Structured protein isolate and related methods

Abstract

Food and / or its ingredients can include a lipid component, a structured protein isolate, and / or any other ingredient. A method for forming a structured protein isolate can include obtaining protein isolate units from a protein source and collecting the structured protein isolate.

Description

Technical Field

[0001] Cross - Reference to Related Applications This application claims the benefit of U.S. Provisional Application No. 63 / 352,773, filed on June 16, 2022, and U.S. Provisional Application No. 63 / 432,915, filed on December 15, 2022, each of which is incorporated herein by reference in its entirety.

[0002] This application is related to U.S. Application No. 17 / 857,871, filed on July 5, 2022, which is incorporated herein by reference in its entirety.

[0003] The present invention generally relates to the field of food science, and more specifically, to novel and useful systems and methods in the field of food science.

Brief Description of the Drawings

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[0005] The following description of embodiments of the present invention is not intended to limit the present invention to these embodiments, but is intended to enable any person skilled in the art to manufacture and use the present invention.

[0006] 1. Overview As shown in FIG. 1, the method can include obtaining protein isolate units from a protein source (S100) and collecting structured protein isolates (S400). However, the method can further or alternatively include any other suitable steps.

[0007] In variations, the method can function to produce foods having target properties (e.g., extensibility properties and / or meltable properties), substitutes for target foods (e.g., analogs), ingredients used to produce foods, and / or any other products.

[0008] 2. Examples In a first example, the method includes obtaining a protein isolate solution (e.g., including protein isolate units) from a protein source (e.g., a plant-based material), diluting the protein isolate solution using water, a poor solvent, and / or any other diluent, separating an insoluble fraction from the diluted protein isolate solution (e.g., by sedimentation, precipitation, fractionation, etc.), and collecting a structured protein isolate (e.g., an aggregate of structured protein isolate) from the insoluble fraction (e.g., collecting the insoluble fraction as a component, where the insoluble fraction includes the structured protein isolate). In a second example, the method includes obtaining a protein isolate solution from a protein source, mixing the protein isolate solution with a lipid component (e.g., emulsifying) to form a protein isolate mixture (e.g., an oil-water emulsion), diluting the protein isolate mixture (e.g., a mixture including the protein isolate and the lipid), separating an insoluble fraction from the diluted protein isolate mixture (e.g., fractionating the insoluble fraction, where the insoluble fraction includes the structured protein isolate), and collecting a structured protein isolate from the insoluble fraction. In a third example, the method includes obtaining a protein isolate solution from a protein source, diluting the protein isolate solution using a diluent including an aqueous solution mixed with a lipid component (e.g., emulsified), separating an insoluble fraction from the diluted protein isolate solution, and collecting a structured protein isolate from the insoluble fraction.

[0009] The collected structured protein isolate can optionally be used to manufacture food products (e.g., plant-based food products). In a first example, the collected structured protein isolate can be mixed with an aqueous component (e.g., water containing a gelling additive), a lipid component, and / or other components, and processed (e.g., emulsified) to form a structured protein isolate emulsion. The structured protein isolate emulsion can be heated (e.g., below the protein denaturation point) and shaped to form a gel. The gel can be a food product (e.g., a fresh cheese replica) and / or can be further processed to manufacture a food product. In a second example, the collected structured protein isolate can be combined with an aqueous component, a lipid component, a microbial culture (e.g., a cheese culture), and / or any other components, and processed (e.g., emulsified) to form a structured protein isolate emulsion. The emulsion can be processed by gelling, fermentation, and / or other methods to manufacture a food product (e.g., an aged cheese replica). In a third example, the collected structured protein isolate is used as a component of a food product (e.g., a dairy product or an alternative to an animal protein).

[0010] 3. Technical Advantages Variations of the technology can provide one or more advantages over the prior art.

[0011] In contrast to certain dairy proteins, plant-based proteins denature when exposed to heat, form new bonds (e.g., form throughout the substrate; form crosslinks, etc.), and form isotropically bonded gels, which can limit stretching and melting. Variations of the technology enable the use of plant-based proteins to manufacture meltable and stretchable products (e.g., food products).

[0012] First, due to a modification of the technology, a mixture of protein, water, and lipid components can exhibit stretching and / or melting properties like those of dairy products when heated. In an example, a plant-based protein solution containing a structured protein isolate (SPI) suspended in water can be mixed with (e.g., emulsified with) a lipid component, and the mixture melts upon heating and / or forms an extensible matrix. In another example, stretching and / or melting properties can be achieved by the SPI itself (e.g., without a lipid component). In the modification, stretching and / or dissolving properties can be achieved without animal-derived products (e.g., animal proteins) and / or soy derivatives.

[0013] Second, due to a modification of the technology, the proportion of carbohydrates (e.g., gums, starches, etc.) used in plant-based alternative foods can be reduced or eliminated while maintaining desirable stretching and / or melting properties. Thereby, the plant-based alternative foods can have a nutritional profile (e.g., including a high protein content) that more closely matches that of a target food (e.g., a dairy product).

[0014] Third, a modification of the technology can induce gelation (e.g., curd formation) in plant-based products. The resulting gel can be used directly as a food and / or as a component in a food. In a specific example, the resulting gel can contain an SPI solution, which is at a target pH (e.g., basic pH, acidic pH, etc.) and / or a target protein concentration. The resulting gel can be used as cheese (e.g., shredable cheese, stretchable cheese, meltable cheese, etc.).

[0015] Fourth, due to variations in the technology, products with unexpected properties can be manufactured. In a first example, a mixture of SPI and lipid components (e.g., heated gels, non-heated gels, etc.) can result in unexpected extensibility properties, as exemplified in FIGS. 8A, 8B, 8C, 10A, 10B, 22, 23A, 23B, 23C, 25A, 25B, 25C, 25D, and 25E. In a second example, a mixture of SPI and lipid components can result in unexpected melting properties, as exemplified in FIGS. 9A, 9B, 21, 23A, 23D, 24, and 25A. In a third example, a mixture of SPI and lipid components can result in unexpected protein unfolding and / or denaturation behavior (e.g., related to gelation behavior), as exemplified in FIG. 12.

[0016] Fifth, variations in the technology can include forming SPI in the presence of lipids, which can result in SPI and / or SPI aggregates (e.g., SPI structures and / or SPI aggregate structures) having increased and stable interactions with the lipids. For example, the lipids can be trapped within the SPI and / or SPI aggregates. In certain examples, these lipid interactions can facilitate extensibility and / or melting properties by allowing "sliding" between SPI and / or SPI aggregates. These interactions can support cohesive gels containing lipid components, and the gels have improved extensibility and / or melting properties.

[0017] Fifth, conventional protein isolation methods can denature proteins. In particular, isoelectric precipitation can denature all or part of the isolated protein. Modifications of the technique include forming SPI without denaturing the constituent proteins and / or denaturing less than a threshold percentage (e.g., 10%, 5%, 2%, 1%, etc.) of the constituent proteins. In examples, this can increase the extensibility, melt characteristics, and / or other properties of products manufactured using SPI. In certain examples, SPI formed without denaturing the constituent proteins can interact with other SPI without forming a bond (e.g., a covalent bond) between the SPI, which can facilitate extension and / or melting.

[0018] However, the systems and methods disclosed herein provide additional advantages.

[0019] 4. Method As shown in FIG. 1, the method can include obtaining a protein isolate unit from a protein source (S100) and collecting a structured protein isolate (S400). The method can optionally include combining the protein isolate unit with a lipid component (S200), diluting the protein isolate unit (S300), processing the structured protein isolate (S500), manufacturing a product containing the structured protein isolate (S600), and / or other suitable steps.

[0020] All or part of the method can be performed iteratively, simultaneously, non-simultaneously, periodically, during food manufacturing, and / or at other suitable times. All or part of the method can be performed automatically, manually, semi-automatically, and / or by other means.

[0021] In examples, the method can include the systems and / or methods described in U.S. Patent Application No. 17 / 857,871, filed July 5, 2022, which is incorporated by reference in its entirety.

[0022] All or part of the method can be carried out without denaturing the protein (e.g., protein isolate unit) and / or by denaturing less than a certain percentage of the proteins in the sample (e.g., in the protein source, protein source solution, protein isolate mixture, structured protein isolate, structured protein isolate mixture, product, any other sample, etc.). For example, the sample is preferably formed and / or processed such that less than a threshold percentage of the proteins in the sample are denatured, but can alternatively be formed and / or processed in other ways. The threshold percentage of protein can be from 0.01% to 50% or any range or value therebetween (e.g., 0.05%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, etc.), or can be less than 0.01% or more than 50%. In a first specific example, the sample is exposed to a pH level less than a first pH threshold (e.g., acid-induced denaturation threshold) and / or greater than a second pH threshold (e.g., base-induced denaturation threshold) during formation and / or processing. The first pH threshold can be from 2 to 6.5 or any range or value therebetween (e.g., 3, 4, 5, 6, etc.), or can be less than 2 or more than 6.5. The second pH threshold can be from 7.5 to 12 or any range or value therebetween (e.g., 8, 9, 10, 11, etc.), or can be less than 7.5 or more than 12. In a second specific example, the sample is exposed to a temperature less than a temperature threshold (e.g., heat denaturation threshold) during formation and / or processing. The temperature threshold can be from 6°C to 100°C or any range or value therebetween (e.g., 70°C, 75°C, 8°C, 85°C, 90°C, etc.), or can be less than 6°C or more than 100°C. Optionally, the sample can be exposed to a temperature above the temperature threshold for less than a threshold period (e.g., 1 second, 2 seconds, 5 seconds, 10 seconds, 15 seconds, 30 seconds, 1 minute, 5 minutes, 10 minutes, 30 minutes, 1 hour, any range or value therebetween, etc.). In a third specific example, the sample is exposed to a salt concentration level less than a salt concentration threshold during formation and / or processing. The salt concentration threshold can be from 0.1 M to 5 M or any range or value therebetween (e.g., 0.1 M to 1 M, 0.5 M to 2 M, 0.8 M to 0.9 M, etc.), or can be less than 0.1 M or more than 5 M. Optionally, the salt concentration threshold can depend on the pH of the sample.The salt concentration threshold can optionally be related to a conductivity threshold of 100 millisiemens to 25,000 millisiemens or any range or value therebetween, or can be less than 100 millisiemens or greater than 25,000 millisiemens. The denaturation threshold (first and / or second pH threshold, temperature threshold, exposure time threshold, salt concentration threshold, etc.) can optionally be determined based on the type of protein.

[0023] The method can be used with one or more sources (e.g., a substrate) and / or source components (e.g., a part of the source), and the protein and / or other components can be obtained from the source and / or source components. Examples of sources include plant substances (such as processed and / or unprocessed plant substances), animal substances (e.g., dairy products such as milk, insects such as Acheta domesticus, meat, etc.), non-animal substances, fungal substances, algal substances, seaweed substances, microbial substances (e.g., bacteria), any organism, food, natural sources, synthetic sources, dairy sources, non-dairy sources, and / or any other source. Examples of source components include nuts, fruits, seeds, beans, stems, leaves, roots, flowers, stamens, shells, and / or any other component of the relevant source. The source can be dried or in solution. The source can be processed (e.g., lipid removal including defatting, mechanical treatment, chemical treatment, extraction, fermentation, protein modification, filtration, concentration, and / or any other treatment) and / or unprocessed. In certain examples, the source can be in a crushed form and / or a powder form. In another specific example, the source can be an oilseed cake. The source can optionally be a protein source (e.g., a source from which protein can be extracted). In certain examples, the protein source can be a concentrated protein source. The protein source can optionally have a protein concentration exceeding a threshold ratio, and the threshold ratio can be 5% to 90% or any range or value in between (e.g., 10%, 20%, 30%, 40%, 50%, 60%, 70%, etc.), or less than 5% or more than 90%. The source can be the whole component (e.g., in its natural state or close thereto), a processed component (e.g., including additives or other components, etc.), and / or any other suitable source.

[0024] Vegetable substances include peas (e.g., pea powder, pea starch, etc.), rice (e.g., rice flour, glutinous rice flour, white rice flour, brown rice flour, etc.), fruits, cassava (e.g., cassava powder), potatoes, cacao beans, truffles, olives, coconut pulp, grape pomace, pumpkins (e.g., pumpkin seeds), cottonseeds, canola, sunflowers (e.g., sunflower seeds), pistachios, almonds, walnuts, walnut fruits, cashew nuts, Brazil nuts, hazelnuts, macadamia nuts, pecan nuts, peanuts, hemp, hops, enoki (e.g., Celtis), oats, rice, poppies, watermelons (e.g., watermelon seeds), chestnuts, chia, flax, quinoa, soybeans, split mung beans, aquafaba, lupini, fenugreek, kiwis, Chinese prickly ash, mustard, sesame, algae, duckweeds (e.g., Spirodela polyrhiza), squashes, chickpeas, pine nuts, citrus fruits (e.g., citrus fiber), broad beans (e.g., broad bean flowers), grapes (e.g., grape pomace), lima beans (e.g., lima bean paste), corn (e.g., zein derived from corn), carrageenan (e.g., kappa-carrageenan); plants selected from the genera Cucurbita, Anacardium, Cannabis, Salvia, Arachis, Brassica, Sesamum, Legume, and / or other genera; plants selected from the families Anacardiaceae, Asteraceae, Leguminosae, Cucurbitaceae, Rosaceae, Lamiaceae, and / or other families, combinations thereof, and / or other vegetable substances may be included. Vegetable substances may include major oilseed crops (e.g., soybeans, rapeseed, sunflowers, sesame, niger, castor, canola, cottonseeds, etc.), minor oilseed crops (coconuts, palm seeds, pumpkins, etc.), and / or other crops or vegetable substances.The plant-based substances may include a single plant-based substance, a mixture of various plant-based substances, animal-based substances (e.g., insect-based substances, mammalian products, etc.) and / or substances from other sources.

[0025] The method can be used with one or more lipid components (e.g., fats, oils, butter, any lipid, etc.). The lipid components are preferably obtained from one or more plant sources (e.g., plant substances), but can alternatively be obtained from animal sources (e.g., dairy butter, lard, tallow, insect fat, etc.) and / or any other source. The lipid components can preferably be triglycerides, but can alternatively be monoglycerides, diglycerides, free fatty acids, phospholipids, and / or any other lipid. The lipid components can be saturated, unsaturated (e.g., monounsaturated, polyunsaturated, etc.), and / or have any other classification. In certain examples, natural antioxidants (e.g., tocopherol, ascorbic acid, carotenoids, flavonoids, amino acids, phospholipids, sterols, etc.) and / or synthetic antioxidants (e.g., BHT) can optionally be used to ensure the chemical stability (e.g., during storage, cooking, etc.) of monounsaturated and / or polyunsaturated lipids. The lipid components can be liquid at the target temperature (e.g., room temperature), solid at the target temperature, and / or be in any other physical state. Examples of lipid components include avocado, mustard, coconut, palm, palm fruit, palm fruit stearin, peanut, canola, cocoa, grape seed, olive, rice bran, safflower, sesame, sunflower, soybean, pumpkin (e.g., pumpkin seeds), kokum, shea, mango, hemp, vegetables, any neutral lipid, synthetic lipid, any combination thereof, lipid species below a threshold ratio (e.g., canola fat), and / or any other fat and / or oil derived from lipids. The lipid components can include combinations (e.g., blends) of lipid components. In a first example, a blend of a lipid that is solid at room temperature (e.g., a fat) and a lipid that is liquid at room temperature (e.g., an oil) can be used. In a second example, blends of different types of plant-based lipids, blends of different types of animal-based lipids, and / or blends of plant-based lipids and animal-based lipids can be used. Optionally, the lipid components can be selected, modified, and / or otherwise processed such that the lipid components are stable at room temperature and / or have a melting profile that matches a target melting profile (e.g., for a target product).Modification of the lipid component includes transesterification, refining, clarification, fractionation, adjustment of the degree of saturation, adjustment of the lipid crystal structure, adjustment of the chain length, adjustment of the melting point, adjustment of the smoke point, and / or modification.

[0026] The method can optionally be used together with phospholipids. Phospholipids can include lecithin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, and / or any other phospholipid, or a combination thereof. The phospholipids are preferably obtained from one or more plant sources, but can additionally or alternatively be obtained from animal sources and / or any other source. In certain examples, the lipid component includes phospholipids (e.g., the lipid component in all or part of the method refers to a mixture of lipids and phospholipids).

[0027] The method can be used with one or more protein isolate units. The protein isolate units can include globulins (e.g., 2S globulin, 11S globulin, 7S globulin, conglycinin, napin, sfa, edestin, amandin, concanavalin, vicilin, legumin, cruciferin, helianthinin, etc.), pseudoglobulins, globular proteins, prolamins, albumins, gluten, binding proteins (e.g., lipoproteins, mucoproteins, etc.), other storage proteins (e.g., albumins, prolamins, gluten, etc.), animal proteins (e.g., casein, insect proteins, etc.), and / or any other suitable proteins, or combinations thereof. In certain examples, the protein (e.g., in a protein source) includes edestin protein (e.g., about 75% - 80%), vicilin protein (e.g., about 20% - 25%), and other proteins (e.g., about 0% - 5%). In another specific example, the protein (e.g., in a protein source) includes globulin (about 65% - 75%), albumin (about 25% - 37%), and sulfur-rich proteins. However, the protein isolate units can include any other suitable protein composition. The protein isolate units can include casein proteins, non-casein proteins, mammalian proteins, non-mammalian proteins, animal proteins, non-animal proteins, and / or any other proteins, or combinations thereof. In certain examples, the protein isolate units can include allergen proteins (e.g., soybean protein, wheat protein, etc.) below a threshold amount, casein, mammalian proteins, and / or animal proteins, and the threshold amount can be 0.1% - 10% or any range or value in between (e.g., 10%, 5%, 3%, 2%, 1%, 0.1%, etc.), or alternatively greater than 10% or less than 0.1% (e.g., 0%).

[0028] A protein isolate unit can be a protein monomer arranged in an oligomeric complex or can contain it and / or can have any other quaternary structure. For example, a protein isolate unit can contain a hexamer (e.g., a stack of trimers). A protein isolate unit preferably has both hydrophilic and hydrophobic regions, or alternatively can have regions that are mostly or completely hydrophilic or hydrophobic (e.g., multiple hydrophilic regions with different degrees of hydrophilicity, regions with similar hydrophilicity / hydrophobicity, etc.). The diameter of a protein isolate unit can be 5 nm to 500 nm or any range or value in between (e.g., 10 nm to 50 nm, 50 nm to 200 nm, 100 nm to 200 nm, greater than 50 nm, less than 200 nm, etc.), or can be less than 5 nm or greater than 500 nm. The thickness of a protein isolate unit can be 5 nm to 500 nm or any range or value in between (e.g., 10 nm to 50 nm, 50 nm to 200 nm, 100 nm to 200 nm, greater than 50 nm, less than 200 nm, etc.), or can be less than 5 nm or greater than 500 nm. The shape of a protein isolate can be spherical, fractal, fibrous, and / or any regular and / or irregular shape. A protein isolate can optionally have a uniform or non-uniform size distribution and shape. One or more components (e.g., lipid components, aqueous components, salts, minerals, etc.) can optionally be bound to the protein isolate unit, located within (e.g., enclosed within) the protein isolate unit (e.g., within an oligomeric complex), located outside (e.g., surrounding) the protein isolate unit, and / or associated with the protein isolate unit in other ways. A protein isolate unit is preferably extracted and / or obtained by other methods such as the S100 method, but can also or alternatively be obtained by other methods. A protein isolate unit can optionally be located within a protein isolate mixture. A protein isolate mixture can contain protein isolate units and one or more other components (e.g., aqueous components, lipid components, etc.). In a specific example, a protein isolate mixture is a protein isolate solution (e.g., containing protein isolate units, an aqueous or non-aqueous liquid, and / or any other components).

[0029] The method can be used with one or more structured protein isolates. A structured protein isolate (SPI) can include a plurality of protein isolate units (e.g., aggregates, clusters, agglomerates, etc.) arranged in a structure. The SPI structure can be spherical (e.g., a shell of protein isolate units), an amorphous structure, and / or any other structure, examples of which are shown in FIGS. 5A, 5B, 5C, and 5D. The SPI structure can optionally be a micelle (e.g., colloquially referred to as a micelle), which can be a true micelle (e.g., having a more hydrophilic region of constituent protein isolate units arranged at the ends of the micelle and a more hydrophobic region arranged at the center of the micelle, or vice versa for an inverse micelle) or a pseudo micelle (e.g., a "micelle" similar to a casein "micelle"), examples of which are shown in FIGS. 5B, 5C, and 5D. The micelle SPI can optionally include one or more layers of protein isolate units (e.g., a layer surrounding a lipid component, a layer surrounding an aqueous component, etc.). The number of protein isolate units within the SPI can be from 2 to 50 or any range or value therebetween (e.g., 2 to 10, at least 2, at least 3, at least 5, at least 10, etc.), or alternatively can be greater than 50. The diameter of the SPI can be from 50 nm to 500 nm or any range or value therebetween (e.g., 100 nm to 500 nm, 100 nm to 200 nm, 150 to 400 nm, 180 nm to 300 nm, etc.), or alternatively can be less than 50 nm or greater than 5000 nm.

[0030] Optionally, an interaction (e.g., a bond) can exist between protein isolate units within the SPI. One or more components (e.g., lipid components, phospholipids, aqueous components, salts, minerals, etc.) can optionally interact with (e.g., bind to, capture, attract, repel, surround, etc.) the SPI, be located within the SPI (e.g., within an oligomeric complex), be located outside the SPI, entangle between the constituent protein isolate units of the SPI, interact with (e.g., bind to, capture, attract, repel, surround, etc.) the constituent protein isolate units of the SPI, and / or associate with the SPI in other ways. The interaction can be a covalent bond, an ionic bond, a hydrogen bond, a van der Waals bond, a London dispersion force, and / or any other bond or interaction. In certain examples, the lipid component is located within the SPI (e.g., encapsulated within the SPI structure), surrounds the SPI, interacts with the SPI, and / or associates with the SPI in other ways. The SPI is preferably formed by the S300 method and / or the S400 method, but can also or alternatively be formed by other methods. In another specific example, the SPI can interact with phospholipids. For example, the phospholipid can promote the encapsulation of the lipid component within the micellar SPI by forming hydrophilic bonds and / or other interactions with the constituent protein isolate units and hydrophobic bonds and / or other interactions with the lipid component (e.g., the phospholipid forms a layer between the protein isolate unit and the lipid component).

[0031] The SPI preferably has both a hydrophilic region and a hydrophobic region, or alternatively, can have regions that are mostly or completely hydrophilic or hydrophobic (e.g., multiple hydrophilic regions with different degrees of hydrophilicity, regions with similar hydrophilicity / hydrophobicity, etc.). The SPI can have a different distribution of hydrophilic and / or hydrophobic regions compared to protein isolate units (e.g., non-aggregated protein isolate units, constituent protein isolate units, etc.). For example, the SPI can have increased or decreased hydrophobicity and / or hydrophilicity in the regions. In a specific example, the SPI can have increased outer surface hydrophobicity compared to protein isolate units (e.g., protein isolate units before forming the SPI). In a first example, the ratio of the area of the outer surface of the hydrophobic SPI can be larger than the ratio of the area of the outer surface of the hydrophobic protein isolate units. The increase in the ratio of the area of the outer surface that is hydrophobic in the SPI compared to the protein isolate units can be from 1% to 50% or any range or value in between (e.g., 2%, 5%, 10%, 25%, etc.), or alternatively less than 1% or more than 50%. In a second example, all or part of the area of the outer surface of the SPI can have a lower polarity than all or part of the area of the outer surface of the protein isolate units. The different distribution of hydrophilic and / or hydrophobic regions in the SPI compared to the protein isolate units can optionally result in an increase in the interaction between the SPI and lipid components, phospholipids, one or more other SPIs, and / or any other components (e.g., an increase in the number of interactions, an increase in the stability of the interactions, an increase in the binding affinity, etc.). In an exemplary example, by increasing the hydrophobicity of all or part of the outer surface of the SPI, the interaction between the SPI and lipid components can be increased (e.g., compared to the interaction between the SPI and water). The different distribution of hydrophilic and / or hydrophobic regions in the SPI compared to the protein isolate units can result in a decrease in the interaction between the SPI and aqueous components, one or more other SPIs, other proteins, and / or any other components (e.g., a decrease in the number of interactions, a decrease in the stability of the interactions, a decrease in the binding affinity, etc.).In an exemplary example, the interaction between SPI and the lipid component can increase compared to the interaction between SPI and water due to an increase in the hydrophobicity of all or part of the outer surface of SPI.

[0032] Differences in the hydrophilic and / or hydrophobic regions of SPI compared to protein isolate units can be related to conformational changes in the constituent protein isolate units within SPI (e.g., conformational changes that occur during aggregation), the arrangement of the constituent protein isolate units within SPI, the interaction between the components and SPI, and / or any other differences between the non-aggregated protein isolate units and SPI (e.g., can be related to the results thereof). In a first specific example, conformational changes in the constituent protein isolate units within SPI result in an increase in the hydrophobicity and / or hydrophilicity of the regions. In a specific example, conformational changes in the constituent protein isolate units within SPI result in an increase in the hydrophobicity of one or more regions of the outer surface of SPI. In an example, the conformational changes of the constituent protein isolate units can be induced by a change in pH, a change in temperature, a change in salt concentration, a change in protein concentration, an interaction between adjacent constituent protein isolate units, an interaction between the constituent protein isolate units and other compounds (e.g., water, salts, polar and / or non-polar solvents, other components, etc.), and / or can be induced in other ways. In a specific example, the interaction (e.g., non-covalent bond, covalent bond, etc.) between the constituent protein isolate units and a second component (e.g., another protein isolate unit) can result in a conformational change of the protein isolate units, and the favorability of this interaction can be increased and / or reduced by a change in the environment (e.g., adjustment of the salt concentration). It is preferred that the conformational changes do not include denaturation (e.g., the conformational changes of the protein isolate units are reversible when the protein isolate units dissociate from SPI), or alternatively, partial or complete denaturation can be included. In a second specific example, one or more constituent protein isolate units can be arranged such that the hydrophilic regions of the constituent protein isolate units face the inside of SPI, and the hydrophobic regions of the constituent protein isolate units face the outside of SPI.

[0033] Structured protein isolates can optionally cluster into one or more aggregates (e.g., SPI aggregates, super-aggregates). SPI aggregates include one or more spheres of SPI (e.g., droplets, micelles, etc.), microfibril aggregates, amorphous aggregates, and / or any other structure of SPI. The number of SPI within an SPI aggregate can be from 2 to 50 or any range or value therebetween (e.g., 2 to 10, 20 to 40, 40 to 50, 30 to 50, greater than 2, greater than 3, greater than 5, greater than 10, etc.), or alternatively, greater than 50. The diameter of an SPI aggregate can be from 100 nm to 100 μm or any range or value therebetween (e.g., 100 nm to 1000 nm, 500 nm to 10,000 nm, 1,000 nm to 50,000 nm, etc.), or alternatively, less than 100 nm or greater than 100 μm. Optionally, interactions (e.g., binding) can exist between SPI within an SPI aggregate. One or more components (e.g., lipid components, phospholipids, aqueous components, salts, minerals, etc.) can optionally interact with, be located within, be located outside of, intertwine between, interact with, and / or associate with SPI aggregates in other ways. In certain examples, lipid components are located between SPI within the aggregate, surround the SPI aggregate, are encapsulated within the SPI aggregate (e.g., as shown in FIGS. 16D and 16E), interact with the SPI aggregate, and / or associate with SPI in other ways. SPI aggregates can optionally be contained within and / or support droplets of an aqueous solution (e.g., within a lipid component) and / or droplets of a lipid component (e.g., within an aqueous solution). Additionally or alternatively, SPI aggregates can be dispersed in both lipid components and water, dried (e.g., dried SPI aggregates), and / or located within any other component. In certain examples, SPI aggregates can optionally interact with phospholipids. For example, phospholipids can promote the encapsulation of lipid components within micellar aggregates of SPI by forming hydrophilic bonds and / or other interactions with SPI and hydrophobic bonds and / or other interactions with lipid components (e.g., phospholipids form a layer between SPI and the lipid component).SPI aggregates can be formed by the S300, S400, S500, and / or S600 methods. An example is shown in FIG. 7.

[0034] The method can optionally be used with an SPI mixture (e.g., an SPI solution). The SPI mixture can optionally contain a protein component, an aqueous component, a lipid component, and / or other components (e.g., impurities, any components in S500, etc.). The protein component can include protein isolate units (e.g., unstructured protein isolate units, structured or otherwise aggregated protein isolate units, etc.), SPI, SPI aggregates, combinations thereof, and / or any other protein. Examples are shown in FIGS. 6A, 6B, 6C, 6D, and 6E. In certain examples, protein isolate units (e.g., aggregated and / or non-aggregated protein isolate units) that exceed a threshold percentage in the protein component of the SPI mixture are not denatured (e.g., at the time of formation of the SPI mixture, before treatment of the SPI mixture, after treatment of the SPI mixture), and the threshold percentage can be 50% to 99% or any range or value therebetween (e.g., 60%, 70%, 80%, 90%, 95%, etc.), or can be less than 50% or greater than 99%. In another specific example, protein isolate units that exceed a threshold percentage in the protein component of the SPI mixture are disposed within the SPI, and the threshold percentage can be 5% to 90% or any range or value therebetween (e.g., 10%, 15%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, etc.), or can be less than 5% or greater than 90%. In a first example, the SPI structure includes a more hydrophobic region inside the SPI (e.g., in contact with a lipid component and / or phospholipid) compared to a more hydrophilic region outside the SPI (e.g., in contact with the aqueous component). An example is shown in FIG. 6A. In a second example, the SPI aggregate includes a more hydrophobic region inside the aggregate compared to a more hydrophilic region outside the aggregate (e.g., in contact with the aqueous component). An example is shown in FIG. 6D. However, the proteins in the protein component can be arranged in other ways.

[0035] Obtaining a protein isolate unit from a protein source (S100) serves the function of extracting protein from the protein source (e.g., protein source components) and / or obtaining a high-protein concentration solution by other means. In a variation, S100 can include grinding the protein source (S120), diluting the protein source to form a protein source solution (S140), optionally adjusting the pH level of the protein source solution (S160), optionally adjusting the salt content of the protein source solution (S165), and optionally forming a protein isolate solution (S180). However, the protein isolate unit can be obtained from the protein source by precipitation (e.g., inducing salting in, salting out, isoelectric point precipitation, etc.), centrifugation, size exclusion, and / or any other protein extraction and / or purification method.

[0036] All or part of S100 (e.g., one or more of S120, S140, S160, S165, or S180) can be performed at one or more target temperatures. The target temperature can be 15°C to 85°C (e.g., 15°C to 30°C, 20°C to 25°C, room temperature, 20°C, etc.), less than 15°C, greater than 85°C, any target temperature in S500, and / or any other target temperature. The target temperature can remain constant throughout the process of S100, vary over time (e.g., vary according to a predetermined cycle), and / or vary in other ways.

[0037] The protein isolate unit is preferably obtained from a protein source such that less than the threshold percentage of the obtained protein isolate unit is denatured, but it can be obtained by other methods. The threshold percentage (e.g., maximum percentage) of the obtained denatured protein isolate unit can be from 0.01% to 50% or any range or value therebetween (e.g., 0.05%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, etc.), or it can be less than 0.01% or greater than 50%. The threshold percentage of the protein isolate unit that can be obtained from the protein source (e.g., the protein yield in the protein isolate solution) can be greater than 40%, 50%, 60%, 70%, 80%, 90%, 50 - 60%, 60 - 70% (e.g., 67%), less than 40%, greater than 60%, greater than 70%, greater than 80%, greater than 90%, and / or any other suitable percentage (e.g., on a weight basis, volume basis, etc.) of the original protein source. Alternatively, S100 can have any other suitable yield.

[0038] S100 can optionally include pulverizing a protein source (S120). S120 can be performed before S140, simultaneously with S140, after S140 (e.g., mixing of the protein source solution), after protein source treatment (e.g., lipid removal), and / or at any other time point. Additionally or alternatively, the protein source can be obtained in a pulverized state (e.g., a pretreated protein source). Examples of pulverization methods include pulverizing, blending, crushing, tumbling, crumbling, atomizing, shaving, grinding, milling, cryo-milling, chopping, homogenization (e.g., using the S500 method), air classification, and / or any other method. In a specific example, S120 can include producing a protein source powder, a pulverized protein source, a powder of the protein source, and / or any other pulverized protein source. In an exemplary example, an air classification system can be used to pulverize a protein source (e.g., a defatted protein source) into a powder, and then the powder can be separated to extract the powder of the protein source. However, the protein source can be pulverized by other methods.

[0039] S100 can optionally include diluting a protein source to form a protein source solution (S140). S140 can be performed after S120 and / or at any other time point. The diluent can include an aqueous solution (e.g., water, deionized water, a mixture of water and other components (e.g., any component of S500), etc.), a mixture of an aqueous solution and a lipid component (e.g., an emulsion), a polar solvent, any organic solvent and / or inorganic solvent, and / or any other diluent. In a specific example, the diluent is a salt solution. The salt solution preferably contains NaCl, but alternatively, any other salt (e.g., a calcium salt, any salt listed in S500, etc.) or a combination of salts can be used. The concentration of the salt (e.g., NaCl, CaCl2, etc.) can be 0.1M to 2M or any range or value therebetween (e.g., 0.7, 0.8, 0.9, etc.), or less than 0.1M or greater than 2M. The protein source can optionally be diluted to achieve the target protein concentration in the protein source solution. The target protein concentration (by weight) can be 1% to 50% or any range or value therebetween (e.g., 5% to 40%, 10% to 15%, 15% to 25%, etc.), or less than 1% or greater than 50%. S140 can optionally include mixing, blending, homogenization (e.g., using the S500 method), and / or any other combination method. However, the protein source can be diluted by other methods.

[0040] S100 can optionally include adjusting the pH level of the protein source solution (S160), which can function to increase the solubility of the protein in the protein source solution (e.g., by making the pH higher than the isoelectric point). S160 can be performed after S140 or at any other time. S160 can include adding one or more acids and / or bases to bring the pH of the protein source solution (and / or components therein) to the target pH. Examples of acids and bases include HCl, NaOH, citric acid, lactic acid, gluconic acid, and / or any food-safe (e.g., in suitable amounts) acid and / or base. The target pH is preferably basic (e.g., above 7, above 8, above 9, etc.), but can alternatively be acidic and / or neutral. For example, the target pH can be in the range of 4 to 11.5 or any value therebetween (e.g., 7 to 10, 8 to 10, etc.), or can be below 4 or above 11.5. However, the pH level of the protein source solution can be adjusted by other methods.

[0041] S100 can optionally include adjusting the salt content of the protein source solution (S165), which can increase the solubility of the protein isolate units in the protein source solution, increase the interaction between the protein and the phospholipid, improve the properties (such as extensional behavior, melting behavior, etc.) and / or nutritional profile (such as calcium concentration) of the product manufactured using the protein source solution, and / or exhibit other functionalities. S165 can be performed after S140, simultaneously with S140, and / or at any other time point. S165 can include increasing or decreasing the salt concentration of the protein source solution and / or its components (such as the protein source) to achieve the target salt concentration. S165 can be performed using the method described in S500. The target salt concentration can be in the range of 0.05M to 5M or any range or value therebetween (such as 0.1M to 1M, 0.5M to 2M, 0.8M to 0.9M, less than 4M, less than 2M, less than 1M, etc.), or it can be less than 0.05M or greater than 5M. The target salt concentration can result in a conductivity in the range of 0.5 to 10,000 millisiemens or any range or value therebetween (such as 1 to 10 millisiemens, 2 to 8 millisiemens, 10 to 100 millisiemens, 100 to 10,000 millisiemens, etc.), or it can be less than 0.5 millisiemens or greater than 10,000 millisiemens. The target salt concentration can optionally be determined based on the type of protein used (such as based on the solubility of the protein species), based on the target properties, and / or by other methods. However, the salt content of the protein source solution can be adjusted by other methods.

[0042] S100 can optionally include forming a protein isolate solution (S180), which can function to form (e.g., extract) protein isolate units from a protein source solution. The protein isolate solution can include protein isolate units, protein isolate unit precursors, and / or any other suitable form of protein isolate. S180 can be performed after S140, after S160, and / or at any other time point. S180 can include separating the protein source solution into an insoluble material and a protein isolate solution (including protein isolate units). Separation of the protein source solution can include decanting, filtration, drying, centrifugation, precipitation, and / or any other separation method. For example, S180 can include centrifuging the protein source solution, and the supernatant is a protein isolate solution containing solubilized protein isolate units. Centrifuges can include decanters, separator centrifuges (e.g., disk stack centrifuges, etc.), tubular centrifuges, membrane centrifuges, and / or any other centrifuge and / or its components. The centrifuge can be a continuous flow centrifuge, a batch centrifuge, and / or any other type of centrifuge. The protein source solution can be centrifuged at a RCF of 500g to 100,000g or any range or value therebetween (e.g., 1,000g to 30,000g, 4,000g to 10,000g, 5,000g, etc.), or it can be centrifuged at a RCF less than 500g or greater than 100,000g. The protein source solution can be centrifuged at an RPM of 100 to 10,000 or any range or value therebetween (e.g., 2,000 to 10,000, 4,000 to 6,000, 5000 to 5,500, less than 10,000, etc.), or it can be centrifuged at an RPM less than 100 or greater than 10,000. The concentration of protein in the protein isolate solution can be 1% to 50% or any range or value therebetween (e.g., 2% to 10%, 2.7%, 7.5%, 5% to 40%, 6.5%, 10% to 15%, 15% to 25%, etc.), or it can be less than 1% or greater than 50%.However, the protein isolate solution can be formed by other methods.

[0043] Additionally or alternatively, S100 can include treating a protein source (e.g., a protein source solution) and / or a protein isolate unit (e.g., a protein isolate solution) using any processing method in S500 (e.g., pH adjustment, salt content adjustment, temperature adjustment, high-pressure assisted extraction, enzyme-assisted extraction, ultrasonic-assisted extraction, other extraction assistance methods, etc.).

[0044] However, the protein isolate unit can be obtained by other methods.

[0045] The method can optionally include combining protein isolates (e.g., combining protein isolate solutions) to form a mixture of protein isolates (e.g., a mixture of protein isolate solutions), and the protein isolates can be obtained (separately) from different protein sources. This can function to form an SPI having a mixed protein composition. In variations, this can increase the range of possible nutritional profiles and / or other properties in products formed from the SPI. The protein isolates can be combined during S100, after S100 (e.g., combining two or more protein isolate solutions formed using the S100 method), during S300 (e.g., simultaneously with dilution), after S300 (e.g., combining diluted protein isolate solutions), and / or at any other time point. In all or part of the method, the protein isolates and / or protein isolate solutions can refer to a mixture of protein isolates and / or a mixture of protein isolate solutions, respectively. However, the protein isolates can be combined by other methods.

[0046] Alternatively, the protein isolate can be obtained from a single protein source (e.g., hemp, sesame, other plant sources, etc.). For example, all or part of the method can use protein isolate units derived from a single protein source (e.g., obtained from a single protein source).

[0047] The method can optionally include modifying the protein (e.g., modifying the protein isolate unit, SPI, and / or any other protein), which can function to improve one or more properties of the protein and / or products obtained from the protein. The protein can be modified before, during, and / or after S100, S200, S300, S400, S500, S600, and / or at any other suitable time. Modification of the protein can include transglutaminase modification, proteolytic modification, other enzyme modifications, glycosylation, saccharification (e.g., catalyzed by food-safe acids and / or any other acids and performed at a temperature below the denaturation point of the protein), phosphorylation (e.g., using sodium trimetaphosphate), acylation, hydrolysis, crosslinking (e.g., using protease, laccase, etc.), other methods at S500 (e.g., heating, shearing, micronization, etc.), and / or any other protein treatment.

[0048] The method can optionally include combining the protein isolate unit with a lipid component (S200), which functions to mix (e.g., emulsify) the lipid in the protein isolate solution so that SPI can be formed in the presence of the lipid (e.g., by S300 and / or S400). S200 can be performed after S100, before S300, before S400, and / or at any other time point.

[0049] S200 can include forming a mixture by combining a protein isolate unit (e.g., a protein isolate solution) and a lipid component, an example of which is shown in FIG. 2. The proportion (by weight) of the lipid component in the mixture can be 0.5% to 50% or any range or value therebetween (e.g., 1% to 20%, 5% to 10%, 1.67%, 5%, 15%, greater than 5%, etc.), or can be less than 0.5% or greater than 50%. Further or alternatively, the ratio of the lipid component to the protein isolate solution can be 1:10 to 10:1 (e.g., by weight, by volume, etc.), any range or ratio value therebetween (e.g., 1:1, 1:2, 2:3, 4:5, etc.), less than 1:10, greater than 10:1, and / or any other suitable ratio. Combining the protein isolate unit (e.g., a protein isolate solution) and the lipid component can include emulsification, mixing, blending, homogenization (e.g., using the S500 method), and / or any other combination method. The mixture (e.g., a protein isolate mixture) can be an emulsion (e.g., a stable emulsion, an unstable emulsion, etc.), a suspension, a colloid, and / or any other mixture.

[0050] In S200, optionally, it can include combining a protein isolate unit and a phospholipid. An example is shown in FIG. 19. For example, the phospholipid can be combined with a lipid component to form a lipid-phospholipid mixture, and then the protein isolate unit (e.g., a protein isolate solution) can be combined with the lipid-phospholipid mixture to form a protein isolate mixture. However, the phospholipid can be mixed into the lipid component during or after combining the lipid component with an aqueous component or the protein isolate mixture, mixed into the protein isolate mixture before combining with the lipid component, mixed into a diluted protein mixture (e.g., the lipid component can be mixed into the diluted protein mixture before, during, and / or after phospholipid mixing), and / or mixed into the solution at any other time point. However, the protein isolate unit, phospholipid, and lipid component can be combined in any order to form a protein isolate mixture. The proportion (by weight or volume) of the phospholipid in the lipid-phospholipid mixture can be 0% to 40% or any range or value in between (e.g., 0% to 5%, 1%, 5% to 15%, etc.), or it can be more than 40%. The proportion (by weight or volume) of the phospholipid in the protein isolate mixture can be 0% to 5% or any range or value in between (e.g., 0.05% to 0.15%, 0.2% to 0.6%, etc.), or it can be more than 5%.

[0051] However, the protein isolate unit and the lipid component can be combined in other ways.

[0052] The method can optionally include diluting the protein isolate units (S300), which serves to promote and / or induce the formation of SPI. For example, a diluent (e.g., a diluting agent, a coagulant, a precipitating agent, etc.) can be added to the protein isolate mixture (e.g., a protein isolate solution or another protein isolate mixture) such that the protein isolate units in the diluted protein isolate mixture become insoluble. S300 can be performed after S100, after S200, and / or at any other point in time. S300 can form a diluted protein isolate mixture (e.g., a diluted protein isolate solution) and / or another product. The protein isolate units to be diluted can be within a protein isolate mixture (e.g., a protein isolate solution, a mixture containing protein isolate units and lipid components, a mixture containing protein isolate units and / or any other components, etc.), within a protein isolate mixture after protein modification, and / or within any other suitable mixture or component containing protein isolate units. In a first specific example, the protein isolate mixture to be diluted can be a protein isolate solution (e.g., from S180). In a second specific example, the protein isolate mixture to be diluted can be a protein isolate unit-lipid component mixture (e.g., from S200).

[0053] S300 can include diluting a protein isolate unit (e.g., a protein isolate mixture) to achieve a target protein concentration. The target protein concentration (by weight) of the diluted protein isolate mixture can be 0.5% - 90% or any range or value therebetween (e.g., 1% - 5%, 1.6%, 1.9%, 5% - 40%, 10% - 15%, 15% - 25%, 25% - 50%, etc.), or it can be less than 0.5% or greater than 90%. Additionally or alternatively, the ratio of the protein isolate mixture (e.g., with or without lipids) to the diluent (e.g., a diluent mixture) can be 1:10 - 10:1 (e.g., by weight, by volume, etc.), any range or ratio value therebetween (e.g., 1:1, 1:2, 1:3, 2:3, 4:5, etc.), less than 1:10, greater than 10:1, and / or any other suitable ratio. Additionally or alternatively, the ratio of the salt concentration in the protein isolate mixture to the salt concentration in the diluted protein isolate mixture can be greater than the dilution threshold. The dilution threshold can be 1 - 10 or any range or value therebetween (e.g., 2, 3, 4, 5, etc.), or it can be less than 1 or greater than 10.

[0054] Diluents can include water (e.g., deionized water, substantially pure water, etc.); aqueous solutions (e.g., water, tap water, a mixture of water and other components (salts, soluble and / or insoluble proteins, emulsifiers, phospholipids, and / or any components in S500, etc.)); non-aqueous solutions; a mixture of an aqueous solution, a lipid component, and optionally a phospholipid (e.g., an emulsion); organic polar solvents (e.g., ethanol, methanol, propanol, acetone, any other alcohol, any other poor solvent); non-polar solvents (e.g., co-solvents); any organic solvent and / or inorganic solvent; coagulants; precipitants; and / or any other liquid. The diluent can optionally be a filtered liquid from all or part of a previous iteration of the method.

[0055] For example, the diluent can be a diluent mixture (such as an emulsion) containing a lipid component, an aqueous solution, and optionally other components (such as phospholipids). The proportion (by weight) of the lipid component in the diluent mixture can be 0.5% to 50% or any range or value therebetween (for example, 1% to 20%, 10% to 20%, 5%, 1.67%, 15%, 20%, etc.), or it can be less than 0.5% or more than 50%. Further or alternatively, the ratio of the lipid component to the diluent can be 1:10 to 10:1 (for example, by weight, by volume, etc.), any range or ratio value therebetween (for example, 1:1, 1:2, 2:3, 4:5, etc.), less than 1:10, more than 10:1, and / or any other suitable ratio. The proportion (by weight or volume) of phospholipids in the diluent can be 0% to 10% or any range or value therebetween (for example, 0.05% to 0.2%), or it can be more than 10%. The proportion (by weight or volume) of phospholipids in the diluted protein isolate mixture can be 0% to 10% or any range or value therebetween (for example, 0.05% to 0.15%), or it can be more than 10%.

[0056] The temperature of the diluent can be 0°C to 35°C or any range or value therebetween (for example, 5°C to 20°C, 20°C to 25°C, etc.), or it can be less than 0°C or more than 35°C. The temperature of the diluent is preferably room temperature, or it can be less than or more than room temperature.

[0057] However, the protein isolate unit can be diluted by other methods, and / or the SPI can be formed by other methods.

[0058] Collecting the structured protein isolate (S400) functions to place the protein isolate units in a structure (e.g., an aggregate, a cluster, any form of aggregate, etc.). S400 can optionally function to place the SPI in one or more SPI aggregates. S400 can be performed after S300, during S300, and / or in combination with S300 (e.g., by diluting the protein isolate units such that the protein isolate units are partially or fully placed in the SPI, and by diluting the protein isolate units, precipitation is induced, etc.), without S300, and / or at any other time point.

[0059] The S400 can include separating a protein isolate mixture (e.g., a diluted protein isolate mixture of the S300) and collecting SPI (e.g., an SPI mixture) from the protein isolate mixture. Separating the protein isolate mixture can use methods including decantation, filtration, drying, centrifugation, causing sedimentation, isoelectric precipitation, poor solvent precipitation (e.g., using a poor solvent diluent in the S300 to separate the diluted protein isolate mixture), precipitation by any solvent exchange process, adjusting the ionic strength (e.g., adding salts and / or removing salts from the protein isolate mixture), adjusting the ratio and / or concentration of any solvent or solute in the protein isolate mixture, hydrolysis, aggregation, gelation, one or more treatments (e.g., temperature adjustment, electrical treatment, pulses, light treatment, radiation, free radicals, sonication, etc.), dialysis, any fractionation method, combinations thereof, and / or any other separation method. The one or more separation methods can optionally use enzymes, proteins, polysaccharides, fats, minerals, salts, acids, bases, gelling agents, aqueous components, lipid components, polar solvents (e.g., poor solvents), nonpolar solvents, any diluent, and / or any other component or chemical substance. In a specific example, a product containing a poor solvent precipitate (ASP) (e.g., a protein component collected using poor solvent precipitation) can be a product with a reduced water / fat binding compared to a product containing SPI collected using aqueous dilution. This reduction in water / fat binding can result in a protein dispersed in excess liquid (after gelation of the product, after heating of the product, etc.).

[0060] In a first variation, S400 can include causing precipitation in a protein isolate mixture (e.g., a diluted protein isolate mixture) and extracting the insoluble fraction (e.g., removing all or part of the supernatant), and all or part of the insoluble fraction (e.g., the sediment and / or precipitate) can include SPI. For example, SPI can be precipitated from a diluted protein isolate mixture that includes protein isolate units, an aqueous component, and optionally a lipid component. In another example, SPI can be extracted (e.g., precipitated, sedimented) from the supernatant. In a specific example, SPI precipitates when the proportion (by weight) of the lipid component in a diluted protein isolate mixture (e.g., one generated using a protein isolate solution having a protein concentration of 6.5% and / or any other concentration) is 0% to 15% or any range or value therebetween (e.g., 5%), or can be greater than 15%. The lipid component can include or exclude phospholipids. The precipitation can optionally be facilitated and / or accelerated using one or more mechanical processing methods. In a specific example, the precipitation can be facilitated using agitation (e.g., by an agitated double-jacket tank), centrifugation, and / or any other mechanical processing method. Throughout all or part of the method, "SPI" can refer to the collected insoluble fraction (e.g., the sediment and / or precipitate).

[0061] In a second variation, S400 can include using shear, pressure, spinning (e.g., centrifugation, rotation, vibration, etc.), other mechanical processing methods in S500, and / or any other mechanical method for separating structured protein isolates from a protein isolate mixture. For example, S400 can include centrifuging a protein isolate mixture (e.g., a diluted protein isolate mixture, an undiluted protein isolate mixture, etc.) and extracting the insoluble fraction (e.g., removing all or part of the supernatant), and all or part of the insoluble fraction (e.g., the precipitate) can contain SPI. Any type of centrifuge can be used (e.g., the types listed in S180). The protein isolate mixture can be centrifuged at an RCF of 500 g to 100,000 g or any range or value therebetween (e.g., 1,000 g to 30,000 g, 4,000 g to 6,000 g, 5,000 g, etc.), or can be centrifuged at an RCF less than 500 g or greater than 100,000 g. In a specific example, the RCF can be less than the centrifugation threshold (e.g., to reduce denaturation of protein isolate units), and the centrifugation threshold can be 1,000 g to 15,000 g or any range or value therebetween (e.g., 5,000 g, 6,000 g, 10,000 g, 50,000 g, etc.), or can be less than 1,000 g or greater than 15,000 g. In another specific example, the RCF can be greater than the high-speed centrifugation threshold, and the high-speed centrifugation threshold can be 10,000 g to 20,000 g or any range or value therebetween (e.g., 14,000 g, 15,000 g, 16,000 g, 16,900 g, etc.), or can be less than 10,000 g or greater than 20,000 g. The protein isolate mixture can be centrifuged at an RPM of 100 to 10,000 or any range or value therebetween (e.g., 2,000 to 10,000, 4,000 to 6,000, 5000 to 5,500, etc.), or can be centrifuged at an RPM less than 100 or greater than 10,000.In certain examples, the RPM can be below the centrifugation threshold, which can be between 1,000 and 15,000 or any range or value in between (e.g., 6,000, 10,000, etc.), or it can be less than 1,000 or greater than 15,000. In another specific example, the RPM can be above the high-speed centrifugation threshold (e.g., this can help isolate smaller molecular weight or soluble proteins), and the high-speed centrifugation threshold can be between 5,000 and 100,000 or any range or value in between (e.g., 10,000, 15,000, 20,000, 25,000, 30,000, etc.), or it can be less than 5,000 or greater than 100,000.

[0062] In a third variation, S400 can include inducing isoelectric precipitation in the protein isolation mixture (e.g., by lowering the pH of the protein separation mixture close to the isoelectric point of the protein) and collecting the isoelectric protein isolate. For example, the pH of the protein isolation mixture can be adjusted to between 3 and 6 or any range or value in between (e.g., 4 - 5.5), or it can be less than 3 or greater than 6. In a first example, SPI can include the isoelectric protein isolate. In a second example, the isoelectric protein isolate (IPI) can be used as SPI in all or part of the method.

[0063] The collected SPI can be an SPI mixture. For example, the SPI mixture can be an insoluble fraction containing SPI (e.g., sediment, precipitate, solid fraction, etc.); a mixture containing the insoluble fraction; a solution containing SPI, an aqueous component, and / or an impurity; a mixture containing SPI, an aqueous component, a lipid component (e.g., derived from S200, a lipid component mixed in a diluent in S300, etc.), and / or an impurity; and / or another mixture containing SPI or can contain them. The total protein concentration (by weight) in the SPI mixture (e.g., the insoluble fraction) can be 5% - 100% or any range or value therebetween (e.g., 10% - 20%, 30% - 50%, 50% - 70%, 44%, 40%, etc.), or can be less than 5%. The remaining weight can contain a lipid component, a diluent, an impurity (e.g., carbohydrate, salt, mineral, etc.), and / or any other suitable component. The carbohydrate concentration (by weight) in the SPI mixture can be 0.005% - 2% or any range or value therebetween (e.g., 0.01% - 0.1%, 0.1% - 0.2%, 0.2% - 1%, 1% - 2%, greater than 0.02%, etc.), or can be less than 0.005% or greater than 2%. The collected SPI can optionally contain SPI aggregates. The threshold ratio (e.g., cumulative protein yield) of the protein derived from the original protein source collected in the SPI mixture can be 40% - 90%, 50% - 70% (e.g., 50%, 60%, 62%, 65%, 70%, etc.), greater than 60%, greater than 90%, less than 40%, and / or any other suitable yield (e.g., by weight, by volume, etc.). The threshold ratio of the protein derived from the protein isolate mixture collected in the SPI mixture can be 50% - 99%, 80% - 90%, 90% - 95% (e.g., 92%), greater than 70%, greater than 80%, greater than 90%, less than 50%, and / or any other suitable yield (e.g., by weight, by volume, etc.). Alternatively, S400 can have other suitable yields.

[0064] The insoluble fraction (e.g., sediment, precipitate, etc.) can contain a solid component (e.g., which can be dried to form a dry substance) and / or a liquid component. For example, the solid component can be 5% - 80% (by weight) of the SPI mixture or any range or value therebetween (e.g., 10% - 50%, 20% - 40%, 33%, greater than 10%, greater than 15%, greater than 20%, greater than 25%, greater than 30%, etc.), or it can be less than 5% or greater than 80% of the SPI mixture. All or part of the remaining liquid component of the SPI mixture can contain an aqueous component (e.g., water), a lipid component, and / or any other component. The protein concentration (by weight) in the solid component (e.g., the purity of the solid component) can be 70% - 99% or any range or value therebetween (e.g., 80% - 99%, 90% - 99%, 85%, 90%, 96%, 97%, 97.5%, 98%, greater than 70%, greater than 80%, greater than 90%, greater than 95%, etc.), or it can be less than 70% or greater than 99%. Other components (e.g., impurities) in the solid component can include salts, minerals, carbohydrates, lipids, and / or any other chemical or chemical component. The concentration (by weight) of other components in the solid component can be 0.1% - 10% or any range or value therebetween (e.g., 0.2% - 5%, 0.5% - 2%, 0.5%, 1%, 1.2%, 1.5%, 2%, greater than 0.5%, greater than 1%, etc.), or it can be less than 0.1% or greater than 10%. The carbohydrate concentration (by weight) in the solid component can be 0.5% - 5% or any range or value therebetween (e.g., 0.1% - 5%, 0.5% - 2%, 0.5%, 1%, 1.2%, 1.5%, 2%, greater than 0.5%, greater than 1%, etc.), or it can be less than 0.05% or greater than 5%.

[0065] However, the structured protein isolate can be collected by other methods.

[0066] The method can optionally include processing a structured protein isolate (S500), which serves the function of preparing an SPI for use in the manufacture of a product. S500 can be performed after S400, during and / or after S600, and / or at any other time point. Further or alternatively, the processing step in S500 can be used at any suitable time point (e.g., before, during, and / or after S100, S200, S300, S400, and / or S600) to process a protein source, a protein isolate unit, a component, and / or a product (e.g., one containing an SPI).

[0067] The treatment of SPI (e.g., SPI mixture) may include addition of components (e.g., dilution, addition of lipid components, etc.), removal of components (e.g., defatting, removal of salts, removal of alcohol, filtration, pressing, draining, etc.), adjustment of pH level (e.g., increase or decrease of acidity as described in S160), adjustment of salt content, mechanical treatment (e.g., homogenization, centrifugation, comminution, pressurization, grinding, shearing, stirring, mixing, etc.), separation of SPI mixture (e.g., SPI solution), temperature adjustment, aging (e.g., aging at a target temperature; aging can promote ripening, fermentation, affinage, maturation, etc.), fermentation, humidification / dehumidification, stirring, standing, adjustment of oxygen level, gelation (e.g., curdling) method, any curdling treatment method (e.g., cutting, stretching, pressing, brining, shaping, etc.), protein modification, combinations thereof, and / or any other treatment method. In certain examples, the gelation method may include adjustment of pH, adjustment of salt content, addition of enzymes, addition of hydrocolloids (e.g., carrageenan, gums, etc.), addition of lipid components (e.g., lipid components having a melting point above room temperature), temperature adjustment, fermentation, aging, extraction and / or extraction assistance methods (e.g., high-pressure assisted extraction, enzyme-assisted extraction, ultrasonic-assisted extraction, etc.), micronization, and / or any other treatment method. In certain examples, the shaping of the SPI mixture may include transferring the SPI mixture to a mold while hot and cooling the SPI mixture (e.g., hardening to form a shaped gel). Any treatment method can be performed once, multiple times, simultaneously, repeatedly, non-simultaneously, sequentially (in any order), and / or at any other time point.

[0068] In a first variation, the treatment of SPI can include adding components to the SPI. Adding components to the SPI can include combining the SPI with one or more components, and combining can include emulsifying, mixing, blending, homogenizing, and / or any other combination method. Examples of components include plant substances, proteins (e.g., protein sources, protein source solutions, protein isolate units, SPI, etc.), lipid components, aqueous components (e.g., water, sucrose solutions, etc.), preservatives, acids and / or bases, macronutrients (e.g., protein, fat, starch, sugar, etc.), nutrients, micronutrients, carbohydrates (e.g., sugars, starches, fibers, polysaccharides such as maltodextrin, gums, etc.), starches (e.g., natural and / or processed starches, potato, tapioca, corn, sago, starch-based texturizers such as Advanta Gel S(trademark), etc.), vitamins, enzymes (e.g., transglutaminase, chymosin, tyrosinase, bromelain, papain, ficain, other cysteine endopeptidases, rennet enzymes and / or rennet-type enzymes, etc.), emulsifiers (e.g., lecithin, etc.), microparticles, hydrocolloids (e.g., thickeners, gelling agents, emulsifiers, stabilizers (starches, gelatin, pectin, etc.), and gums (agar, alginic acid, sodium alginate, guar gum, TIC Pretested(trademark) gum, locust bean gum, beta-glucan, xanthan gum, konjac gum, etc.)), salts (e.g., NaCl, CaCl2, NaOH, KCl, Nal, MgCl2, etc.), minerals (e.g., calcium), chemical cross-linking agents (e.g., transglutaminase) and / or non-cross-linking agents (e.g., L-cysteine), colorants (e.g., natural colorants), flavor compounds (e.g., natural flavoring agents), vinegar (e.g., white vinegar), mold powder, microbial cultures, carbon sources (e.g., to assist fermentation), calcium citrate, any combination thereof, and / or any other components. Microbial cultures can include cultures of cheeses such as blue cheese, camembert cheese, cheddar cheese, alpine cheese, parmesan cheese, swiss cheese, edam cheese, etc., and / or any other microbial cultures, and / or combinations thereof.The ingredients may optionally include, and / or may be excluded from, added animal products, animal-derived ingredients, gums (e.g., polysaccharide thickeners), hydrocolloids, allergens, phospholipids, soy-derived materials, starches, combinations thereof, and / or any other suitable ingredients in amounts less than a threshold amount (e.g., 10%, 5%, 3%, 2%, 1.5%, 1.25%, 1%, 0.5%, 0.1%, etc.). The ingredients are preferably safe for food, or may alternatively be unsafe for food.

[0069] Examples of microbial cultures that can be used may include cheese cultures (e.g., cheese starter cultures), yogurt cultures, wine cultures, beer cultures, and / or other microbial cultures, and / or combinations thereof. For example, microbial cultures may include cultures of cheeses such as blue cheese, camembert cheese, cheddar cheese, alpine cheese, parmesan cheese, swiss cheese, edam cheese, and / or any other microbial cultures, and / or combinations thereof. Examples of microorganisms in the cultures that can be used include Arthrobacter arilaitensis, Arthrobacter bergerei, Arthrobacter globiformis, Arthrobacter nicotianae, Arthrobacter variabilis, Bifidobacterium adolescentis, Bifidobacterium animalis, Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium infantis, Bifidobacterium lactis, Bifidobacterium longum, Bifidobacterium pseudolongum, Bifidobacterium thermophilum, Brachybacterium alimentarium, Brachybacterium tyrofermentans, Brevibacterium aurantiacumaurantiacum), Brevibacterium casei, Brevibacterium linens, Candida colliculosa, Candida kefyr, Candida jefer, Candida krusei, Candida mycoderma, Candida utilis, Candida vini, Candida zeylanoides, Carnobacterium divergens, Carnobacterium maltaromaticum, Corynebacterium ammoniagenes, Corynebacterium casei, Corynebacterium flavescens, Corynebacterium mooreparkense, Corynebacterium variabile, Cystofilobasidium infirmominiatum, Debaryomyces hansenii, Debaryomyces kloeckeri, Enterococcus faecalis, Fusarium domesticum, Geotrichum candidum, Hafnia alvei, Halomonas, Issatchenkia orientalis, Kazachstania equigua (KazachstaniaExigua), Kazachstania unispora, Kluyveromyces lactis, Kluyveromyces marxianus, Kocuria rhizophila, Kocuria varians, Lactobacillus acidipiscis, Lactobacillus acidophilus, Lactobacillus brevis, Lactobacillus bulgaricus, Lactobacillus casei, Lactobacillus coryniformis, Lactobacillus curvatus, Lactobacillus delbrueckii (for example), Lactobacilus delbrueckii bulgaricus, Lactobacilus fermentum, Lactobacillus gasseri, Lactobacillus helveticus, Lactobacillus johnsonii, Lactobacillus kefiranofaciens, Lactobacillus kefiri, Lactobacillus nodensis, Lactobacillus parabrevis, Lactobacillus paracasei, Lactobacillus parakefiri, Lactobacillus paraplantarum Lactobacillusparaplantarum), Lactobacillus pentosus, Lactobacillus perolents, Lactobacillus plantarum, Lactobacillus rhamnosus, Lactobacillus salivarius, Lactobacillus tucceti, Lactococcus lactis (e.g., Lactococcus lactis lactis, Lactococcus lactis cremoris, Lactococcus lactis subsp. lactis biovar, Diacetylactis, etc.), Lactococcus raffinolactis, Lecanicillium lecanii, Leuconostoc citreum, Leuconostoc citovorum, Leuconostoc dextranicum, Leuconostoc pseudomesenteroides, Leuconostoc kimchi, Leuconostoc mesenteroides, Macrococcus caseolyticus, Microbacterium foliorum, Microbacterium gubbeenense, Micrococcus luteus (MicrococcusLuteus), Pediococcus, Penicillium album, Penicillium camemberti, Penicillium caseifulvum, Penicillium chrysogenum, Penicillium commune, Penicillium nalgiovense, Penicillium roqueforti, Pichia fermentans, Propionibacterium acidipropionici, Propionibacterium freudenreichii, Propionibacterium jensenii, Proteus vulgaris, Psychrobacter celer, Rhodosporidium infirmominiatum, Rhodotorula minuta, Saccharomyces cerevisiae, Staphylococcus carnosus, Staphylococcus equorum, Staphylococcus fieurettii, Staphylococcus saphrophyticus, Staphylococcus sciuri carnaticus, Staphylococcus succinus, Staphylococcus vitulinus (StaphylococcusVitulinus, Staphylococcus xylosus, Streptococcus cremori, Streptococcus lactis, Streptococcus lactis subspecies diacetylactis, Streptococcus thermophilus, Streptococcus gallolyticus, Streptococcus salivarius, Trichosporon beigelii, Verticillium lecanii, Yarrowia lipolytica, Zygotorulaspora florentina, their genera, their families, their phyla, and / or any other suitable microorganisms, and / or combinations thereof may be included. In certain examples, the culture is RA21 (e.g., including Lactococcus lactis lactis, Lactococcus lactis cremoris, and Streptococcus thermophilus), CASU (e.g., including Lactococcus lactis lactis, Lactobacillus helveticus, and Streptococcus thermophilus), V022 (e.g., Bifidobacterium lactis, Lactobacillus acidophilus, Lactobacillus delbrueckii bulgaricus(including Lactobacillus delbrueckii bulgaricus, Lactobacillus plantarum, and Streptococcus thermophilus), V061 (e.g., including Bifidobacterium lactis, Lactobacillus acidophilus, Lactobacillus delbrueckii bulgaricus, Streptococcus thermophilus, and Lactobacillus paracasei), V 011 V 053 BT 02 LM 57 FLAV 54 and / or can be any other microbial culture.

[0070] In a first embodiment, adding the component can include diluting the SPI (e.g., using water and / or any other component) to achieve a target protein concentration. The target protein concentration (by weight) (e.g., in the SPI mixture, in the product, in the product intermediate, etc.) can be 0.5% - 90% or any range or value therebetween (e.g., 1% - 5%, 1.6%, 1.9%, 5% - 40%, 1% - 25%, 5% - 20%, 10% - 15%, 15% - 25%, 18% - 22%, 25 - 50%, at least 15%, etc.), or can be less than 0.5% or greater than 90%. Diluting the SPI can optionally function to form a diluted SPI mixture (e.g., a diluted SPI solution), and the diluted SPI mixture can be used as a component and processed by other S500 methods and / or used to manufacture the product by the S600 method.

[0071] In the second embodiment, adding the components may include combining (e.g., emulsifying) SPI (e.g., an SPI mixture) with a lipid component. The target lipid concentration (by weight) (e.g., in a composite SPI mixture, in a product, in an intermediate product, etc.) can be 0.5% to 90% or any range or value therebetween (e.g., 1% to 5%, 1.6%, 1.9%, 5% to 40%, 5% to 30%, 5% to 25%, 10% to 15%, 10% to 20%, 12% to 22%, 20 to 50%, at least 10%, etc.), or alternatively less than 0.5% or greater than 90%. The resulting mixture can be a stable emulsion, an unstable emulsion (e.g., coalesced, creamy, soft-aggregated, broken, etc.), a suspension, a colloid, and / or any other mixture. Optionally, the lipid component and / or SPI can be heated before and / or during addition. Heating the lipid component can optionally cause the lipid component to change from a solid to a liquid (e.g., a molten lipid component), which can facilitate homogenization of the mixture. The lipid component is preferably heated below a threshold temperature (e.g., 85°C) and / or cooled to a temperature below the threshold temperature before combining with SPI so that the proteins in the SPI do not denature, or alternatively can be heated by other methods. The resulting mixture can be used as a final product (e.g., a food) and / or as a component in a downstream process (e.g., S600).

[0072] In certain examples, adding the components can include forming an aqueous solution (e.g., containing the components), optionally heating the aqueous solution, combining the SPI mixture with the aqueous solution and optionally a lipid component (e.g., a molten lipid component), and optionally heating the resulting mixture. The resulting mixture can optionally be shaped. An example is shown in Figure 3. Forming the aqueous solution can include hydrating one or more additives in water. The additives can function to promote gelation, increase the hardness of the gel at room temperature (e.g., to enable a shredable product), adjust the nutritional profile of the product, and / or provide other functions. The additives can include hydrocolloids (e.g., carrageenan, gums, other gelling agents, etc.), saccharides (e.g., glucose), fibers, salts, and / or other additives. The concentration of the hydrocolloid in the aqueous solution can be from 0% to 15% or any range or value therebetween (e.g., 0% to 2%, 0.15% to 0.8%, 0.3% to 2%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), or can be greater than 15%. In certain examples, the concentration of carrageenan in the aqueous solution can be from 0 to 10% or any range or value therebetween (e.g., 0% to 2%, 0.15% to 0.5%, 0.1% to 0.4%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), or can be greater than 10%. In certain examples, the concentration of gum in the aqueous solution can be from 0 to 10% or any range or value therebetween (e.g., 0% to 2%, 0.15% to 0.5%, 0.1% to 0.4%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), or can be greater than 10%. The concentration of sugar in the aqueous solution can be from 0% to 15% or any range or value therebetween (e.g., 0% to 2%, 0.3% to 1%, 0.5%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, at least 0.2%, at least 0.3%, at least 0.5%, etc.), or can be greater than 15%.The aqueous solution can be heated to a temperature of 20°C to 100°C or any range or value therebetween (e.g., heated until boiling), or can be heated or cooled to a temperature below 20°C or above 100°C, or may not be heated or cooled. The SPI mixture, the aqueous solution, and the lipid component can be combined in any order (e.g., combine the SPI mixture and the aqueous solution, then add the lipid component; combine the SPI mixture, the aqueous solution, and the lipid component simultaneously, etc.). The SPI mixture, the aqueous solution, and the lipid component can optionally be combined before, after, or simultaneously with adjusting the temperature to a target temperature (e.g., 70°C, 85°C, 90°C, 95°C, 100°C, etc.) over a target time (e.g., 1 minute, 5 minutes, 10 minutes, 15 minutes, 30 minutes, etc.).

[0073] In the first example, the SPI-lipid component mixture contains SPI in water droplets surrounded by the lipid component. In the second example, the mixture contains SPI in lipid component droplets surrounded by water. In the third example, the mixture contains SPI dispersed throughout the lipid component and aqueous component of the mixture. The droplets can have a diameter (e.g., volume-weighted average diameter or area-weighted average diameter) in the range of 500 nm to 1 mm or any range or value therebetween (e.g., 500 nm to 10,000 nm, 10,000 nm to 0.1 mm, 0.1 mm to 1 mm, etc.), or can be less than 500 nm or greater than 1 mm. The droplets can be generated using an emulsification method, droplet encapsulation technology (e.g., microfluidic droplet encapsulation technology), sonication, suspension technology, other colloid formation technologies, and / or any other technology. The SPI inside or outside the droplets can optionally form aggregates of SPI. However, the mixture can be structured in other ways.

[0074] In certain examples, adding the lipid component can include mixing (e.g., emulsifying) the SPI mixture within the lipid component. While the SPI mixture is in the dispersed phase, it is preferred that the lipid component forms the continuous phase of the emulsion (e.g., water-in-oil emulsion or oleogel). For example, the ratio of the lipid component to the SPI mixture can be from 10:1 to 1:1 (e.g., by weight, by volume, etc.) or any range or ratio value therebetween (e.g., 2:1, 3:2, 5:4, etc.). An emulsion having the lipid component as the continuous phase can result in the arrangement (e.g., the arrangement of SPI) of the proteins within the emulsion that increases the extensional and / or melting properties of the product formed from the emulsion. Alternatively, the SPI mixture can be in the continuous phase and the lipid component can be in the dispersed phase (e.g., oil-in-water emulsion). For example, the ratio of the lipid component to the SPI mixture can be from 1:10 to 1:1 (e.g., by weight, by volume, etc.) or any range or ratio therebetween (e.g., 1:1, 1:2, 2:3, 4:5, etc.). Further, the SPI dispersed throughout the entirety of the lipid and aqueous components can optionally be mixed / homogenized together, whereby either a dispersed medium or a continuous medium (e.g., oil droplets containing SPI dispersed in water containing SPI, or vice versa) is obtained.

[0075] In a third embodiment, components are added such that the nutritional profile of the product produced from the SPI substantially matches a target nutritional profile (e.g., that of a target product).

[0076] However, the components can be added in other ways.

[0077] In a second variation, the treatment of SPI may include adjusting the salt content of SPI, and / or changing the ionic strength of SPI may include increasing or decreasing the salt concentration in SPI to achieve a target salt concentration. The target salt concentration can be 0.05 M to 5 M or any range or value therebetween (e.g., 0.1 M to 1 M, 0.5 M to 2 M, 0.8 M to 0.9 M, less than 4 M, less than 2 M, less than 1 M, etc.), or it can be less than 0.05 M or greater than 5 M. The target salt concentration can result in a conductivity of 0.5 to 10,000 millisiemens or any range or value therebetween (e.g., 1 to 10 millisiemens, 2 to 8 millisiemens, 10 to 100 millisiemens, 100 to 10,000 millisiemens, etc.), or it can be less than 0.5 millisiemens or greater than 10,000 millisiemens. The target salt concentration as a percentage (by weight) (e.g., in an SPI mixture, in a product, in an intermediate product, etc.) can be 0% to 10% or any range or value therebetween (e.g., 0.1% to 5%, 0.5% to 2%, at least 1%, at least 2%, less than 5%, etc.), or it can be greater than 10%. In a specific example, the target concentration of calcium citrate can be 0% to 5% or any range or value therebetween (e.g., 0.1% to 1%, 0.5% to 1%, 0.3% to 2.5%, 0.5% to 2%, 1% to 2%, 1.2% to 2%, at least 0.25%, at least 0.5%, at least 1%, at least 2%, etc.), or it can be greater than 5%. In a first variation, increasing the salt concentration may include adding salt to SPI. Examples of salts can include NaCl, calcium citrate (CaCit), CaCl2, sodium citrate, MgCl2, disodium phosphate, dipotassium phosphate, salts of cations (e.g., divalent cations such as calcium), and / or any other salts. Increasing the salt concentration can optionally function to improve the flavor and / or nutritional profile of a product manufactured using SPI. In a second variation, decreasing the salt concentration may include rinsing, dialysis, washing (e.g., centrifugation, filtration, etc. after washing) of SPI, and / or any other method for decreasing the salt concentration.For example, SPI can be resuspended in deionized water and redeposited to form a structured protein isolate solution having a low salt concentration. Reducing the salt concentration can optionally function to improve the texture profile (e.g., extensibility and / or melt properties) of products manufactured using SPI.

[0078] In a third variation, the treatment of SPI can include applying shear to the SPI (e.g., homogenizing the SPI mixture, homogenizing the SPI including added components, etc.). Applying shear can include mixing, blending, vortexing, homogenizing, pressurizing, and / or any other shear treatment. Applying shear to the SPI can include using a rotor stator system, any other homogenizer device, and / or any other shear application device. The shear application device preferably provides a shear force below a threshold value (e.g., so as not to break the protein structure in the protein solution), or alternatively can provide any shear force. The rotor stator system can be used at 500 rpm to 20,000 rpm or any range or value therebetween (e.g., 5000 to 10,000, 5500, 10,000, etc.), or alternatively can be used below 500 rpm or above 20,000 rpm. The rotor stator system can be used for a period of 10 seconds to 12 hours or any range or value therebetween (e.g., 1 minute, 40 minutes, 1 hour, etc.), or alternatively can be used for less than 10 seconds or more than 12 hours. Alternatively, the rotor station system can be used at any other rpm and for any period of time.

[0079] In a fourth variation, the processing of SPI can include separating the SPI (e.g., separating the SPI from an SPI mixture). Separating the SPI can include decanting, filtration (e.g., crude oil filtration method, microfiltration, ultrafiltration, etc.), drying (e.g., spray drying; examples are shown in FIGS. 20A and 20B), centrifugation, causing sedimentation, and / or any other separation method. In the variation, drying can function to stabilize and / or preserve the SPI (e.g., for downstream use). In a specific example, processing an SPI mixture (e.g., the insoluble fraction collected at S400) can optionally include performing one or more initial processing steps on the SPI mixture (e.g., diluting the SPI mixture, pasteurizing the SPI mixture, etc.), spray drying the (processed) SPI mixture to form dried SPI, optionally rehydrating the dried SPI, optionally processing the rehydrated SPI (e.g., combining the rehydrated SPI with a lipid component), and manufacturing a product using the (processed) rehydrated SPI. The threshold ratio of the protein derived from the original protein source in the separated SPI (e.g., the cumulative protein yield after separating the SPI) can be 5% to 50%, 10% to 20% (e.g., 10%, 14%, 15%, 20%, etc.), greater than 50%, less than 5%, and / or any other suitable yield (e.g., by weight, by volume, etc.).

[0080] In a fifth variation, the processing of the SPI may include adjusting the temperature of the SPI, preferably heating the SPI, but further or alternatively may include cooling the SPI (e.g., cooling after heating, blanching, etc.), and / or adjusting the temperature by other means. Adjusting the temperature can function to gel, pasteurize, ferment, age, cook, polymerize, and / or process the SPI and / or products containing the SPI by other means. Adjusting the temperature can be done using a water bath, oven, refrigerator, freezer, mixer with a heating element, tubular heat exchanger, direct steam injection system, batch system (e.g., glass tank), ultra-high temperature system, plate heat exchanger, microwave, fryer, and / or any other system. Adjusting the temperature preferably includes adjusting the temperature of the SPI to a target temperature over a target time, and / or heating and / or cooling the SPI to a target heating temperature, but further or alternatively may include exposing the SPI to a target temperature (e.g., heating the SPI to a target heating temperature, cooling the SPI to a target cooling temperature, etc.), and / or adjusting the temperature based on any other parameter. The target temperature may preferably be below the denaturation temperature of the protein in the protein component, or alternatively may be above the denaturation temperature. The target temperature can be 0°C to 200°C or any range or value therebetween (e.g., 60°C to 100°C, 80°C to 85°C, 80°C to 90°C, 72°C, 75°C, 80°C, 85°C, less than 85°C, less than 90°C, less than 100°C, 25°C to 200°C, 50°C to 85°C, etc.), or alternatively can be below 0°C or above 200°C. The target time can be 10 seconds to 48 hours or any range or value therebetween (e.g., 1 minute to 1 hour, 5 minutes to 30 minutes, 10 minutes to 15 minutes, 1 minute, 5 minutes, 10 minutes, 15 minutes, 30 minutes, 60 minutes, 80 minutes, less than 15 minutes, less than 30 minutes, less than 60 minutes, etc.), or alternatively can be less than 10 seconds or more than 48 hours (e.g., aging for more than 48 hours).The heating rate can be 0.25 °C / min to 50 °C / min or any range or value therebetween (e.g., 0.5 °C / min to 2 °C / min, 2 °C / min to 20 °C / min, 20 °C / min to 50 °C / min, 2 °C / min to 10 °C / min, 1 °C / min to 5 °C / min, 5 °C / min to 10 °C / min, 10 °C / min to 20 °C / min, 10 °C / min to 15 °C / min, 15 °C / min to 20 °C / min, less than 10 °C / min, less than 5 °C / min, less than 2 °C / min, at least 2 °C / min, at least 5 °C / min, at least 10 °C / min, etc.), or alternatively less than 0.25 °C / min or greater than 50 °C / min. The heating and / or cooling stage may optionally include returning the SPI to a second target temperature (e.g., room temperature) after the heating and / or cooling stage. However, the temperature of the SPI can be adjusted by other methods.

[0081] However, the SPI can be processed by other methods.

[0082] The method can optionally include manufacturing a product having the structured protein isolate S600, which functions to form a food product having target properties (e.g., target extensibility and / or melting properties). S600 can be performed after S400, after S500 (e.g., after any processing step in S500), during S500, and / or at any other time point.

[0083] The product can optionally be a food and / or can be used for manufacturing a food. For example, the product can be a target food substitute (e.g., a similar product, a replica, etc.) (e.g., the product can be a plant-based analogue for animal-based foods) used for manufacturing a target food, a food having target characteristics, and / or any other food, etc. The product can be a vegan product, a food free of animal products and / or a food low in animal products (e.g., compared to the target animal products), a plant-based food (e.g., plant-based cheese), a microorganism-based food, a non-mammal-based food, and / or any other food. Examples of target foods include dairy fats (e.g., ghee, other milk fats, etc.), milk, curd, cheese (e.g., hard cheese, soft cheese, semi-hard cheese, semi-soft cheese, aged cheese, fermented cheese, fresh cheese, etc.), butter, yogurt, cream cheese, dried milk powder, cream, whipped cream, ice cream, coffee cream, other dairy products, egg products (e.g., scrambled eggs), additive ingredients, mammalian meat products (e.g., minced meat, steak, chop, bone, deli meat, sausage, etc.), fish meat products (e.g., fish steak, fillet, etc.), any animal product, and / or any other suitable food. In a specific example, target foods include mozzarella, burrata, feta, brie, ricotta, camembert, shave, cottage cheese, cheddar, parmigiano, pecorino, gruyere, edam, gouda, jarlsberg, and / or other cheeses. In a specific example, the product includes milk analogues (e.g., cow milk, sheep milk, goat milk, camel milk, functional milk analogues of human breast milk, etc.).

[0084] The product is preferably completely plant-based, but further or alternatively, it is mainly plant-based (e.g., 50%, 60%, 70%, 80%, 90%, 95%, 98%, over 99%, etc.), partially plant-based, and / or can have any other suitable plant-based content. The product can optionally exclude all and / or added animal products below the threshold (e.g., excluding animal proteins such as casein), gums (e.g., polysaccharide thickeners), allergenic components (e.g., soybeans, peanuts, wheat, their derivatives, etc.), and / or any other suitable components, and / or can contain them. The added components and / or compounds can include materials that are not present in the plant substrate or other components and / or are heterogeneous to them, materials added as separate components, and / or materials defined separately. The threshold amount can be 0.1% to 10% or any range or value in between (e.g., 10%, 5%, 3%, 2%, 1%, 0.1%, etc.), or alternatively, it can be over 10% or less than 0.1%.

[0085] The product preferably has one or more characteristics that are similar to the characteristics of the target product (e.g., within a predetermined error range such as 1%, 5%, 10%, 20%, 30%, etc.) and / or any other set of target characteristics. Characteristics (e.g., functional characteristics, etc.) include nutritional profile (e.g., macronutrient profile, micronutrient profile, etc.), nutritional quality (e.g., PDCAAS score, etc.), texture (e.g., texture profile, hardness, toughness, puncture, stretch, compression response, mouthfeel, viscosity, granularity, relaxation, adhesiveness, chalkiness, flouriness, astringency, brittleness, tackiness, stretchiness, tear resistance / strength, melt-in-the-mouth, etc.), solubility, melting profile, smoke profile, gelling point, flavor, appearance (e.g., color), aroma, precipitation, stability (e.g., room temperature stability), emulsion stability, ion binding ability, heat capacity, solid fat content, chemical properties (e.g., pH, affinity, surface charge, isoelectric point, hydrophobicity / hydrophilicity, free sulfhydryl group content, chain length, chemical composition, nitrogen level, chirality, stereospecific position, etc.), physicochemical properties, compound concentration (e.g., solid sample fraction, vial headspace, olfactory bulb, post-gustation, etc.), denaturation point, denaturation behavior, aggregation point, aggregation behavior (e.g., micellization ability, micelle stability, etc.), particle size, structure (e.g., microstructure, macrostructure, fat crystal structure, etc.), folding state, folding kinetics, interaction with other molecules (e.g., dextrinization, caramelization, coagulation, shortening, lipid-protein interaction, water interaction, aggregation, micellization, etc.), lipid leakage, water holding capacity and / or binding force, lipid retention capacity and / or binding ability, fatty acid composition (e.g., ratio of saturated / unsaturated lipids, etc.), moisture level, turbidity, characteristics determined using assay tools, and / or any other characteristics may be included.

[0086] Examples of assays and / or assay tools that can be used include differential scanning calorimeters (e.g., to determine properties related to melting, gelation points, denaturation points, etc.), Schreiber tests, ovens (e.g., for Schreiber tests), water baths, texture analyzers, rheometers, spectrophotometers, centrifuges (e.g., to determine properties related to water binding capacity), moisture analyzers (e.g., to determine properties related to water availability), optical microscopes (e.g., to determine properties related to microstructure), atomic force microscopes (e.g., to determine properties related to microstructure), confocal microscopes (e.g., to determine protein association with lipids / water), laser diffraction particle size analyzers (e.g., to determine properties related to emulsion stability), polyacrylamide gel electrophoresis systems, mass spectrometry, gas chromatography, liquid chromatography, thermogravimetric analysis systems, thermal shift (e.g., to determine protein denaturation and / or aggregation behavior), ion chromatography, dynamic light scattering systems (e.g., to determine properties related to particle size, to determine protein aggregation, etc.), zetasizers (e.g., to determine properties related to surface charge), protein concentration assays and / or assay systems, particle size analyzers, sensory panels (e.g., to determine properties related to texture, flavor, appearance, etc.), capillary electrophoresis SDS (e.g., to determine protein concentration), spectroscopy (e.g., fluorescence spectroscopy, circular dichroism, etc.; to determine folding state, folding rate, denaturation temperature, etc.), absorbance spectroscopy (e.g., to determine protein hydrophobicity), CE-IEF (e.g., to determine protein isoelectric point / charge), total protein quantification, high-temperature gelation, microbial cloning, Turbiscan (e.g., to determine properties related to emulsion stability), stereospecific analysis, olfactometers, electrophysiological tests (e.g., electrophysiological tests of human olfactometers), psychophysical tests (e.g., psychophysical tests of human olfactometers), and / or any other assay and / or assay tool is included.

[0087] The product can optionally have target elongation characteristics. The elongation characteristics of the product are preferably measured using an elongation assay procedure, but additionally or alternatively, can be measured using other tensile test methods and / or measured by other means. In an example, the elongation assay procedure involves placing a sample containing the target mass of the product (e.g., 15 g, 20 g, 25 g, 30 g, 50 g, 100 g, 500 g, 1000 g, any range or value between these, etc.) into a well, heating the sample (e.g., using an oven with the sample covered in foil), optionally measuring the sample temperature, elongating the sample at a constant extension rate (e.g., 2 mm / second, 5 mm / second, 10 mm / second, 15 mm / second, 20 mm / second, any range or value between these, etc.), and recording when the sample strand is completely severed. In an exemplary example, a sample of the product (e.g., covered in foil) is heated for 15 minutes, and the heated product can be analyzed at an ambient temperature of 20 - 21°C using a texture analyzer (e.g., in the extension mode, using a test speed of 5 mm / second, a post-test speed of 40 mm / second, and a target distance of 270 mm). In a first specific example, the sample can be heated at a target heating temperature (e.g., 50°C, 70°C - 85°C, 60°C - 75°C, 75°C, 80°C, 85°C, 100°C, 150°C, 200°C, 225°C, 230°C, 240°C, 250°C, 275°C, 300°C, any range or value between these, etc.) for a target heating time (e.g., 1 minute, 5 minutes, 10 minutes, 15 minutes, 20 minutes, 30 minutes, 1 hour, any range or value between these, etc.) (e.g., in an oven and / or any other heating device). In a second specific example, the sample can be heated to achieve a target (internal) temperature in the sample (e.g., 50°C, 70°C - 85°C, 60°C - 75°C, 75°C, 80°C, 85°C, 90°C - 110°C, 100°C - 105°C, 100°C, 103°C, 150°C, 200°C, 225°C, 230°C, 240°C, 250°C, 275°C, 300°C, any range or value between these, any other target temperature, etc.) over a target time (e.g., 1 minute - 5 minutes, 1 minute, 2 minutes, 3 minutes, 4 minutes, 5 minutes, 10 minutes, 30 minutes, any range or value between these, any other target time, etc.).In a third specific example, the sample can be heated according to a predetermined temperature cycle. The sample is preferably not shredded before heating, or alternatively can be shredded. The extension of the sample preferably starts within a threshold time after the sample is heated, or alternatively can be performed at any other time point. The threshold time can be from 5 seconds to 5 minutes or any range or value therebetween (e.g., 10 seconds, 15 seconds, 20 seconds, 30 seconds, 1 minute, etc.), or alternatively can be less than 5 seconds or more than 5 minutes. The sample can optionally be exposed to ambient temperature (e.g., 20°C to 22°C) and / or target temperature (e.g., 20°C to 300°C or any range or value therebetween, any other target temperature) during extension. The extension assay procedure can be performed using a cheese extension test apparatus or any other tensile test apparatus. In a specific example, a cheese extension test apparatus (e.g., Texture Technologies TA-426N (trademark) used with a TA.XTPlus (trademark) texture analyzer) includes a well for holding a product sample (e.g., a melted product), a lifting plate with a hook (the initial position is submerged in the product near or in the well), and a ring that holds a part of the product near the well (e.g., the end of the sample) so that the product extends when the lifting plate with the hook rises.

[0088] The extension characteristics determined using the extension assay procedure can include break distance (e.g., elongation at complete break), peak force, extension toughness (e.g., work for elongation, normalized work, etc.), and / or any other extension metric. In a specific example, the product can be characterized by a break distance (measured using the extension assay procedure) of from 25 mm to 500 mm or any range or value therebetween (e.g., 50 mm to 400 mm, 100 mm to 300 mm, greater than 50 mm, greater than 75 mm, greater than 100 mm, greater than 125 mm, greater than 150 mm, greater than 200 mm, greater than 250 mm, etc.), or alternatively can be characterized by a break distance of less than 25 mm or more than 500 mm. Examples of extension assay data are shown in FIGS. 22, 23A, 23B, 23C, 25A, 25B, 25C, 25D, and 25E.

[0089] The product can optionally have target rheological properties (e.g., examples are shown in FIGS. 11A and 11B). The rheological properties of the product can be measured using a creep test (e.g., stress relaxation test, etc.), any test performed using a rheometer, and / or any other test. In the example, the creep test includes preparing a sample of the product having a target initial thickness (e.g., 1 mm, 2 mm, 3 mm, 4 mm, 5 mm, 10 mm, any range or value therebetween, etc.), mass (e.g., 1 g, 2 g, 2.5 g, 3 g, 3.5 g, 4 g, etc.), and / or target initial diameter (e.g., 10 mm, 15 mm, 20 mm, 25 mm, 30 mm, 50 mm, 100 mm, any range or value therebetween, etc.), filling the rheometer (e.g., MCR702 MultiDrive (trademark)) with the gel at a target temperature (e.g., room temperature, other target temperature, e.g., as described above for the elongation test, etc.), deforming the product at a constant initial strain (0.05%, 0.1%, 0.2%, 0.5%, 1%, 2%, 5%, any range or value therebetween, any strain within the linear viscoelastic region, etc.), and at a target frequency (e.g., 0.25 Hz, 0.5 Hz, 1 Hz, 1.5 Hz, 2 Hz, 5 Hz, any range or value therebetween, etc.) over a target time (e.g., 30 seconds, 1 minute, 2 minutes, 5 minutes, any range or value therebetween, any other target time, etc.), deforming the product at a constant creep strain (10%, 25%, 40%, 50%, 60%, 75%, any range or value therebetween, any strain within the non-linear viscoelastic region, etc.), and at a target frequency (e.g., the same or different frequency as the initial strain frequency; 0.25 Hz, 0.5 Hz, 1 Hz, 1.5 Hz, 2 Hz, 5 Hz, any range or value therebetween, etc.) over a target time, and deforming the product at a constant recovery strain (0.05%, 0.1%, 0.2%, 0.5%, 1%, 2%, 5%, any range or value therebetween, any strain within the linear viscoelastic region, etc.), and at a target frequency (e.g., the same or different frequency as the creep frequency; 0.25 Hz, 0.5 Hz, 1 Hz, 1.5 Hz, 2 Hz, 5 Hz, any range or value therebetween, etc.) over a target time.Rheological properties determined using creep include recovery of storage modulus (e.g., G’ recovery rate = (final G’ - initial G’) / initial G’), shear stress vs. shear strain profile, and / or any other property. In certain examples, the product can be characterized by a recovery of storage modulus of 50% to 99% or any range or value therebetween (e.g., 70% to 99%, 90% to 95%, greater than 60%, greater than 70%, greater than 75%, greater than 80%, greater than 90%, etc.), or alternatively by a recovery of storage modulus less than 50% or greater than 99%. Examples of creep test data are shown in FIGS. 26A, 26B, 26C, 26D, 26E, and 26F.

[0090] The product can optionally have target melting properties. The melting properties of the product are preferably measured using the Schreiber test, but additionally or alternatively, can be measured by differential scanning calorimetry, other melting assays, and / or other methods. In an example, the Schreiber test can include preparing a sample of the product having a target initial mass (e.g., 1 g, 2 g, 3 g, 3.5 g, 4 g, 5 g, 10 g, 20 g, 50 g, any range or value therebetween, etc.) and a target initial diameter (e.g., 10 mm, 15 mm, 20 mm, 25 mm, 30 mm, 50 mm, 100 mm, any range or value therebetween, etc.), heating the sample (e.g., optionally on a glass Petri dish with a cover), and measuring the final surface area of the sample and / or any other melting metric. The final surface area (e.g., the surface area of the melt) can optionally be measured by analyzing an image of the sample. In a first specific example, the sample can be heated at a target heating temperature (e.g., 50 °C, 70 °C - 85 °C, 60 °C - 75 °C, 75 °C, 80 °C, 85 °C, 100 °C, 150 °C, 200 °C, 230 °C, 250 °C, 300 °C, 400 °C, any range or value therebetween, any other target temperature, etc.) for a target heating time (e.g., 1 minute, 5 minutes, 6 minutes, 10 minutes, 15 minutes, 20 minutes, 30 minutes, 1 hour, any range or value therebetween, any other target time, etc.). In a second specific example, the sample can be heated to achieve a target temperature (e.g., 50 °C, 70 °C - 85 °C, 60 °C - 75 °C, 75 °C, 80 °C, 85 °C, 100 °C, 150 °C, 200 °C, 230 °C, 250 °C, 300 °C, 400 °C, any range or value therebetween, any other target temperature, etc.) in the sample over a target time (e.g., 1 minute - 10 minutes, 1 minute, 5 minutes, 6 minutes, 10 minutes, 15 minutes, 20 minutes, 30 minutes, 1 hour, any range or value therebetween, any other target time, etc.). The melting properties determined using the Schreiber test can include the change in area / mass and / or any other property. In a specific example, the product is 0.5 cm 2 / g to 10 cm 2 / g or any range or value therebetween (e.g., 1 cm 2 / g to 6 cm 2 / g, 0.5 cm 2 / g ultrasound, 1 cm 2 / g ultrasound, 2 cm 2 / g ultrasound, 3 cm 2 It can be characterized by the change in area / mass (measured using the Schreiber test) such as / g ultrasound, or alternatively 0.5 cm 2 less than / g or 10 cm 2 It can be characterized by the change in area / mass of / g ultrasound. Examples of Schreiber test data are shown in FIGS. 21, 23A, 23D, 24, and 25A.

[0091] The product can optionally have target shredding characteristics and / or grating characteristics. For example, the product can be shredded when exposed to a load of 0.5 kg to 10 kg (e.g., using a hood processor, etc.), or alternatively can be shredded when exposed to a load less than 0.5 kg or greater than 10 kg. Shredding can be evaluated quantitatively (e.g., shred size, shred force, etc.) and / or qualitatively (e.g., a qualitative metric from 0 to 1, etc.).

[0092] The product can optionally be thermoreversible (e.g., meltable upon heating, stretchable upon heating, etc.), thermo-irreversible, non-thermoreversible, and / or can have any heat response characteristics. For example, the product can be thermoreversible for at least one heating cycle, one or more heating-cooling cycles (e.g., melt-solidification cycles), a threshold number of heating-cooling cycles (e.g., 1, 2, 3, 5, 10, 50, etc.), and / or can be thermoreversible in other ways. Alternatively, the product can be non-thermoreversible and can form a gel, semi-solid, or solid when heated. However, the product can have other suitable sets of heat response and / or heat characteristics.

[0093] The product can include SPI (e.g., in an aqueous solution, in a lipid component, in a mixture, in dry SPI, etc.), aggregates of SPI, mixtures of SPI with other components (e.g., any component in S500) (e.g., gels, liquids, etc.), and / or can have any other formulation and / or structure. The product can optionally contain SPI that is either contained or uncontained (e.g., the lipid component and / or other components can be pooled and separated from SPI). The manufacture of the product can optionally include any S500 manufacturing method and any food manufacturing method.

[0094] Sample images of extended products (e.g., gels, etc.) manufactured using SPI are shown in FIGS. 13A - 13N, FIGS. 14A - 14AA, FIGS. 15A - 15D, and FIGS. 16A - 16F. In a variant, plant - based products (e.g., vegan products, hemp - protein - based products, sesame - protein - based products, etc.) can have the same or a similar structure as dairy products. Exemplary images of extended dairy products (e.g., the target product) are shown in FIGS. 17A - 17L. A comparative example of an extended product and a dairy product is shown in FIG. 18.

[0095] In a first variation, the manufacture of the product may include manufacturing a mixture (e.g., a gel) containing SPI and a lipid component (e.g., the mixture is the product). For example, the manufacture of the product may include collecting SPI (e.g., the insoluble fraction) by S400, diluting the SPI with an aqueous solution by S500 to form an SPI solution (e.g., an insoluble fraction solution), mixing (e.g., emulsifying) the SPI solution with the lipid component by S500 to form a mixture (e.g., an emulsion), optionally heating the mixture by S500, and optionally shaping the heated mixture by S500. An example is shown in FIG. 4. The mixture (e.g., after heating and cooling) preferably forms a gel, and the gel can exhibit target properties after initial heating, after reheating, and / or at any other time point. In a specific example, the target temperature of reheating (e.g., the target heating temperature and / or the target temperature of the mixture) can be 30°C to 300°C or any range or value therebetween (e.g., 200°C), or it can be less than 30°C or greater than 300°C. The target time of reheating can be 1 minute to 24 hours (e.g., 5 to 20 minutes, more than 10 minutes, etc.), or it can be less than 1 minute or greater than 24 hours. The manufacture of the product may optionally include adding a microbial culture (e.g., to SPI, the SPI solution, the mixture, etc.) and fermenting it. Fermentation can be carried out before heating the mixture, simultaneously with heating the mixture (e.g., heating the mixture includes fermenting the mixture), after heating the mixture, without heating the mixture (e.g., the mixture can be gelled by fermenting the mixture), and / or at any other time point. Fermentation after heating the mixture may include inoculating the gelled mixture with a culture broth, and the microbial culture in the broth can penetrate the gel. However, fermentation can be carried out in other ways. The resulting product is stretchable at room temperature and / or when heated. The resulting product can melt at a higher temperature (e.g., 100°C, 200°C, etc.). The resulting product can maintain its stretching and melting properties regardless of repeated heating / cooling cycles. However, the resulting product can have any other suitable set of properties.

[0096] In a second variation, the manufacture of the product includes using SPI as a component in the product. The SPI (e.g., an SPI solution, a mixture containing SPI, etc.) can be combined with other components (e.g., other proteins, carbohydrates, lipid components, any components in S500, etc.), and the resulting mixture can be processed (e.g., by the S500 method, other food manufacturing methods, etc.) to form the product.

[0097] In a third variation, the manufacture of the product includes manufacturing a component containing SPI (e.g., the component is the product). In a first example, the SPI is dried by S500, and the component contains the dried SPI. In a second example, the SPI undergoes protein modification, and the component contains the modified SPI. However, the SPI can be processed in other ways (e.g., using the S500 method) to generate the component.

[0098] However, the product can be manufactured by other methods.

[0099] In a first variation, the product is a liquid mixture. For example, the product is an emulsion of a lipid component and an SPI solution, and the emulsion can optionally be heated thereafter to induce gelation of the product and / or to induce the extensibility and / or melting properties of the product. In a first exemplary example, the liquid mixture is poured onto and / or spread on a food (e.g., pizza, bread, etc.), and subsequent heating (e.g., baking, broiling, grilling, etc.) causes the product to form a stretchy, melted cheese-like structure. In a second exemplary example, the liquid mixture can be a milk analogue (e.g., a functional milk).

[0100] In a second variant, the product is a gel. For example, the product can be a mixture comprising SPI that has been heated to form an aggregating gel and optionally cooled. In this example, the SPI can optionally form SPI aggregates. This gelation optionally imparts stability to the product (e.g., to enable transportation, for use in food manufacturing, etc.). The gel product can optionally then be heated (e.g., by a second heating step) to induce stretching and / or melting properties in the product. In another example, the product can be a cooled emulsion, where the emulsion is formed from a fat that has been heated above its melting point prior to emulsifying with the SPI. In an exemplary example, this variant of the product can be cut, scraped, grated, minced, ground in other ways, or used as a single block. Small pieces of the product can be placed on food (e.g., pizza, bread, etc.) and heated (e.g., baked, grilled, broiled), and subsequent heating (e.g., baking, grilling, broiling, etc.) causes the product to form a stretchy, melted cheese-like structure.

[0101] In a third variant, the product is a stretchable and / or meltable product. For example, the product can be a mixture of SPI and a lipid component that is heated to form a stretchable gel product and / or a meltable product. Examples of stretchable gel products are shown in FIGS. 8A, 8B, 8C, and 22. Examples of stretchability data for stretchable gel products are shown in FIGS. 10A and 10B. Examples of meltable products are shown in FIGS. 9A, 9B, 21, and 24. An example of differential scanning calorimetry data for a stretchable gel product is shown in FIG. 12. In a particular example, the product can be heated to an internal temperature of 50°C to 300°C (e.g., 70°C to 100°C, 85°C, 200°C, 250°C, etc.) and / or maintained at that temperature.

[0102] In a fourth variant, the product includes dried SPI (e.g., dried using the S500 method). The dried SPI can be in powder form and / or any other form. The dried SPI is then rehydrated and used as a component in the manufacture of the product and / or can be used in other ways.

[0103] The product can be implemented in various food manufacturing use cases. In a first embodiment, the product is used directly as food (e.g., the product is a final food, the product is a main basis of the final food, etc.). In a first exemplary example, the product is a liquid product (e.g., an emulsion and / or other mixture) that functions as a liquid dairy product analogue (e.g., a liquid mozzarella analogue), and the liquid product can then be heated to form a melted dairy product analogue (e.g., a melted mozzarella analogue). In a second exemplary example, the product is a stretchable dairy product analogue (e.g., a soft cheese analogue) at room temperature or near room temperature. In a third exemplary example, the product is a cohesive gel (e.g., the cohesive gel has no stretchability at room temperature, the cohesive gel has stretchability at room temperature, etc.), and the cohesive gel stretches and / or melts when heated (e.g., the product can be a cheese substitute for shredded cheese, sliced cheese, and / or block cheese). In a second embodiment, the product is used as a main substrate in food manufacturing. In a third embodiment, the product is used as an additive component in food manufacturing and functions to increase the stretch and / or melt properties of the final food. For example, the final food can be manufactured using a mixture of SPI, other proteins, lipid components, microorganisms, and / or any other components (e.g., fermentation can be optionally performed at any point during the food manufacturing process). However, the product can be used in other ways.

[0104] In the first example, the product (e.g., product A, 15% by weight of total protein and 35% by weight of lipid) contains an emulsion comprising a lipid component and an SPI mixture, and the SPI mixture is the insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation (in a variation, all or most of the extracted protein is not denatured). In the second example, the product (e.g., product H, 18% by weight of total protein and 35% by weight of lipid) contains an emulsion comprising a lipid component and an SPI mixture, and the SPI mixture is the insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation (in a variation, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution (e.g., in the case of product A and product H; SPI contains aggregates of hemp protein isolate), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0105] In the third example, the product (e.g., product B, 15% by weight of total protein) contains a solution comprising an SPI mixture, and the SPI mixture is the insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation (in a variation, all or most of the extracted protein is not denatured). In the fourth example, the product (e.g., product I, 15% by weight of total protein) contains a solution comprising an SPI mixture, and the SPI mixture is the insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation (in a variation, all or most of the extracted protein is not denatured). In the fifth example, the product (e.g., product M) contains a solution comprising an SPI mixture (8% by weight), and the SPI mixture is the insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation (in a variation, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution (e.g., in the case of product B, product I, and product M), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0106] In the sixth example, the product (e.g., product C, 15% by weight of total protein and 35% by weight of lipid) includes an emulsion containing a lipid component and an IPI mixture, and the IPI mixture is the insoluble fraction (e.g., precipitate) of a protein isolate solution collected using the isoelectric precipitation method (in a variant, all or most of the extracted protein is not denatured). In the seventh example, the product (e.g., product J, 18% by weight of total protein and 35% by weight of lipid) includes an emulsion containing a lipid component and an IPI mixture, and the IPI mixture is the insoluble fraction (e.g., precipitate) of a protein isolate solution collected using the isoelectric precipitation method (in a variant, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution, a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0107] In the eighth example, the product (e.g., product D, 15% by weight of total protein) includes a solution containing an IPI mixture, and the IPI mixture is the insoluble fraction (e.g., precipitate) of a protein isolate solution collected using the isoelectric precipitation method (in a variant, all or most of the extracted protein is not denatured). In the ninth example, the product (e.g., product K, 18% by weight of total protein) includes a solution containing an IPI mixture, and the IPI mixture is the insoluble fraction (e.g., precipitate) of a protein isolate solution collected using the isoelectric precipitation method (in a variant, all or most of the extracted protein is not denatured). In the tenth example, the product (e.g., product O) includes a solution containing an IPI mixture (8% by weight), and the IPI mixture is the insoluble fraction (e.g., precipitate) of a protein isolate solution collected using the isoelectric precipitation method (in a variant, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution (e.g., in the case of products D, K, and O), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0108] In the 11th example, the product (e.g., Product E, 15% by weight of total protein and 35% by weight of lipid) contains an emulsion comprising a lipid component and an ASP mixture, and the ASP mixture is the insoluble fraction of a protein isolate solution collected using poor solvent precipitation (in a variation, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution (e.g., in the case of Product E), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0109] In the 12th example, the product (e.g., Product F, 15% by weight of total protein) contains a solution comprising an ASP mixture, and the ASP mixture is the insoluble fraction of a protein isolate solution collected using poor solvent precipitation (in a variation, all or most of the extracted protein is not denatured). In the 13th example, the product (e.g., Product N) contains a solution comprising an ASP mixture (8% by weight), and the ASP mixture is the insoluble fraction of a protein isolate solution collected using poor solvent precipitation (in a variation, all or most of the extracted protein is not denatured). In certain examples, the insoluble fraction is extracted from a hemp protein isolate solution (e.g., in the case of Product F and Product N), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0110] In the 14th example, the product (e.g., Product G, 15% by weight of total protein and 35% by weight of lipid) contains an emulsion comprising a lipid component and hemp powder. In the 12th example, the product (e.g., Product L, 18% by weight of total protein and 35% by weight of lipid) contains an emulsion comprising a lipid component and hemp powder.

[0111] In a first specific example, the method includes obtaining a protein isolate solution (e.g., containing protein isolate units) from a protein source (e.g., plants, microorganisms, algae, fungi, seaweeds, or other non-dairy / non-animal substances), using the protein isolate solution to prepare / generate a structured protein isolate by precipitation / separation / sedimentation, etc. (i.e., diluting the soluble protein with an aqueous or non-aqueous solvent, i.e., water, a poor solvent, and / or any other diluent, and by isoelectric precipitation, heat or shear-induced precipitation, etc.), fractionating the structured protein isolate from the solution (e.g., by filtration, centrifugation, dialysis, drying, etc.), and collecting the structured protein isolate (e.g., aggregates of the structured protein isolate) as a component. In a second specific example, the method includes obtaining a protein isolate solution from a protein source, mixing the protein isolate solution with a lipid component having different protein:lipid ratios (e.g., 0 to 50% protein: 0 to 40% lipid, etc.) (e.g., emulsifying) to form a lipid-protein isolate mixture (e.g., an oil-water emulsion), precipitating / separating / sedimenting the lipid-protein mixture by diluting with an aqueous or non-aqueous solvent, i.e., water, a poor solvent, and / or any other diluent, performing isoelectric precipitation, heat or shear-induced precipitation, etc., fractionating the lipid-protein isolate (e.g., a structured protein isolate containing a lipid component) from the solution (e.g., by filtration, centrifugation, dialysis, drying, etc.), and collecting the lipid-protein isolate as a component. In a third specific example, the method includes obtaining a protein isolate solution from a protein source, diluting the protein isolate solution using a diluent containing an aqueous solution mixed with a lipid component (e.g., emulsified), fractionating the structured isolate from the solution (e.g., by filtration, centrifugation, dialysis, drying, etc.), and collecting the structured isolate as a component.

[0112] As used herein, "substantially" or other approximating terms (e.g., "about," "approximately," etc.) can be within a given error threshold or within an acceptable range of a metric, component, or other criterion (e.g., within 0.001%, 0.01%, 0.1%, 1%, 2%, 5%, 10%, 15%, 20%, 30% of the criterion, or within any range or value within those ranges).

[0113] Embodiments of the system and / or method can include all combinations and permutations of various system components and various method processes, and one or more instances of the methods and / or processes described herein can be performed by, and / or using, one or more instances of the systems, elements, and / or entities described herein, non-simultaneously (e.g., sequentially), contemporaneously (e.g., concurrently, in parallel, etc.), or in other suitable orders. The components and / or processes of the following systems and / or methods can be used with, in addition to, instead of, or otherwise integrated with all or part of the systems and / or methods disclosed in the applications described above (each of which is incorporated by reference in its entirety).

[0114] As will be appreciated by those skilled in the art, modifications and changes can be made to the preferred embodiments of the present invention without departing from the scope of the present invention as defined in the following claims, as can be recognized from the detailed description above, the drawings, and the claims.

Claims

1. A composition comprising a protein mixture containing an isolated structured protein, wherein each isolated structured protein contains an aggregate of at least three protein isolate units, said protein isolate units are obtained from a plant source, at least 20% of the protein isolate units in said protein mixture are arranged in said isolated structured protein, and said isolated structured protein is extracted from the insoluble fraction of a solution.

2. The composition according to claim 1, further comprising a lipid component derived from a plant.

3. The composition according to claim 1, wherein said protein mixture is spray-dried.

4. The composition according to claim 1, wherein said isolated structured protein has an increased surface hydrophobicity compared to non-aggregated protein isolate units.

5. The composition according to claim 1, wherein the diameter of said isolated structured protein is at least 50 nm.

6. The composition according to claim 1, wherein said plant source comprises a single plant source.

7. A composition comprising a protein component and a lipid component, wherein said protein component contains an isolated structured protein, each isolated structured protein contains an aggregate of at least three protein isolate units, said protein isolate units are obtained from a plant source, and at least 90% of the protein isolate units in said protein component are not denatured.

8. The composition according to claim 7, wherein said protein component does not contain an animal protein.

9. The composition according to claim 7, wherein said protein component does not contain a soy-derived product.

10. The composition according to claim 7, wherein said composition contains a fermented cheese replica, said composition further contains a microbial culture, and said composition is fermented.

11. The composition according to claim 7, wherein said composition contains a fresh cheese replica and said composition is a gelled emulsion.

12. The composition according to claim 7, wherein said composition is shredable.

13. The composition is about 1 cm ２ / g to about 6 cm ２ / g change in area / mass as measured by the Schreiber test (initial diameter of about 25 mm, initial mass of about 3.5 g, heated at about 230 °C for about 6 minutes), the composition according to claim 7.

14. The composition according to claim 7, characterized by a breaking distance of at least 100 mm when measured by an elongation assay procedure (about 30 g sample, heated at about 200 °C for about 15 minutes, elongation at about 20 °C at 5.00 mm / second).

15. Obtaining protein isolate units from a plant source, Diluting the protein isolate units to form a diluted protein isolate mixture; Collecting an insoluble fraction from the diluted protein isolate mixture, wherein the insoluble fraction comprises structured protein isolates, and each structured protein isolate comprises aggregated protein isolate units; said collecting; Manufacturing a plant-based food comprising the insoluble fraction and a lipid component, wherein the food is characterized by a breaking distance of at least 100 mm when measured by an elongation assay procedure; said manufacturing; A plant-based food obtained by a process comprising.

16. The food according to claim 15, wherein the elongation assay procedure comprises heating a sample of about 30 g at about 200 °C for about 15 minutes and elongating the sample at about 20 °C at about 5.00 mm / second.

17. The food according to claim 15, wherein diluting the protein isolate units comprises diluting a protein isolate solution comprising the protein isolate units and a salt, and the ratio of the salt concentration of the protein isolate solution to the salt concentration of the diluted protein isolate mixture is at least 3.

18. The composition comprises a plant-based cheese, and manufacturing the composition comprises Diluting the insoluble fraction with an aqueous solution to form a diluted insoluble fraction; Forming an emulsion comprising the diluted insoluble fraction and the lipid component; Heating the emulsion to a temperature below the denaturation temperature of the protein isolate units; Forming the emulsion into a gel, wherein the plant-based food comprises the gel; said forming; The food according to claim 15, comprising.

19. The food according to claim 18, wherein the aqueous solution comprises a hydrocolloid.

20. The food according to claim 15, wherein at least 0.5% of the dry components of the insoluble fraction comprises a carbohydrate.

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