Structured protein isolates and related methods

Abstract

A food product and / or ingredients thereof may comprise 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

[0001] CROSS-REFERENCE TO RELATED APPLICATIONS

[0002] 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 by reference in its entirety.

[0003] This application is related to U.S. application No. 17 / 857,871 filed on July 5, 2022, which is incorporated by reference in its entirety. Technical Field

[0004] The present invention relates generally to the field of food science and, more particularly, to new and useful systems and methods in the field of food science. BRIEF DESCRIPTION OF THE DRAWINGS

[0006] Figure 1 is a schematic representation of a variation of this approach.

[0007] Figure 2 A first example of this method is depicted.

[0008] Figure 3 A second example of this method is depicted.

[0009] Figure 4 A third example of this method is depicted.

[0010] Figure 5A , Figure 5B , Figure 5C and Figure 5D A schematic example of a cross-section of a structured protein isolate (SPI) is depicted.

[0011] Fig. 6A Depicted is a first schematic example of a cross-section of an SPI mixture comprising an SPI encapsulating a lipid component, wherein the outer region is more hydrophilic than the inner region.

[0012] Figure 6B A second schematic illustration of a cross-section of a SPI mixture comprising SPI and a phospholipid encapsulating lipid component is depicted.

[0013] Figure 6C A third schematic illustration of a cross-section of a SPI mixture comprising SPI and a phospholipid encapsulating lipid component is depicted.

[0014] Fig.6D Depicted is a fourth schematic example of a cross-section of a SPI mixture comprising SPI aggregates encapsulating a lipid component, wherein the outer region is more hydrophilic than the inner region.

[0015] Fig. 6EA fifth schematic illustration of a cross-section of a SPI mixture comprising SPI aggregates and a phospholipid encapsulating lipid component is depicted.

[0016] Figure 7 Illustrative examples of transmission electron micrographs of SPIs are depicted. A) Single SPI. B) SPI aggregates. C) SPI aggregates. D) SPI dispersed in oil droplets.

[0017] Fig. 8A , Figure 8B and Figure 8C Exemplary images of stretchable products are depicted.

[0018] Fig.9A and Fig. 9B Exemplary images of meltable products are depicted.

[0019] Fig. 10A Examples of force versus time data (eg, from a ductility probe) for the products, dairy cheese and zein gel, are depicted.

[0020] Fig. 10B Examples of force versus time data (eg, from a ductility probe) for a product heated at different temperatures are depicted.

[0021] Fig.11A Depicted are examples of low-distortion Lissajous plots for products made using SPI derived from industrial hemp (hemp), sesame, pumpkin and watermelon protein sources.

[0022] Fig. 11B Depicted are examples of highly deformed Lissajous plots for products made using SPI derived from hemp, sesame, pumpkin, and watermelon protein sources; the hemp and sesame products exhibit similar nonlinear responses.

[0023] Fig.12 Depicted are examples of differential scanning calorimetry results (eg, measuring melting curves) for products made using SPI derived from industrial hemp, sesame, pumpkin, and watermelon protein sources.

[0024] Figure 13A-13N Depicted are exemplary images of products made using industrial hemp-derived SPI. Images were captured using an 18MP AmScope digital microscope camera (e.g., Model-MU1803-HS) and an optical microscope with a 4× lens (e.g., Nikon Labophot-2 microscope).

[0025] Figure 14A-14AADepicted are exemplary images of products made using sesame-derived SPI. Images were captured using an 18 MP AmScope digital microscope camera and an optical microscope with a 4× lens.

[0026] Figures 15A-15D Depicted are exemplary images of products made using pumpkin-derived SPI. Images were captured using an 18 MP AmScope digital microscope camera and an optical microscope with a 4× lens.

[0027] Figures 16A-16F Depicted are exemplary images of products made using watermelon-derived SPI. Images were captured using an 18 MP AmScope digital microscope camera and an optical microscope with a 4× lens.

[0028] Figures 17A-17L An exemplary image of mozzarella cheese is depicted. The image was captured using an 18MP AmScope digital microscope camera and an optical microscope with a 4× lens.

[0029] Fig.18 Depicted are exemplary images of products made using SPI compared to mozzarella cheese.

[0030] Fig.19 An illustrative example of forming an SPI is depicted.

[0031] Fig. 20A and Fig. 20B A specific example of the method is depicted.

[0032] Fig.21 Images after heating in a Schreiber test are depicted for the following products (target heating temperature was 230°C): Product A (15% total protein by weight; 35% lipid by weight) comprising SPI (insoluble fraction collected using aqueous dilution) and a lipid component; Product B (15% total protein by weight) comprising SPI without a lipid component; Product C (15% total protein by weight) comprising an isoelectric precipitation isolate (IPI) (insoluble fraction collected using isoelectric precipitation) and a lipid component; Product D of IPI without a lipid component (15% total protein by weight); Product E comprising an antisolvent precipitate (ASP) (e.g., an insoluble fraction collected using antisolvent precipitation) and a lipid component (15% total protein by weight; 35% lipid by weight); Product F comprising ASP without a lipid component (15% total protein by weight); Product G comprising industrial hemp powder and a lipid component (15% total protein by weight; 35% lipid by weight); commercial plant-based cheese; and dairy cheese (e.g., mozzarella cheese).

[0033] Fig. 22Depicted Fig.21 Images of the products depicted in the figure taken at or near failure distance during ductility measurement (target heating temperature of 250°C; extension rate of 5 mm / s), namely: Product A; Product B; Product C; Product D; Product; Product F; and Product G; commercial plant-based cheese; and dairy cheese.

[0034] Fig.23A Depicted Fig.21 An example of data of melting measurements (final surface area determined using the Schreiber test, with a target heating temperature of 230°C) and tensile measurements (failure distance determined using ductility measurement, with a target heating temperature of 250°C and an extension rate of 5 mm / s) for the products depicted in, namely: Product A, Product E, Product C, Product G, dairy cheese, and commercial plant-based cheese.

[0035] Fig. 23B Depicted Fig.21 Examples of normalized work versus failure distance data for the products depicted in (determined using a ductility assay with a target heating temperature of 250°C and an extension rate of 5 mm / s), namely: Product A, Product E, Product C, Product G, dairy cheese, and commercial plant-based cheese.

[0036] Fig.23C Depicts comparison of lipid components (from Fig.21 Product C, Product A and Product E) and lipid-free (from Fig.21 Example of data for the failure distances of products (determined using a ductility measurement with a target heating temperature of 250°C and an elongation rate of 5 mm / s) of Product D, Product B, and Product F.

[0037] Fig.23D Depicts comparison of lipid components (from Fig.21 Product C, Product A and Product E) and lipid-free (from Fig.21 Example of data for the final surface area of ​​the products (determined using the Schreiber test with a target heating temperature of 230°C) of Product D, Product B and Product F).

[0038] Fig.24 Images after heating in a Schreiber test (target heating temperature of 230°C) are depicted for the following products: Product H comprising SPI and a lipid component (18% total protein by weight; 35% lipid by weight); Product I comprising SPI without a lipid component (18% total protein by weight); Product J comprising IPI and a lipid component (18% total protein by weight; 35% lipid by weight); and Product K comprising IPI without a lipid component (18% total protein by weight).

[0039] Fig.25A An example of data depicting melting measurements (final surface area determined using the Schreiber test, with a target heating temperature of 230°C) versus tensile measurements (failure distance determined using ductility determination, with a target heating temperature of 200°C and an extension rate of 5 mm / s) for the following products: Fig.24 The product H, from Fig.24 Product J, and Product L comprising industrial hemp powder and a lipid component (18% total protein by weight; 35% lipid by weight), and dairy cheese.

[0040] Fig.25B Depicted is a comparison of products containing lipid components (from Fig.24 Product H and Product J) and the product without lipid components (from Fig.24 Example of data for failure distances of Product I and Product K) (determined using ductility measurements with a target heating temperature of 200°C and an elongation rate of 5 mm / s).

[0041] Fig.25C An example of normalized work versus failure distance data (determined using ductility measurements with a target heating temperature of 200°C and an extension rate of 5 mm / s) is depicted for the following products: Fig.25A products (Product H, Product J and Product L); dairy cheese; and commercial plant-based cheese.

[0042] Fig.25D Depicted is an example of data comparing the distance to failure of products having ductility determination target heating temperatures of 200°C and 250°C.

[0043] Fig.25E Depicted is an example of data comparing the normalized work for products with ductility determination target heating temperatures of 200°C and 250°C.

[0044] Figure 26A-26FExamples of data (determined using creep testing with constant strain (50% strain at 1 Hz frequency)) are depicted for Product M containing SPI (a mixture containing 8% SPI by weight; SPI contains 33% protein by weight), Product N containing ASP (a mixture containing 8% ASP by weight; ASP contains 50% protein by weight), and Product O containing IPI (a mixture containing 8% IPI by weight; IPI contains 43% protein by weight). The data show that Product M and Product N behave like connected gels (e.g., strongly connected gels), and that Product O behaves like a weakly connected gel. The data show that Product M and Product N become stiffer over time (e.g., indicating strain hardening behavior), and that Product O behaves like a viscous material (e.g., a disconnected or weakly connected gel).

[0045] Details

[0046] The following description of embodiments of the invention is not intended to limit the invention to those embodiments, but rather is intended to enable any person skilled in the art to make and use the invention.

[0047] 1. Overview

[0048] like Figure 1 As shown in FIG. 5 , the method may include: obtaining a protein isolate unit S100 from a protein source, and collecting a structured protein isolate S400. However, the method may additionally or alternatively include any other suitable steps.

[0049] In variations, the method can be used to produce: a food product having target properties (eg, stretch properties and / or meltability properties), a substitute (eg, an analogue) of a target food product, an ingredient for making a food product, and / or any other product.

[0050] 2. Examples

[0051] In a first example, the method includes: obtaining a protein isolate solution (e.g., containing protein isolate units) from a protein source (e.g., plant matter); diluting the protein isolate solution using water, an antisolvent and / or any other diluent; separating an insoluble fraction from the diluted protein isolate solution (e.g., sedimentation, precipitation, fractionation, etc.); and collecting a structured protein isolate (e.g., an aggregate of a structured protein isolate) from the insoluble fraction (e.g., collecting an insoluble fraction as a component, wherein the insoluble fraction includes a 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 containing a protein isolate and a lipid); separating an insoluble fraction from the diluted protein isolate mixture (e.g., fractionation of the insoluble fraction, wherein the insoluble fraction includes a 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 comprising an aqueous solution mixed (e.g., emulsified) with a lipid component; separating an insoluble fraction from the diluted protein isolate solution; and collecting a structured protein isolate from the insoluble fraction.

[0052] The collected structured protein isolate can optionally be used to produce food (e.g., plant-based food). In a first example, the collected structured protein isolate can be combined with an aqueous component (e.g., water with a gelling additive), a lipid component, and / or other ingredients, and treated (e.g., emulsified) to form a structured protein isolate emulsion. The structured protein isolate emulsion can be heated (e.g., below the denaturation point of the protein) and molded to form a gel. The gel can be a food (e.g., a fresh cheese replica) and / or further processed to produce a food. 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 ingredient, and treated (e.g., emulsified) to form a structured protein isolate emulsion. The emulsion can be gelled, fermented, and / or otherwise processed to produce a food (e.g., an aged cheese replica). In a third example, the collected structured protein isolate is used as an ingredient in a food (e.g., a dairy or animal protein substitute).

[0053] 3.Technological advantages

[0054] Variations of this technique may confer one or more advantages over conventional techniques.

[0055] In contrast to certain dairy proteins, plant-based proteins denature and form new bonds (e.g., spanning the entire substrate; forming cross-links; etc.) when exposed to heat, resulting in isotropically connected gels that can limit stretching and melting. Variations of this technology can enable the preparation of meltable, stretchable products (e.g., foods) using plant-based proteins.

[0056] First, variations of the technology can cause a mixture of protein, water, and lipid components to exhibit stretching and / or melting properties similar to dairy products when heated. In one example, a plant-based protein solution comprising a structured protein isolate (SPI) suspended in water can be mixed (e.g., emulsified) with a lipid component, wherein the mixture melts and / or forms a stretchable matrix when heated. In another example, the stretching and / or melting properties can be achieved by the SPI itself (e.g., without the lipid component). In a variation, the stretching and / or melting properties can be produced without animal-derived products (e.g., animal protein) and / or without soy derivatives.

[0057] Second, variations of the technology can reduce or eliminate the percentage of carbohydrates (e.g., gums, starches, etc.) used in plant-based food substitutes while maintaining desired stretch and / or melting properties. This can enable plant-based food substitutes to have a nutritional profile (e.g., including high protein content) that is more closely aligned with a target food (e.g., a dairy food).

[0058] Third, variations 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 include a solution of SPI, wherein the SPI solution is at a target pH (e.g., alkaline pH, acidic pH, etc.) and / or a target protein concentration. The resulting gel can be used as a cheese (e.g., shreddable cheese, stretchable cheese, meltable cheese, etc.).

[0059] Fourth, variations of the technique can produce products with unexpected properties. In the first example, mixtures of SPI and lipid components (e.g., heated gel, unheated gel, etc.) can result in unexpected tensile properties; Fig. 8A , Figure 8B , Figure 8C , Fig. 10A , Fig. 10B , Fig. 22 , Fig.23A , Fig. 23B , Fig.23C , Fig.25A , Fig.25B , Fig.25C , Fig.25D and Fig.25EIn the second example, a mixture of SPI and lipid components can lead to unexpected melting properties; Fig.9A , Fig. 9B , Fig.21 , Fig.23A , Fig.23D , Fig.24 and Fig.25A An example is shown in In a third example, a mixture of SPI and lipid components can lead to unexpected protein unfolding and / or denaturation behavior (e.g., associated with gelation behavior); Fig.12 An example is shown in FIG.

[0060] Fifth, variations of the technology may include forming SPI in the presence of lipids, which may result in SPI and / or SPI aggregates (e.g., SPI structures and / or SPI aggregate structures) that may have increased stable interactions with the lipids. For example, lipids may be trapped within SPI and / or SPI aggregates. In specific examples, these lipid interactions may promote stretching and / or melting properties by enabling "slippage" between SPI and / or SPI aggregates. These interactions may support cohesive gels comprising lipid components, wherein the gel has improved stretching and / or melting properties.

[0061] Sixth, conventional methods for separating proteins may denature the proteins. In particular, isoelectric precipitation methods may denature all or part of the separated proteins. Variations of this technology may include forming SPIs without denaturing the constituent proteins and / or by denaturing less than a threshold proportion (e.g., 10%, 5%, 2%, 1%, etc.) of the constituent proteins. In an example, this can increase the stretching, melting, and / or other properties of the product produced using the SPI. In a specific example, the SPI formed without denaturing the constituent proteins can interact with other SPIs without forming bonds (e.g., covalent bonds) between the SPIs; this can promote stretching and / or melting.

[0062] However, the systems and methods disclosed herein may provide additional advantages.

[0063] 4. Methods

[0064] like Figure 1 As shown in , the method may include: obtaining a protein isolate unit from a protein source S100, and collecting a structured protein isolate S400. The method may optionally include combining a protein isolate unit with a lipid component S200, diluting a protein isolate unit S300, processing a structured protein isolate S500, producing a product having a structured protein isolate S600, and / or any other suitable step.

[0065] All or part of the method can be performed iteratively, simultaneously, asynchronously, periodically, during food production, and / or at any other suitable time. All or part of the method can be performed automatically, manually, semi-automatically, and / or in other ways.

[0066] In an example, the method may include a system and / or method as described in U.S. Application No. 17 / 857,871, filed on July 5, 2022, which is incorporated by reference in its entirety.

[0067] All or part of the method can be carried out without denaturing protein (e.g., protein isolate unit) and / or by denaturing protein less than a threshold percentage in a sample (e.g., in a protein source, a protein source solution, a protein isolate mixture, a structured protein isolate, a structured protein isolate mixture, a product, any other sample, etc.). For example, the sample is preferably formed and / or processed so that the protein denaturation less than the threshold percentage in the sample is carried out, but can be formed and / or processed in other ways selectively. The threshold percentage of protein can be between 0.01%-50% or any range or value therebetween (e.g., 0.05%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, etc.), but can be selectively less than 0.01% or greater than 50%. In a first specific example, the sample is exposed to a pH level lower than a first pH threshold (e.g., an acid-induced denaturation threshold) and / or higher than a second pH threshold (e.g., an alkali-induced denaturation threshold) during formation and / or processing. The first pH threshold may be between 2-6.5 or any range or value therebetween (e.g., 3, 4, 5, 6, etc.), but may be optionally less than 2 or greater than 6.5. The second pH threshold may be between 7.5-12 or any range or value therebetween (e.g., 8, 9, 10, 11, etc.), but may be optionally less than 7.5 or greater than 12. In a second specific example, the sample is exposed to a temperature below a temperature threshold (e.g., a thermal denaturation threshold) during formation and / or processing. The temperature threshold may be between 60°C-100°C or any range or value therebetween (e.g., 70°C, 75°C, 80°C, 85°C, 90°C, etc.), but may be optionally less than 60°C or greater than 100°C. The sample may optionally be exposed to a temperature above the temperature threshold for a period of time below the threshold (e.g., 1s, 2s, 5s, 10s, 15s, 30s, 1min, 5min, 10min, 30min, 1hr, any range or value therebetween, etc.). In a third specific example, the sample is exposed to a salt concentration level below a salt concentration threshold during formation and / or treatment. The salt concentration threshold may be between 0.1M-5M or any range or value therebetween (e.g., 0.1M-1M, 0.5M-2M, 0.8M-0.9M, etc.), but may be optionally less than 0.1M or greater than 5M. The salt concentration threshold may optionally depend on the pH of the sample. The salt concentration threshold may optionally be associated with a conductivity threshold between 100 millisiemens-25,000 millisiemens or any range or value therebetween, but may be optionally less than 100 millisiemens or greater than 25,000 millisiemens. Denaturation thresholds (first and / or second pH thresholds, temperature thresholds, exposure time thresholds, salt concentration thresholds, etc.) may optionally be determined based on protein type.

[0068] The method can be used with one or more sources (e.g., substrates) and / or source components (e.g., a portion of a source), wherein the protein and or other ingredients can be derived from the source and / or the source component. Examples of sources include: plant matter (e.g., processed and / or unprocessed plant matter), animal matter (e.g., milk such as cow's milk, insects such as house crickets (Acheta domesticus), meat, etc.), non-animal matter, fungal matter, algae matter, seaweed matter, microbial matter (e.g., bacteria), any organism, food, naturally occurring source, synthetic source, dairy source, non-dairy source and / or any other source. Examples of source components include: nuts, fruits, seeds, beans, stems, leaves, roots, flowers, stamens, muscles, shells and / or any other components of related sources. The source can be dry or in solution. The source can be processed (e.g., lipid removal, including defatting, mechanical treatment, chemical treatment, extraction, fermentation, protein modification, filtration, enrichment and / or any other treatment) and / or unprocessed. In a specific example, the source can be in a ground and / or powdered 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 a specific example, the protein source can be an enriched protein source. The protein source can optionally have a protein concentration greater than a threshold percentage, wherein the threshold percentage can be between 5%-90% or any range or value therebetween (e.g., 10%, 20%, 30%, 40%, 50%, 60%, 70%, etc.), but can be optionally less than 5% or greater than 90%. The source can be a complete ingredient (e.g., in or near its natural state), a processed ingredient (e.g., including additives or other ingredients, etc.), and / or any other suitable source.

[0069] Plant matter can include: peas (e.g., pea flour, pea starch, etc.), rice (e.g., rice flour, glutinous rice flour, white rice flour, brown rice flour, etc.), fruits, cassava (e.g., tapioca flour), potatoes, cocoa beans, truffles, olives, coconut meat, grape pomace, pumpkin (e.g., pumpkin seeds), cotton seeds, rapeseed, sunflower (e.g., sunflower seeds), pistachios, almonds, walnuts, walnuts, cashews, Brazil nuts, hazelnuts, macadamia nuts, pecans, peanuts, industrial hemp, hops , hackberry (e.g., celtis), oats, rice, watermelon (e.g., watermelon seeds), chestnuts, chia, flax, quinoa, soy, split mung bean, aquafaba, lupine, fenugreek, kiwi, peppercorns, mustard, sesame, algae, duckweed (e.g., lemna), pumpkin, chickpeas, pine nuts, citrus (e.g., citrus fiber), broad beans (e.g., broad bean flowers), grapes (e.g., grape pomace), lima beans (e.g., lima pods), beans) (e.g., lima beans), corn (e.g., zein 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 family Anacardiaceae, Asteraceae, Leguminosae, Cucurbits, Rosaceae, Lamiaceae, and / or other families; combinations thereof and / or any other plant matter. The plant matter may include primary oilseed production (e.g., soybean, rapeseed, sunflower, sesame, niger, castor, canola, cottonseed, etc.), secondary oilseed production (coconut, palm seed, pumpkin, etc.), and / or other crops or plant matter. Plant matter can include a single species of plant matter, a mixture of various plant matter, include animal matter (eg, insect matter, mammalian products, etc.), and / or include matter from any other source.

[0070] The method can be used together with one or more lipid components (e.g., fat, oil, butter, any lipid, etc.). The lipid component is preferably derived from one or more plant sources (e.g., plant matter), but can be alternatively derived from animal sources (e.g., dairy butter, lard, tallow, insect fat, etc.) and / or any other source. The lipid component is preferably triglyceride, but can be alternatively monoglyceride, diglyceride, free fatty acid, phospholipid and / or any other lipid. The lipid component can be saturated, unsaturated (e.g., monounsaturated, polyunsaturated, etc.) and / or have any other classification. In a specific example, natural antioxidants (e.g., tocopherol, ascorbic acid, carotenoids, flavonoids, amino acids, phospholipids, sterols, etc.) and / or synthetic antioxidants (e.g., BHT) can be optionally used to ensure the chemical stability (e.g., during storage, cooking, etc.) of monounsaturated and / or polyunsaturated lipids. The lipid component can be liquid at target temperature (e.g., room temperature), can be solid at target temperature, and / or can be the material of any other state. The example of lipid component includes fat and / or oil from: 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 seed), Indian garcinia (kokum), shea, mango, industrial hemp, vegetables, any neutral lipid, synthetic lipid, any combination thereof, lipid type (e.g., canola fat) and / or any other lipid that does not contain or is less than threshold percentage. Lipid component can include a combination (e.g., blend) of lipid component. In a first example, a blend of a lipid (e.g., fat) that is solid at room temperature and a blend of a lipid (e.g., oil) that is liquid at room temperature can be used. In a second example, a blend of plant-based lipids of different varieties, a blend of animal-based lipids of different varieties and / or a blend of plant-based and animal-based lipids can be used. Optionally, the lipid component can be selected, modified and / or otherwise processed so that the lipid component is stable at room temperature and / or has a melting property curve that matches the target melting property curve (e.g., for the target product). Lipid component modification includes transesterification, refining, clarification, classification, adjusting saturation, adjusting lipid crystal structure, adjusting chain length, adjusting melting point, adjusting smoke point and / or modification.

[0071] The method can be optionally used together with phospholipids.Phospholipids can include lecithin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine and / or any other phospholipids or its combination.Phospholipids preferably derive from one or more plant sources, but can additionally or selectively derive from animal sources and / or any other source.In an instantiation, lipid component includes phospholipids (for example, wherein the lipid component in all or part of the method refers to a mixture of lipid and phospholipids).

[0072] The method can be used with one or more protein isolate units. The protein isolate unit can include: globulins (e.g., 2S globulin, 11S globulin, 7S globulin, conglutin, napin, sfa, edestin, amandin, concanvalin, vicilin, legumin, cruciferin, helianthinin, etc.), pseudoglobulins, globular proteins, prolamins, albumins, gluten, conjugated proteins (e.g., lipoproteins, mucins, etc.), other storage proteins (e.g., albumins, prolamins, gluten, etc.), animal proteins (e.g., caseins, insect proteins, etc.), and / or any other suitable proteins or combinations thereof. In one embodiment, the protein (e.g., in the protein source) includes edema (e.g., about 75%-80%), vicilin (e.g., about 20%-25%), and other proteins (e.g., about 0%-5%). In another embodiment, the protein (e.g., in the protein source) includes globulin (about 65%-75%), albumin (about 25%-37%), and sulfur-rich protein. However, the protein isolate unit may include any other suitable protein composition. The protein isolate unit may include casein, non-casein, mammalian protein, non-mammalian protein, animal protein, non-animal protein, and / or any other protein or combination thereof. In one particular example, the protein isolate unit may contain less than a threshold amount of allergen protein (e.g., soy protein, wheat protein, etc.), casein, mammalian and / or animal protein, wherein the threshold amount may be between 0.1%-10% or any range or value therebetween (e.g., 10%, 5%, 3%, 2%, 1%, 0.1%, etc.), but may alternatively be greater than 10% or less than 0.1% (e.g., 0%).

[0073] The protein isolate unit can be or comprise the protein monomer that is arranged into oligomeric complex and / or has any other quaternary structure.For example, the protein isolate unit can comprise hexamer (for example, stacked trimer).The protein isolate unit preferably has hydrophilic and hydrophobic regions, but can have most or all of hydrophilic or hydrophobic regions (for example, more than one hydrophilic region with different hydrophilicity degrees, have similar hydrophilic / hydrophobic regions etc.) selectively.The diameter of the protein isolate unit can be between 5nm-500nm or any scope or value therebetween (for example, 10nm-50nm, 50nm-200nm, 100nm-200nm, greater than 50nm, less than 200nm etc.), but can be less than 5nm or greater than 500nm selectively. The thickness of the protein isolate unit can be between 5nm-500nm or any range or value therebetween (e.g., 10nm-50nm, 50nm-200nm, 100nm-200nm, greater than 50nm, less than 200nm, etc.), but can be selectively less than 5nm or greater than 500nm. The shape of the protein isolate can be spherical, fractal, fibrous and / or any regular and / or irregular shape. The protein isolate can optionally have a homogeneous or heterogeneous size distribution and shape. One or more ingredients (e.g., lipid component, aqueous component, salt, mineral substance, etc.) can optionally be combined with the protein isolate unit, be located at (e.g., be captured in) the protein isolate unit (e.g., in the oligomeric complex), be located at the protein isolate unit outside (e.g., around) and / or otherwise associate with the protein isolate unit. The protein isolate unit is preferably extracted and / or otherwise obtained via the S100 method, but can additionally or selectively otherwise obtain. The protein isolate unit can be optionally located in the protein isolate mixture. The protein isolate mixture can comprise a protein isolate unit and one or more other compositions (e.g., aqueous components, lipid components, etc.). In an instantiation, the protein isolate mixture is a protein isolate solution (e.g., comprising a protein isolate unit, aqueous or non-aqueous liquid and / or any other composition).

[0074] The method can be used with one or more structured protein isolates. A structured protein isolate (SPI) can include more than one protein isolate unit arranged in a structure (e.g., aggregates, clusters, agglomerates, etc.). The SPI structure can be a sphere (e.g., a shell of a protein isolate unit), an amorphous structure, and / or any other structure; Figure 5A , Figure 5B , Figure 5C and Figure 5DExamples are shown in . The SPI structure can optionally be a micelle (e.g., colloquially referred to as a micelle), where the micelle can be a true micelle (e.g., the more hydrophilic regions of the units making up the protein isolate are arranged toward the edges of the micelle, and the more hydrophobic regions are arranged toward the center of the micelle, or vice versa, such as in a reverse micelle) or a pseudo-micelle (e.g., a "micelle" similar to a casein "micelle"); Figure 5B , Figure 5C and Figure 5D Examples are shown in . The micellar SPI may optionally contain one or more layers of protein isolate units (e.g., surrounding a lipid component, surrounding an aqueous component, etc.). The number of protein isolate units within the SPI may be between 2-50 or any range or value therebetween (e.g., 2-10, at least 2, at least 3, at least 5, at least 10, etc.), but may optionally be greater than 50. The diameter of the SPI may be between 50nm-5000nm or any range or value therebetween (e.g., 100nm-500nm, 100nm-200nm, 150nm-400nm, 180nm-300nm, etc.), but may optionally be less than 50nm or greater than 5000nm.

[0075] Interactions (e.g., bonds) may optionally be present between protein isolate units within the SPI. One or more ingredients (e.g., lipid components, phospholipids, aqueous components, salts, minerals, etc.) may optionally interact (e.g., bonds, capture, attract, repel, surround, etc.) with the SPI, be located within the SPI (e.g., within an oligomeric complex), be located outside the SPI, be entangled between the constituent protein isolate units of the SPI, interact (e.g., bonds, capture, attract, repel, surround, etc.) with the constituent protein isolate units of the SPI, and / or associate with the SPI in other ways. Interactions may be covalent bonds, ionic bonds, hydrogen bonds, van der Waals bonds, London dispersion forces, and / or other bonds or interactions. In a specific example, the lipid component may be: located within the SPI (e.g., encapsulated within the SPI structure), surround the SPI, interact with the SPI, and / or associate with the SPI in other ways. The SPI is preferably formed via the S300 and / or S400 methods, but may be formed additionally or alternatively in other ways. In another specific example, the SPI may interact with the phospholipids. For example, the phospholipids can facilitate encapsulation of lipid components within 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 components (e.g., the phospholipids form a layer between the protein isolate units and the lipid components).

[0076] The SPI preferably has both hydrophilic and hydrophobic regions, but may alternatively have regions that are mostly or entirely hydrophilic or hydrophobic (e.g., more than one hydrophilic region with different degrees of hydrophilicity, regions with similar hydrophilicity / hydrophobicity, etc.). The SPI may have a differential distribution of hydrophilic and / or hydrophobic regions relative to the protein isolate unit (e.g., relative to an unaggregated protein isolate unit, relative to a composed protein isolate unit, etc.). For example, the SPI may have increased and / or decreased hydrophobicity and / or hydrophilicity of the region. In a specific example, the SPI may have increased external surface hydrophobicity relative to the protein isolate unit (e.g., the protein isolate unit before forming the SPI). In a first example, the proportion of the hydrophobic external surface region of the SPI may be greater than the proportion of the external surface region of the hydrophobic protein isolate unit. The increase in the proportion of the hydrophobic external surface region of the SPI relative to the protein isolate unit may be between 1%-50% or any range or value therebetween (e.g., 2%, 5%, 10%, 25%, etc.), but may alternatively be less than 1% or greater than 50%. In a second example, the polarity of all or part of the outer surface area of ​​the SPI can be less than the polarity of all or part of the outer surface area of ​​the protein isolate unit. The hydrophilic and / or hydrophobic regions of the SPI can optionally cause an increase in the interaction between the SPI and the lipid component, phospholipids, one or more other SPIs and / or any other components relative to the differential distribution of the protein isolate unit (e.g., an increase in the number of interactions, an increase in the stability of interactions, an increase in bond affinity, etc.). In an illustrative example, an increase in the hydrophobicity of all or part of the outer surface of the SPI can increase the interaction between the SPI and the lipid component (e.g., relative to the interaction between the SPI and water). The hydrophilic and / or hydrophobic regions of the SPI can optionally cause a decrease in the interaction between the SPI and the aqueous component, one or more other SPIs, other proteins and / or any other components relative to the differential distribution of the protein isolate unit (e.g., a decrease in the number of interactions, a decrease in the stability of interactions, a decrease in bond affinity, etc.). In an illustrative example, an increase in the hydrophobicity of all or part of the outer surface of the SPI can increase the interaction between the SPI and the lipid component relative to the interaction between the SPI and water.

[0077] The differential distribution of hydrophilic and / or hydrophobic regions of SPI relative to protein isolate units can be related to (e.g., caused by) the conformational changes of the constituent protein isolate units in the SPI (e.g., conformational changes occurring during aggregation), the arrangement of the constituent protein isolate units in the SPI, the interactions between the components and the SPI, and / or any other differences between the unaggregated protein isolate units and the SPI. In the first specific example, the conformational changes of the constituent protein isolate units in the SPI can increase the hydrophobicity and / or hydrophilicity of the region. In a specific example, the conformational changes of the constituent protein isolate units in the SPI can increase the hydrophobicity of one or more regions on the outer surface of the SPI. In an example, the conformational changes of the constituent protein isolate units can be induced by: pH changes, temperature changes, salt concentration changes, protein concentration changes, interactions between adjacent constituent protein isolate units, interactions between constituent protein isolate units and other compounds (e.g., water, salt, polar and / or non-polar solvents, other ingredients, etc.), and / or induced in other ways. In a specific example, the interaction (e.g., non-covalent bond, covalent bond, etc.) between the constituent protein isolate unit and the second component (e.g., another protein isolate unit) can result in a conformational change in the protein isolate unit; the tendency of this interaction can increase and / or decrease with changes in the environment (e.g., adjusting the salt concentration). The conformational change preferably does not include denaturation (e.g., when the protein isolate unit dissociates from the SPI, the conformational change of the protein isolate unit is reversible), but can optionally include partial or complete denaturation. In a second specific example, one or more constituent protein isolate units can be arranged so that the hydrophilic region of the constituent protein isolate unit is positioned to face the inside of the SPI, and the hydrophobic region of the constituent protein isolate unit is positioned to face the outside of the SPI.

[0078] The structured protein isolate may optionally be aggregated into one or more aggregates (SPI aggregates, superaggregates). The SPI aggregates may comprise one or more SPI spheres (e.g., droplets, micelles, etc.), fibril aggregates, amorphous aggregates, and / or any other structure of more than one SPI. The number of SPIs within the SPI aggregate may be between 2-50 or any range or value therebetween (e.g., 2-10, 20-40, 40-50, 30-50, greater than 2, greater than 3, greater than 5, greater than 10, etc.), but may optionally be greater than 50. The diameter of the SPI aggregate may be between 100nm-100μm or any range or value therebetween (e.g., 100nm-1000nm, 500nm-10,000nm, 1,000nm-50,000nm, etc.), but may optionally be less than 100nm or greater than 100μm. Interactions (e.g., bonds) may optionally be present between the SPIs within the SPI aggregate. One or more ingredients (e.g., lipid components, phospholipids, aqueous components, salts, minerals, etc.) can optionally interact with, be located within, be located outside, be entangled between, interact with, and / or otherwise associate with the SPI aggregates. In specific examples, the lipid components can be: located between the SPIs in the aggregates, surround the SPI aggregates, be encapsulated within the SPI aggregates (e.g., Fig.16D and Fig.16E ), interact with SPI aggregates, and / or otherwise associate with SPI. SPI aggregates may optionally be contained in aqueous solution droplets and / or support aqueous solution droplets (e.g., within a lipid component), and / or be contained in lipid component droplets and / or support lipid component droplets (e.g., within an aqueous solution). Additionally or alternatively, SPI aggregates may be distributed in both lipid components and water, be dry (e.g., dry SPI aggregates), and / or be located within any other component. In a specific example, SPI aggregates may optionally interact with phospholipids. For example, phospholipids may promote the encapsulation of lipid components within micellar SPI aggregates 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 lipid components). SPI aggregates may be formed via S300, S400, S500, and / or S600 methods. Figure 7 An example is shown in .

[0079] The method can optionally be used with an SPI mixture (e.g., an SPI solution). The SPI mixture can optionally include a protein component, an aqueous component, a lipid component, and / or other ingredients (e.g., impurities, any ingredient 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. Fig. 6A , Figure 6B , Figure 6C , Fig.6D and Fig. 6E An example is shown in . In one specific example, protein isolate units (e.g., aggregated and / or non-aggregated protein isolate units) greater than a threshold ratio in the protein component of the SPI mixture are not denatured (e.g., when the SPI mixture is formed, before the SPI mixture is processed, after the SPI mixture is processed, etc.), wherein the threshold ratio may be between 50%-99% or any range or value therebetween (e.g., 60%, 70%, 80%, 90%, 95%, etc.), but may be optionally less than 50% or greater than 99%. In another specific example, protein isolate units greater than a threshold ratio in the protein component of the SPI mixture are arranged into SPI, wherein the threshold ratio may be between 5%-90% or any range or value therebetween (e.g., 10%, 15%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, etc.), but may be optionally less than 5% or greater than 90%. In a first example, the SPI structure comprises more hydrophobic regions within the interior of the SPI (eg, interfacing with lipid components and / or phospholipids) relative to more hydrophilic regions on the exterior of the SPI (eg, interfacing with aqueous components). Fig. 6A An example is shown in . In a second example, the SPI aggregates comprise more hydrophobic regions within the interior of the aggregate relative to more hydrophilic regions on the exterior of the aggregate (eg, interacting with aqueous components). Fig.6D An example is shown in . However, the proteins in the protein component can be arranged in other ways.

[0080] Obtaining protein isolate from protein source unit S100 plays the role of extracting protein from protein source (e.g., protein source component) and / or otherwise obtaining high protein concentration solution. In a variation, S100 may include: pulverizing protein source S120, diluting protein source to form protein source solution S140, optionally adjusting pH level of protein source solution S160, optionally adjusting salt content of protein source solution S165, and optionally forming protein isolate solution S180. However, the following methods may be used to obtain protein isolate unit from protein source: precipitation (e.g., salting in, salting out, induction isoelectric precipitation, etc.), centrifugation, size exclusion and / or any other protein extraction and / or purification method.

[0081] All or part of S100 (e.g., one or more of S120, S140, S160, S165, or S180) may be performed at one or more target temperatures. The target temperature may be between 15°C-85°C (e.g., 15°C-30°C, 20°C-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 may be kept constant during S100, vary over time (e.g., according to a predetermined cycle, etc.), and / or vary in other ways.

[0082] The protein isolate unit is preferably obtained from a protein source so that the protein isolate unit obtained less than a threshold value percentage is denatured, but can be otherwise carried out. The threshold value percentage (e.g., maximum percentage) of the denatured protein isolate unit obtained can be between 0.01%-50% or any scope or value therebetween (e.g., 0.05%, 1%, 2%, 5%, 10%, 15%, 20%, 25% etc.), but can be selectively less than 0.01% or greater than 50%. The threshold percentage of protein isolate units that can be obtained from a protein source (e.g., the protein yield in the protein isolate solution) can be greater than 40%, 50%, 60%, 70%, 80%, 90%, between 50-60%, between 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 proportion (e.g., by weight, by volume, etc.) of the original protein source; alternatively, S100 can have any other suitable yield.

[0083] S100 may optionally include pulverizing a protein source S120. S120 may be performed before S140, simultaneously with S140, after S140 (e.g., blending a protein source solution), after protein source treatment (e.g., lipid removal), and / or at any other time. Additionally or alternatively, a protein source may be obtained in a pulverized state (e.g., a pretreated protein source). Examples of pulverization methods include: pulverization, blending, crushing, tumbling, crushing, atomization, shaving, grinding, milling, frozen grinding, chopping, homogenization (e.g., using the S500 method), air classification, and / or any other method. In a specific example, S120 may include producing a protein source powder, a ground protein source, a protein source powder, and / or any other pulverized protein source. In an illustrative example, an air classifier system may be used to grind a protein source (e.g., a defatted protein source) into powder, and then separate the powder to extract a protein source powder. However, the protein source may be pulverized in other ways.

[0084] S100 may optionally include diluting a protein source to form a protein source solution S140. S140 may be performed after S120 and / or at any other time. The diluent may include an aqueous solution (e.g., water, deionized water, a mixture of water and other ingredients, such as any ingredient in S500, etc.), a mixture of an aqueous solution and a lipid component (e.g., an emulsion), a polar solvent, any organic and / or inorganic solvent, and / or any other diluent. In a specific example, the diluent is a saline solution. The saline solution preferably includes NaCl, but any other salt (e.g., calcium salt, any salt listed in S500, etc.) or a combination of salts may be optionally used. The concentration of the salt (e.g., NaCl, CaCl2, etc.) may be between 0.1M-2M or any range or value therebetween (e.g., 0.7M, 0.8M, 0.9M, etc.), but may be optionally less than 0.1M or greater than 2M. The protein source may be optionally diluted to reach a target protein concentration in the protein source solution. The target protein concentration (by weight) may be between 1%-50% or any range or value therebetween (e.g., 5%-40%, 10%-15%, 15%-25%, etc.), but may alternatively be less than 1% or greater than 50%. S140 may optionally include mixing, blending, homogenization (e.g., using S500 method), and / or any other combined method. However, the protein source may be diluted in other ways.

[0085] S100 may optionally include adjusting the pH level of the protein source solution S160, which acts to increase the solubility of the protein in the protein source solution (e.g., by increasing the pH to above the isoelectric point). S160 may be performed after S140 and / or at any other time. S160 may include adding one or more acids and / or bases to bring the pH of the protein source solution (and / or the components therein) to a target pH. Examples of acids and bases include: HCl, NaOH, citric acid, lactic acid, gluconic acid, and / or any food-safe (e.g., in relevant amounts) acid and / or base. The target pH is preferably alkaline (e.g., greater than 7, greater than 8, greater than 9, etc.), but may alternatively be acidic and / or neutral. For example, the target pH may be between 4-11.5 or any range or value therebetween (e.g., 7-10, 8-10, etc.), but may alternatively be less than 4 or greater than 11.5. However, the pH level of the protein source solution may be adjusted in other ways.

[0086] S100 may optionally include adjusting the salt content of the protein source solution S165, which serves to increase the solubility of the protein isolate unit in the protein source solution, increase the interaction between the protein and the phospholipid, improve the characteristics (e.g., stretching behavior, melting behavior, etc.) and / or nutritional profile (e.g., calcium concentration) of the product produced using the protein source solution, and / or perform other functions. S165 may be performed after S140, simultaneously with S140, and / or at any other time. S165 may include increasing or decreasing the salt concentration in the protein source solution and / or the components therein (e.g., protein source) to achieve a target salt concentration. S165 may be performed using the method described in S500. The target salt concentration may be between 0.05M-5M or any range or value therebetween (e.g., 0.1M-1M, 0.5M-2M, 0.8M-0.9M, less than 4M, less than 2M, less than 1M, etc.), but may be selectively less than 0.05M or greater than 5M. The target salt concentration can result in a conductivity between 0.5 millisiemens and 10,000 millisiemens or any range or value therebetween (e.g., 1 millisiemens to 10 millisiemens, 2 millisiemens to 8 millisiemens, 10 millisiemens to 100 millisiemens, 100 millisiemens to 10,000 millisiemens, etc.), but can optionally 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 (e.g., based on the solubility of the protein type), the target characteristics, and / or in other ways. However, the salt content of the protein source solution can be adjusted in other ways.

[0087] S100 may optionally include forming a protein isolate solution S180, which plays a role in forming (e.g., extracting) a protein isolate unit from a protein source solution. The protein isolate solution may include a protein isolate unit, a protein isolate unit precursor, and / or any other suitable form of protein isolate. S180 may be performed after S140, after S160, and / or at any other time. S180 may include separating a protein source solution into insoluble matter and a protein isolate solution (containing a protein isolate unit). Separating a protein source solution may include decantation, filtration, drying, centrifugation, allowing sedimentation to occur, and / or any other separation method. For example, S180 may include a centrifugal protein source solution, wherein the supernatant is a protein isolate solution comprising a dissolved protein isolate unit. Centrifugation may include or use: a decanter, a separator centrifuge (e.g., a disc stack centrifuge), a tubular centrifuge, a membrane separator, and / or any other centrifuge and / or its components. Centrifugation may be continuous flow centrifugation, intermittent centrifugation, and / or any other type of centrifugation. The protein source solution may be centrifuged at an RCF of between 500 g-100,000 g or any range or value therebetween (e.g., 1,000 g-30,000 g; 4,000 g-10,000 g; 5,000 g; etc.), but may alternatively be centrifuged at an RCF of less than 500 g or greater than 100,000 g. The protein source solution may be centrifuged at an RPM of between 100-10,000 or any range or value therebetween (e.g., 2,000-10,000; 4,000-6,000; 5000-5,500; less than 10,000; etc.), but may alternatively be centrifuged at an RPM of less than 100 or greater than 10,000. The protein concentration in the protein isolate solution can be between 1%-50% or any range or value therebetween (e.g., 2%-10%, 2.7%, 7.5%, 5%-40%, 6.5%, 10%-15%, 15%-25%, etc.), but can be selectively less than 1% or greater than 50%. However, the protein isolate solution can be formed in other ways.

[0088] S100 may additionally or alternatively 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 of the treatment methods in S500 (e.g., adjusting pH, adjusting salt content, adjusting temperature, high pressure assisted extraction, enzyme assisted extraction, ultrasound assisted extraction, other extraction assisted methods, etc.).

[0089] However, the protein isolate unit may be obtained in other ways.

[0090] The method may 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), wherein the protein isolates may (separately) be derived from different protein sources. This may serve to form an SPI with a mixed protein composition. In a variation, this may increase the range of possible nutritional profiles and / or other features in the product formed by the SPI. Protein isolates may be combined during S100, after S100 (e.g., wherein two or more protein isolate solutions formed using the S100 method are combined), during S300 (e.g., simultaneously with dilution), after S300 (e.g., combining diluted protein isolate solutions) and / or at any other time. In all or part of the method, protein isolates and / or protein isolate solutions may refer to a mixture of protein isolates and / or a mixture of protein isolate solutions, respectively. However, protein isolates may be combined in other ways.

[0091] Alternatively, the protein isolate can be derived from a single protein source (e.g., industrial hemp, sesame, any other plant source, etc.). For example, all or part of the method can use protein isolate units derived from (e.g., obtained from) a single protein source.

[0092] The method may optionally include modified proteins (e.g., modified: protein isolate units, SPI and / or any other proteins), which serve to improve one or more characteristics of the protein and / or its product. The protein may be modified before, during and / or after: S100, S200, S300, S400, S500, S600 and / or any other suitable time. Protein modification may include transglutaminase modification, proteolytic modification, other enzymatic modification, glycosylation, glycation (e.g., via food safe acid and / or any other acid catalysis, at a temperature equal to or below the denaturation point of the protein, etc.), phosphorylation (e.g., using sodium trimetaphosphate), acylation, hydrolysis, cross-linking (e.g., using proteases, laccases, etc.), other methods in S500 (e.g., heating, shearing, micronization, etc.), and / or any other protein treatment.

[0093] The method may optionally include combining the protein isolate unit with a lipid component S200, which functions to mix (e.g., emulsify) the lipids in the protein isolate solution so that SPI can be formed in the presence of lipids (e.g., via S300 and / or S400). S200 may be performed after S100, before S300, before S400, and / or at any other time.

[0094] S200 may include forming a mixture by combining a protein isolate unit (e.g., a protein isolate solution) and a lipid component; Figure 2 In the mixture, the percentage of lipid component (by weight) can be between 0.5%-50% or any scope or value therebetween (for example, 1%-20%, 5%-10%, 1.67%, 5%, 15%, greater than 5%, etc.), but can be selectively less than 0.5% or greater than 50%. Additionally or selectively, the ratio of lipid component to protein isolate solution can be 1:10-10:1 (for example, by weight, by volume, etc.), any scope or ratio therebetween (for example, 1:1, 1:2, 2:3, 4:5, etc.), lower than 1:10, higher than 10:1 and / or any other suitable ratio. Protein isolate unit (for example, protein isolate solution) and lipid component combination can include emulsification, mixing, blending, homogenization (for example, using S500 method) and / or any other combination method. The mixture (eg, a protein isolate mixture) can be an emulsion (eg, a stable emulsion, an unstable emulsion, etc.), a suspension, a colloid, and / or any other mixture.

[0095] S200 may optionally include combining a protein isolate unit with a phospholipid. Fig.19 In the embodiment of the present invention, phospholipid can be combined with lipid component to form lipid-phospholipid mixture, wherein then protein isolate unit (for example, protein isolate solution) is combined with lipid-phospholipid mixture to form protein isolate mixture. However, phospholipid can be mixed into lipid component during or after lipid component and aqueous component or protein isolate mixture combination, mixed into protein isolate mixture before being combined with lipid component, mixed into dilute protein mixture (for example, wherein lipid component can be mixed into dilute protein mixture before, during and / or after phospholipid mixing), and / or mixed into solution at any other time. However, protein isolate unit, phospholipid and lipid component can be combined in any order to form protein isolate mixture. In lipid-phospholipid mixture, the percentage of phospholipid (by weight or volume) can be between 0%-40% or any range or value therebetween (for example, 0%-5%, 1%, 5%-15% etc.), but can be selectively greater than 40%. The percentage of phospholipids in the protein isolate mixture (by weight or volume) may be between 0%-5% or any range or value therebetween (e.g., 0.05%-0.15%, 0.2%-0.6%, etc.), but may alternatively be greater than 5%.

[0096] However, the protein isolate units and lipid components may be combined in other ways.

[0097] The method may optionally include diluting the protein isolate unit S300, which plays a role in promoting and / or inducing the formation of SPI. For example, a diluent (e.g., a diluent, a coagulant, a precipitant, etc.) may be added to a protein isolate mixture (e.g., a protein isolate solution or other protein isolate mixtures) so that the protein isolate unit is insoluble in the diluted protein isolate mixture. S300 may be performed after S100, after S200, and / or at any other time. S300 may form a diluted protein isolate mixture (e.g., a diluted protein isolate solution) and / or other products. The diluted protein isolate unit may be in the following: a protein isolate mixture (e.g., a protein isolate solution; a mixture comprising a protein isolate unit and a lipid component; a mixture comprising a protein isolate unit and / or any other component, etc.), a protein isolate mixture after protein modification, and / or any other suitable mixture or component comprising a protein isolate unit. In a first specific example, the diluted protein isolate mixture may be a protein isolate solution (e.g., from S180). In a second embodiment, the diluted protein isolate mixture can be a protein isolate unit-lipid component mixture (eg, from S200).

[0098] S300 can include diluting protein isolate unit (for example, protein isolate mixture) to realize target protein concentration.The target protein concentration (by weight) of the protein isolate mixture of dilution can be between 0.5%-90% or any scope or value therebetween (for example, 1%-5%, 1.6%, 1.9%, 5%-40%, 10%-15%, 15%-25%, 25%-50% etc.), but can be selectively less than 0.5% or greater than 90%.Additionally or selectively, the ratio of protein isolate mixture (for example, with or without lipid) and diluent (for example, diluent mixture) can be 1:10-10:1 (for example, by weight, by volume etc.), any scope therebetween or ratio (for example, 1:1, 1:2, 1:3, 2:3, 4:5 etc.), lower than 1:10, higher than 10:1 and / or any other suitable ratio. Additionally or selectively, the ratio between the salt concentration in the protein isolate mixture and the salt concentration in the protein isolate mixture of dilution can be greater than the dilution threshold. The dilution threshold can be between 1-10 or any scope or value therebetween (e.g., 2,3,4,5 etc.), but can be selectively less than 1 or greater than 10.

[0099] The diluent may include water (e.g., deionized water, substantially pure water, etc.); an aqueous solution (e.g., water; tap water; a mixture of water and other ingredients, such as salts, soluble and / or insoluble proteins, emulsifiers, phospholipids, and / or any ingredient in S500, etc.); a non-aqueous solution; a mixture of an aqueous solution, a lipid component, and optionally a phospholipid (e.g., an emulsion); an organic polar solvent (e.g., ethanol, methanol, propanol, acetone, any other alcohol, any other antisolvent); a non-polar solvent (e.g., a cosolvent); any organic and / or inorganic solvent; a coagulant; a precipitant; and / or any other liquid. The diluent may optionally be filtered liquid from a previous iteration of all or part of the method.

[0100] For example, the diluent can be a diluent mixture (e.g., an emulsion) comprising a lipid component, an aqueous solution and optional other ingredients (e.g., phospholipids), wherein the percentage (by weight) of the lipid component in the diluent can be between 0.5%-50% or any range or value therebetween (e.g., 1%-20%, 10%-20%, 5%, 1.67%, 15%, 20%, etc.), but can be selectively less than 0.5% or greater than 50%. Additionally or selectively, the ratio of the lipid component to the diluent can be 1:10-10:1 (e.g., by weight, by volume, etc.), any range or ratio 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. The percentage of phospholipids in the diluent (by weight or volume) can be between 0%-10% or any range or value therebetween (e.g., 0.05%-0.2%), but can be optionally greater than 10%. The percentage of phospholipids in the diluted protein isolate mixture (by weight or volume) can be between 0%-10% or any range or value therebetween (e.g., 0.05%-0.15%), but can be optionally greater than 10%.

[0101] The temperature of the diluent may be between 0°C-35°C or any range or value therebetween (e.g., 5°C-20°C, 20°C-25°C, etc.), but may alternatively be lower than 0°C or higher than 35°C. The temperature of the diluent is preferably room temperature, but may alternatively be lower or higher than room temperature.

[0102] However, the protein isolate unit may be diluted in other ways, and / or the SPI may be formed in other ways.

[0103] Collecting structured protein isolate S400 serves to arrange the protein isolate units into structures (e.g., agglomerates, clusters, aggregates of any form, etc.). S400 may optionally serve to arrange the SPI into one or more SPI aggregates. S400 may be performed after S300, during S300, and / or in conjunction with S300 (e.g., wherein diluting the protein isolate units partially or completely arranges the protein isolate units into SPIs, wherein diluting the protein isolate units induces precipitation, etc.), without S300, and / or at any other time.

[0104] S400 can include separating a protein isolate mixture (e.g., a diluted protein isolate mixture from S300) to collect SPI from the protein isolate mixture (e.g., a SPI mixture). Separating the protein isolate mixture can use methods including decantation, filtration, drying, centrifugation, allowing sedimentation to occur, isoelectric precipitation, antisolvent precipitation (e.g., using an antisolvent diluent in S300 and separating the diluted protein isolate mixture), precipitation via any solvent exchange process, adjusting ionic strength (e.g., adding salt to the protein isolate mixture and / or removing salt therefrom), 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., adjusting temperature, electrical treatment, pulses, light treatment, radiation, free radicals, sound treatment, etc.), dialysis, any fractionation method, combinations thereof, and / or any other separation method. 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., antisolvents), non-polar solvents, any diluents, and / or any other ingredients or chemicals. In a specific example, a product containing an antisolvent precipitate (ASP) (e.g., a protein component collected using an antisolvent precipitate) can produce a product with reduced water / fat binding relative to a product containing an SPI collected using an aqueous diluent; this reduced water / fat binding can result in the protein being dispersed in excess liquid (after gelation of the product, after heating of the product, etc.).

[0105] In a first variation, S400 may include allowing sedimentation to occur in a protein isolate mixture (e.g., a diluted protein isolate mixture) and extracting an insoluble fraction (e.g., removing all or part of a supernatant), wherein all or part of the insoluble fraction (e.g., a sediment and / or precipitate) may contain SPI. For example, SPI may be precipitated from a diluted protein isolate mixture comprising a protein isolate unit, an aqueous component, and optionally a lipid component. In another example, SPI may be extracted (e.g., precipitated, precipitated, etc.) from a supernatant. In a specific example, when the percentage (by weight) of lipid components in a diluted protein isolate mixture (e.g., produced using a protein isolate solution having a protein concentration of 6.5% and / or any other concentration) is between 0%-15% or any range or value therebetween (e.g., 5%) but may be optionally greater than 15%, SPI precipitates. The lipid component may or may not include phospholipids. One or more mechanical treatment methods may optionally be used to promote and / or accelerate sedimentation. In specific examples, agitation (e.g., via a stirred double jacket tank), centrifugation, and / or any other mechanical treatment method can be used to promote sedimentation. In all or part of this method, "SPI" can refer to the collected insoluble fraction (e.g., sediment and / or precipitate).

[0106] In a second variation, S400 may include using a mechanical treatment method, including shearing, pressurization, rotation (e.g., centrifugation, rotation, vibration, etc.), other mechanical treatment methods in S500, and / or any other mechanical method for separating structured protein isolate from a protein isolate mixture. For example, S400 may include centrifuging a protein isolate mixture (e.g., a diluted protein isolate mixture, an undiluted protein isolate mixture, etc.) and extracting an insoluble fraction (e.g., removing all or part of the supernatant), wherein all or part of the insoluble fraction (e.g., a precipitate) may contain SPI. Any type of centrifuge may be used (e.g., the type listed in S180). The protein isolate mixture may be centrifuged at an RCF of 500 g-100,000 g or any range or value therebetween (e.g., 1,000 g-30,000 g; 4,000 g-6,000 g; 5,000 g; etc.), but may be optionally centrifuged at an RCF of less than 500 g or greater than 100,000 g. In one embodiment, the RCF may be lower than the centrifugation threshold (e.g., to reduce denaturation of the protein isolate unit), wherein the centrifugation threshold may be between 1,000 g-15,000 g or any range or value therebetween (e.g., 5,000 g; 6,000 g; 10,000 g; 50,000 g; etc.), but may be optionally less than 1,000 g or greater than 15,000 g. In another embodiment, the RCF may be higher than the high-speed centrifugation threshold, wherein the high-speed centrifugation threshold may be between 10,000 g-20,000 g or any range or value therebetween (e.g., 14,000 g, 15,000 g, 16,000 g, 16,900 g, etc.), but may be optionally less than 10,000 g or greater than 20,000 g. The protein isolate mixture can be centrifuged at an RPM between 100-10,000 or any range or value therebetween (e.g., 2,000-10,000; 4,000-6,000; 5000-5,500; etc.), but can be optionally centrifuged at an RPM less than 100 or greater than 10,000. In a specific example, the RPM can be below a centrifugation threshold, wherein the centrifugation threshold can be between 1,000-15,000 or any range or value therebetween (e.g., 6,000, 10,000, etc.), but can be optionally less than 1,000 or greater than 15,000. In another embodiment, the RPM can be above a high speed centrifugation threshold (e.g., which can help separate smaller molecular weight or soluble proteins), where the high speed centrifugation threshold can be between 5,000-100,000 or any range or value therebetween (e.g., 10,000, 15,000, 20,000, 25,000, 30,000, etc.), but can alternatively be less than 5,000 or greater than 100,000.

[0107] In a third variation, S400 includes inducing isoelectric precipitation in a protein isolate mixture (e.g., reducing the pH of the protein isolate mixture to near or to the isoelectric point of the protein) to collect isoelectric protein isolates. For example, the pH of the protein isolate mixture can be adjusted to a pH between 3-6 or any range or value therebetween (e.g., 4-5.5), but can be optionally less than 3 or greater than 6. In a first example, the SPI can include isoelectric protein isolates. In a second example, an isoelectric protein isolate (IPI) can be used as an SPI in all or part of the method.

[0108] The collected SPI can be a mixture of SPI. For example, the SPI mixture can be or include the following: an insoluble fraction containing SPI (e.g., sediment, precipitate, solid fraction, etc.); a mixture containing an insoluble fraction; a solution containing SPI, an aqueous component, and / or impurities; a mixture containing SPI, an aqueous component, a lipid component (e.g., from S200, a lipid component mixed into a diluent from S300, etc.) and / or impurities; and / or any other mixture containing SPI. The total protein concentration (by weight) in the SPI mixture (e.g., in the insoluble fraction) can be between 5%-100% or any range or value therebetween (e.g., 10%-20%, 30%-50%, 50%-70%, 44%, 40%, etc.), but can be optionally less than 5%. The remainder by weight can include lipid components, diluents, impurities (e.g., carbohydrates, salts, minerals, etc.) and / or any other suitable components. The carbohydrate concentration (by weight) in the SPI mixture can be between 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.), but can optionally be less than 0.005% or greater than 2%. The collected SPI can optionally contain SPI aggregates. The threshold percentage (e.g., cumulative protein yield) of protein from the original protein source collected in the SPI mixture can be between 40%-90%, between 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 percentage of protein from the protein isolate mixture collected in the SPI mixture can be between 50%-99%, between 80%-90%, between 90%-95% (e.g., 92%), above 70%, above 80%, above 90%, below 50%, and / or any other suitable yield (e.g., by weight, by volume, etc.). Alternatively, S400 can have any other suitable yield.

[0109] The insoluble fraction (e.g., sediment, precipitate, etc.) may include a solid component (e.g., which may be dried to form a dry material) and / or a liquid component. For example, the solid component may 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.), but may alternatively be less than 5% or greater than 80% of the SPI mixture. All or part of the remaining liquid component of the SPI mixture may include an aqueous component (e.g., water), a lipid component, and / or any other ingredient. The protein concentration (by weight) in the solid component (e.g., the purity of the solid component) can be between 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.), but can be optionally less than 70% or greater than 99%. Other components (e.g., impurities) of the solid component can include salts, minerals, carbohydrates, lipids and / or any other chemical substances or ingredients. The concentration (by weight) of other components in the solid component can be between 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.), but can be optionally less than 0.1% or greater than 10%. The carbohydrate concentration (by weight) in the solid component can be between 0.05%-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.), but can alternatively be less than 0.05% or greater than 5%.

[0110] However, the structured protein isolate may be collected in other ways.

[0111] The method may optionally include processing structured protein isolate S500, which serves to prepare the SPI for manufacturing the product. S500 may be performed after S400, during and / or after S600, and / or at any other time. Additionally or alternatively, the processing steps in S500 may be used at any suitable time (e.g., before, during and / or after S100, S200, S300, S400, and / or S600) to process protein sources, protein isolate units, ingredients, and / or products (e.g., containing SPI).

[0112] Processing the SPI (e.g., an SPI mixture) can include: adding ingredients (e.g., diluting, adding lipid components, etc.), removing ingredients (e.g., defatting, removing salts, removing alcohol, filtering, pressing, draining, etc.), adjusting pH levels (e.g., increasing or decreasing acidity; as described in S160), adjusting salt content, mechanical treatment (e.g., homogenization, centrifugation, chopping, pressurizing, crushing, shearing, stirring, mixing, etc.), separating the SPI mixture (e.g., an SPI solution), adjusting temperature, aging (e.g., at a target temperature; where aging can promote maturation, fermentation, affinage, maturation, etc.), fermentation, humidification / dehumidification, stirring, standing, adjusting oxygen levels, gelation (e.g., curdling) methods, any curd processing method (e.g., cutting, stretching, pressing, brining, molding, etc.), modified protein, combinations thereof, and / or any other processing method. In specific examples, the gelation process may include: adjusting pH, adjusting salt content, adding enzymes, adding hydrocolloids (e.g., carrageenan, gums, etc.), adding lipid components (e.g., lipid components with melting points above room temperature), adjusting temperature, fermentation, aging, extraction and / or extraction-assisted methods (e.g., high pressure-assisted extraction, enzyme-assisted extraction, ultrasound-assisted extraction, etc.), micronization, and / or any other processing method. In a specific example, molding the SPI mixture may include: transferring the SPI mixture to a mold at an elevated temperature and allowing the SPI mixture to cool (e.g., solidify to form a molded gel). Any processing method may be performed once, more than once, simultaneously, iteratively, asynchronously, sequentially (in any order), and / or at any other time.

[0113] In a first variation, processing the SPI may include adding ingredients to the SPI. Adding ingredients to the SPI may include combining the SPI with one or more ingredients, wherein the combination may include emulsification, mixing, blending, homogenization, and / or any other combination method. Examples of ingredients may include: plant matter, protein (e.g., protein source, protein source solution, protein isolate unit, SPI, etc.), lipid component, aqueous component (e.g., water, sucrose solution, etc.), preservative, acid and / or base, macronutrients (e.g., protein, fat, starch, sugar, etc.), nutrients, micronutrients, carbohydrates (e.g., sugar, starch, fiber, polysaccharides such as maltodextrin, gums, etc.), starch (e.g., natural and / or modified starch; potato, tapioca, corn, sago, starch-based texturizing agents such as Advanta Gel S TMetc.), vitamins, enzymes (e.g., transglutaminase, chymosin, tyrosinase, bromelain, papain, ficin, other cysteine ​​endopeptidases, rennet enzyme and / or chymosin-type enzymes, etc.), emulsifiers (e.g., lecithin), microparticles, hydrocolloids (e.g., thickeners, gelling agents, emulsifiers, stabilizers, etc.); such as starch, gelatin, pectin and gums such as: agar, alginic acid, sodium alginate, guar gum, The invention also provides a method for preparing the present invention. The method comprises the steps of: preparing the present invention ... The ingredients may optionally include no and / or include less than a threshold amount (e.g., 10%, 5%, 3%, 2%, 1.5%, 1.25%, 1%, 0.5%, 0.1%, etc.) of added: animal products, animal-derived ingredients, gums (e.g., polysaccharide thickeners), hydrocolloids, allergens, phospholipids, soy derivatives, starches, combinations thereof, and / or any other suitable ingredients. The ingredients are preferably food safe, but may alternatively not be food safe.

[0114] Examples of microbial cultures that can be used include cheese cultures (e.g., cheese starter cultures), yogurt cultures, wine cultures, beer cultures, and / or any other microbial cultures and / or combinations thereof. For example, the microbial cultures can include cultures for 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 culture 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 thermophilus, Brachybacterium alimentarium, Brachybacterium tyrofermentans, Brevibacterium aurantiacum, Brevibacterium casei, Brevibacterium linens, Candida colliculosa, Candida kefyr, Candida jefer, Candida krusei, Candida mycoderma, Candida utilis, Candida vini, Candida zeylanoides, Carnobacteriumdivergens), Carnobactrium maltaromaticum, Corynebacterium ammoniagenes, Corynebacterium casei, Corynebacterium flavescens, Corynebacterium mooreparkense, Corynebacterium variabile, Cystofilobasidium infirmominiatum, Debaryomyces shansenii, Debaryomyces kloeckeri, Enterococcus faecalis, Fusarium domesticum, Geotrichum candidum, Hafnia alvei, Halomonas, Issatchenkia orientalis, Kazachstania exigua, Kazachstania unispora, Kluyveromyces lactis lactis, Kluyveromyces marxianus, Kocuria rhizophila, Kocuria varians, Lactobacillus acidipiscis, Lactobacillus acidophilus, Lactobacillus brevis, Lactobacillus bulgaricus, Lactobacillus casei, Lactobacillus coryniformis, Lactobacillus curvatus, Lactobacillus delbrueckii (e.g., Lactobacillus delbrueckiibulgaricus), Lactobacillus fermentum, Lactobacillus gasseri, Lactobacillus helveticus, Lactobacillus spp.helveticus), Lactobacillus johnsonii, Lactobacillus kefiranofaciens, Lactobacillus kefiri, Lactobacillus nodensis, Lactobacillus parabrevis, Lactobacillus paracasei, Lactobacillus parakefiri, Lactobacillus paraplantarum, Lactobacillus pentosus, Lactobacillus perolens, Lactobacillus plantarum, Lactobacillus rhamnosus, Lactobacillus salivari ... salivarius), Lactobacillus succeti, Lactococcus lactis (e.g., Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. cremoris, Lactococcus lactis subsp. lactis biovar. Diacetylactis, etc.), Lactococcus raffinolactis, Lecanicillium lecanii, Leuconostoc citreum, Leuconostoc citovorum, Leuconostoc dextranicum, Leuconostoc pseudomesenteroides, Leuconostockimchi, Leuconostoc mesenteroides, mesenteroides, Macrococcus caseolyticus, Microbacterium foliorum, Microbacterium gubbeenense, Micrococcus luteusluteus), 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 fleurettii, Staphylococcus saprophyticus, Staphylococcus sciuricarnaticus, Staphylococcus succinus, Staphylococcus vitulinus, Staphylococcus xylosus, Streptococcus cremoris, Streptococcus lactis, Streptococcus lactis subspecies diacetylactis, Streptococcus thermophilus, Streptococcus gallolyticus, Streptococcus salivarius, Throchosporonbeigelii, Verticillium lecanii, Yarrowialipolytica, Zygotorulaspora florentina, its genus, its family, its phylum, and / or any other suitable microorganism and / or combination thereof. In a specific example, the culture can be: RA21 (e.g., Lactococcus lactis lactis, Lactococcus lactis cremoris and Streptococcus thermophilus), CASU (e.g., including Lactococcus lactis lactis, Lactobacillus helveticus and Streptococcus thermophilus), V022 (e.g., including Bifidobacterium animalis, Lactobacillus acidophilus, Lactobacillus delbrueckii bulgaricus, Lactobacillus plantarum and Streptococcus thermophilus), V061 (e.g., including Bifidobacterium animalis, Lactobacillus acidophilus, Lactobacillus delbrueckii bulgaricus, Streptococcus thermophilus and Lactobacillus paracasei), V011, V053, BT02, LM57, FLAV54 and / or any other microbial culture.

[0115] In a first embodiment, adding ingredients can include diluting the SPI (e.g., using water and / or other ingredients) 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 between 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.), but can be optionally less than 0.5% or greater than 90%. Dilution of the SPI can optionally serve to form a diluted SPI mixture (e.g., a diluted SPI solution), wherein the diluted SPI mixture can be used as an ingredient and processed via other S500 methods and / or used to produce a product via the S600 method.

[0116] In a second embodiment, the addition of ingredients can include combining (e.g., emulsifying) the SPI (e.g., SPI mixture) with a lipid component. The target lipid concentration (by weight) (e.g., in the combined SPI mixture, in the product, in the product intermediate, etc.) can be between 0.5%-90% or any range or value therebetween (e.g., 1%-5%, 1.6%, 1.9%, 5%-40%, 5%-30%, 5%-25%, 10%-15%, 10%-20%, 12%-22%, 20%-50%, at least 10%, etc.), but can be optionally less than 0.5% or greater than 90%. The resulting mixture can be a stable emulsion, an unstable emulsion (e.g., coalesce, cream, flocculation, rupture, etc.), a suspension, a colloid, and / or any other mixture. Optionally, the lipid component and / or the SPI can be heated before and / or during addition. Heating the lipid component may optionally convert the lipid component from a solid to a liquid (e.g., a melted lipid component), which may facilitate homogenization of the mixture. Prior to combining with the SPI, the lipid component is preferably heated to a temperature below a threshold temperature (e.g., 85° C.) and / or allowed to cool to a temperature below a threshold temperature so that the protein in the SPI is not denatured, but may be optionally heated in other ways. The resulting mixture may be used as a final product (e.g., food) and / or as an ingredient for downstream processing (e.g., S600).

[0117] In one embodiment, adding the ingredients comprises: forming an aqueous solution (e.g., with the ingredients), optionally heating the aqueous solution, combining the SPI mixture with the aqueous solution and optionally the lipid component (e.g., melted lipid component), and optionally heating the resulting mixture. The resulting mixture may optionally be molded. Figure 3. Forming an aqueous solution may include hydrating one or more additives in water. The additive may promote gelation, enhance the gel hardness at room temperature (e.g., so that the product can be shredded), adjust the nutritional profile of the product and / or provide other functions. The additive may include a hydrocolloid (e.g., carrageenan, gum, other gelling agents, etc.), sugar (e.g., glucose), fiber, salt and / or any other additive. The concentration of the hydrocolloid in the aqueous solution may be between 0%-15% or any range or value therebetween (e.g., 0%-2%, 0.15%-0.8%, 0.3%-2%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), but may be optionally greater than 15%. In a specific example, the concentration of carrageenan in the aqueous solution can be between 0-10% or any range or value therebetween (e.g., 0%-2%, 0.15%-0.5%, 0.1%-0.4%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), but can optionally be greater than 10%. In a specific example, the concentration of gum in the aqueous solution can be between 0-10% or any range or value therebetween (e.g., 0%-2%, 0.15%-0.5%, 0.1%-0.4%, 0.3%, 0.5%, 0.6%, 1%, 2%, 5%, less than 5%, less than 2%, less than 1%, etc.), but can optionally be greater than 10%. The concentration of sugar in the aqueous solution can be between 0%-15% or any range or value therebetween (e.g., 0%-2%, 0.3%-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.), but can optionally be greater than 15%. The aqueous solution can be heated to a temperature between 20°C-100°C or any range or value therebetween (e.g., heated to boiling), but can optionally be heated or cooled to a temperature below 20°C or above 100°C, or not heated or cooled. The SPI mixture, aqueous solution, and lipid component can be combined in any order (e.g., combining the SPI mixture and aqueous solution, then adding the lipid component; combining the SPI mixture, aqueous solution, and lipid component simultaneously; etc.). The SPI mixture, aqueous solution, and lipid components 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.) for a target time (e.g., 1 min, 5 min, 10 min, 15 min, 30 min, etc.).

[0118] In the first example, the SPI-lipid component mixture includes SPI in water droplets surrounded by lipid components. In the second example, the mixture includes SPI in lipid component droplets surrounded by water. In the third example, the mixture includes SPI distributed in the lipid and aqueous components of the mixture. The diameter of the droplets (e.g., volume weighted average diameter or area weighted average diameter) can be between 500nm-1mm or any range or value therebetween (e.g., 500nm-10,000nm, 10,000nm-0.1mm, 0.1mm-1mm, etc.), but can be optionally less than 500nm or greater than 1mm. Emulsification methods, droplet encapsulation techniques (e.g., microfluidic droplet encapsulation techniques), ultrasonic processing, suspension techniques, other colloid formation techniques and / or any other techniques can be used to generate droplets. SPI inside or outside the droplets can optionally form SPI aggregates. However, the mixture can be constructed in other ways.

[0119] In a specific example, adding a lipid component includes mixing (e.g., emulsifying) an SPI mixture in the lipid component. The lipid component preferably forms a continuous phase of an emulsion, while the SPI mixture is in a dispersed phase (e.g., a water-in-oil emulsion or an oleogel). For example, the ratio between the lipid component and the SPI mixture may be between 10:1-1:1 (e.g., by weight, by volume, etc.) or any range or ratio therebetween (e.g., 2:1, 3:2, 5:4, etc.). An emulsion having a lipid component as a continuous phase may result in an arrangement of proteins in the emulsion (e.g., an arrangement of SPI) that increases the tensile properties and / or melting properties of a product formed by the emulsion. Alternatively, the SPI mixture may be in a continuous phase, while the lipid component is in a dispersed phase (e.g., an oil-in-water emulsion). For example, the ratio between the lipid component and the SPI mixture may be 1:10-1:1 (e.g., by weight, by volume, etc.) or any range or ratio therebetween (e.g., 1:1, 1:2, 2:3, 4:5, etc.). Furthermore, the SPI distributed in the lipid and aqueous components can optionally be mixed / homogenized together to obtain one or the other as a dispersed or continuous medium (eg, oil droplets containing SPI dispersed in water containing SPI, or vice versa).

[0120] In a third embodiment, ingredients are added so that the nutritional profile of the product produced by the SPI substantially matches a target nutritional profile (eg, for a target product).

[0121] However, the ingredients may be added in other ways.

[0122] In a second variation, processing the SPI may include adjusting the salt content of the SPI and / or changing the ionic strength of the SPI, and may include increasing or decreasing the salt concentration in the SPI to achieve a target salt concentration. The target salt concentration may be between 0.05M-5M or any range or value therebetween (e.g., 0.1M-1M, 0.5M-2M, 0.8M-0.9M, less than 4M, less than 2M, less than 1M, etc.), but may be optionally less than 0.05M or greater than 5M. The target salt concentration may result in a conductivity between 0.5-10,000 millisiemens or any range or value therebetween (e.g., 1-10 millisiemens, 2-8 millisiemens, 10-100 millisiemens, 100-10,000 millisiemens, etc.), but may be optionally less than 0.5 millisiemens or greater than 10,000 millisiemens. The target salt concentration percentage (by weight) (e.g., in the SPI mixture, in the product, in the product intermediate, etc.) can be between 0%-10% or any range or value therebetween (e.g., 0.1%-5%, 0.5%-2%, at least 1%, at least 2%, less than 5%, etc.), but can optionally be greater than 10%. In a specific example, the target concentration of calcium citrate can be between 0%-5% or any range or value therebetween (e.g., 0.1%-1%, 0.5%-1%, 0.3%-2.5%, 0.5%-2%, 1%-2%, 1.2%-2%, at least 0.25%, at least 0.5%, at least 1%, at least 2%, etc.), but can optionally be greater than 5%. In a first variation, increasing the concentration of the salt comprises adding the salt to the SPI. Examples of salts include: NaCl, calcium citrate (CaCit), CaCl2, sodium citrate, MgCl2, disodium phosphate, dipotassium phosphate, salts with cations (e.g., divalent cations, such as calcium), and / or any other salt. Increasing the concentration of salt can optionally serve to improve the flavor and / or nutritional profile of the product produced using SPI. In a second variation, reducing the concentration of salt includes flushing the SPI, dialysis, washing (e.g., centrifugation after washing, filtration, etc.), and / or any other method of reducing the concentration of salt. For example, the SPI can be resuspended in deionized water, and sedimentation can be allowed to occur again to form a structured protein isolate solution with a lower salt concentration. Reducing the concentration of salt can optionally serve to improve the texture profile (e.g., stretchability and / or meltability) of the product produced using SPI.

[0123] In a third variation, processing the SPI may include applying shear to the SPI (e.g., homogenizing a SPI mixture, homogenizing the SPI with an added ingredient, etc.). Applying shear may include mixing, blending, vortexing, homogenizing, applying pressure, and / or any other shearing treatment. Applying shear to the SPI may include using a rotor-stator system, any other homogenizing device, and / or any other shearing applying device. The shearing applying device preferably applies a shear force below a threshold value (e.g., so as not to destroy the protein structure in the protein solution), but any shear force may be applied selectively. The rotor-stator system may be used between 500rpm-20,000rpm or any range or value therebetween (e.g., 5000rpm-10,000rpm, 5500rpm, 10,000rpm, etc.), but may be used selectively below 500rpm or above 20,000rpm. The rotor-stator system can be used for a period of time between 10 seconds and 12 hours or any range or value therebetween (e.g., 1 min, 40 min, 1 hour, etc.), but can optionally be used for less than 10 seconds or greater than 12 hours. Alternatively, the rotor-stator system can be used at any other rpm and for any amount of time.

[0124] In a fourth variation, processing the SPI may include separating the SPI (e.g., separating the SPI from the SPI mixture). Separating the SPI may include decantation, filtration (e.g., crude oil filtration methods, microfiltration, ultrafiltration, etc.), drying (e.g., spray drying; exemplified in Fig. 20A and Fig. 20B ), centrifugation, allowing sedimentation to occur, and / or any other separation method. In variations, drying can serve to stabilize and / or preserve the SPI (e.g., for downstream use). In one specific example, processing the SPI mixture (e.g., the insoluble fraction collected in S400) includes: optionally subjecting the SPI mixture to one or more initial processing steps (e.g., diluting the SPI mixture, pasteurizing the SPI mixture, etc.), spray drying the (treated) SPI mixture to form a dried SPI, rehydrating the dried SPI, optionally processing the rehydrated SPI (e.g., combining the rehydrated SPI with a lipid component), and using the (treated) rehydrated SPI to produce a product. The threshold percentage of protein from the original protein source in the separated SPI (e.g., the cumulative protein yield after separating the SPI) can be between 5%-50%, between 10%-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.).

[0125] In a fifth variation, processing the SPI may include adjusting the temperature of the SPI, preferably including heating the SPI, but may additionally or alternatively include cooling the SPI (e.g., heating then cooling, blanching, etc.) and / or otherwise adjusting the temperature. Adjusting the temperature may play a role in gelling, pasteurizing, fermenting, aging, cooking, polymerizing, and / or otherwise treating the SPI and / or a product containing the SPI. A water bath, an oven, a refrigerator, a freezer, a mixer with a heating element, a tubular heat exchanger, a direct steam injection system, a vat system (e.g., a glass jar), an ultra-high temperature system, a plate heat exchanger, a microwave oven, a fryer, and / or any other system may be used to adjust the temperature. Adjusting the temperature preferably includes adjusting the temperature of the SPI to a target temperature for a target time and / or heating and / or cooling the SPI at a target heating temperature, but may additionally or alternatively include exposing the SPI to a target temperature (e.g., heating the SPI at a target heating temperature, cooling the SPI at a target cooling temperature, etc.) and / or adjusting the temperature based on any other parameter. The target temperature is preferably below the denaturation temperature of the protein in the protein component, but may alternatively be at or above the denaturation temperature. The target temperature may be between 0°C-200°C or any range or value therebetween (e.g., 60°C-100°C, 80°C-85°C, 80°C-90°C, 72°C, 75°C, 80°C, 85°C, less than 85°C, less than 90°C, less than 100°C, 25°C-200°C; 50°C-85°C, etc.), but may alternatively be less than 0°C or greater than 200°C. The target time can be between 10 seconds and 48 hours or any range or value therebetween (e.g., 1 min-1 hour, 5 min-30 min, 10 min-15 min, 1 min, 5 min, 10 min, 15 min, 30 min, 60 min, 80 min, less than 15 min, less than 30 min, less than 60 min, etc.), but optionally can be less than 10 seconds or greater than 48 hours (e.g., aging lasts for greater than 48 hours). The heating rate can be between 0.25°C / min-50°C / min or any range or value therebetween (for example, 0.5°C / min-2°C / min, 2°C / min-20°C / min, 20°C / min-50°C / min, 2°C / min-10°C / min, 1°C / min-5°C / min, 5°C / min-10°C / min, 10°C / min-20°C / min, 10°C / min-15°C / min, 15°C / min-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.), but can optionally be less than 0.25°C / min or greater than 50°C / min.Any heating and / or cooling phase may include returning the SPI to a second target temperature (eg, room temperature) after the heating and / or cooling phase. However, the temperature of the SPI may be adjusted in other ways.

[0126] However, SPI may be processed in other ways.

[0127] The method may optionally include producing a product having a structured protein isolate S600, which functions to form a food having a target characteristic (e.g., a target stretching property and / or a meltable characteristic). S600 may be performed after S400, after S500 (e.g., after any processing step in S500), during S500, and / or at any other time.

[0128] The product may optionally be a food and / or be used to make a food. For example, the product may be: a substitute (e.g., an analog, imitation, etc.) for a target food (e.g., the product may be a plant-based analog for an animal food), used to make a target food, a food with a target characteristic, and / or any other food. The product may be a vegan product, a food containing no animal products and / or having less animal products (e.g., relative to a target animal product), a plant-based food (e.g., a plant-based cheese), a microbial-based food, a non-mammalian-based food, and / or any other food. Examples of target foods include: dairy lipids (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, 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., ground meat, steak, chops, bones, deli meat, sausages, etc.), fish products (e.g., fish fillets, etc.), any animal product and / or any other suitable food. In a specific example, the target food includes mozzarella, burrata, feta, brie, ricotta, camembert, chevre, cottage cheese, cheddar, parmigiano, pecorino, gruyere, edam, gouda, jarlsberg, and / or any other cheese. In a specific example, the product comprises a milk analog (e.g., a functional milk analog of cow's milk, sheep's milk, goat's milk, camel's milk, human milk, etc.).

[0129] The product is preferably entirely plant matter, but may additionally or alternatively be primarily plant matter (e.g., more than 50%, 60%, 70%, 80%, 90%, 95%, 98%, 99%, etc.), partially plant matter, and / or have any other suitable plant matter content. The product may optionally exclude and / or include less than a threshold amount of total and / or added animal products (e.g., excluding animal proteins such as casein), gums (e.g., polysaccharide thickeners), allergenic ingredients (e.g., soy, peanuts, wheat, derivatives thereof, etc.), and / or any other suitable ingredient. Added ingredients and / or compounds may include substances that are not present in the plant matrix or other ingredients and / or are foreign to the plant matrix or other ingredients, substances added as separate ingredients, and / or substances that are otherwise defined. The threshold amount may be between 0.1%-10% or any range or value therebetween (e.g., 10%, 5%, 3%, 2%, 1%, 0.1%, etc.), but may alternatively be greater than 10% or less than 0.1%.

[0130] The product preferably has one or more properties that are similar to the target product (e.g., within a predetermined margin of error, such as 1%, 5%, 10%, 20%, 30%, etc.) and / or similar to any other set of target properties. Characteristics (e.g., functional properties) can include: nutritional profile (e.g., macronutrient profile, micronutrient profile, etc.), nutritional quality (e.g., PDCAAS score), texture (e.g., texture profile, hardness, toughness, puncture, stretch, compression response, mouthfeel, viscosity, granularity, looseness, stickiness, chalkiness, powdery, astringency, brittleness, stickiness, stretchability, tear resistance / strength, mouth melting, etc.), solubility, melting curve, smoke curve, gel point, flavor, appearance (e.g., color), aroma, precipitation, stability (e.g., room temperature stability), emulsion stability, ion binding capacity, heat capacity, solid fat content, chemical properties (e.g., pH, affinity, surface charge, isoelectric point, hydrophobicity / hydrophilicity, free thiol group content, chain length, chemical

[0013] The invention also relates to a method for preparing a polymeric substance comprising: a) a polymeric substance having a molecular weight of 500 and / or 500 nm; b) a polymeric substance having a molecular weight of 500 and / or 500 nm; c) a polymeric substance having a molecular weight of 500 and / or 500 nm; and d) a polymeric substance having a molecular weight of 500 and / or 500 nm. The method also relates to a method for preparing a polymeric substance comprising: a polymeric substance having a molecular weight of 500 and / or 500 nm; and b) a polymeric substance having a molecular weight of 500 and / or 500 nm. The method also relates to a polymeric substance having a molecular weight of 500 and / or 500 nm.

[0131] Examples of assays and / or assay tools that can be used include: differential scanning calorimeter (e.g., for determining properties related to melting, gel point, denaturation point, etc.), Schreiber test, oven (e.g., for Schreiber test), water bath, texture analyzer, rheometer, spectrophotometer, centrifuge (e.g., for determining properties related to water binding capacity), moisture analyzer (e.g., for determining properties related to water availability), optical microscope (e.g., for determining properties related to microstructure), atomic force microscope (e.g., for determining properties related to microstructure), confocal microscope (e.g., for determining protein association with lipid / water), laser diffraction particle size analyzer (e.g., for determining properties related to emulsion stability), polyacrylamide gel electrophoresis system, mass spectrometry, gas chromatography, liquid chromatography, thermogravimetric analysis system, thermal shift (e.g., for determining protein denaturation and / or aggregation behavior), ion chromatography, dynamic light scattering system (e.g., for determining properties related to particle size, for determining protein aggregation, etc.), Zetasizer (e.g., for determining properties related to surface charge), protein concentration determination and / or measurement system, particle size analyzer, sensory panel (sensor panels, e.g., for determining properties related to texture, flavor, appearance, aroma, etc.), capillary electrophoresis SDS (e.g., for determining protein concentration), spectroscopy (e.g., fluorescence spectroscopy, circular dichroism, etc.; for determining folding state, folding kinetics, denaturation temperature, etc.), absorption spectroscopy (e.g., for determining protein hydrophobicity), CE-IEF (e.g., for determining protein isoelectric point / charge), total protein quantification, high temperature gelation, microbial cloning, Turbiscan (e.g., for determining properties related to emulsion stability), stereospecific analysis, olfactometer, electrophysiological tests (e.g., of human olfactometer), psychophysical tests (e.g., of human olfactometer), and / or any other assay and / or assay tool.

[0132] The product may optionally have a target tensile property. The tensile property of the product is preferably measured using a ductility determination procedure, but other tension test methods may be used additionally or selectively and / or measured in other ways. In an example, the ductility determination procedure may include: a sample of a product comprising a target mass (e.g., 15 g, 20 g, 25 g, 30 g, 50 g, 100 g, 500 g, 1000 g, any range or value therebetween) is placed in a hole, the sample is heated (e.g., using an oven and the sample is covered in foil), the sample temperature is optionally measured, the sample is stretched with a constant rate of extension (e.g., 2 mm / s, 5 mm / s, 10 mm / s, 15 mm / s, 20 mm / s, any range or value therebetween), and the complete break of the sample strand is recorded when it occurs. In an illustrative example, a sample of the product can be heated for 15 minutes (e.g., covered in foil), and the heated product can be analyzed using a texture analyzer (e.g., in tension mode, with a test speed of 5 mm / sec, a post-test speed of 40 mm / sec, and a target distance of 270 mm) at an ambient temperature between 20° C. and 21° C. In a first specific example, the sample can be heated (e.g., in an oven and / or other heating device) 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 therebetween, etc.) for a target heating time (e.g., 1 min., 5 min., 10 min., 15 min., 20 min., 30 min., 1 hr., any range or value therebetween, etc.). In a second specific example, the sample can be heated to reach a target (internal) temperature (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 therebetween, any other target temperature, etc.) for a target time (e.g., 1 min-5 min, 1 min, 2 min, 3 min, 4 min, 5 min, 10 min, 30 min, any range or value therebetween, 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 chopped before heating, but can be optionally chopped. Stretching the sample preferably starts within a threshold time after heating the sample, but can be optionally performed at any other time. The threshold time may be between 5 s and 5 min or any range or value therebetween (eg, 10 s, 15 s, 20 s, 30 s, 1 min, etc.), but may alternatively be less than 5 s or greater than 5 min.During stretching, the sample can be optionally exposed to ambient temperature (e.g., 20° C.-22° C.) and / or a target temperature (e.g., 20° C.-300° C. or any range or value therebetween, any other target temperature). The ductility determination procedure can be performed using a cheese ductility apparatus or any other tensile testing apparatus. In a specific example, a cheese ductility apparatus (e.g., Texture Technologies TA-426N. TM , with TA.XTPlus TM The texture analyzer (for use with a texture analyzer) may include a hole for holding a sample of a product (e.g., a molten product), a hook-shaped lifting plate (initial position immersed in the product, at or near the hole), and a ring for holding a portion of the product at or near the hole (e.g., at the edge of the sample) so that the product can be stretched when the hook-shaped lifting plate is raised.

[0133] Tensile properties determined using the ductility determination procedure can include failure distance (e.g., extension at complete fracture), peak force, tensile toughness (e.g., work of extension, normalized work, etc.), and / or any other measure of stretchability. In a specific example, a product can be characterized by a failure distance (measured using the ductility determination procedure) between 25 mm-500 mm, or any range or value therebetween (e.g., 50 mm-400 mm, 100 mm-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.), but the product can alternatively be characterized by a failure distance less than 25 mm or greater than 500 mm. Examples of ductility determination data are provided in Fig. 22 , Fig.23A , Fig. 23B , Fig.23C , Fig.25A , Fig.25B , Fig.25C , Fig.25D and Fig.25E Shown in.

[0134] The product may optionally have targeted rheological properties (e.g. Fig.11A and Fig. 11B). The rheological properties of the product can be measured using a creep test (e.g., a stress relaxation test), any test performed using a rheometer, and / or any other test. In one example, the creep test can include: preparing a product sample 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.), a mass (e.g., 1 g, 2 g, 2.5 g, 3 g, 3.5 g, 4 g, etc.), and / or 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.); loading the gel into a rheometer (e.g., MCR 702 MultiDrive) at a target temperature (e.g., room temperature, any other target temperature, such as those temperatures described above for stretchability testing, etc.); TM the product is strained for a target time (e.g., 30 sec, 1 min, 2 min, 5 min, any range or value therebetween, any other target time, etc.) 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.) with 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.); the product is strained for a target time (e.g., 30 sec, 1 min, 2 min, 5 min, any range or value therebetween, any other target time, etc.) at a target frequency (e.g., a frequency that is the same or different from the initial strain frequency; 0.25 Hz, 0.5 Hz, 1 Hz, 1.5 Hz, 2 Hz, 5Hz, any range or value therebetween, etc.) with a constant creep strain (10%, 25%, 40%, 50%, 60%, 75%, any range or value therebetween, any strain within the nonlinear viscoelastic region, etc.) to strain the product for a target time; and at a target frequency (e.g., a frequency that is the same or different from the creep frequency, 0.25Hz, 0.5Hz, 1Hz, 1.5Hz, 2Hz, 5Hz, any range or value therebetween, etc.) with 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.) to strain the product for a target time. Rheological properties determined using creep may include storage modulus recovery (e.g., G' recovery percentage = (final G'-initial G') / initial G'), shear stress and shear strain distribution, and / or any other properties. In a specific example, the product can be characterized as having a storage modulus recovery of between 50%-99% or any range or value therebetween (e.g., 70%-99%, 90%-95%, greater than 60%, greater than 70%, greater than 75%, greater than 80%, greater than 90%, etc.), but can alternatively be characterized as having a storage modulus recovery of less than 50% or greater than 99%. Examples of creep test data are provided in Fig.26A , Fig.26B , Fig.26C , Fig.26D , Fig.26E and Fig.26F Shown in.

[0135] The product may optionally have a target melting property. The melting property of the product is preferably measured using the Schreiber test, but differential scanning calorimetry, other melting determination methods and / or otherwise measured may be used additionally or alternatively. In an example, the Schreiber test may include: preparing a product sample with a target initial mass (e.g., 1g, 2g, 3g, 3.5g, 4g, 5g, 10g, 20g, 50g, any range or value therebetween) and a target initial diameter (e.g., 10mm, 15mm, 20mm, 25mm, 30mm, 50mm, 100mm, any range or value therebetween), heating the sample (e.g., on a glass culture dish, optionally covered), and measuring the final surface area and / or any other melting measurement of the sample. The final surface area (e.g., the surface area melted) may optionally be measured by analyzing the 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 min, 5 min, 6 min, 10 min, 15 min, 20 min, 30 min, 1 hr, 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 in the sample (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 time (e.g., 1 min-10 min, 1 min, 5 min, 6 min, 10 min, 15 min, 20 min, 30 min, 1 hr, any range or value therebetween, any other target time, etc.). The melting properties determined using the Schreiber test can include changes in area / mass and / or any other properties. In one specific example, the product can be characterized by a change in area / mass (measured using the Schreiber test) within 0.5 cm 2 / g-10cm 2 / g or any range or value therebetween (e.g., 1 cm 2 / g-6cm 2 / g, greater than 0.5cm 2 / g, greater than 1cm2 / g, greater than 2cm 2 / g, greater than 3cm 2 / g, etc.), but may alternatively be characterized by a change in area / mass of less than 0.5 cm 2 / g or greater than 10cm 2 / g. An example of Schreiber test data is Fig.21 , Fig.23A , Fig.23D , Fig.24 and Fig.25A Shown in.

[0136] The product may optionally have targeted shredding and / or grinding properties. For example, the product may be shredded when exposed to a load between 0.5 kg and 10 kg (e.g., using a food processor), but may alternatively be shredded when exposed to a load less than 0.5 kg or greater than 10 kg. Shredding may be assessed quantitatively (e.g., shred size, shredding force, etc.) and / or qualitatively (e.g., a qualitative measure from 0 to 1).

[0137] The product can optionally be thermoreversible (e.g., meltable when heated, stretchable when heated, etc.), thermoirreversible, non-thermoreversible, and / or have any thermoresponsive properties. For example, the product can be thermoreversible for at least one heating cycle, for one or more heating-cooling cycles (e.g., melting-curing cycles), for a threshold number of heating-cooling cycles (e.g., 1, 2, 3, 5, 10, 50, etc.), and / or otherwise thermoreversible. Alternatively, the product can be non-thermoreversible and form a gel, semisolid, or solid when heated. However, the product can have a set of any other suitable thermoresponsiveness and / or properties.

[0138] The product may include: SPI (e.g., in aqueous solution, in a lipid component, in a mixture, in dried SPI, etc.), SPI aggregates, mixtures of SPI with other ingredients (e.g., any ingredient in S500) (e.g., gel, liquid, etc.), and / or have any other formulation and / or structure. The product may optionally include SPI with or without inclusion (e.g., where the lipid component and / or other ingredients can be combined and separated from the SPI). Producing the product may optionally include any S500 manufacturing method and / or any food manufacturing method.

[0139] An exemplary image of a stretched product (e.g., a gel) made using SPI is shown in Figure 13A-13N , Figure 14A-14AA , Figures 15A-15D and Figures 16A-16FIn variations, plant-based products (e.g., vegan products, hemp protein-based products, sesame protein-based products, etc.) can have the same or similar structure as dairy products. An exemplary image of a stretched dairy product (e.g., a target product) is shown in Figures 17A-17L An example of a comparison between a stretched product and a dairy product is shown in Fig.18 Shown in.

[0140] In a first variation, producing a product may include producing a mixture (e.g., a gel) comprising SPI and a lipid component (e.g., the mixture is a product). For example, producing a product may include collecting SPI (e.g., an insoluble fraction) via S400; diluting SPI with an aqueous solution to form an SPI solution (e.g., an insoluble fraction solution) via S500; mixing (e.g., emulsifying) the SPI solution with a lipid component to form a mixture (e.g., an emulsion) via S500; optionally heating the mixture via S500; and optionally molding the heated mixture via S500. Example Figure 4 As shown in . The mixture (e.g., after heating and cooling) preferably forms a gel, wherein the gel may exhibit target properties after initial heating, after reheating, and / or at any other time. In a specific example, the target temperature for reheating (e.g., the target heating temperature and / or target temperature of the mixture) may be between 30°C-300°C or any range or value therebetween (e.g., 200°C), but may be optionally less than 30°C or greater than 300°C. The target time for reheating may be between 1min-24hr (e.g., 5min-20min, greater than 10min, etc.), but may be optionally less than 1min or greater than 24hr. Producing a product may optionally include adding a microbial culture (e.g., adding to SPI, adding to an SPI solution, adding to a mixture, etc.) and fermenting. Fermentation may be performed before heating the mixture, simultaneously with heating the mixture (e.g., wherein heating the mixture includes fermenting the mixture), after heating the mixture, without heating the mixture (e.g., wherein fermenting the mixture may gel the mixture), and / or at any other time. Fermentation after heating the mixture may include inoculating the gelled mixture with a culture broth, wherein the microbial culture in the culture broth can penetrate the gel. However, fermentation may be performed in other ways. The resulting product may be stretchable at room temperature and / or when heated. The resulting product may melt at a higher temperature (e.g., 100° C., 200° C., etc.). Despite repeated heating / cooling cycles, the resulting product may still maintain stretchability and melting properties. However, the resulting product may have a set of any other suitable properties.

[0141] In a second variation, producing a product includes using SPI as an ingredient in the product. SPI (e.g., SPI solution, mixture containing SPI, etc.) can be combined with other ingredients (e.g., other proteins, carbohydrates, lipid components, any ingredient in S500, etc.), wherein the resulting mixture can be processed (e.g., via S500 method, via other food manufacturing methods, etc.) to form a product.

[0142] In a third variation, producing a product comprises making a component comprising the SPI (e.g., wherein the component is the product). In a first example, the SPI can be dried via S500, wherein the component comprises dried SPI. In a second example, the SPI undergoes protein modification, wherein the component comprises modified SPI. However, the SPI can be processed in other ways (e.g., using the S500 method) to produce the component.

[0143] However, the product may be made in other ways.

[0144] In the first variation, the product is a liquid mixture. For example, the product can be an emulsion of a lipid component and an SPI solution, wherein the emulsion can be optionally subsequently heated to induce product gelation and / or induce tensile properties and / or melting properties in the product. In the first illustrative example, the liquid mixture can be poured and / or spread onto food (e.g., pizza, bread, etc.), wherein subsequent heating (e.g., baking, grilling, broiling, etc.) forms a cheese-like structure of extensibility, melting of the product. In the second illustrative example, the liquid mixture can be a milk analog (e.g., functional milk).

[0145] In the second variation, the product is a gel. For example, the product can be a mixture comprising SPI, which is heated and optionally cooled to form a viscous gel. In this example, SPI can optionally form SPI aggregates. This gelation can optionally provide product stability (for example, can be transported, used for food manufacturing, etc.). The gel product can be optionally subsequently heated (for example, via the second heating stage) to induce stretching properties and / or melting properties in the product. In another example, the product can be a cooled emulsion, wherein the emulsion is formed by fat, and the fat is heated to a melting point or higher than a melting point before being emulsified with SPI. In an illustrative example, the product of this variation can be cut, shaved, ground, chopped, otherwise crushed or used in a whole piece. The block of the product can be placed on food (for example, pizza, bread, etc.) and heated (for example, baked, grilled, grilled, etc.), wherein the subsequent heating (for example, baked, grilled, grilled, etc.) forms a cheese-like structure of extensibility and melting of the product.

[0146] In a third variation, the product is a stretchable and / or molten product. For example, the product can be a mixture of SPI and a lipid component that is heated to form a stretchable gel and / or molten product. Examples of stretchable gel products are Fig. 8A , Figure 8B , Figure 8C and Fig. 22 Examples of ductility data for stretchable gel products are shown in Fig. 10A and Fig. 10B An example of a melt product is shown in Fig.9A , Fig. 9B , Fig.21 and Fig.24 An example of differential scanning calorimetry data for a stretchable gel product is shown in Fig.12 In one specific example, the product can be heated to and / or maintained at an internal temperature of 50°C-300°C (eg, 70°C-100°C, 85°C, 200°C, 250°C, etc.).

[0147] In a fourth variation, the product comprises dried SPI (e.g., dried using the S500 method). The dried SPI may be in powder form and / or any other form. The dried SPI may then be rehydrated, used as an ingredient to produce a product, and / or used in other ways.

[0148] The product can be realized in a variety of food manufacturing use cases. In the first embodiment, the product is directly used as food (e.g., the product is a final food, the product is the main basis of the final food, etc.). In the first illustrative example, the product is a liquid product (e.g., emulsion and / or other mixture) acting as a liquid dairy analog (e.g., a liquid mozzarella cheese analog), wherein the liquid product can be subsequently heated to form a melted dairy analog (e.g., a melted mozzarella cheese analog). In the second illustrative example, the product is a dairy analog (e.g., a soft cheese analog) that is stretchable at room temperature or near room temperature. In the third illustrative example, the product is a viscous gel (e.g., wherein the viscous gel is not stretchable at room temperature, wherein the viscous gel is stretchable at room temperature, etc.), wherein the viscous gel stretches and / or melts when heated (e.g., wherein the product can be a cheese substitute for shredded, sliced ​​and / or block cheese). In the second embodiment, the product is used as the main substrate in food manufacturing. In a third embodiment, the product is used as an additive ingredient in food manufacturing, where the product serves to increase the stretchability and / or melting properties of the final food. For example, a mixture of SPI, other proteins, lipid components, microorganisms, and / or any other ingredients can be used to make a final food (e.g., where fermentation can optionally be performed at any time during the food manufacturing process). However, the product can be used in other ways.

[0149] In a first example, the product (e.g., Product A; 15% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and an SPI mixture, wherein the SPI mixture is an insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation, and in a variation, all or most of the extracted protein is not denatured. In a second example, the product (e.g., Product H; 18% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and an SPI mixture, wherein the SPI mixture is an insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation, and in a variation, all or most of the extracted protein is not denatured. In a specific example, the insoluble fraction is extracted from an industrial hemp protein isolate solution (e.g., for Product A and Product H; wherein the SPI contains aggregates of industrial hemp protein isolate), a sesame protein isolate solution, a pumpkin protein isolate solution, a combination thereof, and / or any other protein isolate solution.

[0150] In a third example, the product (e.g., Product B; 15% total protein by weight) comprises a solution containing an SPI mixture, wherein the SPI mixture is an insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation, and in a variation, all or most of the extracted protein is not denatured. In a fourth example, the product (e.g., Product I; 15% total protein by weight) comprises a solution containing an SPI mixture, wherein the SPI mixture is an insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation, and in a variation, all or most of the extracted protein is not denatured. In a fifth example, the product (e.g., Product M) comprises a solution containing an SPI mixture (8% by weight), wherein the SPI mixture is an insoluble fraction of a protein isolate solution collected using dilution and sedimentation / precipitation, and in a variation, all or most of the extracted protein is not denatured. In specific examples, the insoluble fraction is extracted from an industrial hemp protein isolate solution (e.g., for 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.

[0151] In a sixth example, the product (e.g., Product C; 15% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and an IPI mixture, wherein the IPI mixture is an insoluble fraction (e.g., a precipitate) of a protein isolate solution collected using isoelectric precipitation, and in a variation, all or most of the extracted protein is not denatured. In a seventh example, the product (e.g., Product J; 18% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and an IPI mixture, wherein the IPI mixture is an insoluble fraction (e.g., a precipitate) of a protein isolate solution collected using isoelectric precipitation, and in a variation, all or most of the extracted protein is not denatured. In a specific example, the insoluble fraction is extracted from an industrial hemp protein isolate solution, a sesame protein isolate solution, a pumpkin protein isolate solution, a combination thereof, and / or any other protein isolate solution.

[0152] In an eighth example, the product (e.g., Product D; 15% total protein by weight) comprises a solution containing an IPI mixture, wherein the IPI mixture is an insoluble fraction (e.g., precipitate) of a protein isolate solution collected using isoelectric precipitation, and in a variation, all or most of the extracted protein is not denatured. In a ninth example, the product (e.g., Product K; 18% total protein by weight) comprises a solution containing an IPI mixture, wherein the IPI mixture is an insoluble fraction (e.g., precipitate) of a protein isolate solution collected using isoelectric precipitation, and in a variation, all or most of the extracted protein is not denatured. In a tenth example, the product (e.g., Product O) comprises a solution containing an IPI mixture (8% by weight), wherein the IPI mixture is an insoluble fraction (e.g., precipitate) of a protein isolate solution collected using isoelectric precipitation, and in a variation, all or most of the extracted protein is not denatured. In specific examples, the insoluble fraction is extracted from an industrial hemp protein isolate solution (e.g., for Product D, Product K, and Product O), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0153] In an eleventh example, the product (e.g., Product E; 15% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and an ASP mixture, wherein the ASP mixture is an insoluble fraction of a protein isolate solution collected using antisolvent precipitation, and in variations, all or a substantial portion of the extracted protein is not denatured. In specific examples, the insoluble fraction is extracted from an industrial hemp protein isolate solution (e.g., for Product E), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0154] In a twelfth example, the product (e.g., Product F; 15% total protein by weight) comprises a solution containing an ASP mixture, wherein the ASP mixture is an insoluble fraction of a protein isolate solution collected using antisolvent precipitation, and in a variation, all or a majority of the extracted protein is not denatured. In a thirteenth example, the product (e.g., Product N) comprises a solution containing an ASP mixture (8% by weight), wherein the ASP mixture is an insoluble fraction of a protein isolate solution collected using antisolvent precipitation, and in a variation, all or a majority of the extracted protein is not denatured. In specific examples, the insoluble fraction is extracted from an industrial hemp protein isolate solution (e.g., for Product F and Product N), a sesame protein isolate solution, a pumpkin protein isolate solution, combinations thereof, and / or any other protein isolate solution.

[0155] In the fourteenth example, the product (e.g., product G; 15% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and industrial hemp powder. In the twelfth example, the product (e.g., product L; 18% total protein by weight and 35% lipid by weight) comprises an emulsion containing a lipid component and industrial hemp powder.

[0156] 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., plant, microbial, algae, fungus, seaweed or other non-dairy / non-animal material); using the protein isolate solution to prepare / produce a structured protein isolate via precipitation / separation / sedimentation, etc. (i.e., by diluting soluble protein with an aqueous or non-aqueous solvent (i.e., water, antisolvent and / or any other diluent); isoelectric precipitation, heat or shear induced precipitation, etc.); fractionating the structured protein isolate from the solution (e.g., filtering, centrifuging, dialysis, drying, etc.); and collecting the structured protein isolate (e.g., aggregates of the structured protein isolate) as an ingredient. In a second specific example, the method includes: obtaining a protein isolate solution from a protein source; mixing (e.g., emulsifying) the protein isolate solution with a lipid component at different protein:lipid ratios (e.g., 0-50% protein: 0-40% lipid, etc.) to form a lipid-protein isolate mixture (e.g., oil-water emulsion); precipitating / separating / precipitating the lipid protein mixture by diluting with an aqueous or non-aqueous solvent (i.e., water, antisolvent and / or any other diluent); isoelectric precipitation, heat or shear induced precipitation, etc.; allowing lipid protein isolates (e.g., structured protein isolates containing lipid components) to be fractionated from the solution (e.g., filtration, centrifugation, dialysis, drying, etc.); and collecting lipid protein isolates as components. In a third specific example, the method includes: obtaining a protein isolate solution from a protein source; diluting the protein isolate solution with a diluent containing an aqueous solution mixed (e.g., emulsified) with a lipid component; allowing structured isolates to be fractionated from the solution (e.g., filtration, centrifugation, dialysis, drying, etc.); and collecting structured isolates as components.

[0157] As used herein, “substantially” or other approximate terms (e.g., “about,” “approximately,” etc.) can be within a predetermined error threshold or tolerance of a measurement, composition, or other reference (e.g., within 0.001%, 0.01%, 0.1%, 1%, 2%, 5%, 10%, 15%, 20%, 30%, any range or value therein of the reference).

[0158] Embodiments of the systems and / or methods may include every combination and arrangement of the various system components and various method processes, wherein one or more instances of the methods and / or processes described herein may be performed asynchronously (e.g., sequentially), simultaneously (e.g., concurrently, in parallel, etc.), or in any other suitable order by and / or using one or more instances of the systems, elements, and / or entities described herein. The components and / or processes of the attached systems and / or methods may be used with, substituted for, or otherwise integrated with all or part of the above-described systems and / or methods disclosed in this application, each of which is incorporated by reference in its entirety.

[0159] As those skilled in the art will recognize from the foregoing detailed description and from the accompanying drawings and claims, modifications and variations may be made to the preferred embodiments of the invention without departing from the scope of the invention defined in the appended claims.

Claims

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

2. The composition according to claim 1, further comprising a lipid component of plant origin.

3. The composition of claim 1, wherein the protein mixture is spray dried.

4. The composition of claim 1, wherein the structured protein isolate has an increased surface hydrophobicity relative to unaggregated protein isolate units.

5. The composition of claim 1, wherein the structured protein isolate has a diameter of at least 50 nm.

6. The composition of claim 1, wherein the plant source comprises a single plant source.

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

8. The composition of claim 7, wherein the protein component does not include animal protein.

9. The composition of claim 7, wherein the protein component does not include soy derivatives.

10. The composition of claim 7, wherein the composition comprises a fermented cheese replica, wherein the composition further comprises a microbial culture, wherein the composition is fermented.

11. The composition of claim 7, wherein the composition comprises a fresh cheese replica, wherein the composition is a gelled emulsion.

12. The composition of claim 7, wherein the composition is shreddable.

13. The composition of claim 7, wherein the composition is characterized by an area / mass ratio determined by the Schreiber test of from about 1 cm 2 / g to about 6cm 2 / g change (about 25 mm initial diameter; about 3.5 g initial mass; heating at about 230°C for about 6 min).

14. The composition of claim 7, wherein the composition is characterized by a failure distance of at least 100 mm as determined by the Ductility Test Procedure (about 30 g sample; heating at about 200°C for about 15 min; extension at about 20°C 5.00 mm / sec).

15. A plant-based food obtained by a process comprising: ● Obtaining protein isolate units from plant sources; ● diluting the protein isolate unit 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, each structured protein isolate comprising aggregated protein isolate units; and ● A plant-based food product comprising the insoluble fraction and a lipid component is produced, wherein the food product is characterized by a failure distance of at least 100 mm as determined by a ductility determination procedure.

16. The food product according to claim 15, wherein the ductility determination procedure comprises: Heat about 30 g of the sample at about 200°C for about 15 min; and stretching the sample at about 5.00 mm / sec at about 20°C.

17. The food product of claim 15, wherein diluting the protein isolate unit comprises diluting a protein isolate solution comprising the protein isolate unit and salt, wherein the ratio between the salt concentration in the protein isolate solution and the salt concentration in the diluted protein isolate mixture is at least 3.

18. The food product of claim 15, wherein the composition comprises a plant-based cheese, wherein producing 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 unit; and ● The emulsion is molded to form a gel, wherein the plant-based food comprises the gel.

19. The food product of claim 18, wherein the aqueous solution comprises a hydrocolloid.

20. The food product of claim 15, wherein at least 0.5% of the dry components of the insoluble fraction comprises carbohydrates.

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