a final concentration of 8S mung bean globulin of 61 milligrams / milliliter, and leghemoglobin of 6.5 milligrams / milliliter. Approximately 400 milligrams of transglutaminase powder was added to the solution, which was mixed thoroughly, and divided into two 50 milliliter Falcon tubes, and incubated overnight at room temperature. The final total protein concentration was 67.5 milligrams / milliliter of total protein. The muscle tissue replica formed an opaque reddish-brown gel, with small amounts (<1 milliliter) of inclusions of a dark red liquid of venous blood. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 187 EXAMPLE 3: INCREASE IN TENSILE STRENGTH OF ADIPOSE TISSUE REPLICA A 40-milliliter aliquot of rice bran oil and a 40-milliliter aliquot of mung bean protein (114 milligrams / milliliter) were combined in a 250-milliliter Pyrex beaker. The beaker was placed in a water bath and emulsified using ultrasonics with a Branson Sonifer 450 with a 12 millimeter tip for a 60 percent duty cycle for 6 minutes at power level 5. In a 18 centimeter x 18 centimeter x 2.5 centimeter synthetic rubber plastic ice cube tray from Ikea, 48 milligrams of electrospun fibers (from the connective tissue of Example 14) were spread longitudinally and as homogeneously as possible across the bottom of a triangular mold measuring 13.97 centimeters x 1.27 centimeters x 1.5875 centimeters. Approximately 20 milliliters of the rice bran oil / mung bean protein emulsions were then poured on top of the fibers. 20 milliliters of the additional emulsions were then poured into a smooth mold of similar size in the same tray to be used as a control. The ice cube tray was floated in boiling water for 15 minutes, removed, and cooled to room temperature. Using a razor blade, each of the resulting gels was cut into 3 segments, each measuring 4.66 centimeters. QQCI I n / l 7Π7 / Β / ΥΙΛΙ 188 long with a cross-sectional area of ​​1 square centimeter. A Stable Micro Systems TA XTExpress Enhanced Texture Analyzer with an attached TA-96B probe was used to evaluate tensile strength. The fiber containing the fat replicate had a tensile strength of 23 kPa, while the fat replicate without fibers had a tensile strength of 20 kPa. EXAMPLE 4: REPLICA OF ADIPOSE TISSUE WITH A HIGH AVERAGE OF FAT A replica of adipose tissue comprising an oil-protein emulsion formed with 3.3 percent w / v pea globulin, 70 percent v / v oil consisting of an equal blend of coconut oils, cocoa, olive, and palm oil, and 0.5 percent w / v lecithin, was crosslinked with 2 percent transglutaminase (Ajinomoto Activa® TI). After draining and dehydrating, the resulting gel was medium soft and the fat content was confirmed to be 75 percent (w / w). An adipose tissue matrix was formed comprising a protein-oil emulsion with 1.6 percent w / v RuBisCo and 80 percent v / v cocoa butter. The resulting gel was smooth. EXAMPLE 5: METHOD FOR PREPARING REPLICAS OF ADIPOSE TISSUE The oils are fused if necessary by heating to room temperature or gently heated. If the oils QQCI I n / l 7Π7 / Β / Υ 189 are solid at room temperature, they remain close to the melting point during the remainder of the procedure. The proteins are obtained by the specified protocols (see Example 1). The lecithin was weighed and resuspended in water, and then sonicated to create a homogeneous solution. Components were combined in the specified proportions and brought to volume with buffer if necessary (20 mM sodium phosphate, pH 7.4, with 50 mM sodium chloride), then homogenized or sonicated to control size. of particles within an emulsion. The emulsions were then gelled by either: (a) heating / cooling, (b) crosslinking with a transglutaminase enzyme, or (c) heating / cooling followed by the addition of a transglutaminase enzyme. Control samples (no heating / cooling or transglutaminase crosslinking treatments) were prepared for comparisons. Emulsions stabilized by the heating / cooling treatment were prepared by placing the emulsion in a 90°C to 100°C water bath for five minutes, then the samples were allowed to cool slowly to room temperature. Transglutaminase cross-link stabilized emulsions were prepared by adding 2 percent w / v transglutaminase and incubated at 37°C for 12 to 18 hours. Emulsions stabilized by heating / cooling followed by the addition of transglutaminase enzyme QQCI I n / l 7Π7 / Β / Υ 190 were first prepared using the heating / cooling protocol, followed by the addition of the enzyme once the samples had cooled to room temperature. All emulsions were incubated for 8 to 12 hours at 37°C. EXAMPLE 6: METHOD FOR ANALYZING FABRIC REPLICAS ADIPOSE After different gelling treatments, the gelled emulsions are brought to room temperature for evaluation. The total volume of the gelled emulsions, and the volumes of water and / or oil in separate phases (if the gelled emulsions are not in a single phase) are recorded. The firmness of the adipose tissue replica is evaluated by gently touching the gelled emulsions with the tip of the finger. Baking experiments are carried out by transferring the dough to a heated surface and measuring the temperature of the liquid immediately after baking. EXAMPLE 7: REPLICA OF ADIPOSE TISSUE OF FAT BEEF A replica of adipose tissue was made by gelling a solution of purified 8S mung bean protein emulsified with equal amounts of cocoa butter, coconut butter, olive oil, and palm oil. Mung bean 8S protein was purified as described in Example 1, and had a concentration of 140 milligrams / milliliter in 20 mM potassium phosphate, pH 7.4, 400 mM NaCl. A mixture of fat was prepared by melting the QQCI I n / l 7Π7 / Β / Υ 191 individual fats from the solid state to the liquid state at 45°C for 30 minutes. The individual fats (cocoa butter, coconut butter, olive oil and palm oil) were then mixed in a liquid state in a ratio of 1:1:1:1 (by volume / volume). A fat-protein emulsion was formed by mixing 70 percent w / v liquid fat with 4.2 percent w / v 8S mung bean protein, and 0.4 percent w / v mung bean lecithin. soybean, and emulsified by shaking for 30 seconds, followed by sonication for 1 minute. After homogenization, the fat-protein emulsion was in a single liquid phase as judged by visual observation. An adipose tissue replica emulsion was stabilized by cross-linking with 0.2 percent weight / volume transglutaminase enzyme at 37°C for 12 hours. Another fatty tissue replica was stabilized by gelling the proteins by heating to 100°C in a water bath, followed by cooling to room temperature. The resulting adipose tissue replicates were single phase. The adipose tissue replica matrix formed by transglutaminase was a softer solid than the adipose tissue replica matrix formed by heat / cold-induced gelation. EXAMPLE 8: A REPLICA OF ADIPOSE TISSUE OF FAT WAGYU BEEF A replica of adipose tissue was made by gelling an emulsion QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 192 of purified pea globulin proteins and equal amounts of cocoa butter, coconut butter, olive oil and palm oil. Pea globulin proteins were purified as described in Example 1 and had a concentration of 100 milligrams / milliliter, in 20 mM potassium phosphate at pH 8, 400 mM NaCl. A fat mixture was prepared by melting the individual fats from the solid state to the liquid state at 45°C for 30 minutes. The individual fats (cocoa butter, mango butter, olive oil) were then mixed in liquid state, in a ratio of 2:1:1 (olive oil: cocoa butter: mango butter) by volume / volume. A fat-protein emulsion was formed by mixing a liquid fat mixture with a 5 percent weight / volume solution of pea globulins in a 1:1 ratio, and emulsified using a handheld homogenizer in the maximum setting for 30 seconds. After homogenization, the fat-protein emulsion was in a single liquid phase as judged by visual observation. The emulsion was stabilized by crosslinking with 0.2 percent w / v transglutaminase enzyme at 37°C for 12 hours. The resulting adipose tissue replica was in a single phase, was a soft solid, and was salty in taste. EXAMPLE 9: REPLICA OF ADIPOSE TISSUE WITH DISTRIBUTION OF RES FATTY ACIDS QQCI I n / l 7Π7 / Β / Υ 193 A replica of adipose tissue was made by gelling an emulsion of purified pea globulin proteins and equal amounts of cocoa butter, mango butter, olive oil, and rice bran oil. Pea globulin proteins were purified as described in Example 1, and had a concentration of 100 milligrams / milliliter, in 20 mM potassium phosphate at pH 8, 400 mM NaCl. A fat mixture was prepared by melting the individual fats from solid to liquid state at 45°C for 30 minutes. The individual fats (cocoa butter, mango butter, olive oil and rice bran oil) were then mixed in a liquid state, in a ratio of 1:1:1:1 volume / volume. A fat-protein emulsion was formed by mixing 50 percent w / v liquid fat mixture with 5 percent w / v pea globulins, and emulsified using a handheld homogenizer on the setting. maximum for 30 seconds. After homogenization, the fat-protein emulsion was in a single liquid phase as judged by visual observation. The emulsion was stabilized by cross-linking with 0.2 weight / volume percent transglutaminase enzyme at 37°C for 12 hours. The resulting adipose tissue replica was in a single phase, was a soft solid, and was salty in taste. EXAMPLE 10: REPLICA OF ADIPOSE TISSUE WHERE THE FIRMNESS OF THE FAT TISSUE IS CONTROLLED AT REFRIGERATION AND AMBIENT TEMPERATURES BY MEANS OF qqci i η / ι ζηζ / Ε / γ 194 MELTING TEMPERATURE OF FAT IN THE REPLICA OF ADIPOSE TISSUE An adipose tissue replica made as a stable emulsion of RuBisCo with sunflower oil is milder than an adipose tissue replica made as a stable emulsion of RuBisCo and cocoa butter. Adipose tissue replicas were formed with 0.18 percent, 1.6 percent, and 2.4 percent w / v RuBisCo with 70 percent, 80 percent, and 90 percent w / v shortenings. sunflower or cocoa. Each adipose tissue replica containing cocoa butter was firmer than the corresponding replicas formed with sunflower oil. Adipose tissue replicates comprising 0.18 percent, 1.6 percent, and 2.4 percent w / v RuBisCo with 70 percent, 80 percent, and 90 percent w / v butter of cocoa were solid at room temperature, but melted at near mouth temperature. In adipose tissue replicas formed with varying concentrations of RuBisCo (0.18, 1.6, 1.9 percent w / v) and 70 to 80 percent v / v sunflower oil, the replicas were firmer with increasing amounts. of protein in the adipose tissue replica matrix. Adipose tissue replicates with 0.18 weight / volume percent RuBisCo were very soft; adipose tissue replicates with 1.6 percent w / v RuBisCo were soft; and adipose tissue replicates with 1.9 percent weight / volume RuBisCo qqci i η / ι ζηζ / Ε / γ 195 were of medium firmness. Adipose tissue replicas made as a stable emulsion of 8S mung bean protein with sunflower oil were smoother than adipose tissue replicas made as a stable emulsion of 8S mung bean protein and cocoa butter. Adipose tissue replicas were formed with 2 percent, 1 percent, and 0.5 percent w / v of 8S mung bean with 70 percent, 80 percent, and 90 percent w / v. volume of sunflower or cocoa butter. Each adipose tissue replica containing cocoa butter was firmer than the corresponding replica formed with sunflower oil. Adipose tissue replicas made in the form of stable emulsions of 8S mung bean proteins with canola oil are milder than the corresponding adipose tissue replicas made in the form of stable emulsions of 8S mung bean proteins with a mixture in equal parts of coconut, cocoa, olive and palm oils. Adipose tissue replicas were formed with 1.4 percent w / v 8S mung bean protein with 50 percent, 70 percent, and 90 percent w / v sunflower oils or oil blend. . Each adipose tissue replica containing a mixture of oils was firmer than the corresponding replica formed with sunflower oil. An adipose tissue replica comprising 1.4 percent w / v 8S mung bean protein with 50 percent, 70 percent, and 90 percent w / v a mixture QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 196 equal of coconut, cocoa, olive, and palm oil, was solid at room temperature but melted at the temperature close to that of the mouth. The adipose tissue replica made as a stable emulsion of soy proteins with sunflower oil was smoother than the adipose tissue replica made as a stable emulsion of soy proteins and cocoa butter. Adipose tissue replicas were formed with 0.6 percent, 1.6 percent, and 2.6 percent weight / volume soybeans with 50 percent, 70 percent, 80 percent, and 90 percent in volume / volume of sunflower or oil mixture. Each adipose tissue replica containing oil mixture was firmer than the corresponding replica formed with sunflower oil. Adipose tissue replicates comprising 0.6 percent, 1.6 percent, and 2.6 percent weight / volume soy protein with 50 percent, 70 percent, 80 percent, and 90 percent percent cocoa butter by volume / volume were solid at room temperature but melted at near mouth temperature. EXAMPLE 11: COOKING A REPLICA OF ADIPOSE TISSUE: THE STRUCTURE OF THE FAT TISSUE MATRIX CONTROLS THE MELTING POINT DURING COOKING An adipose tissue comprising a stabilized protein-oil emulsion constructed as described in Example 5 and Example 6 above, formed with 2 percent weight / volume RuBisCo and 50 percent, 70 percent, and 90 percent in QQCI I n / l 7Π7 / Β / Υ 197 volume / volume of cocoa butter, melted at a higher temperature when formed in a heat / cold denaturation and at a lower temperature than when formed by cross-linking with a transglutaminase. EXAMPLE 12: COOKING OF ADIPOSE TISSUE: THE STRUCTURAL ARRANGEMENT AND ORGANIZATION OF PROTEINS AND FATS WITHIN A MATRIX OF FAT TISSUE CONTROLS THE AMOUNT OF FAT RELEASED AND OF FAT RETAINED BY THE REPLICA OF ADIPOSE TISSUE DURING COOKING During cooking of an adipose tissue replica matrix comprising a protein-oil emulsion formed with 2 percent weight / volume RuBisCo and 50 percent, 70 percent, or 90 percent butter cocoa in volume / volume, the mass of the adipose tissue replica was retained after cooking when the adipose tissue replica was formed by heat / cold denaturation than when it was formed by cross-linking with a transglutaminase. The released mass was liquid and appeared oily. During cooking of the adipose tissue replica matrix comprising an oil-protein emulsion formed with 2.6 and 0.6 percent weight / volume soy protein and 50 percent, 70 percent, or 90 percent by volume / volume of cocoa butter, more mass was retained from the adipose tissue replica when it was formed after heat / cold denaturation than when it was formed by cross-linking with qqci i η / ι ζηζ / Ε / γ 198 transglutaminase. The released mass was liquid and appeared oily. EXAMPLE 13: COOKING A REPLICA OF ADIPOSE TISSUE: THE CONCENTRATION OF PARTICULAR PROTEINS WITHIN THE FAT TISSUE MATRIX CONTROLS THE MASS OF THE REPLICA OF ADIPOSE TISSUE THAT REMAINS AFTER COOKING A series of adipose tissue replicas constructed from 1.4 percent w / v 8S mung bean protein with 90 percent w / v canola oil and 0.45 percent w / v soy lecithin were homogenized and increasing concentrations of sunflower oleosins in varying concentrations were added to the emulsion. The concentration of oleosin had a molar ratio variation from 1:10 to 1:106 of oleosins to triglycerides. An increase in mass retention after cooking was observed when the proportion of oleosins to QQCI I n / l 7Π7 / Β / Υ oil was higher in the adipose tissue replica. A series of adipose tissue replicas formed with different concentrations of RuBisCo with 70 percent vol / vol sunflower oil retained more mass during cooking as the concentration of RuBisCo was increased. The adipose tissue replicas containing 0 percent weight / volume RuBisCo melted completely, while the 1.9 percent weight / volume RuBisCo retained 10 percent mass, and the adipose tissue replica containing the 2.4 percent weight / volume RuBisCo retained 20 percent of the mass during cooking. 199 EXAMPLE 14: CONNECTIVE TISSUE ANALOGUE Replicas of connective tissue fibers were made by electrospinning a solution of mung bean globulin (22.5 milligrams / milliliter) containing 400 mM sodium chloride, 6.75 percent weight / volume polyvinyl alcohol, and trace amounts of sodium azide. (0.007 percent weight / volume). The resulting solution was pumped at 3 microliters / minute using a syringe pump, a 5 milliliter syringe through a Teflon tube, and a 21 gauge blunt needle. The needle was connected to a positive terminal of a feeding set. Spellman CZE 30 kV high voltage voltage was set to 17 kV and set 12 centimeters from an aluminum drum (about 12 centimeters long, 5 centimeters in diameter) that was wrapped in aluminum foil. The drum was attached to a shaft that was rotated by an IKA RW20 motor at approximately 220 revolutions per minute (rpm). The shaft was connected to a ground terminal of the high voltage feeder. The protein / polymer fibers that accumulated on the sheet were scraped and used as the connective tissue replicas. EXAMPLE 15: EXTENSION OF THE LIFE OF REDUCED LEGHEMOGLOBIN (HEMO-FE2*) Equine myoglobin was purchased from Sigma. Myoglobin was resuspended at 10 milligrams / milliliter in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl. SDS-PAGE analysis suggested that the protein purity was approximately 90 percent. Soybean leghemoglobin was purified from soybean nodules. QQCI I n / l 7Π7 / Β / ΥΙΛΙ 200 Glycine max root by means of ammonium sulfate precipitation (60 percent / 90 percent fractionation) as detailed in Example 1. The resuspended 90 percent ammonium sulfate leghemoglobin was further purified by exchange chromatography of anions (5 milliliter HiTrap Q FF FPLC column) in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl. Leghemoglobin was eluted in the flow through fractions. SDS-PAGE analysis suggested that the protein purity was approximately 70 percent. Leghemoglobin was buffer exchanged into 20 mM potassium phosphate, pH 7.4, 100 mM NaCl, and concentrated to 10 milligrams / milliliter on 3.5 kDa membrane concentrators. Carbon monoxide treatment: Myoglobin at milligrams / milliliter in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl, and leghemoglobin at 10 milligrams / milliliter in 20 mM potassium phosphate, pH 7.4, 100 mM NaCl, They were first degassed under vacuum for 1 hour at 4°C, then perfused with carbon monoxide gas for 2 minutes. The globins were then reduced from the heme-Fe3+ state to heme-Fe2+ by the addition of 10 mM sodium dithionite, 0.1 mM sodium hydroxide, for 2 minutes. Sodium dithionite and sodium hydroxide were removed from the protein solution using size exclusion chromatography (PD-10 desalting column) in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl, and potassium phosphate. 20 mM, pH 7.4, 100 mM NaCl, respectively. QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 201 Globin fractions were collected as a peak of red fractions, as assessed by visual estimation. UV-VIS spectra confirmed the presence of the heme-Fe2+ state for both proteins. After desalination, the solution was again perfused with gas for another 2 minutes. The color of the solutions was evaluated by taking UV-Vis spectra (250 nanometers to 700 nanometers) every 20 minutes using the nanodroplet spectrophotometer. Control samples were not treated with carbon monoxide. Sodium nitrite treatment: Myoglobin at 10 milligrams / milliliter in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl, and leghemoglobin at 10 milligrams / milliliter in 20 mM potassium phosphate, pH 7.4, 100 mM NaCl, were reduced from the heme-Fe3+ state to the heme-Fe2+ state by adding 10 mM sodium dithionite, 0.1 mM sodium hydroxide for 2 minutes. Sodium dithionite and sodium hydroxide were removed from the protein solution using size exclusion chromatography (PD-10 desalting column) in 20 mM potassium phosphate, pH 8.0, 100 mM NaCl, and potassium phosphate. 20 mM potassium, pH 7.4, 100 mM NaCl, respectively. Globin fractions were collected as the peak red fractions, as assessed by visual estimation. UV-VIS spectra confirmed the presence of the heme-Fe2+ state for both proteins. Sodium nitrite was then added to a final concentration of 1 mM starting from 100 nitrite. QQCI I n / l 7Π7 / Β / Υ 202 mM in phosphate buffer, pH 7.4. The lifetime of the heme-Fe2+ state was followed by recording UV-VIS spectra (from 250 to 700 nanometers), using the spectrophotometer as a function of time. Control samples were not treated with sodium nitrite. Data analysis of heme-Fe2+ lifetimes for myoglobin and leghemoglobin samples treated with carbon monoxide and sodium nitrite was carried out in Microsoft Excel by plotting the amplitude of peak absorbance at the wavelength of 540 nanometers. The baseline absorbance at 540 nanometers was determined by the UV-vis spectral state of the globin solutions before the addition of any additives, reduction of dithionite, or desalination. The integrated curve fitting function was used to produce the line of exponential best fit, the exponent of which refers directly to the half-life of the peak amplitude. The lifetimes of the heme-Fe2+ state and the combined red color of myoglobin and leghemoglobin solutions in the absence of carbon monoxide and sodium nitrite were approximately 6 hours and approximately 4 hours, respectively. The addition of sodium nitrite extended the lifetime of the heme-Fe2+ state and the combined red color to more than seven days. The addition of carbon monoxide extended the lifetime of the heme-Fe2+ state and the combined red color to more than two QQCI I n / l 7Π7 / Ε / ΥΙΛΙ weeks. 203 EXAMPLE 16: PREPARATION OF MEAT REPLICAS WHERE THE SIZE OF THE PARTICLES OF THE INDIVIDUAL UNITS OF THE TISSUE REPLICA IS VARY TO CONTROL THE GENERATION OF AROMA DURING COOKING The muscle tissue replica and the adipose tissue replica were prepared separately, and then combined into a meat tissue replica, such that the size of the individual tissue replica units was varied to control the generation of aroma during cooking. Individual replicas of fat, muscle, and connective tissue were constructed as follows. A replica of muscle tissue was prepared as in Example 2. The replica of muscle tissue formed an opaque gel of a reddish-brown color, with small amounts (< 1 milliliter) of inclusions of a dark red liquid the color of the venous blood. A connective tissue replica was prepared as in Example 14. A adipose tissue replica was prepared as in Example 7. Meat replicates with a lean to fat ratio of 85 / 15 were prepared by combining the individual muscle, connective and adipose tissues in such a way that the particle size of the individual tissue replicates was varied. (a) 2.1 grams of muscle replica with 0.9 grams of fat replica pieces of size 5 to 10 millimeters (coarse mixture); (b) 2.1 grams of muscle replica with 0.9 qqci i η / ι ζηζ / Ε / γ 204 grams of fat replica chopped to a size of 2 to 3 millimeters (fine mixture); and (c) 2.1 grams of muscle replica with 0.9 grams of fat replica mixed completely to a size < 1 millimeter (mixture). The muscle-only control sample contained 3 grams of muscle replicate alone. The fat-only control sample contained 3 grams of fat replica alone as particles of 5 to 10 millimeter size. Meat, muscle, and fat samples were cooked in sealed glass jars at 150°C for 10 minutes. The aroma profiles of the samples were analyzed by a panel of tasters, and by GS-MS. Sensory olfactory analysis of meat replica samples carried out by a panel of tasters suggested that the size of individual tissue units and the extent of their mixing within meat tissue replicas were correlated with the generation of different aromas. The cooked replica muscle tissue itself generated aromas associated with store-bought, slightly citrusy, star anise sauce. The cooked adipose tissue replica itself generated aromas associated with moldy, rancid, and sweet aromas. The cooked meat tissue replica (coarse particle size) generated aromas of sweet, slightly moldy, store-bought sauce and star anise. The cooked meat tissue replica (fine particle size) generated aromas associated with soy sauce, mold, slightly rancid, and beef broth. The meat tissue replica QQCI I n / l 7Π7 / Β / Υ 205 cooked (very fine particle size) generated aromas associated with sweet, mold, and soy sauce. All samples with the exception of the adipose tissue replica generated aromas associated with the smell of burnt meat, although to varying intensities. Analysis of the GCMS data indicated that the size of the individual tissue units and the extent of their mixing within the meat tissue replicas had profound effects on the generation of the aroma compounds after cooking. In particular, multiple aromatic compounds associated with fruit / green bean / metal (2-pentyl-furan) aromas appeared; walnut / green (4-methyl-thiazole); peanut butter / mold (pyrazine, ethyl); raw / roasted / earthy potato (Pyrazine, 2,3-dimethyl); vinegar (acetic acid); spice / caramel / almond (5-methyl-2-furancarboxaldehyde); cream (butyrolactone); sweet (2,5-dimethyl-3-(3-methylbutyl I)-pi raz i na); old fruit / beer (2-cyclopenten-1-one, 2-hydroxy¡-3methyl); mold / nut / coumarin / liquor / nogada / bread (3-acetyl-1 H-pyrroline); coconut / wood / sweet (pantolactone); penetrant (1 -H-pyrrole-2,2carboxaldehyde, 1-methyl); mint (caprolactam); toasted caramel (4H-pyran-4-one, 2,3-dihydro-3,5-dihydrox¡-6-methyl), only in the mixed meat replicas, but not in the meat replicas individual fabrics. Some other aromatic compounds appeared, for example, associated with gasoline-like (nonane, 2,6dimethyl), petroleum-like (3-hexene, 3-methyl) aromas; sour / rotten / fishy (pyridine); oil / wood / yogurt (acetoin); fat / honey / citrus (octanal); pungent / sweet / caramel (2-propanone, QQCI I n / l 7Π7 / Β / Υ 206 -hydroxyl), and walnut / burnt green (ethenyl-pyrazine), only in the individual tissue replicates, but did not accumulate in the mixed meat replicates. Additionally, the levels to which all of the above compounds accumulated during cooking depended on the sizes of the tissue units and the way they were mixed (coarse particle size, fine particle size, or very fine particle size (mixed)). In a similar manner to beef tissue replication, the structural organization and particle size of beef tissues were found to modify the response of beef tissues to cooking. For example, the flavor of meat is modified by the size of the particles. Beef samples were prepared as follows: beef muscle and beef fat samples were cut separately with a knife, and: (a) ground, where the knife-cut tissue cubes were passed through a conventional meat grinder. An 80 / 20 (w / w) lean / fat ground beef sample was prepared by mixing muscle and fat tissue cubes in the appropriate ratio prior to grinding. This sample preparation is referred to as a mixture of fine-sized particles. (b) The particle size of ground tissue was further reduced by freezing the ground tissue in liquid nitrogen, and crushing it using a mortar and pestle to obtain a powder. very fine (particle size < 1 millimeter). This sample preparation is referred to a mixture of particles of a very fine size. All QQCI I n / l 7Π7 / Β / ΥΙΛΙ 207 samples were cooked in sealed life flasks at 150°C for 10 minutes. The aroma profiles of the samples were analyzed by a panel of tasters, and by GC-MS, as described in Example 1. The muscle-only control sample contained 3 grams of muscle tissue alone. The fat-only control sample contained 3 grams of fat tissue alone. The ground beef sample contained 3 grams of an 80 / 20 (w / w) muscle / fat mixture. Sensory olfactory analysis of beef samples carried out by a panel of tasters suggested that the size of individual tissue units and the extent of their mixing within the samples were correlated with the generation of different aromas. The cooked beef muscle itself generated the typical aromas associated with cooked ground beef. The replica fat tissue cooked by itself generated slightly sweet aromas, and aromas associated with burnt mushrooms. The ground beef cooked with the mixture of fine-sized particles generated the typical aromas associated with cooked ground beef, with the presence of slightly sweet aromas characteristic of cooked fat. Ground beef cooked with the very fine particle size mixture generated aromas associated with cooked ground beef, but the slightly sweet aroma characteristic of cooked fat was not detected. Analysis of the GCMS data indicated that the particle size of the individual tissue units has an effect on the generation of the aromatic compounds after qqci i η / ι ζηζ / Ε / γ 208 cooking. In particular, the generation and / or amount of multiple aromatic compounds by the individual tissue samples or the ground beef sample varied in correlation with tissue particle size. Some of the aromatic compounds that differed between fine and very fine particle size of muscle tissue are as follows: 4H-pyran-4-one, 2,3-dihydro-3,5dihydroxy-6-methyl, 3-acetyl-1 H-pyrroline, 1-(6-methyl-2-pyrazin¡l)-1 ethanone, 2,5-dimethyl-3-(3-methyl-butyl)-pyrazine, 2-furan -carboxyaldehyde, 5-methyl, acetic acid, ethenyl-pyrazine, pyrazine, 2,3dimethyl, 2-propanone, 1-hydroxyl, octanal, acetoin, 4-methyl-thiazole, pseudo-2-pentyl-furan, 2- pentylfuran. Some of the aromatic compounds that differed between the fine and very fine particle size of the fatty tissue are: tr i eti I en g I i col: 4H-pyran-4-one, 2,3-dihydro3,5-dihydrox¡- 6-methyl, caprolactam, 1 -(6-methyl-2-pyrazin¡l)-1 ethanone, 2-cyclopenten-1-one, 2-hydroxy-3-methyl, butyrolactone, 2furan-carboxy-aldehyde , 5-methyl, ethanone, 1 - (2-furanilo), acetic acid, 2-ethyl-5-methyl-pyrazine, pyrazine, 2,3-dimethyl, pyrazine, ethyl, octanal, acetoin, 4-methyl-thiazole, pseudo-2-pentyl-furan, pyridine, nonane, 2,6-dimethyl. Some of the aromatic compounds that differed between a fine and very fine particle size of the 80 / 20 muscle / fat sample were: 4H-pyran-4-one, 2,3-dihydro-3,5dihydroxy-6-methyl , caprolactam, 1 H-1 -pyridine, 3-carbonitrile, 4-ethyl2-oxo-2,5,1 -H-pyrrole-2-2carboxaldehyde, 1- methyl, 2-cyclopenten-1one, 2-hydroxy-3- methyl, 2,5-dimethyl-3-(3-methyl-butyl)-pyrazine, butyrolactone, 2-furan-carboxy-aldehyde, 5-methyl, ethanone, 1-(2 QQCI I n / l 7Π7 / Β / ΥΙΛΙ 209 furanyl), acetic acid, ethenyl-pyrazine, 2-ethyl-5-methyl-pyrazine, pyrazine, 2,3-dimethyl; 2-propanone, 1 -hydroxyl, octanal, acetoin, 2-pentyl-furan. EXAMPLE 17: LEGHEMOGLOBIN CONTRIBUTION TO FLAVOR Beef flavors and aromas can be created in non-meat consumables by adding heme proteins. Ground chicken (90 percent lean, 10 percent fat) is strained through cheesecloth and mixed with recombinant soy leghemoglobin or recombinant bovine myoglobin to a final concentration of 0.5 to 1.0 percent w / w. Recombinant heme proteins were expressed in E. coli and purified by nickel affinity purification, as described in Example 1. Before being mixed with chicken, heme proteins were reduced with 20 mM sodium dithionite. Sodium dithionite was removed from the sample with a Zeba desalting column (Thermo Scientific). The leghemoglobin was desalted in 20 mM potassium phosphate, pH 7.4, 100 mM NaCl. The myoglobin was desalted in either 20 mM potassium phosphate, pH 7.4, 100 mM NaCI or 20 mM sodium citrate, pH 6.0, 100 mM NaCI. The reduced heme protein samples were divided into two, and half of the sample was bubbled with carbon monoxide (CO) for 2 min. After mixing the heme protein samples with ground chicken, the mixture was poured into nugget-shaped molds and incubated overnight at 4°C. The nuggets were cooked 210 baked or pan fried at 165°C until each nugget reached an internal temperature of 165°C. A panel of judges tested the nuggets with just chicken, chicken mixed with regulator, chicken mixed with either leghemoglobin or myoglobin + / - CO, or beef (90 percent lean, 10 percent fat). The judges answered a survey to evaluate the aroma and flavor of each nugget. The judges ranked the aroma and flavor of each nugget as follows: 1 = chicken, 2 = chicken + light beef, 3 = 50 / 50 chicken + beef, 4 = beef + light chicken, 5 = meat beef. The average scores received for each nugget are shown in Table 2. Percentages indicate final heme protein concentration w / w (abbreviations: KP = 20 mM potassium phosphate, pH 7.4, 100 mM NaCI buffer. NC = 20 mM Na citrate, pH 6.0, 100 NaCI buffer mM, n / d = not determined). The addition of recombinant leghemoglobin or myoglobin to chicken resulted in an increase in beef aroma and flavor. Beef flavor and aroma perception levels increased with myoglobin and leghemoglobin content. Leghemoglobin and myoglobin provide the same benefit for flavor and aroma. TABLE 2 QQCI I n / l 7Π7 / Β / ΥΙΛΙ Baked Fried in Pan Aroma Flavor Aroma Flavor Chicken 1 1 1 1 211 Baked Fried in Pan Aroma Flavor Aroma Flavor Chicken KP 1 1 2.5 1.2 Chicken NC 1.5 1.5 1.5 1 Chicken 0.5% legH KP 1.5 2.5 3.67 3.2 Chicken 0.5% legH + CO KP 2.5 2.5 2.67 2.2 Chicken 0.5% Mió NC 2 2 1.5 2.4 Chicken 0.5% Mio+CO NC 2 2 2.5 3 Chicken 0.5% Mio + CO KP 2.5 2.5 2.33 2 Chicken 0.8% Mio+CO NC 2 3 4 2.6 Chicken 1% Mio NC 4.5 4 n / a n / a Chicken 1% LegH NC 4 4 n / a n / a Ans 5 5 5 5 EXAMPLE 18: PREPARATION OF A NON-DAIRY LIQUOR CREAM A cream liqueur was made from a sunflower creamer, RuBisCo and whiskey (Jameson). A creamy sunflower fraction was made by mixing sunflower seeds in sodium phosphate QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 212 mM pH 8.0, 400 mM sodium chloride buffer. Seed debris was pelleted by centrifugation at 5000 g for 20 minutes, and the cream fraction was collected. The cream fraction was resuspended in 10 mM potassium phosphate buffer, pH 7.4, and collected by centrifugation at 5000 g, for 20 minutes. RuBisCo was purified as described in Example 1 and used as a 25 milligram / milliliter stock solution in 20 mM potassium phosphate, pH 7.0, 150 mM NaCI. In one example, cream liqueur was prepared as follows: 11.4 percent w / v sunflower cream fraction, 40 percent w / v Jameson Whiskey, 0.4 to 1.6 percent w / v RuBisCo, 0.5 percent w / v vanilla extract, 0.5 percent w / v espresso, and 1.5 percent w / v chocolate powder. The resulting mixture was homogenized at 5,000 psi (350 kg / cm2). In another example, the cream liqueur was made from a sunflower creamer and whiskey (Jameson) and sugar: 11.4 percent w / v sunflower creamer, 40 percent w / v Jameson Whiskey , 0.5 percent volume / volume vanilla extract, 0.5 percent volume / volume espresso coffee, 1.5 percent weight / volume chocolate powder, and 8 percent weight / volume sugar. Beverages were served either at room temperature or chilled. The resulting drinks were beige to 213 light chocolate. Tasting results suggested that the drink had a very creamy alcoholic flavor similar to dairy liqueur cream. The refrigerated product was preferred. The emulsion was stable at room temperature for at least 1 week (maximum test time). EXAMPLE 19: CHOCOLATE SPREAD A spreadable chocolate was made from 34 percent (w / w) cane sugar, 22 percent (w / w) cocoa powder, 19 percent (w / v) creamy pistachio fraction, and 12 percent (w / v) percent (volume / volume) of almond milk. Cane sugar and cocoa powder (Ghirarde11i) were purchased commercially. Skim almond milk was made as follows: Almonds were blanched by immersion in water at 100°C for 30 seconds. The blanched almonds were recovered and cooled by immersion in ice-cold water. The almonds were air dried. The almonds were rehydrated by immersion in water at 2°C for 16 hours. The rehydrated almonds were drained, mixed with water at a 1:2 weight / volume ratio, and blended in a Vitamix blender for 5 minutes. The mixed suspension was collected in a refrigerated container and stirred with a frozen cooling rod to cool. Once the suspension was cooled to 10°C, the suspension was placed at 2°C for up to 12 hours. The cream and almond cream were separated by centrifugation at 7480 g for 30 minutes at 4°C. The almond milk was separated into 3 layers, a qqci i η / ι ζηζ / Ε / γ 214 dense agglomerate of insoluble solids, a clear to translucent watery layer (referred to as skim almond milk), and a lighter, creamy, opaque layer (referred to as almond cream). The almond milk was then pasteurized at 75°C for 16 seconds, refrigerated, and stored at 2°C. A pistachio cream fraction was prepared by mixing the pistachios in a buffer of 100 mM sodium carbonate, pH 9.5, with 400 mM sodium chloride, and 1 mM EDTA, and then centrifuged at 5000 x g for 20 minutes. The cream fraction was collected and washed in the same regulator once again. After centrifugation at 5000 g for 20 min, the cream fraction was collected and washed in 20 mM sodium phosphate buffer, pH 7.4, with 50 mM sodium chloride and 1 mM EDTA. After centrifugation at 5000 g for 20 minutes, the cream fraction was collected and washed once more in neutral buffer (pH of 7.4), centrifuged at 5000 g for 20 minutes. The pistachio cream fraction was collected and stored at 4°C. The chocolate spread was made as follows. Cane sugar was melted in almond milk, cocoa powder was added to the sugar and milk mixture, with stirring and melted. The sugar, milk and cocoa were then added to the creamy pistachio fraction and beaten together. The resulting mixture was then poured into molds and allowed to rest for 24 hours at QQCI I n / l 7Π7 / Β / Υ refrigeration and freezing temperatures. 215 In another example, the chocolate spread was made from 42 percent (w / w) cane sugar, 27 percent (w / w) cocoa powder, 31 percent (w / w) a sunflower cream fraction , and 23 percent (volume / volume) skim almond milk. All ingredients and procedures other than the creamy sunflower fraction were as described above. The creamy sunflower fraction was created from mixing sunflower seeds in 5 times the weight to volume of a 40 mM potassium phosphate solution, pH 8, with 400 mM NaCl, 1 mM EDTA, then cooled to 20°C, and then the suspension was centrifuged. The top cream layer was removed and mixed in the same regulator, followed by heating for 1 hour at 40°C. The suspension was cooled to 20°C, then centrifuged; The cream layer was removed and mixed with 5 times the weight by volume of 100 mM sodium carbonate, pH 10, with 400 mM NaCl, and then centrifuged. The top layer was then mixed with 5 times the weight by volume of water, and centrifuged again; The resulting creamy fraction is very creamy, white, and neutral tasting. In another example, a spreadable chocolate was made from 37 percent (w / w) cane sugar, 23 percent (w / w) cocoa powder, 13 percent (w / w) sunflower cream fraction , and 7 percent (w / w) cocoa butter, and 20 percent w / v skim almond milk. 216 In another example, a chocolate spread was made from 37 percent (w / w) cane sugar, 23 percent (w / w) cocoa powder, 13 percent (v / w) sunflower creamer , and 7 percent (w / w) coconut oil, and 20 percent v / v skim almond milk. In another example, a chocolate spread was made from 37 percent (w / w) cane sugar, 23 percent (w / w) cocoa powder, 13 percent (w / w) sunflower creamer , and 7 percent (w / w) palm oil, and 20 percent v / v skimmed almond milk. In another example, a chocolate spread was made from 1.8 percent (w / w) cane sugar, 1.13 percent (w / w) cocoa powder, 88 percent (w / v) pistachio creamer. , and 9 percent skim almond milk, whisking together equal amounts of the spreads described above and pistachio oil. In another example, a chocolate spread was made from 8.5 percent (w / w) cane sugar, 5.4 percent (w / w) cocoa powder, 81 percent (w / v) sunflower creamer , and 4.6 percent (by volume / volume) skim almond milk, using the above-described blend of chocolate spread with sunflower cream in a 2:1 ratio. Visual and textural inspection of all products suggested that they formed stable, solid, and creamy spreads at 217 room temperature. All products were firm solids at refrigeration and freezing temperatures. The tasting results of all the products suggested a very pleasant, rich and creamy texture with the melting of the product in the mouth reviewed positively by the tasters. Individual tasters' preferences varied with respect to liking or disliking pistachio flavor, coconut flavor, preference for more or less sweet product, and more or less cocoa flavor. One particular sample is described as being similar to a milk chocolate spread, since the creamy sunflower fraction contributed a neutral flavor. EXAMPLE 20: GENERATION OF A REPLICA OF ADIPOSE TISSUE Adipose tissue replicas were generated using the ingredients listed in Table 3. QQCI I n / l 7Π7 / Κ / ΥΙΛΙ TABLE 3 Adipose Tissue Replica Ingredient % Coconut oil 65 Pea vicilin protein in regulator 21.3 Cocoa butter 10 Regulator 2.7 > 218 n c c Lecithin Suspension, 50 mg / mL 1 Total 100 QQCI Lecithin (SOLECMRF deoiled soy lecithin, The Solae Company, St. Louis, MO) was prepared at a concentration of 50 milligrams / ml in 20 mM potassium phosphate, 100 mM NaCl, buffered to pH 8.0, and sonicated ( Sonifier Analog Cell Disruptor model 102C, BRANSON Ultrasonics Corporation, Danbury, Connecticut) for 30 seconds. Pea vicilin protein was supplied as a liquid containing approximately 140 milligrams / gram pea vicilin in 20 mM potassium phosphate, 100 mM NaCl, buffered to pH 8.0. Coconut oil (Shay and Company, Milwaukie, OR) and cocoa butter (Cocoa Family, Duarte, CA) were melted by heating to 50°C to 70°C, then combined and kept warm until needed. The protein buffer solution, additional buffer, and lecithin suspension were mixed in a 32-ounce (907.2 gram) size metal beaker and equilibrated at room temperature. An emulsion was formed using a handheld homogenizer (OMNI model GLH equipped with 20-millimeter G20-195ST generating probe, OMNI International, Kennesaw, GA). The homogenizer probe was put into the mixture 219 lecithin protein and set to speed 4. The heated oil was then added slowly over the course of approximately 2 minutes while continuously moving the probe around the mixture. The emulsion was then heat established by placing the metal beaker in a 95°C water bath. Using a clean spatula, the emulsion was stirred every 20 seconds for 3 minutes total. The beaker was then removed from the water bath and stored at 4°C for several hours until completely cooled. EXAMPLE 21: GENERATION OF RAW FABRIC REPLICA A raw tissue replica was generated using the ingredients listed in Table 4. QQCI I n / l 7Π7 / Β / ΥΙΛΙ TABLE 4 Raw Tissue Replica Ingredient % Regulator 41.6 Heme protein in regulator 26.7 Pea legume in regulator, dry 12.1 Pea vicilin in regulator, dry 9.4 Flavor precursor mixture, 17x 6.2 220 Raw Tissue Replica Ingredient % Transglutaminase Preparation 4 Total 100 QQCI I n / l 7Π7 / Β / Υ The buffer was 20 mM potassium phosphate, 100 mM NaCl, pH 7.4. Heme protein was prepared at a concentration of 55 milligrams / gram in 20 mM potassium phosphate, 100 mM NaCl, buffer at pH 7.4. The precursor of the 17x flavor precursor mixture is described in Example 27. The pea legume was prepared in 20 mM potassium phosphate, 500 mM NaCl, buffer to pH 8, and then lyophilized before use. The final protein concentration of the dried material was 746 milligrams / gram. Pea vicilin was prepared in 20 mM potassium phosphate, 200 mM NaCl, buffer at pH 8, and then lyophilized before use. The final protein concentration of the dried material was 497 milligrams / gram. The liquid ingredients (regulator, heme, and the aroma precursor mixture) were mixed in a plastic beaker. Next, the pea legume was added and dried; The pea vicilin was allowed to rehydrate completely while gently stirring for 1 hour at room temperature. 221 environment. The dry transglutaminase preparation (ACTIVA® TI, Ajinomoto, Fort Lee, NJ) was then added and stirred for approximately 5 minutes until dissolved. Stirring was then turned off and the mixture was allowed to gel at room temperature until firm. After the gel had formed the raw tissue replicas were stored refrigerated until use. EXAMPLE 22: REPLICA OF HARD CONNECTIVE TISSUE A hard connective tissue replica was made as follows using isolated soy protein (Supro EX38, Solae), wheat gluten (Cargill), and bamboo fiber (Alpha-Fiber B-200, The Ingredient House). The purified proteins were freeze-dried and ground using a standard coffee grinder. Commercially available soy protein isolate and wheat gluten powders were used as received. The connective tissue replica contained 49 percent isolated soy protein, 49 percent wheat gluten, and 2 percent bamboo fiber. The ingredients were mixed thoroughly and loaded into the loading tube of the batch feeder of the extruder. A twin-shaft extruder (Nano 16, Leistritz Extrusion Corp.) was used, with a high-pressure water injection pump (Eldex), and custom-made die nozzles (stainless steel tube, 3 millimeters in diameter, 15 centimeters in length, pressure rated 3000+ PSI (210 kg / cm2)) joined by a tube connection of two Hy-Lok ferrules and one QQCI I n / l 7Π7 / Ε / ΥΙΛΙ 222 custom-made die with a threaded nozzle and a flow channel 10 millimeters internal diameter (ID) and 20 millimeters long. The dry mixture was fed to the extruder at a speed of 1 gram / minute. The water was fed by the pump into the second zone of the extruder barrel. The water feed rate was adjusted to the dry mix feed rate, such as to provide the 55 percent moisture level in the final extrudate. A temperature gradient was maintained along the extruder barrel as follows: feed zone - 25°C, zone 1 at 30°C, zone 2 at 60°C, zone 3 at 130°C, zone 4 at 130 °C. The active matrix plate was neither heated nor cooled. The die nozzle was actively cooled (by applying the wet tissue replica) to maintain the temperature of the extruded material below 100°C. The hard connective tissue replica obtained by this procedure was a dark grayish (cappuccino) colored material in the form of 3 millimeter thick filaments that had a tensile strength similar to that of animal connective tissue (3 MPa). EXAMPLE 23: REPLICA OF SOFT CONNECTIVE TISSUE A soft connective tissue replica was made as in Example 22, except that the water feed rate was adjusted to the dry mix feed rate to provide a 60 percent moisture level in the product. 223 final extruded. A temperature gradient was maintained across the extruder barrel as follows: feed zone at 25°C, zone 1 at 30°C, zone 2 at 60°C, zone 3 at 115°C, zone 4 at 115 °C. The active matrix plate was neither heated nor cooled. The die nozzle was actively cooled (by applying wet tissue) to maintain the temperature of the extruded material below 1 00°C. The soft connective tissue replica obtained by this process was a light grayish material in the form of 3 millimeter thick filaments that had a low tensile strength (<0.1 MPa) and had a significant propensity to split longitudinally into bands and thin fibers. EXAMPLE 24: PRO...

Claims

1. A method for imparting an aroma associated with beef to ground chicken, comprising adding a non-animal heme-containing protein to raw ground chicken to a final concentration of 0.5% to 1% (w / w), thereby producing raw ground chicken with added heme protein, wherein cooking the raw ground chicken with added heme protein results in the production of an increased amount of at least two volatile compounds having an aroma associated with beef relative to the amount of the two volatile compounds produced after cooking raw ground chicken lacking the added heme protein.

2. The method according to claim 1, wherein the non-animal heme-containing protein is a heme-containing protein from a plant, fungus, algae, protozoan, or bacteria.

3. The method according to claim 1, wherein the non-animal heme-containing protein is a leghemoglobin, a flavohemoglobin, a Hellgate I globin, an erythrocruorin, a protoglobin, a cyanoglobin, a chlorocruorin, a truncated hemoglobin including HbN and HbO, a truncated globin 2 / 2, a hemoglobin 3 including Glb3, a cytochrome, or a peroxidase. 4 - The method according to claim 1, wherein the non-animal heme-containing protein has a sequence of 259 amino acids with at least 70% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27.

5. The method according to claim 4, wherein the non-animal heme-containing protein has an amino acid sequence with at least 80% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27.

6. The method according to claim 1, wherein the two volatile compounds are selected from the group consisting of propanal, butanal, 2-ethylfuran, heptanal, octanal, trans-2-(2-pentenyl)furan, (Z)-2-heptenal, (E)-2-octenal pyrrole, 2,4-dodecadienal, 1-octanal, (Z)-2-decenal, and 2-undecenal.

7. A method for imparting an aroma associated with beef to ground chicken, comprising adding a non-animal heme-containing protein to raw ground chicken to a final concentration of 0.1% to 1% (w / w), thereby producing raw ground chicken with added heme protein, wherein cooking the raw ground chicken with added heme protein results in the production of an increased amount of at least two volatile compounds having an aroma associated with beef relative to the amount of the two volatile compounds produced after cooking raw ground chicken lacking the added heme protein.

8. The method according to claim 7, comprising adding the non-animal heme-containing protein to raw ground chicken to a final concentration of 0.5% to 1% (w / w). 9 - The method according to claim 7, wherein the non-animal heme-containing protein is a heme-containing protein from a plant, fungus, algae, protozoan, or bacteria.

10. The method according to claim 7, wherein the non-animal heme-containing protein is a leghemoglobin, a flavohemoglobin, a Hellgate I globin, an erythrocruorin, a protoglobin, a cyanoglobin, a chlorocruorin, a truncated hemoglobin including HbN and HbO, a truncated globin 2 / 2, a hemoglobin 3 including Glb3, a cytochrome, or a peroxidase.

11. The method according to claim 7, wherein the non-animal heme-containing protein has an amino acid sequence with at least 70% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27.

12. The method according to claim 11, wherein the non-animal heme-containing protein has an amino acid sequence with at least 80% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27.

13. The method according to claim 7, wherein the two volatile compounds are selected from the group consisting of propanal, butanal, 2-ethylfuran, heptanal, octanal, trans QQCI I n / l 7P7 / K / YILI 261 2-(2-pentenyl)furan, (Z)-2-heptenal, (E)-2-octenal pyrrole, 2,4-dodecadienal, 1-octanal, (Z)-2-decenal, and 2-undecenaL 14. A method for imparting an aroma associated with beef to ground chicken, comprising adding a non-animal heme-containing protein to raw ground chicken, thereby producing raw ground chicken with added heme protein, wherein cooking the raw ground chicken with added heme protein results in the production of an increased amount of at least two volatile compounds having an aroma associated with beef relative to the amount of the two volatile compounds produced after cooking raw ground chicken lacking the added heme protein, wherein the at least two volatile compounds are selected from the group consisting of propanal, butanal, 2-ethylfuran, heptanal, octanal, trans-2-(2-pentenyl)furan, (Z)-2-heptenal, (E)-2-octenal, pyrrole, 2,4-dodecadienal, 1-octanal, (Z)-2-decenal, and 2-undecenaL 15. The method according to claim 14, wherein the non-animal heme-containing protein is a heme-containing protein from a plant, fungus, algae, protozoan, or bacteria.

16. The method according to claim 14, wherein the non-animal heme-containing protein has an amino acid sequence with at least 70% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27. 17.- The method according to claim 16, in 262 wherein the non-animal heme-containing protein has an amino acid sequence with at least 80% sequence homology to any of the amino acid sequences set out in SEQ ID Nos: 1-17 or 21-27.

18. The method according to claim 14, wherein the non-animal heme-containing protein is a leghemoglobin, a flavohemoglobin, a Hellgate I globin, an erythrocruorin, a protoglobin, a cyanoglobin, a chlorocruorin, a truncated hemoglobin including HbN and HbO, a truncated globin 2 / 2, a hemoglobin 3 including Glb3, a cytochrome, or a peroxidase.

19. The method according to claim 14, comprising adding the non-animal heme-containing protein to raw ground chicken to a final concentration of 0.1% to 1% (w / w).

20. The method according to claim 19, comprising adding the non-animal heme-containing protein to raw ground chicken to a final concentration of 0.5% to 1% (w / w).