Materials and methods for protein production

Abstract

This document relates to materials and methods for protein production, such as proteins having low flavor or low color profiles and food products comprising the proteins.

Description

[0001] This application is a divisional application of the invention patent application filed on March 1, 2021, with application number 202180022974.8 and invention title "Materials and methods for protein production".

[0002] Cross-references to related applications

[0003] This application claims priority to U.S. Provisional Application Serial No. 62 / 983,558, filed February 28, 2020 and U.S. Provisional Application Serial No. 62 / 993,675, filed March 23, 2020, each of which is incorporated herein by reference in its entirety.

[0004] Description of text files submitted electronically

[0005] The contents of the XML file submitted electronically are incorporated herein by reference in their entirety: A new XML-formatted sequence list was created based on the sequence list of the parent case (a computer-readable copy of filename: 38767_0246WO1.txt, dated March 1, 2021, with a file size of approximately 56 kilobytes). Technical Field

[0006] This invention relates to methods for purifying proteins, and more specifically to methods for purifying proteins to help reduce color, odor, and flavor associated with the protein's source. The invention also relates to foods containing purified proteins. Background Technology

[0007] The success of foods that mimic animal-derived foods (e.g., cheese or meat) largely depends on the production of functional proteins that can be manipulated and have low flavor profiles, making the protein source difficult to identify based on the flavor profile of the food imitation. A protein purification method that ensures food safety and results in minimal undesirable color, odor, and flavor in the purified protein would be useful. Summary of the Invention

[0008] This document is based, at least in part, on the use of precipitation to produce protein compositions.

[0009] In one aspect, a low-flavor protein composition is provided. This low-flavor protein composition typically comprises at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof; wherein said various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0010] In some embodiments, the low-flavor protein composition has a brightness of at least 86 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the low-flavor protein composition has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the low-flavor protein composition has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0011] In some embodiments, the low-flavor protein composition has a chromaticity value of less than 14. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 12. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 10. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 8. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 6.

[0012] In some embodiments, the low-flavor protein composition comprises less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis).

[0013] In some embodiments, lipids include one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids.

[0014] In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are at least 90% soybean protein on a dry weight basis.

[0015] In some embodiments, the low-flavor protein composition further comprises at least one of a preservative, an antioxidant, or a shelf-life extender.

[0016] In some embodiments, the preservative, antioxidant, or shelf-life extender includes at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, *Carnobacterium divergens* M35, *Carnobacterium maltaromaticum* cb1, *Carnosum* 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, erythorbic acid. (acid), lauroyl arginine ethyl ester, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, lecithin citrate, Leuconostoc, methyl paraben, methyl-p-hydroxybenzoate, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propyl paraben, propyl-p-hydroxybenzoate, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium dithionite, sodium isoascorbate Sodium iso-ascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methyl-p-hydroxybenzoic acid, sodium salt of propyl-p-hydroxybenzoic acid, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0017] In some embodiments, the low-flavor protein composition is in the form of a solution, suspension, or emulsion. In some embodiments, the low-flavor protein composition is in the form of a solid or powder.

[0018] In some embodiments, the low-flavor protein composition has an average particle size of about 5 μm to about 40 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 40 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 30 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 20 μm at its maximum size.

[0019] In some embodiments, the low-flavor protein composition is in the form of an extrusion. In some embodiments, the extrusion is substantially in granular form.

[0020] In some embodiments, the particles have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the particles have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0021] In some embodiments, the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The bulk density. In some embodiments, the extrudate has a moisture content of about 5% to about 10%. In some embodiments, the extrudate has a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate has a fat content of less than about 1.0%. In some embodiments, the extrudate has a sugar content of less than about 1%.

[0022] In some embodiments, the extrudate has a hydration ratio of about 2.5 to about 3 after hydration for about 60 minutes at room temperature. In some embodiments, the extrudate has a hydration time of less than about 30 minutes. In some embodiments, the extrudate has a pH of about 5.0 to about 7.5 upon hydration.

[0023] In some embodiments, the extrudate has a bite strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0024] In some embodiments, the low-flavor protein composition has a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the low-flavor protein composition has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w or up to about 0.005% w / w).

[0025] In some embodiments, the low-flavor protein composition has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0026] In some embodiments, the low-flavor protein composition exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0027] In some embodiments, the low-flavor protein composition is a protein concentrate. In some embodiments, the low-flavor protein composition is a protein isolate.

[0028] It also provides a food comprising any low-flavor protein composition as described herein.

[0029] In another aspect, a low-color protein composition is provided. This low-color protein composition typically comprises at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof; wherein said various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both, and wherein said low-color protein composition has a lightness value of at least 86 and a chromaticity value of less than 14, or both, on a scale from 0 (black control value) to 100 (white control value).

[0030] In some embodiments, the low-color protein composition has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the low-color protein composition has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0031] In some embodiments, the low-color protein composition has a chromaticity value of less than 14. In some embodiments, the low-color protein composition has a chromaticity value of less than 12. In some embodiments, the low-color protein composition has a chromaticity value of less than 10. In some embodiments, the low-color protein composition has a chromaticity value of less than 8. In some embodiments, the low-color protein composition has a chromaticity value of less than 6.

[0032] In some embodiments, the low-color protein composition comprises less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis).

[0033] In some embodiments, lipids include one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids.

[0034] In some embodiments, a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof constitute at least 90% soybean protein on a dry weight basis.

[0035] In some embodiments, the low-color protein composition further comprises at least one of a preservative, an antioxidant, or a shelf-life extender.

[0036] In some embodiments, the preservative, antioxidant, or shelf-life extender includes at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, egg white, etc. Phospholipid citrate, Leuconostoc mesylate, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0037] In some embodiments, the low-color protein composition is in the form of a solution, suspension, or emulsion. In some embodiments, the low-color protein composition is in the form of a solid or powder.

[0038] In some embodiments, the low-color protein composition has an average particle size of about 5 μm to about 40 μm at its maximum size. In some embodiments, the low-color protein composition has an average particle size of about 10 μm to about 40 μm at its maximum size. In some embodiments, the low-color protein composition has an average particle size of about 10 μm to about 30 μm at its maximum size. In some embodiments, the low-color protein composition has an average particle size of about 10 μm to about 20 μm at its maximum size.

[0039] In some embodiments, the low-color protein composition is in the form of an extrusion. In some embodiments, the extrusion is substantially in granular form.

[0040] In some embodiments, the particles have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the particles have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0041] In some embodiments, the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The bulk density. In some embodiments, the extrudate has a moisture content of about 5% to about 10%. In some embodiments, the extrudate has a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate has a fat content of less than about 1.0%. In some embodiments, the extrudate has a sugar content of less than about 1%.

[0042] In some embodiments, the extrudate has a hydration ratio of about 2.5 to about 3 after hydration for about 60 minutes at room temperature. In some embodiments, the extrudate has a hydration time of less than about 30 minutes. In some embodiments, the extrudate has a pH of about 5.0 to about 7.5 upon hydration.

[0043] In some embodiments, the extrudate has an interlocking strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0044] In some embodiments, the low-color protein composition has a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the low-color protein composition has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w, or up to about 0.005% w / w).

[0045] In some embodiments, the low-color protein composition has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0046] In some embodiments, the low-color protein composition exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change upon cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed upon heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0047] In some embodiments, the low-color protein composition is a protein concentrate. In some embodiments, the low-color protein composition is a protein isolate.

[0048] A food product comprising any low-color protein composition as described herein is also provided.

[0049] On the other hand, protein concentrates are provided. Such protein concentrates typically contain at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof; and at least 9% by dry weight of one or more insoluble carbohydrates, wherein the plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0050] In some embodiments, the protein concentrate has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the protein concentrate has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0051] In some embodiments, the protein concentrate has a chromaticity value of less than 14. In some embodiments, the protein concentrate has a chromaticity value of less than 12. In some embodiments, the protein concentrate has a chromaticity value of less than 10. In some embodiments, the protein concentrate has a chromaticity value of less than 8. In some embodiments, the protein concentrate has a chromaticity value of less than 6.

[0052] In some embodiments, the protein concentrate includes less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis).

[0053] In some embodiments, lipids include one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids.

[0054] In some embodiments, a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof constitute at least 90% soybean protein on a dry weight basis.

[0055] In some embodiments, the protein concentrate further comprises at least one of a preservative, an antioxidant, or a shelf-life extender.

[0056] In some embodiments, the preservative, antioxidant, or shelf-life extender includes at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, egg white, etc. Phospholipid citrate, Leuconostoc mesylate, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0057] In some embodiments, the protein concentrate is in the form of a solution, suspension, or emulsion. In some embodiments, the protein concentrate is in the form of a solid or powder.

[0058] In some embodiments, the protein concentrate has an average particle size of about 5 μm to about 40 μm at its maximum size. In some embodiments, the protein concentrate has an average particle size of about 10 μm to about 40 μm at its maximum size. In some embodiments, the protein concentrate has an average particle size of about 10 μm to about 30 μm at its maximum size. In some embodiments, the protein concentrate has an average particle size of about 10 μm to about 20 μm at its maximum size.

[0059] In some embodiments, the protein concentrate is in the form of an extrusion. In some embodiments, the extrusion is substantially in granular form.

[0060] In some embodiments, the particles have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the particles have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0061] In some embodiments, the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The bulk density. In some embodiments, the extrudate has a moisture content of about 5% to about 10%. In some embodiments, the extrudate has a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate has a fat content of less than about 1.0%. In some embodiments, the extrudate has a sugar content of less than about 1%.

[0062] In some embodiments, the extrudate has a hydration ratio of about 2.5 to about 3 after hydration for about 60 minutes at room temperature. In some embodiments, the extrudate has a hydration time of less than about 30 minutes. In some embodiments, the extrudate has a pH of about 5.0 to about 7.5 upon hydration.

[0063] In some embodiments, the extrudate has an interlocking strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0064] In some embodiments, the protein concentrate has a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the protein concentrate has a sodium level of up to about 1% w / w (e.g., up to about 0.5, up to about 0.1, up to about 0.05, up to about 0.01 or up to about 0.005% w / w).

[0065] In some embodiments, the protein concentrate has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0066] In some embodiments, the protein concentrate exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0067] It also provides a food product that includes any protein concentrate as described herein.

[0068] In another aspect, protein isolates are provided. Such protein isolates typically comprise at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof; and less than 8% by dry weight of one or more insoluble carbohydrates, wherein the plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0069] In some embodiments, the protein isolate has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the protein isolate has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0070] In some embodiments, the protein isolate has a chromaticity value of less than 14. In some embodiments, the protein isolate has a chromaticity value of less than 12. In some embodiments, the protein isolate has a chromaticity value of less than 10. In some embodiments, the protein isolate has a chromaticity value of less than 8. In some embodiments, the protein isolate has a chromaticity value of less than 6.

[0071] In some embodiments, the protein isolate comprises less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis). In some embodiments, the lipids include one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids.

[0072] In some embodiments, a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof constitute at least 90% soybean protein on a dry weight basis.

[0073] In some embodiments, the protein isolate further comprises at least one of a preservative, an antioxidant, or a shelf-life extender.

[0074] In some embodiments, the preservative, antioxidant, or shelf-life extender includes at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, egg white, etc. Phospholipid citrate, Leuconostoc mesylate, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0075] In some embodiments, the protein isolate is in the form of a solution, suspension, or emulsion. In some embodiments, the protein isolate is in the form of a solid or powder.

[0076] In some embodiments, the protein isolate has an average particle size of about 5 μm to about 40 μm at its maximum size. In some embodiments, the protein isolate has an average particle size of about 10 μm to about 40 μm at its maximum size.

[0077] In some embodiments, the protein isolate has an average particle size of about 10 μm to about 30 μm at its maximum size. In some embodiments, the protein isolate has an average particle size of about 10 μm to about 20 μm at its maximum size.

[0078] In some embodiments, the protein isolate is in the form of an extrusion. In some embodiments, the extrusion is substantially in granular form.

[0079] In some embodiments, the particles have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the particles have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0080] In some embodiments, the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The bulk density. In some embodiments, the extrudate has a moisture content of about 5% to about 10%. In some embodiments, the extrudate has a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate has a fat content of less than about 1.0%. In some embodiments, the extrudate has a sugar content of less than about 1%.

[0081] In some embodiments, the extrudate has a hydration ratio of about 2.5 to about 3 after hydration for about 60 minutes at room temperature. In some embodiments, the extrudate has a hydration time of less than about 30 minutes. In some embodiments, the extrudate has a pH of about 5.0 to about 7.5 upon hydration.

[0082] In some embodiments, the extrudate has an interlocking strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0083] In some embodiments, the protein isolate has a protein dispersibility index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the protein isolate has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w or up to about 0.005% w / w).

[0084] In some embodiments, the protein isolate has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0085] In some embodiments, the protein isolate exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0086] It also provides a food product that includes any protein isolate as described herein.

[0087] In one aspect, a low-flavor protein composition is provided, produced by a method generally comprising: (a) adding an aqueous solution to a source protein composition to form a solution of dissolved proteins; (b) optionally removing solids from the solution of dissolved proteins; (c) adding an organic solvent to the solution of dissolved proteins to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form a low-flavor protein composition, wherein the low-flavor protein composition comprises a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof, and wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0088] In some embodiments, step (a) is performed at a pH of about 6.0 to about 9.0. In some embodiments, step (a) is performed at a pH of about 7.5 to about 8.5. In some embodiments, step (a) is performed at a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0).

[0089] In some embodiments, step (b) includes centrifugation, filtration, or a combination thereof.

[0090] In some embodiments, prior to step (c), the pH of the solution of dissolved proteins is adjusted to about 4.0 to about 9.0. In some embodiments, prior to step (c), the pH of the solution of dissolved proteins is adjusted to about 5.5 to about 7.5. In some embodiments, prior to step (c), the pH of the solution of dissolved proteins is adjusted to about 6.0 to about 7.0. In some embodiments, prior to step (c), the pH of the solution of dissolved proteins is adjusted to about 4.0 to about 7.0 (e.g., adjusted to about 4.0 to about 6.0, adjusted to about 4.5 to about 6.0, adjusted to about 4.5, or adjusted to about 6.0). In some embodiments, prior to step (c), the solution of dissolved protein is heated at a temperature of about 70°C to about 100°C (e.g., about 80°C to about 100°C, about 85°C to about 100°C, about 85°C to about 95°C, about 90°C to about 100°C, about 85°C to about 90°C, about 90°C to about 95°C, or about 95°C to about 100°C) for, for example, for about 10 seconds to about 30 minutes (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). In some embodiments, prior to step (C), the organic solvent and / or the solution of dissolved protein is cooled to a temperature of, for example, about -20°C to about 10°C (e.g., about -20°C to about 4°C). In some embodiments, prior to step (C), the solution of dissolved protein is heated and then cooled.

[0091] In some embodiments, step (c) includes adding an organic solvent. In some embodiments, step (c) includes adding an organic solvent to a final concentration of about 5% (v / v) to about 70% (v / v). In some embodiments, step (c) includes adding an organic solvent to a final concentration of about 10% (v / v) to about 50% (v / v). In some embodiments, step (c) includes adding an organic solvent to a final concentration of about 20% (v / v) to about 30% (v / v). In some embodiments, step (c) includes adding an organic solvent to a final concentration of about 40% (v / v) to about 90% (v / v) (e.g., a final concentration of about 40% (v / v) to about 70% (v / v), a final concentration of about 40% (v / v) to about 60% (v / v), or a final concentration of about 45% (v / v) to about 55% (v / v).

[0092] In some embodiments, the pH is adjusted by adding an acid. In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid.

[0093] In some embodiments, step (d) includes centrifugation, filtration, or a combination thereof.

[0094] In some embodiments, the organic solvent is ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol). In some embodiments, the organic solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone.

[0095] In some embodiments, the method further includes (e) washing the low-flavor protein composition with an organic detergent solvent. In some embodiments, the method further includes (e) washing the low-flavor protein composition with an aqueous detergent solvent. In some embodiments, the method further includes (e) washing the low-flavor protein composition first with an organic detergent solvent and then with an aqueous detergent solvent, or vice versa.

[0096] In some embodiments, the organic washing solvent is ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol, or up to 20%, up to 15%, up to 10%, or up to 5% ethanol). In some embodiments, the organic washing solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone.

[0097] In some embodiments, the organic washing solvent in step (e) is the same as the organic solvent in step (c).

[0098] In some embodiments, the aqueous detergent solvent is water. In some embodiments, the aqueous detergent solvent has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0. In some embodiments, the aqueous detergent solvent may contain a buffer.

[0099] In some embodiments, the method further comprises drying the low-flavor protein composition. In some embodiments, drying includes spray drying, pad drying, freeze drying, or oven drying.

[0100] In some embodiments, the source protein composition is based on at least 90% by dry weight of a portion or derivative of any of plants, algae, fungi, bacteria, protozoa, invertebrates, or any of them, or a combination thereof. In some embodiments, the source protein composition is based on at least 90% by dry weight of defatted soy flour, defatted pea flour, or a combination thereof. In some embodiments, the source protein composition is a soy protein composition, and the isoflavone content of the low-flavor protein composition is less than 90% by dry weight of the isoflavone content of the source protein composition. In some embodiments, the source protein composition is a soy protein composition, and the isoflavone content of the low-flavor protein composition is less than 70% by dry weight of the isoflavone content of the source protein composition. In some embodiments, the source protein composition is a soy protein composition, and the isoflavone content of the low-flavor protein composition is less than 50% by dry weight of the isoflavone content of the source protein composition. In some embodiments, the source protein composition is a soy protein composition, and the isoflavone content of the low-flavor protein composition is less than 30% by dry weight of the isoflavone content of the source protein composition. In some embodiments, the source protein composition is a soy protein composition, and the isoflavone content of the low-flavor protein composition is less than 10% by dry weight of the isoflavone content of the source protein composition.

[0101] In some embodiments, when cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 90% of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0102] In some embodiments, when cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 70% of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0103] In some embodiments, when cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 50% of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0104] In some embodiments, when cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 30% of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0105] In some embodiments, when cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 10% of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0106] In some embodiments, when cooked in a seasoned broth, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of the amount of one or more soy flavor compounds, said soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0107] In some embodiments, when cooked in a seasoned broth, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, produces at least 5% (e.g., at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100% or more) of one or more volatile compounds from the meat volatiles group, said volatile compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0108] In some embodiments, when cooked in a seasoned broth, a 1% (w / v) suspension of a low-flavor protein composition, based on the dry weight of the protein composition, produces at least 5% (e.g., at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100% or more) of one or more volatile compounds from the meat volatiles group, said volatile compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0109] In some embodiments, one or more soybean flavor compounds include at least one compound selected from the group consisting of hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonenal, (E,Z)-2,6-nonadienal and (E,E)-2,4-decadienal.

[0110] In some embodiments, the low-flavor protein composition has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value). In some embodiments, the low-flavor protein composition has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0111] In some embodiments, the low-flavor protein composition has a chromaticity value of less than 14. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 12. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 10. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 8. In some embodiments, the low-flavor protein composition has a chromaticity value of less than 6.

[0112] In some embodiments, the low-flavor protein composition comprises less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis). In some embodiments, the lipids comprise one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids.

[0113] In some embodiments, a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof constitute at least 90% soybean protein on a dry weight basis.

[0114] In some embodiments, the low-flavor protein composition further comprises at least one of a preservative, an antioxidant, or a shelf-life extender.

[0115] In some embodiments, the preservative, antioxidant, or shelf-life extender includes at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, egg white, etc. Phospholipid citrate, Leuconostoc mesylate, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0116] In some embodiments, the low-flavor protein composition is in the form of a solution, suspension, or emulsion. In some embodiments, the low-flavor protein composition is in the form of a solid or powder.

[0117] In some embodiments, the low-flavor protein composition has an average particle size of about 5 μm to about 40 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 40 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 30 μm at its maximum size. In some embodiments, the low-flavor protein composition has an average particle size of about 10 μm to about 20 μm at its maximum size.

[0118] In some embodiments, the low-flavor protein composition is in the form of an extrusion. In some embodiments, the extrusion is substantially in granular form.

[0119] In some embodiments, the particles have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the particles have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0120] In some embodiments, the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The bulk density. In some embodiments, the extrudate has a moisture content of about 5% to about 10%. In some embodiments, the extrudate has a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate has a fat content of less than about 1.0%. In some embodiments, the extrudate has a sugar content of less than about 1%.

[0121] In some embodiments, the extrudate has a hydration ratio of about 2.5 to about 3 after hydration for about 60 minutes at room temperature. In some embodiments, the extrudate has a hydration time of less than about 30 minutes. In some embodiments, the extrudate has a pH of about 5.0 to about 7.5 upon hydration.

[0122] In some embodiments, the extrudate has an interlocking strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0123] In some embodiments, the low-flavor protein composition has a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the low-flavor protein composition has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w or up to about 0.005% w / w).

[0124] In some embodiments, the low-flavor protein composition has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0125] In some embodiments, the low-flavor protein composition exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0126] In some embodiments, the low-flavor protein composition is a protein concentrate. In some embodiments, the low-flavor protein composition is a protein isolate.

[0127] A food comprising a low-flavor protein composition as described herein.

[0128] In another aspect, this document provides a protein composition comprising at least 50% by dry weight of a plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof, and less than 1.2% by dry weight of fat, wherein said plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0129] The implementation may include one or more of the following characteristics: The protein composition may have a lightness of at least 86 on a scale from 0 (black control value) to 100 (white control value). The protein composition may have a lightness of at least 90 on a scale from 0 (black control value) to 100 (white control value). The protein composition may have a chromaticity value of less than 14. The protein composition may have a chromaticity value of less than 12. The protein composition may have a chromaticity value of less than 10. The composition may have a chromaticity value of less than 8. The protein composition may have a chromaticity value of less than 6. The protein composition may contain less than about 0.5% lipids on a dry weight basis. The lipids may contain one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids. Various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof may be at least 90% soybean protein on a dry weight basis. The composition may further comprise at least one of a preservative, an antioxidant, or a shelf-life extender. The protein composition may be in the form of a solution, suspension, or emulsion. The protein composition may be in the form of a solid or powder. The protein composition may have an average particle size of about 5 μm to about 40 μm at its maximum size. The protein composition may have an average particle size of about 10 μm to about 40 μm at its maximum size. The protein composition may have an average particle size of about 10 μm to about 30 μm at its maximum size. The protein composition may have an average particle size of about 10 μm to about 20 μm at its maximum size. The protein composition is in the form of an extrudate. The extrudate may be substantially in the form of granules. The granules have an average maximum size of about 3 mm to about 5 mm. Less than about 20% (w / w) of the granules may have a maximum size of less than 1 mm. Less than about 5% (w / w) of the granules may have a maximum size of more than 1 cm. The extrudate may have a content of about 0.25 to about 0.4 g / cm³. 3The extrudate may have a moisture content of about 5% to about 10%. The extrudate may have a protein content of about 65% to about 100% on a dry weight basis. The extrudate may have a fat content of less than about 1.0%. The extrudate may have a sugar content of less than about 1%. After hydration at room temperature for about 60 minutes, the extrudate may have a hydration ratio of about 2.5 to about 3. The extrudate may have a hydration time of less than about 30 minutes. The extrudate may have a pH of about 5.0 to about 7.5 when hydrated. The extrudate may have a bite strength of about 2000 g to about 4000 g at a hydration ratio of about 3. The protein composition may be a protein concentrate. The protein composition may be a protein isolate. This document also provides food products that include any of the protein compositions provided herein.

[0130] In another aspect, a method for producing a low-flavor protein composition is provided. Such a method typically comprises: (a) adding an aqueous solution to a source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form a low-flavor protein composition, wherein the low-flavor protein composition may comprise a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0131] The implementation may include one or more of the following features: Step (a) may be performed at a pH of about 6.0 to about 9.0. Step (a) may be performed at a pH of about 7.5 to about 8.5. Step (a) may be performed at a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0). Step (b) may include centrifugation, filtration, or a combination thereof. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 4.0 to about 9.0. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 5.5 to about 7.5. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 6.0 to about 7.0. Prior to step (c), the pH of the solution of dissolved protein can be adjusted to about 4.0 to about 7.0 (e.g., to about 4.0 to about 6.0, to about 4.5 to about 6.0, to about 4.5 or about 6.0). In some embodiments, prior to step (c), the solution of dissolved protein is heated at a temperature of about 70°C to about 100°C (e.g., about 80°C to about 100°C, about 85°C to about 100°C, about 85°C to about 95°C, about 90°C to about 100°C, about 85°C to about 90°C, about 90°C to about 95°C, or about 95°C to about 100°C) for a duration of, for example, about 10 seconds to about 30 minutes (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). In some embodiments, prior to step (C), the organic solvent and / or the solution of dissolved protein is cooled to a temperature of, for example, from about -20°C to about 10°C (e.g., from about -20°C to about 4°C). In some embodiments, prior to step (C), the solution of dissolved protein is heated and then cooled. Step (C) may include adding an organic solvent. Step (C) may include adding an organic solvent to a final concentration of about 5% to about 70% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 10% to about 50% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 20% to about 30% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 40% to about 90% (v / v) (e.g., a final concentration of about 40% to about 70% (v / v), a final concentration of about 40% to about 60% (v / v), or a final concentration of about 45% to about 55% (v / v)). pH may be adjusted by adding an acid.In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid. Step (d) may include centrifugation, filtration, or a combination thereof. The organic solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol). In some embodiments, the organic solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The method may further include (e) washing the low-flavor protein composition with an organic washing solvent. The method may further include (e) washing the low-flavor protein composition with an aqueous washing solvent. The method may further include (e) washing the low-flavor protein composition first with an organic washing solvent and then with an aqueous washing solvent, or vice versa. The organic washing solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol, or up to 20%, up to 15%, up to 10%, or up to 5% ethanol). In some embodiments, the organic washing solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The organic washing solvent in step (e) may be the same as the organic solvent in step (c). The aqueous washing solvent may be water. In some embodiments, the aqueous washing solvent has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0. In some embodiments, the aqueous washing solvent may contain a buffer. The method may further include drying the low-flavor protein composition. Drying may include spray drying, pad drying, freeze drying, or oven drying. The source protein composition may be based on at least 90% by dry weight of a portion or derivative of a plant, algae, fungus, bacteria, protozoa, invertebrate, any one thereof, or a combination thereof. The source protein composition may be based on defatted soy flour, defatted pea flour, or a combination thereof, with a dry weight of at least 90%. The source protein composition may be a soy protein composition, and the isoflavone content of the low-flavor protein composition may be less than 90% of the isoflavone content of the source protein composition based on dry weight. The source protein composition may be a soy protein composition, and the isoflavone content of the low-flavor protein composition may be less than 70% of the isoflavone content of the source protein composition based on dry weight. The source protein composition may be a soy protein composition, and the isoflavone content of the low-flavor protein composition may be less than 50% of the isoflavone content of the source protein composition based on dry weight. The source protein composition may be a soy protein composition, and the isoflavone content of the low-flavor protein composition may be less than 30% of the isoflavone content of the source protein composition based on dry weight. The source protein composition may be a soy protein composition, and the isoflavone content of the low-flavor protein composition may be less than 10% of the isoflavone content of the source protein composition based on dry weight.When cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can produce no more than 90% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can produce no more than 70% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can produce no more than 50% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can generate no more than 30% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being generated by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in water, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can generate no more than 10% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being generated by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in a seasoned broth, a 1% (w / v) suspension of the low-flavor protein composition, based on the dry weight of the low-flavor protein composition, can produce no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). In some embodiments, the protein composition produces no more than 90% (e.g., no more than 70%, 50%, 30%, or 10%) of the amount of one or more volatile compounds from a group of volatile compounds produced by solvent-assisted flavor extraction (SAFE) from said source protein composition. One or more soybean flavor compounds include at least one compound selected from the group consisting of hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonenal, (E,Z)-2,6-nonadienal and (E,E)-2,4-decadienal.The low-flavor protein composition can have a lightness value of at least 88 on a scale from 0 (black control value) to 100 (white control value). When cooked in flavored broth, a 1% (w / v) suspension of the low-flavor protein composition, based on its dry weight, can produce at least 5% (e.g., at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100% or more) of one or more volatile compounds from the meat volatiles group, said volatile compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). The low-flavor protein composition can have a lightness value of at least 90 on a scale from 0 (black control value) to 100 (white control value). The low-flavor protein composition can have a chromaticity value of less than 14. The low-flavor protein composition can have a chromaticity value of less than 12. The low-flavor protein composition can have a chromaticity value of less than 10. The low-flavor protein composition may have a color value of less than 8. The low-flavor protein composition may have a color value of less than 6. The low-flavor protein composition may contain less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis). The lipids may contain one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids. Various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof may be at least 90% soybean protein on a dry weight basis. The low-flavor protein composition may contain at least one of preservatives, antioxidants, or shelf-life extenders. The low-flavor protein composition may be in the form of a solution, suspension, or emulsion. The low-flavor protein composition may be in the form of a solid or powder. The low-flavor protein composition may have an average particle size of about 5 μm to about 40 μm at its maximum size. The low-flavor protein composition may have an average particle size of about 5 μm to about 40 μm at its maximum size. The low-flavor protein composition can have an average particle size of about 10 μm to about 30 μm at its maximum size. The low-flavor protein composition can have an average particle size of about 10 μm to about 20 μm at its maximum size. The low-flavor protein composition can be in the form of an extrudate. The extrudate can be substantially in the form of granules. The granules can have an average maximum size of about 3 mm to about 5 mm. Less than about 20% (w / w) of the granules can have a maximum size of less than 1 mm. Less than about 5% (w / w) of the granules can have a maximum size of more than 1 cm. The extrudate can have a g / cm³ content of about 0.25 to about 0.4 g. 3The extrudate has a bulk density of about 5% to about 10%. The extrudate may have a protein content of about 65% to about 100% on a dry weight basis. The extrudate may have a fat content of less than about 1.0%. The extrudate may have a sugar content of less than about 1%. After hydration at room temperature for about 60 minutes, the extrudate may have a hydration ratio of about 2.5 to about 3. The extrudate may have a hydration time of less than about 30 minutes. The extrudate may have a pH of about 5.0 to about 7.5 when hydrated. The extrudate may have a bite strength of about 2000 g to about 4000 g at a hydration ratio of about 3. In some embodiments, the low-flavor protein composition has a protein dispersibility index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the low-flavor protein composition has a sodium level of up to about 1% w / w (e.g., up to about 0.5%, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w, or up to about 0.005% w / w). In some embodiments, the low-flavor protein composition has a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer. In some embodiments, the low-flavor protein composition exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C.In some embodiments, the storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C. The low-flavor protein composition may be a protein concentrate. The low-flavor protein composition may be a protein isolate.

[0132] This article also provides a food comprising a low-flavor protein composition produced by any of the methods described herein.

[0133] In another aspect, methods for preparing detoxifying protein compositions are provided. Such methods typically comprise: (a) adding an aqueous solution to a source protein composition to form a solution of dissolved proteins; (b) optionally removing solids from the solution of dissolved proteins; (c) adding an organic solvent to the solution of dissolved proteins to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form a detoxifying protein composition, wherein the detoxifying protein composition may comprise a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, and invertebrate proteins, wherein the source protein composition may be unsuitable for human consumption.

[0134] The implementation may include one or more of the following features: The source protein composition may contain one or more toxins in an amount sufficient to harm humans. The source protein composition may be a cotton poplar source protein composition. The source protein composition may contain more than 450 ppm of gossypol. The detoxifying protein composition may contain less than 450 ppm of gossypol. The detoxifying protein composition may contain less than 300 ppm of gossypol. The detoxifying protein composition may contain less than 100 ppm of gossypol. The detoxifying protein composition may contain less than 10 ppm of gossypol. In some embodiments, the detoxifying protein composition as described herein may contain one or more toxins in an amount less than that in the source protein composition. In some cases, the toxin content of the detoxifying protein composition may be less than about 90% of the toxin content of the source protein composition (e.g., less than about 70%, 50%, 30%, or 10%). Non-limiting examples of toxins include gossypol (e.g., in cotton poplar), vicine or convicine glycosides (e.g., in broad beans), cyanogenic glycosides (e.g., in cassava or bamboo), glucosinolates (e.g., in cruciferous vegetables), and glycoalkaloids (e.g., in potatoes and Solanum plants). Step (a) can be carried out at a pH of about 6.0 to about 9.0. Step (a) can be carried out at a pH of about 7.5 to about 8.5. Step (a) can be carried out at a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0). Step (b) may include centrifugation, filtration, or a combination thereof. Prior to step (c), the pH of the solution of dissolved proteins can be adjusted to about 4.0 to about 9.0. Prior to step (c), the pH of the solution of dissolved proteins can be adjusted to about 5.5 to about 7.5. Prior to step (c), the pH of the solution of dissolved protein can be adjusted to about 6.0 to about 7.0. Prior to step (c), the pH of the solution of dissolved protein can be adjusted to about 4.0 to about 7.0 (e.g., adjusted to about 4.0 to about 6.0, adjusted to about 4.5 to about 6.0, adjusted to about 4.5 or adjusted to about 6.0).In some embodiments, prior to step (c), the solution of dissolved protein is heated, for example for about 10 seconds to about 30 minutes (e.g., about 80°C to about 100°C, about 85°C to about 100°C, about 85°C to about 95°C, about 90°C to about 100°C, about 85°C to about 90°C, about 90°C to about 95°C, or about 95°C to about 100°C) at a temperature of about 70°C to about 100°C (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). In some embodiments, prior to step (C), the organic solvent and / or the solution of dissolved protein is cooled to a temperature of, for example, from about -20°C to about 10°C (e.g., from about -20°C to about 4°C). In some embodiments, prior to step (C), the solution of dissolved protein is heated and then cooled. Step (C) may include adding an organic solvent. Step (C) may include adding an organic solvent to a final concentration of about 5% to about 70% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 10% to about 50% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 20% to about 30% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 40% to about 90% (v / v) (e.g., a final concentration of about 40% to about 70% (v / v), a final concentration of about 40% to about 60% (v / v), or a final concentration of about 45% to about 55% (v / v)). pH may be adjusted by adding an acid. In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid. Step (d) may include centrifugation, filtration, or a combination thereof. The organic solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol). In some embodiments, the organic solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The method may further include (e) washing the low-flavor protein composition with an organic washing solvent. The method may further include (e) washing the low-flavor protein composition with an aqueous washing solvent. The method may further include (e) washing the low-flavor protein composition first with an organic washing solvent and then with an aqueous washing solvent, or vice versa.The organic washing solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol, or up to 20%, up to 15%, up to 10%, or up to 5% ethanol). In some embodiments, the organic washing solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The organic washing solvent in step (e) may be the same as the organic solvent in step (c). The aqueous washing solvent may be water. In some embodiments, the aqueous washing solvent may have a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0. In some embodiments, the aqueous washing solvent may contain a buffer. The method may further comprise drying the detoxified protein composition. Drying may comprise spray drying, pad drying, freeze drying, or oven drying. The source protein composition may be based on at least 90% by dry weight of a portion or derivative of a plant, algae, fungus, bacteria, protozoa, invertebrate, any one thereof, or a combination thereof.

[0135] In another aspect, methods for extracting small molecules from protein source compositions are provided. Such methods typically involve: (a) adding an aqueous solution to the source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; and (d) separating the solid phase and the liquid phase to form a solution rich in small molecules.

[0136] The implementation may include one or more of the following features: The source protein composition may be a soybean-derived protein composition. The solution rich in small molecules may contain isoflavones. The solution rich in small molecules may contain isoflavones, pigments (e.g., chlorophyll, anthocyanins, carotenoids, and betaine), flavor compounds (e.g., soybean flavor compounds), saponins, toxins (e.g., gossypol), natural products (e.g., plant natural products, pharmacologically active natural products), metabolites (e.g., primary metabolites and / or secondary metabolites), and / or phospholipids (e.g., lecithin). The small molecules may have a molecular weight of up to 900 Daltons (e.g., up to 800 Daltons, up to 700 Daltons, up to 600 Daltons, or up to 500 Daltons). Step (a) may be carried out at a pH of about 6.0 to about 9.0. Step (a) may be carried out at a pH of about 7.5 to about 8.5. Step (a) may be performed at a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0). Step (b) may include centrifugation, filtration, or a combination thereof. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 4.0 to about 9.0. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 5.5 to about 7.5. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 6.0 to about 7.0. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 4.0 to about 7.0 (e.g., adjusted to about 4.0 to about 6.0, adjusted to about 4.5 to about 6.0, adjusted to about 4.5, or adjusted to about 6.0). In some embodiments, prior to step (c), the dissolved protein solution is heated, for example for about 10 seconds to about 30 minutes (e.g., about 80°C to about 100°C, about 85°C to about 100°C, about 85°C to about 95°C, about 90°C to about 100°C, about 85°C to about 90°C, about 90°C to about 95°C, or about 95°C to about 100°C) at a temperature of about 70°C to about 100°C (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). In some embodiments, prior to step (C), the organic solvent and / or the solution of dissolved protein is cooled to a temperature of, for example, about -20°C to about 10°C (e.g., about -20°C to about 4°C). In some embodiments, prior to step (C), the solution of dissolved protein is heated and then cooled. Step (C) may include the addition of an organic solvent.Step (c) may include adding an organic solvent to a final concentration of about 5% (v / v) to about 70% (v / v). Step (c) may include adding an organic solvent to a final concentration of about 10% (v / v) to about 50% (v / v). Step (c) may include adding an organic solvent to a final concentration of about 20% (v / v) to about 30% (v / v). Step (c) may include adding an organic solvent to a final concentration of about 40% (v / v) to about 90% (v / v) (e.g., a final concentration of about 40% (v / v) to about 70% (v / v), a final concentration of about 40% (v / v) to about 60% (v / v), or a final concentration of about 45% (v / v) to about 55% (v / v). pH may be adjusted by adding an acid. In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid. Step (d) may include centrifugation, filtration, or a combination thereof. The organic solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol). In some embodiments, the organic solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The method may further include (e) washing the low-flavor protein composition with an organic washing solvent. The method may further include (e) washing the low-flavor protein composition with an aqueous washing solvent. The method may further include (e) washing the low-flavor protein composition first with an organic washing solvent and then with an aqueous washing solvent, or vice versa. The organic washing solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol, or up to 20%, up to 15%, up to 10%, or up to 5% ethanol). In some embodiments, the organic washing solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The organic washing solvent in step (e) may be the same as the organic solvent in step (c). The aqueous washing solvent may be water. In some embodiments, the aqueous washing solvent has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0. In some embodiments, the aqueous washing solvent may contain a buffer. The method may further comprise drying the low-flavor protein composition. Drying may comprise spray drying, pad drying, freeze drying, or oven drying. The source protein composition may be based on at least 90% by dry weight of a portion or derivative of any of plants, algae, fungi, bacteria, protozoa, invertebrates, or any of them, or a combination thereof.

[0137] In another aspect, food products are provided. Such food products optionally contain fat; optionally one or more flavor precursor compounds; and at least 10% by dry weight of a low-flavor protein composition comprising at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof, and wherein said variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially aggregated, denatured, or both.

[0138] The implementation scheme may include one or more of the following characteristics: The food may be plant-based. The food may be algae-based. The food may be fungus-based. The food may be invertebrate-based. The fat may comprise at least one fat selected from the group consisting of corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flaxseed oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango oil, cocoa butter, wheat germ oil, rice bran oil, and combinations thereof. One or more flavor precursors may include at least one compound selected from the group consisting of glucose, ribose, cysteine, cysteine ​​derivatives, thiamine, alanine, methionine, lysine, lysine derivatives, glutamic acid, glutamic acid derivatives, IMP, GMP, lactic acid, maltodextrin, creatine, alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, valine, linoleic acid, and mixtures thereof. Suitable flavor precursors may include sugars, sugar alcohols, sugar derivatives, oils (e.g., vegetable oils), free fatty acids, α-hydroxy acids, dicarboxylic acids, amino acids and their derivatives, nucleosides, nucleotides, vitamins, peptides, protein hydrolysates, extracts, phospholipids, lecithin, and organic molecules. The food may be a meat analogue. The food may be in the form of minced meat, sausage, or chunks of meat. The food product may be a dairy analogue (e.g., milk, fermented milk, yogurt, cream, butter, cheese, custard, ice cream, gelato, or frozen yogurt). The food product may be free of animal products. Fat may be present in the food at an amount of about 5% to about 80% of its dry weight. Fat may be present in the food at an amount of about 10% to about 30% of its dry weight. The food product may be fat-free. The food product may further contain about 0.01% to about 5% of heme-containing protein by dry weight. The food product may be a beverage (e.g., sports drinks, protein shakes, protein pills, energy drinks, caffeinated beverages, coffee beverages (e.g., milk coffee), milk, fermented milk, smoothies, carbonated beverages, alcoholic beverages, infant formula, or meal replacements). Fat may be present in the food at an amount of about 0.01% to about 5% of the beverage weight. This beverage may be fat-free. The low-flavor protein composition may have a brightness of at least 86 on a scale from 0 (black control value) to 100 (white control value). The low-flavor protein composition may have a luminance of at least 88 on a scale from 0 (black control value) to 100 (white control value). The low-flavor protein composition may have a chromaticity value of less than 14. The low-flavor protein composition may have a chromaticity value of less than 12. The low-flavor protein composition may have a chromaticity value of less than 10. The low-flavor protein composition may have a chromaticity value of less than 8.The low-flavor protein composition may have a color value of less than 6. The low-flavor protein composition may contain less than about 1.2% lipids on a dry weight basis (e.g., less than about 1.0% or less than about 0.5% lipids on a dry weight basis). The lipids may contain one or more of fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, or phospholipids. Various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof may be at least 90% soybean protein on a dry weight basis. The food may further contain at least one of preservatives, antioxidants, or shelf-life extenders. The low-flavor protein composition may be in the form of a solution, suspension, or emulsion. The low-flavor protein composition may be in the form of a solid or powder. The low-flavor protein composition may have an average particle size of about 5 µm to about 40 µm at its maximum size. The low-flavor protein composition can have an average particle size of about 10 µm to about 30 µm in maximum size. The low-flavor protein composition can have an average particle size of about 10 µm to about 20 µm in maximum size. The low-flavor protein composition can be in the form of an extrudate. The extrudate can be substantially in the form of granules. The granules can have an average maximum size of about 3 mm to about 5 mm. Less than about 20% (w / w) of the granules can have a maximum size of less than 1 mm. Less than about 5% (w / w) of the granules can have a maximum size of more than 1 cm. The extrudate can have a g / cm³ content of about 0.25 to about 0.4 g. 3The extrudate has a bulk density of about 5% to about 10%. The extrudate may have a protein content of about 65% to about 100% on a dry weight basis. The extrudate may have a fat content of less than about 1.0%. The extrudate may have a sugar content of less than about 1%. After hydration at room temperature for about 60 minutes, the extrudate may have a hydration ratio of about 2.5 to about 3. The extrudate may have a hydration time of less than about 30 minutes. The extrudate may have a pH of about 5.0 to about 7.5 when hydrated. The extrudate may have a bite strength of about 2000 g to about 4000 g at a hydration ratio of about 3. In some embodiments, the low-flavor protein composition has a protein dispersibility index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the low-flavor protein composition has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w, or up to about 0.005% w / w). The low-flavor protein composition may have a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in aqueous solutions (e.g., water) or beverages. The aqueous solutions or beverages may have a pH of about 4.5 to about 8.0, about 4.5 to about 7.0, about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer. In some embodiments, the low-flavor protein composition exhibits temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C.In some embodiments, the storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C. The low-flavor protein composition may be a protein concentrate. The low-flavor protein composition may be a protein isolate.

[0139] In another aspect, methods for preparing food products are provided. Such methods typically involve combining fats, one or more optional flavor precursor compounds, and a low-flavor protein composition, said low-flavor protein composition being produced by a method comprising: (a) adding an aqueous solution to the source protein composition to form a solution of dissolved proteins; (b) optionally removing solids from the solution of dissolved proteins; (c) adding an organic solvent to the solution of dissolved proteins to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form the low-flavor protein composition.

[0140] In another aspect, methods for reducing perceived protein source flavor in plant-based foods are provided. Such methods typically involve combining fat, one or more flavor precursor compounds, and a low-flavor protein composition, said low-flavor protein composition being produced by a method comprising: (a) adding an aqueous solution to the source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form the low-flavor protein composition, wherein at least 5% by weight of the protein content in the food may contain the low-flavor protein composition, thereby reducing the perceived protein source flavor in the food compared to foods with similar protein content but lacking the low-flavor protein composition.

[0141] The implementation may include one or more of the following features: Step (a) may be performed at a pH of about 6.0 to about 9.0. Step (a) may be performed at a pH of about 7.5 to about 8.5. Step (a) may be performed at a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0). Step (b) may include centrifugation, filtration, or a combination thereof. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 4.0 to about 9.0. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 5.5 to about 7.5. Prior to step (c), the pH of the solution of dissolved protein may be adjusted to about 6.0 to about 7.0. Prior to step (c), the pH of the solution of dissolved protein can be adjusted to about 4.0 to about 7.0 (e.g., to about 4.0 to about 6.0, to about 4.5 to about 6.0, to about 4.5 or to about 6.0). In some embodiments, prior to step (c), the solution of dissolved protein is heated, for example for about 10 seconds to about 30 minutes (e.g., about 80 degrees Celsius to about 100 degrees Celsius, about 85 degrees Celsius to about 100 degrees Celsius, about 85 degrees Celsius to about 95 degrees Celsius, about 90 degrees Celsius to about 100 degrees Celsius, about 85 degrees Celsius to about 90 degrees Celsius, about 90 degrees Celsius to about 95 degrees Celsius, or about 95 degrees Celsius to about 100 degrees Celsius) at a temperature of about 70 degrees Celsius to about 100 degrees Celsius (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). In some embodiments, prior to step (C), the organic solvent and / or the solution of dissolved protein is cooled to a temperature of, for example, about -20°C to about 10°C (e.g., about -20°C to about 4°C). In some embodiments, prior to step (C), the solution of dissolved protein is heated and then cooled. Step (C) may include adding an organic solvent. Step (C) may include adding an organic solvent to a final concentration of about 5% (v / v) to about 70% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 10% (v / v) to about 50% (v / v). Step (C) may include adding an organic solvent to a final concentration of about 20% (v / v) to about 30% (v / v).Step (c) may include adding an organic solvent to a final concentration of about 40% (v / v) to about 90% (v / v) (e.g., to a final concentration of about 40% (v / v) to about 70% (v / v), about 40% (v / v) to about 60% (v / v), or about 45% (v / v) to about 55% (v / v). The pH may be adjusted by adding an acid. In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid. Step (d) may include centrifugation, filtration, or a combination thereof. The organic solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol). In some embodiments, the organic solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The method may further include (e) washing the low-flavor protein composition with an organic washing solvent. The method may further include (e) washing the low-flavor protein composition with an aqueous washing solvent. The method may further include (e) washing the low-flavor protein composition first with an organic washing solvent and then with an aqueous washing solvent, or vice versa. The organic washing solvent may be ethanol (e.g., at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, at least 99.5%, or 100% ethanol, or up to 20%, up to 15%, up to 10%, or up to 5% ethanol). In some embodiments, the organic washing solvent is selected from the group consisting of ethanol, propanol, isopropanol, methanol, and acetone. The organic washing solvent in step (e) may be the same as the organic solvent in step (c). The aqueous washing solvent may be water. In some embodiments, the aqueous washing solvent has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0. In some embodiments, the aqueous washing solvent may contain a buffer. The method may further include drying the low-flavor protein composition. Drying may include spray drying, pad drying, freeze drying, or oven drying. The source protein composition may be based on at least 90% by dry weight of a portion or derivative of any of plants, algae, fungi, bacteria, protozoa, invertebrates, or any of them, or a combination thereof. The food may be plant-based. The food may be algae-based. The food may be fungi-based. The food may be invertebrate-based. The fat may comprise at least one fat selected from the group consisting of corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flaxseed oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango oil, cocoa butter, wheat germ oil, rice bran oil, and combinations thereof.One or more flavor precursors include at least one compound selected from the group consisting of glucose, ribose, cysteine, cysteine ​​derivatives, thiamine, alanine, methionine, lysine, lysine derivatives, glutamic acid, glutamic acid derivatives, IMP, GMP, lactic acid, maltodextrin, creatine, alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, valine, linoleic acid, and mixtures thereof.

[0142] In any embodiment of this document, the preservative, antioxidant, or shelf-life extender may comprise at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglyceride or diglyceride, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin. Lecithin citrate, Leuconostoc mesylate, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0143] As used herein, “low-flavor” in relation to a protein composition means that the protein composition has less flavor than its source (e.g., soybean, if a soybean protein composition is described). For example, less (e.g., no more than 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of one or more compounds produces a distinctive flavor associated with the protein source. In some embodiments, a low-flavor protein composition may have almost no flavor of its own. In some cases, a low-flavor protein composition has less flavor than known protein compositions (e.g., commercial soybean protein isolates, such as those described herein). Less flavor can be determined, for example, by a trained human expert panel, or, for example, by measuring one or more volatile compounds that are generally understood to contribute flavor and / or aroma. In some embodiments, a low-flavor protein composition may have a discriminability index of at least 1.0 (e.g., at least 1.5, 2.0, 2.5, or 3.0). In some embodiments, when evaluated by a trained descriptive team using the Spectrum method, the low-flavor protein composition is described as having low intensity of one or more of the following: oxidized / putrid flavor, cardboard flavor, astringent flavor, bitter flavor, vegetable complex flavor, and sweet fermented flavor. In some embodiments, when evaluated by a trained descriptive team using the Spectrum method, the low-flavor protein composition is described as having low intensity of one or more of the following: bean flavor, fatty flavor, green flavor, pea flavor, earthy flavor, hay-like flavor, grass flavor, putrid flavor, leaf flavor, cardboard flavor, spicy flavor, pungent flavor, medicinal flavor, metallic flavor, and broth flavor.

[0144] As used herein, "low color" in the context of a protein composition means that the protein composition has a lighter color than its source (e.g., soybean, if a soybean protein composition is described). For example, fewer of one or more compounds that produce color in the protein. In some embodiments, a low-color protein composition may have very little of its own color. In some cases, a low-color protein composition has less color than known protein compositions (e.g., commercial soybean protein isolates, such as those described herein). Having less color can be determined, for example, by measuring the lightness and / or chromaticity of the protein composition. In some embodiments, a low-color protein composition may have a lightness value of at least about 86 (e.g., at least about 88, 90, 92, or 94). In some embodiments, a low-color protein composition may have a chromaticity value of less than about 12 (e.g., less than about 10, 8, or 6).

[0145] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. Although the invention may be practiced with similar or equivalent methods and materials to those described herein, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated herein by reference in their entirety. In case of conflict, this specification (including definitions) shall prevail. Furthermore, materials, methods, and examples are illustrative only and are not intended to be limiting.

[0146] Details of one or more embodiments of this disclosure are set forth in the accompanying drawings and the following description. Other features, objects, and advantages of the invention will be apparent from the description and drawings and the claims. The word "comprising" in the claims may be replaced by "consistently consisting of" or "comprises of" according to standard patent law practice. Attached Figure Description

[0147] Figure 1A This is an exemplary flowchart for preparing a protein composition according to some embodiments.

[0148] Figure 1B This is an exemplary flowchart for preparing a protein composition according to some embodiments.

[0149] Figure 1C Exemplary phospholipid contents of protein compositions prepared according to some embodiments are shown.

[0150] Figure 1D Exemplary protein contents in the supernatant according to some embodiments are shown.

[0151] Figure 1E This is an exemplary flowchart for preparing proteins according to some embodiments.

[0152] Figure 2A Exemplary data are shown on the production of several soy flavor compounds when the exemplary SPI produced as described herein is cooked in a flavor broth (referred to as FLB_EtOH), compared to commercial products cSPC-1 and cSPI-1, as well as a flavor broth control (FLB) alone.

[0153] Figure 2B Exemplary data are shown on the production of several meat flavor compounds when the exemplary SPI produced as described herein is cooked in flavored broth (FLB_EtOH), compared with commercial products cSPC-1 F and cSPI-1, as well as a flavored broth control (FLB) alone.

[0154] Figure 2CExemplary data on the production of several soybean flavor compounds, compared to commercial products cSPI-1, cSPI-2, cSPC-1, and cSPC-2, are shown when exemplary SPI (pureSPI, pureSPI) and exemplary SPC (pureSPC, pureSPC) produced as described herein are each cooked in water.

[0155] Figure 2D Exemplary data are shown on the production of several soy flavor compounds when the exemplary SPI and exemplary SPC produced as described herein are each cooked in flavor broth (FLB_purified SPI and FLB_purified SPC, respectively), compared with commercial products cSPI-1, cSPI-2, cSPC-1 and cSPC-2, and a separate flavor broth control (FLB).

[0156] Figure 3A Exemplary genistein contents of some exemplary protein compositions produced as described herein are shown.

[0157] Figure 3B Exemplary daidzein content is shown for some exemplary protein compositions produced as described herein.

[0158] Figure 3C Exemplary daidzein contents of some exemplary protein compositions produced as described herein are shown.

[0159] Figure 4A A comparison is shown against a black background of two commercial SPCs (cSPC-1 and cSPC-2), two commercial SPIs (cSPI-1 and cSPI-2), an exemplary SPC (purified SPC) produced as described herein, and an exemplary SPI (purified SPI) produced as described herein.

[0160] Figure 4B A comparison is shown of two commercial SPCs (cSPC-1 and cSPC-2), two commercial SPIs (cSPI-1 and cSPI-2) on a white background, an exemplary SPC (purified SPC) produced as described herein, and an exemplary SPI (purified SPI) produced as described herein.

[0161] Figure 4C A comparison is shown on a white and black background of commercial rapeseed protein isolate (cRPI) and exemplary RPI (purified RPI) produced as described herein.

[0162] Figure 4D A comparison is shown between starch, several commercial protein products, and an exemplary SPI (purified SPI) produced as described herein.

[0163] Figure 4E A comparison of starting materials (top row) with exemplary protein compositions (bottom row) produced as described herein, comprising protein compositions derived from soybean, pea, canola seed, and spinach, is shown.

[0164] Figure 4F The diagram shows a comparison of starting materials (top row) with exemplary protein compositions (bottom row) produced as described herein, including protein compositions derived from crickets, mealworms, beef, and yeast.

[0165] Figure 4G A comparison of the colors of exemplary protein compositions produced as described herein and subjected to different drying methods is shown.

[0166] Figure 4H A comparison of the colors of exemplary protein compositions produced under various conditions as described herein is shown.

[0167] Figure 5A This is a bar chart of brightness data for various commercial protein products and exemplary corresponding protein compositions produced as described herein.

[0168] Figure 5B This is a bar chart of chromaticity data for various commercial protein products and exemplary corresponding protein compositions produced as described herein.

[0169] Figure 6A The conditions for a six-point test (hexadtest) for evaluating exemplary protein compositions produced as described herein are shown.

[0170] Figure 6B It shows Figure 6A A bar chart showing the results of the six-point test.

[0171] Figure 7 An exemplary milk-based beverage is shown, produced using a commercial soy protein isolate (cSPI-2) and an exemplary protein isolate (purified SPI) produced as described herein.

[0172] Figure 8A Microscopic images of an exemplary protein composition precipitated by ethanol (left) and an exemplary protein composition precipitated by acid (right) are shown.

[0173] Figure 8B Exemplary particle size distribution data are shown for an exemplary protein composition precipitated by ethanol (single peak) and an exemplary protein composition precipitated by acid (bipeak).

[0174] Figure 9AThe storage modulus and loss modulus of purified SPI by cold precipitation are shown as a function of temperature cycling from 25°C to 95°C.

[0175] Figure 9B The storage modulus and loss modulus of purified SPI precipitated at room temperature are shown as a function of temperature cycling from 25°C to 95°C.

[0176] Figure 9C The storage modulus of purified SPI precipitated at room temperature, purified SPI precipitated by cold precipitation, and commercial cSPI-3 are shown in the temperature range of 25°C to 95°C.

[0177] Figure 10 A bar chart showing sodium levels in two commercial SPIs (cSPI-1 and cSPI-3) and an exemplary SPI (purified SPI) produced as described herein is presented.

[0178] Figure 11 Bar charts are shown for two commercial SPIs (cSPI-2 and cSPI-3), three replicas of purified SPI, and the contents of isoflavones, soy saponins, and phosphatidylcholine-36:4 in soybean flour. The y-axis is in ppm. Detailed Implementation

[0179] This document relates to materials and methods for protein production. In particular, it relates to materials and methods for producing proteins using precipitation. In general, this document provides protein compositions and methods and materials for purifying proteins, thereby producing protein compositions that can be used, for example, in food products, such as meat and dairy derivatives or substitutes.

[0180] Unless otherwise stated, when percentages are given in this document, they are percentages on a dry weight basis.

[0181] As used herein, the term “about” has its usual meaning in the context of effort to allow for reasonable variation in quantities that can achieve the same effect, and in this document also refers to a value plus or minus 10% of the given value. For example, “about 20” means or includes quantities from 18 to 22 and including 22.

[0182] The protein compositions described herein (e.g., low-flavor protein isolates or low-color protein compositions) can be produced from any suitable protein source composition. Non-limiting examples of protein source compositions include parts or derivatives of plants, algae, fungi, bacteria, protozoa, invertebrates, and any of them. As used herein, a “part” of plants, algae, fungi, bacteria, protozoa, and invertebrates comprises fragments of these, such as leaves or stems of plants, or legs of invertebrates. As used herein, a “derivative” of plants, algae, fungi, bacteria, protozoa, and invertebrates comprises products derived from these, such as freeze-dried plant leaves, commercial soy protein powder, concentrates or isolates, or invertebrate powders.

[0183] Non-limiting examples of suitable plants include cotton poplar (e.g., Celtis conferta), cottonseed (the seeds of cotton plants, e.g., upland cotton (Gossypium hirsutum), island cotton (Gossypium barbadense), Asian cotton (Gossypium arboretum), herbaceous cotton (Gossypium herbaceum), etc.), soybean (e.g., soybean (Glycinemax)), carob tree (e.g., Fabaceae sp.), peanut (e.g., peanut (Arachis hypogaea)), mesquite tree (e.g., mesquite genus (Prosopis sp.)), lupin (e.g., lupinus sp.)), lentil (e.g., lentil (Lens culinaris), lentil (Lens esculenta), etc.), tamarind tree (e.g., tamarind (Tamarindus indica)), chickpea (e.g., chickpea (Cicer)). arietinum), farrow (e.g., cultivated emmer wheat (Triticum turgidum dicoccum)), spelt wheat (e.g., spelt wheat (Triticum aestivum spelta)), pea (e.g., pea (Pisum sativum)), alfalfa (e.g., purple alfalfa (Medicago sativa)), clover (e.g., clover (Trifolium sp.)), legumes (e.g., from the Fabaceae family), hemp (e.g., hemp (Cannabis sativa)), hemp seeds (the seeds of the hemp plant), sea pea (e.g., Salicornia sp.)), rye (e.g., rye (Secale cereal)), sorghum (e.g., sorghum spp.)), teff (e.g., teff (Eragrostis tef)), freekeh (e.g., durum wheat variety (Triticum turgidum var.)). Quinoa (e.g., *Chenopodium quinoa*), rice (e.g., *Oryza sativa*), buckwheat (e.g., *Fagopyrum esculentum*), amaranth (e.g., *Amaranthus cruentus*), barley (e.g., *Hordeum vulgare*), maize (e.g., *Zea mays*), and broken wheat (e.g., *Triticum ssp.*).(e.g., *Triticum monococcum*), wheat (e.g., *Triticum aestivum*, *Triticum turgidum*, etc.), wild rice (e.g., *Zizania* spp.), Khorasan cereals (e.g., *Triticum turgidum turanicum*), millet (e.g., *Panicum miliaceum*, *Pennisetum glaucum*, *Setaria italica*, *eleusine coracana*, *digitaria exilis*, etc.), chia seeds (e.g., *Salvia hispanica*), oats (e.g., *Avena sativa*), triticale (e.g., *Triticosecale*), alfalfa, cassava (e.g., *Manihot esculenta*), lentils (*lablab*). Beans (e.g., lentils (Lablab purpureus)), moringa, cabbage (e.g., kale (Brassica oleracea)), stinging nettles (e.g., Urtica dioica)), mosses (from the Bryophyta sensu stricto family), bamboo (e.g., from the Bambusoideae subfamily), etc. Plants can include legumes and legumes.

[0184] Non-limiting examples of suitable algae include cyanobacteria (e.g., blue-green algae) such as Spirulina (e.g., Arthrospira platensis, Arthrospira maximus, etc.), species from the genus Chlorella, and Aphanizomenon flos-aquae. Some algae are multicellular and include seaweed such as Rhodophyta (red algae), Chlorophyta or Charophyta / Chainella (green algae), and Phaeophyta (brown algae). Some examples of red algae may include species from the genus Porphyra (laminaria) and Palmaria palmate (dulse). Some examples of green algae include *Caulerpa lentillifera* (seagrapes), *Ulva lactuca* (sea lettuce), and *Chlamydomonas reinhardtii*. Some examples of brown algae include *Macrocystis* (kelp), *Sargassum* (seaweed mats), brown algae from the Fucophyales order, and *Ascophyllum nodosum* (e.g., giant kelp).

[0185] Non-limiting examples of suitable fungi include brewer's yeast (e.g., nutritional yeast, brewer's yeast, etc.), *Brettanomyces bruxellensis*, *Brettanomyces anomalus*, *Brettanomyces custersianus*, *Brettanomyces naardenensis*, *Brettanomyces nanus*, *Dekkera bruxellensis*, *Dekkera anomala*, *Candidastellata*, *Schizosaccharomyces pombe*, *Torulaspora delbrueckii*, *Zygosaccharomyces bailii*, *Pichia pastoris* (in some cases, also known as *Komagataella phaffii*, *K. pastoris*). (Pasteurella pastoris or K. pseudopastoris). Some suitable fungi may contain cell proteins derived from Fusarium venenatum.Other suitable types of fungi can include edible mushroom species, such as Agaricus bisporus, Pleurotus ostreatus, Lentinula edodes, Auricularia auricula-judae, Volvariella volvacea, Flammulina velutipes, Tremella fuciformis, Hypsizygus tessellatus, Stropharia rugosoannulata, Cyclocybe aegerita, Hericium erinaceus, Boletus edulis, Calbovista subsculpta, Calvatiagigantean, Cantharellus cibarius, Craterellus tubaeformis, and Clitocybe. The following fungi are listed: *Craterellus cornucopioides*, *Grifola frondosa*, *Gyromitraesculenta*, *Hericium erinaceus*, *Hydnum repandum*, *Lactarius deliciosus*, *Morchella*, *Pleurotus ostreatus*, *Tricholoma matsutake*, and *Tuber* sp., among others.

[0186] Non-limiting examples of suitable bacteria include methanogenic bacteria capable of producing syngas fermentation (e.g., Methylococcus capsulatus), Methylophilus methylotrphus, Rhodobacter capsulatus bacterial species (e.g., Homoacetobacter spp.), and so on. Some examples of suitable bacteria can be bacterial species capable of producing single-cell proteins, such as Bacillus cereus, Bacillus licheniformis, Bacillus pumilis, Bacillus subtilis, Corynobacterium ammoniagenes, Corynebacterium glutamicum, Cupriavidus necator, Escherichia coli, IRU1 halophilic bacteria, Ralstonia sp., Brevibacillus sagri, Aneurunibacillus sp., Methylomonas sp., Rhizosperic diazotrophs, Rhodopseudomonas palustris, and so on.

[0187] Non-limiting examples of suitable protozoa include Trichomonas, Pyrsonympha, Trichomonas, Isotricha, Entodinium, and so on.

[0188] Non-limiting examples of suitable invertebrates include spider species (e.g., the Thai zebra-legged spider (Haplopelma albostriatum), other arthropods such as scorpions (e.g., Typhlochactasmitchelli, Heterometrus swammerdami, etc.), crickets (e.g., from Orthoptera), ants (e.g., from Hymenoptera), silkworms and / or moths (e.g., from Lepidoptera), beetles (e.g., from Coleoptera), flies (e.g., from Diptera), etc.

[0189] In one aspect, this document provides a method for preparing a protein composition. In some embodiments, the protein composition may be a protein concentrate. In some embodiments, the protein composition may be a protein isolate. In some embodiments, the protein composition may be a low-flavor protein isolate. In some embodiments, the protein composition may be a low-color protein composition. In some embodiments, the protein composition may be a low-color protein composition as a protein concentrate. In some embodiments, the protein composition may be a low-color protein composition as a protein isolate. In some embodiments, the protein composition may be a low-flavor and low-color protein composition as a protein isolate.

[0190] In some cases, the methods described herein may include one or more steps or conditions that contribute to maintaining and / or increasing the function of the protein in the protein composition. As described herein, functional proteins may have one or more (e.g., two or more, three or more, four or more, or five or more) of the following properties: a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15); and a concentration up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w, or up to about 0.005%). The aqueous solution has the following characteristics: a sodium content (w / w); a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water), wherein the aqueous solution may have a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0; and / or the aqueous solution may contain a buffer; and the aqueous solution can be heated within a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). Exhibiting temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity), wherein the temperature-dependent change can be at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold) and the temperature-dependent change can be substantially irreversible (e.g., when cooling within the same temperature range, the magnitude of the change can be up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.5% of the magnitude observed when heating).1%), with a storage modulus and / or loss modulus reaching a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C; a storage modulus and / or loss modulus reaching a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C; and a viscosity reaching a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 1. ... The values ​​of Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s, and / or the viscosity at 95°C reaching at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s); and the ability to form a gel upon heating (e.g., at a pH of about 7.0, about 25 to about 250 mg / mL (e.g., about 25 mg / mL to about 50 mg / mL, about 25 mg / mL to about 100 mg / mL)). Suspensions of approximately 25 mg / mL to approximately 150 mg / mL, approximately 25 mg / mL to approximately 200 mg / mL, approximately 50 mg / mL to approximately 250 mg / mL, approximately 100 mg / mL to approximately 250 mg / mL, approximately 150 mg / mL to approximately 250 mg / mL, or approximately 200 mg / mL to approximately 250 mg / mL; thermally transforming into a gel upon heating to approximately 65°C; thermally denaturing during incubation at approximately 50°C to approximately 85°C, wherein more than approximately 80% of the protein is denatured after approximately 20 minutes at approximately 85°C, as measured by differential scanning calorimetry (DSC) or differential scanning fluorescence assay (DSF); in a solution or suspension of purified protein at approximately 50 mg / mL (5% w / v) or higher than approximately 50 mg / mL (5% w / v), the protein forms an independent gel (with, for example, 100 mg / mL) upon heating at approximately 85°C or higher for approximately 20 minutes. (Pa storage modulus); can be measured from about pH 5.5 to about pH 10.0% denaturation and gelation; can denature and gel in solutions with an ionic strength (I) below about 0.5 M, when I is calculated based on the concentration of non-protein solutes; particle size distributions D10, D50, and D90 are less than about 0.1 µm, 1.0 µm, and 5 µm, respectively, at a protein concentration of about 10 mg / mL; exhibits enzymatic activity; or has a particle size distribution greater than or equal to about 50 μm in a pH range from about 4.0 to about 8.0. 2 Emulsion activity index (EAI) of / g protein.

[0191] In some embodiments, a method for preparing a protein composition includes: (a) adding an aqueous solution to a source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; and (d) separating the solid phase and the liquid phase to form a protein composition comprising a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins (e.g., insects and / or arachnids) proteins, or combinations thereof.

[0192] In some embodiments of any of the methods described herein, an aqueous solution may be added to the source protein composition to form a dissolved protein. In some embodiments, the protein composition may be in the form of a solid (e.g., powder), suspension, solution, or emulsion. In some embodiments, the aqueous solution may be water. In some embodiments, the aqueous solution may contain a buffer. The buffer may be any food-grade buffer (e.g., a buffer containing sodium phosphate, potassium phosphate, calcium phosphate, sodium acetate, potassium acetate, sodium citrate, calcium citrate, sodium bicarbonate, sodium lactate, potassium lactate, sodium malate, potassium malate, sodium gluconate, and / or potassium gluconate) at a concentration of about 2 mM to about 200 mM (e.g., about 2 mM to about 10 mM, about 10 mM to about 20 mM, about 10 mM to about 30 mM, about 20 mM to about 30 mM, about 30 mM to about 40 mM, about 40 mM to about 50 mM, about 50 mM to about 100 mM, or about 100 mM to about 200 mM). The aqueous solution may contain any other suitable components (e.g., salts, such as sodium chloride or potassium chloride).

[0193] The source protein composition can be any suitable source protein composition. In some embodiments, the source protein composition can be based on at least 90% by dry weight of a portion or derivative of plants, algae, fungi, bacteria, protozoa, invertebrates, or any of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of plants, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of algae, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of fungi, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of bacteria, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of protozoa, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be based on at least 90% by dry weight of invertebrates, any portion or derivative of them, or a combination thereof. In some embodiments, the source protein composition can be defatted. In some embodiments, the source protein composition can be flour or flakes (e.g., white soybean flakes). In some embodiments, the source protein composition may be based on defatted soy flour, defatted pea flour, or a combination thereof, with a dry weight of at least 90%.

[0194] In some embodiments, the solution of dissolved protein may have a pH of about 4.0 to about 9.0 (e.g., about 4.0 to about 8.0, about 4.0 to about 7.0, about 4.0 to about 6.0, about 4.0 to about 5.0, about 5.0 to about 9.0, about 6.0 to about 9.0, about 7.0 to about 9.0, about 8.0 to about 9.0). In some embodiments, the aqueous solution may have a pH of about 7.5, about 8.0, or about 8.5. In some embodiments, the solution of dissolved protein may have a pH of about 6.0 to about 9.0. In some embodiments, the solution of dissolved protein may have a pH of about 7.5 to about 8.5. In some embodiments, the solution of dissolved protein may have a pH of about 7.0 to about 11.0 (e.g., about 7.0 to about 10.0, about 8.0 to about 10.0, about 8.0 to about 9.0, or about 8.0).

[0195] In some cases, the pH may fall within this range without adjustment. For example, the pH may fall within this range in response to the addition of an aqueous solution to the source protein to produce a solution of dissolved protein. In some cases, the pH may be adjusted to fall within this range. In some embodiments, an acid (e.g., hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, lactic acid, etc.) may be added to the solution of dissolved protein to lower the pH. In other embodiments, a base (e.g., potassium hydroxide, sodium hydroxide, etc.) may be added to the solution of dissolved protein to increase the pH. In other embodiments, the pH may fall within the range in response to a combination of acid and base added to the solution of dissolved protein. In other embodiments, the pH may be maintained within the range in response to a buffer (e.g., [tris(hydroxymethyl)methylamino]propanesulfonic acid, 2-(bis(2-hydroxyethyl)amino)acetic acid, etc.) added to the solution of dissolved protein.

[0196] In some embodiments, the pH of the solution of dissolved protein can be adjusted by adding an acid and / or a base. In some embodiments, the pH of the solution of dissolved protein can be adjusted to about 4.0 to about 9.0 (e.g., about 4.0 to about 8.0, about 4.0 to about 7.0, about 4.0 to about 6.0, about 4.0 to about 5.0, about 5.0 to about 9.0, about 6.0 to about 9.0, about 7.0 to about 9.0, about 8.0 to about 9.0). In some embodiments, the pH of the solution of dissolved protein can be adjusted to about 4.0 to about 5.0. In other embodiments, the pH of the solution of dissolved protein can be adjusted to about 4.5. In some embodiments, the pH of the solution of dissolved protein can be adjusted to about 5.5 to about 7.5. In other embodiments, the pH of the solution of dissolved protein can be adjusted to about 5.5 to about 6.5. In some embodiments, the pH of the solution of dissolved protein can be adjusted to about 6.0 to about 7.0. In some embodiments, the pH of the solution of dissolved proteins can be adjusted to about 5.5, 6.0, 6.5 or 7.0.

[0197] Optionally, solids can be removed from the solution of dissolved proteins. Solids can be removed by any suitable method. In some embodiments, solids can be removed by centrifugation, filtration, or a combination thereof. In some embodiments, solid removal may include avoiding agitation for a threshold time period and aspirating the liquid portion from the solution of dissolved proteins. For example, the solution of dissolved proteins may be left undisturbed for a threshold time period such that any solids from the solution of dissolved proteins settle to the bottom of the container. In this case, liquid may be aspirated from the solution of dissolved proteins to remove the liquid from the solids settled to the bottom of the container. In some instances, avoiding agitation for a threshold time period may be combined with other methods such as centrifugation and / or filtration. Specifically, in some instances, the solution of dissolved proteins may be left undisturbed for a threshold time period, the liquid portion may be removed from the undisturbed solution of dissolved proteins, and filtration and / or centrifugation may be performed to further remove solids from the solution of dissolved proteins.

[0198] In some embodiments, the solution of dissolved protein may be heated before adding organic solvents and / or acids to the solution of dissolved protein. Without being bound by any particular theory, it is believed that heating the solution of dissolved protein can lead to the formation of larger protein structures (e.g., larger flocs, or aggregates of particles with a cheese-curd-like structure) and / or disrupt intermolecular interactions between proteins and other components (e.g., fats, carbohydrates, or small molecules such as flavor compounds or pigments). The solution of dissolved protein may be heated for any suitable amount of time, for example, from about 10 seconds to about 30 minutes (e.g., about 10 seconds to about 20 minutes, about 10 seconds to about 30 seconds, about 10 seconds to about 1 minute, about 10 seconds to about 2 minutes, about 10 seconds to about 5 minutes, about 10 seconds to about 10 minutes, about 10 seconds to about 15 minutes, about 30 seconds to about 20 minutes, about 1 minute to about 30 minutes, about 1 minute to about 20 minutes, about 2 minutes to about 20 minutes, about 5 minutes to about 20 minutes, about 10 minutes to about 20 minutes, or about 15 minutes to about 20 minutes). The solution of dissolved protein can be heated at any suitable temperature, for example, from about 70°C to about 100°C (e.g., from about 80°C to about 100°C, from about 85°C to about 100°C, from about 85°C to about 95°C, from about 90°C to about 100°C, from about 85°C to about 90°C, from about 90°C to about 95°C, or from about 95°C to about 100°C).

[0199] In some embodiments, the solution of dissolved protein and / or organic solvent may be cooled before the organic solvent and / or acid are added to the solution of dissolved protein. The solution of dissolved protein and / or organic solvent may be cooled to a temperature of, for example, about -20°C to about 10°C (e.g., about -20°C to about 4°C). In some embodiments, the solution of dissolved protein is heated and then cooled before the organic solvent and / or acid are added to the solution of dissolved protein.

[0200] An organic solvent can be added to a solution of dissolved protein. Adding an organic solvent can form a solid phase (e.g., a protein composition) from the liquid phase of the solution of dissolved protein (e.g., a precipitation). Non-limiting examples of suitable organic solvents may include methanol, propanol, isopropanol, EtOH (ethanol), and acetone. For example, an organic solvent can be added to about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) to about 70% (v / v), about 20% (v / v) to about 70% (v / v), about 20% (v / v) to about 70% (v / v), or about 5% (v / v) to about 70% (v / v). The final concentrations of approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40% or approximately 50% (v / v) to approximately 60% (v / v). In some embodiments, methanol may be added to about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) to about 70% (v / v), about 20% (v / v) The final concentrations of approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40%, or approximately 50% (v / v) to approximately 60% (v / v).In some embodiments, isopropanol may be added to about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) to about 70% (v / v), about 20% (v / v) to about 70% (v / v), or about 5% (v / v) to about 70% (v / v). The final concentrations of approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40% (v / v), or approximately 50% (v / v) to approximately 60% (v / v). In some embodiments, EtOH may be added to about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) to about 70% (v / v), about 20% (v / v) The final concentrations of approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40% (v / v), or approximately 50% (v / v) to approximately 60% (v / v).In some embodiments, acetone may be added to about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) to about 70% (v / v), about 20% (v / v) The final concentrations of approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40%, or approximately 50% (v / v) to approximately 60% (v / v). In some embodiments, the pH of the solution of dissolved proteins may be about 6.0, and the final concentration of the organic solvent (e.g., ethanol) may be about 5% (v / v) to about 70% (v / v) (e.g., about 5% (v / v) to about 10% (v / v), about 5% (v / v) to about 20% (v / v), about 5% (v / v) to about 30% (v / v), about 5% (v / v) to about 40% (v / v), about 5% (v / v) to about 50% (v / v), about 5% (v / v) to about 60% (v / v), about 10% (v / v) The concentrations of the dissolved protein solution can be approximately 70% (v / v), approximately 20% (v / v) to approximately 70% (v / v), approximately 30% (v / v) to approximately 70% (v / v), approximately 40% (v / v) to approximately 70% (v / v), approximately 50% (v / v) to approximately 70% (v / v), approximately 60% (v / v) to approximately 70% (v / v), approximately 20% (v / v) to approximately 50% (v / v), approximately 20% (v / v) to approximately 30% (v / v), approximately 30% (v / v) to approximately 40%, or approximately 50% (v / v) to approximately 60% (v / v). In some embodiments, the pH of the solution of dissolved protein can be approximately 6.0, and the final concentration of the organic solvent (e.g., ethanol) can be approximately 50%. In some embodiments, the pH of the solution of dissolved protein can be approximately 4.5 to approximately 6.0, and the final concentration of the organic solvent (e.g., ethanol) can be approximately 40% to approximately 70%. In some embodiments, the pH of the solution of dissolved protein may be about 6.0, and the final concentration of the organic solvent (e.g., ethanol) may be about 40% to about 70%. In some embodiments, the pH of the solution of dissolved protein may be about 4.5, and the final concentration of the organic solvent (e.g., ethanol) may be about 25% (v / v). In some embodiments, the organic solvent does not contain carbon dioxide (e.g., supercritical carbon dioxide).

[0201] Organic solvents can be added to a solution of dissolved proteins at any suitable temperature. In some embodiments, the organic solvent can be added to the solution of dissolved proteins at approximately ambient temperature (e.g., room temperature). In some embodiments, the organic solvent can be added to the solution of dissolved proteins at a temperature of about 10°C to about 25°C (e.g., about 10°C to about 15°C, about 10°C to about 20°C, about 15°C to about 25°C, or about 20°C to about 25°C). In some embodiments, the organic solvent can be cooled. Without being bound by any particular theory, it is believed that using frozen organic solvents may help preserve some of the protein's functions. In some embodiments, the organic solvent can be added to the solution of dissolved proteins at a temperature of about -20°C to about 10°C (e.g., about -20°C to about -10°C, about -20°C to about 0°C, about -20°C to about 4°C, about -10°C to about 10°C, about 0°C to about 10°C, or about 4°C to about 10°C).

[0202] An acid may be added to a solution of dissolved protein. The addition of the acid can form a solid phase (e.g., a precipitate) from the liquid phase of the solution of dissolved protein (e.g., a protein composition). In some embodiments, the acid is selected from the group consisting of hydrochloric acid, acetic acid, citric acid, tartaric acid, malic acid, folic acid, fumaric acid, and lactic acid. In some embodiments, the acid is hydrochloric acid.

[0203] When an organic solvent and / or acid is added, the solution of dissolved protein can be at any suitable temperature. In some embodiments, when an organic solvent is added, the solution of dissolved protein can be approximately ambient temperature (e.g., room temperature). In some embodiments, when an organic solvent is added, the solution of dissolved protein can be at a temperature of about 10°C to about 25°C (e.g., about 10°C to about 15°C, about 10°C to about 20°C, about 15°C to about 25°C, or about 20°C to about 25°C). In some embodiments, when an organic solvent is added, the solution of dissolved protein can be cooled. Without being bound by any particular theory, it is believed that cooling the solution of dissolved protein when an organic solvent is added may help preserve some of the protein's functions. In some embodiments, the solution of dissolved protein can be at a temperature of about 2°C to about 10°C (e.g., about 2°C to about 4°C, about 2°C to about 5°C, about 2°C to about 8°C, about 4°C to about 10°C, about 5°C to about 10°C, or about 8°C to about 10°C).

[0204] The separation of precipitated protein (solid phase) from the solution (liquid phase) can be achieved by any suitable method to form a protein composition (e.g., a low-flavor protein composition or a low-color protein composition). In some embodiments, the solid phase can be removed by centrifugation, filtration, or a combination thereof. In other embodiments, solid phase removal can include suppressing agitation for a threshold time period and aspirating the liquid phase from a location away from the solid phase. For example, a solution of dissolved protein (containing an organic solvent) can be left undisturbed for a continuous threshold time period, allowing the solid phase from the solution of dissolved protein to precipitate at the bottom of the container. In this case, the liquid phase from the solution of dissolved protein can be aspirated to remove the liquid phase from the solid phase precipitated at the bottom of the container. In another example, suppressing agitation for a threshold time period can be combined with other methods such as centrifugation and / or filtration. Specifically, in some instances, a solution of dissolved protein can be left undisturbed for a continuous threshold time period, allowing the liquid phase to be removed from the undisturbed solution of dissolved protein, and filtration and / or centrifugation can be used to further remove any remaining solid phase fraction from the aspirated liquid phase.

[0205] Protein compositions (e.g., solid phases) may optionally be washed with one or more washing solvents (e.g., organic washing solvents, aqueous washing solvents (e.g., water or buffers), or mixtures of aqueous washing solvents (e.g., water) and organic washing solvents). In some embodiments, the washing solvent may be a mixture of water and organic washing solvents, for example, the washing solvent may contain 0%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90% (v / v) of organic washing solvent. Non-limiting examples of suitable organic washing solvents may include methanol, propanol, isopropanol, EtOH, and acetone. Organic washing solvents may be used to wash solid phases containing precipitated proteins. In some embodiments, the organic washing solvent may be the same organic solvent used for precipitation. In some embodiments, the organic washing solvent may be a different organic solvent than the organic solvent used for precipitation. In some cases, the washing step may be repeated one or more times, wherein the washing solvent (e.g., selected from the washing solvents described herein) is selected independently for each washing step. For example, in some embodiments, the washing solvent used for the first washing step may contain about 70% (v / v) to about 100% (v / v) of ethanol, and repeated washing steps may use a washing solvent that may contain about 0% (v / v) to about 20% (v / v) of ethanol. The protein composition (e.g., a solid phase) may optionally be washed first with an organic washing solvent and then with an aqueous washing solvent, or vice versa.

[0206] In some cases, the protein composition (e.g., before redissolution) may have a protein dispersibility index of about 3 to about 20 (e.g., about 3 to about 18, about 3 to about 15, about 3 to about 12, about 3 to about 10, about 3 to about 8, about 3 to about 5, about 5 to about 20, about 8 to about 20, about 10 to about 20, about 12 to about 20, about 15 to about 20, about 18 to about 20, about 5 to about 15, or about 8 to about 12).

[0207] In some embodiments of any of the methods described herein, the protein composition may be treated (e.g., after optional washing). A non-limiting example of treatment is redissolution.

[0208] In some cases, the protein composition may be at least partially redissolved. Without being bound by any particular theory, it is believed that at least partial redissolution can result in increased functionality or greater ease of use of the protein composition in food applications. In some embodiments, the redissolved protein may be dissolved at a concentration of about 1.5 mg / mL to about 50 mg / mL (e.g., about 1.5 mg / mL to about 5.0 mg / mL, about 1.5 mg / mL to about 4.0 mg / mL, about 2.0 mg / mL to about 4.0 mg / mL, about 1.5 mg / mL to about 20 mg / mL, about 1.5 mg / mL to about 10 mg / mL, about 10 mg / mL to about 50 mg / mL, about 10 mg / mL to about 40 mg / mL, about 10 mg / mL to about 30 mg / mL, about 10 mg / mL to about 20 mg / mL, about 20 mg / mL to about 50 mg / mL, or about 20 mg / mL to about 40 mg / mL). In some embodiments, pH variation may be used to dissolve the protein composition. In some embodiments, the pH of the protein composition may be adjusted to at least 7 (e.g., at least 8, at least 9, at least 10, or at least 11). In some embodiments, after a pH change, the protein composition may be further neutralized (e.g., to a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, or about 7.0). In some embodiments, an enzyme may be used to dissolve the protein, such as a protein glutaminase, a protein asparaginase, or a protein deamidase.

[0209] Protein compositions can be dried. Protein compositions can be dried by any suitable method. For example, protein compositions can be dried by spray drying, pad drying, freeze drying (e.g., lyophilization), oven drying (e.g., at about 70°C to about 90°C, such as about 80°C), and combinations thereof.

[0210] Therefore, this document provides a method for preparing a protein composition, the method comprising (a) adding an aqueous solution to a source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) optionally heating the solution of dissolved protein; (d) optionally adjusting the pH of the solution of dissolved protein to about 4.0 to about 9.0; (e) optionally cooling the solution of dissolved protein to about 0°C to about 10°C; (f) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; (g) separating the solid phase and the liquid phase to form a protein composition; (h) optionally washing the protein composition with a washing solvent; and (i) optionally treating the protein composition.

[0211] The protein composition therein comprises at least 50% by dry weight of various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, and invertebrate proteins.

[0212] In some embodiments, the method may include steps (a), (b), (f), and (g). In some embodiments, the method may include steps (a), (b), (c), (f), and (g). In some embodiments, step (c) occurs after step (b). In some embodiments, step (b) occurs after step (c). In some embodiments, the method may include steps (a), (b), (d), (f), and (g). In some embodiments, step (d) occurs after step (b). In some embodiments, the method may include steps (a), (b), (e), (f), and (g). In some embodiments, step (e) occurs after step (b). In some embodiments, step (b) occurs after step (e). In some embodiments, the method may include steps (a), (b), (c), (d), (f), and (g). In some embodiments, steps (b), (c), and (d) are performed in the order of (b), (c), and (d). In some embodiments, (b), (c), and (d) are performed in the order of (c), (b), and (d). In some embodiments, steps (b), (c), and (d) are performed in the order of (b), (d), and (c). In some embodiments, the method may include steps (a), (b), (c), (e), (f), and (g). In some embodiments, steps (b), (c), and (e) are performed in the order of (b), (c), and (e). In some embodiments, steps (b), (c), and (e) are performed in the order of (c), (b), and (e). In some embodiments, steps (b), (c), and (e) are performed in the order of (b), (e), and (c). In some embodiments, the method may include steps (a), (b), (c), (d), (e), (f), and (g). In some embodiments, steps (b), (c), (d), and (e) are performed in the order of (b), (c), (d), and (e). In some embodiments, steps (b), (c), (d), and (e) are performed in the order of (c), (b), (d), and (e). In some embodiments, steps (b), (c), (d), and (e) are performed in the order of (b), (d), (e), and (c). In some embodiments, steps (b), (c), (d), and (e) are performed in the order of (b), (d), (c), and (e). In some embodiments, the method may include steps (a), (c), (f), and (g). In some embodiments, the method may include steps (a), (c), (d), (f), and (g). In some embodiments, step (c) is performed before step (d). In some embodiments, step (d) is performed before step (c). In some embodiments, the method may include steps (a), (c), (d), (e), (f), and (g).In some embodiments, steps (c), (d), and (e) are performed in the order of (c), (d), and (e). In some embodiments, steps (c), (d), and (e) are performed in the order of (d), (e), and (c). In some embodiments, steps (c), (d), and (e) are performed in the order of (d), (c), and (e). In some embodiments, the method may include steps (a), (d), (f), and (g). In some embodiments, the method may include steps (a), (d), (e), (f), and (g). In some embodiments, step (d) is performed before step (e). In some embodiments, the method may include steps (a), (e), (f), and (g). In some embodiments, the method may include steps (a), (e), (f), and (g). In some embodiments of any method described herein, the method may include step (h). In some embodiments, step (h) is repeated once or more. In some embodiments, in the repetition of step (h), the washing solvent is the same as in the first step (h). In some embodiments, in the repetition of step (h), the washing solvent is different from the washing solvent in the first step (h). In some embodiments of any method described herein, the method may include step (i). In some embodiments, the method may further include drying the protein composition. In some embodiments, drying may include spray drying, pad drying, freeze drying, or oven drying.

[0213] In some embodiments, the source protein composition may comprise one or more isoflavones. In some embodiments, the source protein composition may be a soybean-derived protein composition and may comprise one or more isoflavones (e.g., genistein, soy isoflavones, daidzein, or combinations thereof). In some embodiments, the methods described herein may result in a reduction in the content of one or more isoflavones in the protein composition compared to the source protein composition. For example, based on dry weight, the protein composition may have an isoflavone content of less than 90% (e.g., less than 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, or less) of the isoflavone content of the source protein composition.

[0214] In some embodiments, the source protein composition may comprise one or more sphingolipids, disaccharides (e.g., sucrose), oligosaccharides (e.g., raffinose, stachyose), phytoestrogens, lignans, O-methylated isoflavones (e.g., gentianin, chickpea sprout A), phytoalexins, coumarins (e.g., coumestrol), phytotoxins, phytochemicals, carotenoids, or pterocarpans (e.g., glyceollidin I and II, soybean antitoxins (soybean antitoxins I, II, III, and IV)). In some embodiments, the methods described herein, compared to the source protein composition, can result in a reduction in the content of one or more sphingolipids, disaccharides (e.g., sucrose), oligosaccharides (e.g., raffinose, stachyose), phytoestrogens, lignans, O-methylated isoflavones (e.g., gentiopicrin, chickpea stigmatin A), phytoalexins, coumarins (e.g., estradiol), phytotoxicants, phytochemicals, carotenoids, or stigmolides (e.g., glycine, glyceollidin I and II, soybean antitoxins (soybean antitoxins I, II, III, and IV)). For example, based on dry weight, the content of the protein composition can be less than 90% of the content of the source protein composition (e.g., less than 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, or less).

[0215] In some embodiments, the protein composition may produce fewer of the one or more flavor compounds (e.g., soy flavor compounds) during cooking compared to the amount of one or more flavor compounds (e.g., soy flavor compounds) produced by cooking the source protein composition. Non-limiting examples of the one or more flavor compounds (e.g., soy flavor compounds) are hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonenal, (E,Z)-2,6-nonadienal, and (E,E)-2,4-decadienal. For example, when cooking in water, a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) may produce no more than 90% (e.g., soy flavor compounds) of the amount of one or more flavor compounds (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). Similarly, when cooking in a flavored broth, a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) may produce no more than 90% (e.g., soy flavor compounds) of the amount of one or more flavor compounds (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in a seasoned broth (e.g., a protein containing reducing sugars, sulfur-containing amino acids, and heme), a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) can produce at least 5% (e.g., at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, or more) of one or more volatile compounds from the meat volatiles group, said volatile compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0216] In some embodiments, a set of volatiles from any protein composition as described herein may be evaluated. As defined herein, “volatile group 1” includes 1-hexanol, 1-octen-3-ol, 1-octen-3-one, 1-pentanol, 2-butanol, 2-decanol, 2-decenal, 2-nonanol, 2,4-decadienal, acetophenone, butyric acid, 2-pentyl-furan, hexanal, hexanoic acid, octanoic acid, pentanol, and valeric acid. In some embodiments, “volatile group 1” consists of 1-hexanol, 1-octen-3-ol, 1-octen-3-one, 1-pentanol, 2-butanol, 2-decanol, 2-decenal, 2-nonanol, 2,4-decadienal, acetophenone, butyric acid, 2-pentyl-furan, hexanal, hexanoic acid, octanoic acid, pentanol, and valeric acid.

[0217] As defined herein, “volatile group 2” includes pentanal, hexanal, 2-pentylfuran, 2,4-decadienal, 2,6-nonadienal, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, 2-decenal, 1-pentanol, acetophenone, 2-decanone, 2-nonanone, 2-butanol, 4-ethylbenzaldehyde, butyric acid, valeric acid, hexanoic acid, and octanoic acid. In some embodiments, “volatile group 2” consists of pentanal, hexanal, 2-pentylfuran, 2,4-decadienal, 2,6-nonadienal, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, 2-decenal, 1-pentanol, acetophenone, 2-decanone, 2-nonanone, 2-butanol, 4-ethylbenzaldehyde, butyric acid, valeric acid, hexanoic acid, and octanoic acid.

[0218] As defined herein, “volatile group 3” includes pentanal, hexanal, 2-pentylfuran, 2,4-decadienal, 2-nonenal, 2,6-nonadienal, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, 2-decenal, 1-pentanol, acetophenone, 2-decanone, 2-nonanone, 2-butanol, 4-ethylbenzaldehyde, butyric acid, valeric acid, hexanoic acid, and octanoic acid. In some embodiments, “volatile group 3” consists of pentanal, hexanal, 2-pentylfuran, 2,4-decadienal, 2-nonenal, 2,6-nonadienal, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, 2-decenal, 1-pentanol, acetophenone, 2-decanone, 2-nonanone, 2-butanol, 4-ethylbenzaldehyde, butyric acid, valeric acid, hexanoic acid, and octanoic acid.

[0219] As defined herein, “volatile group 4” includes butyric acid, valeric acid, hexanoic acid, and octanoic acid. In some embodiments, “volatile group 4” consists of butyric acid, valeric acid, hexanoic acid, and octanoic acid.

[0220] As defined herein, “volatile group 5” includes 1-octen-3-ol, 1-hexanol, and 1-pentanol. In some embodiments, “volatile group 5” consists of 1-octen-3-ol, 1-hexanol, and 1-pentanol.

[0221] As defined herein, “volatile group 6” includes pentanal, hexanal, 2,4-decadienal, 2-nonenal, 2,6-nonadienal, 2-decenal, and 4-ethylbenzaldehyde. In some embodiments, “volatile group 6” consists of pentanal, hexanal, 2,4-decadienal, 2-nonenal, 2,6-nonadienal, 2-decenal, and 4-ethylbenzaldehyde.

[0222] As defined herein, “volatile group 7” includes 2-pentylfuran. In some embodiments, “volatile group 7” consists of 2-pentylfuran.

[0223] As defined herein, “volatile group 8” includes 1-octen-3-one, acetophenone, 2-decanone, 2-nonanone, and 2-butanol. In some embodiments, “volatile group 8” consists of 1-octen-3-one, acetophenone, 2-decanone, 2-nonanone, and 2-butanol.

[0224] As defined herein, “volatile group 9” includes 4-ethylbenzaldehyde, acetophenone, 2-butanol, butyric acid, 1-pentanol, 2-pentylfuran, pentaldehyde, pentanoic acid, 1-hexanol, hexanal, and hexanoic acid. In some embodiments, “volatile group 9” consists of 4-ethylbenzaldehyde, acetophenone, 2-butanol, butyric acid, 1-pentanol, 2-pentylfuran, pentaldehyde, pentanoic acid, 1-hexanol, hexanal, and hexanoic acid.

[0225] As defined herein, “volatile group 10” includes 1-octen-3-ol, 1-octen-3-one, octanoic acid, 2,6-nonadienal, 2-nonanone, 2-nonenal, 2,4-decadienal, 2-decanone, and 2-decenal. In some embodiments, “volatile group 10” consists of 1-octen-3-ol, 1-octen-3-one, octanoic acid, 2,6-nonadienal, 2-nonanone, 2-nonenal, 2,4-decadienal, 2-decanone, and 2-decenal.

[0226] As defined herein, the “meat volatiles group” includes 2,3-butanedione, 2,3-pentanedione, thiazole, 2-acetylthiazole, benzaldehyde, 3-methylbutanal, 2-methylbutanal, thiophene, and pyrazine.

[0227] In some embodiments, the protein composition may produce fewer of the one or more volatile compounds that can affect flavor during cooking compared to the amount of one or more volatile compounds produced by cooking the source protein composition. Without being bound by any particular theory, it is believed that the reduction in the amount of volatiles that can affect flavor during cooking can allow the protein composition to be used in a wide range of foods. Non-limiting examples of one or more volatile compounds that can affect flavor include volatile compounds from any of the groups 1-10 of volatiles. For example, when cooked in water, a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) may produce no more than 90% of the amount of one or more volatile compounds (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). For example, when cooked in a seasoned broth, a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) may generate no more than 90% of the amount of one or more volatile compounds (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) generated by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). When cooked in a seasoned broth, a 1% (w / v) suspension of the protein composition (based on the dry weight of the protein composition) may generate at least 5% (e.g., at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, or more) of one or more volatile compounds in the meat volatiles group, generated by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition). In some embodiments, the flavored broth includes one or more (e.g., two or more, three or more, four or more, or five or more) flavor precursor molecules or compounds. One or more flavor precursors may include at least one compound selected from the group consisting of: glucose, ribose, cysteine, cysteine ​​derivatives, thiamine, alanine, methionine, lysine, lysine derivatives, glutamic acid, glutamic acid derivatives, IMP, GMP, lactic acid, maltodextrin, creatine, alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, valine, linoleic acid, and mixtures thereof.Suitable flavor precursors may comprise sugars, sugar alcohols, sugar derivatives, oils (e.g., vegetable oils), free fatty acids, α-hydroxy acids, dicarboxylic acids, amino acids and their derivatives, nucleosides, nucleotides, vitamins, peptides, protein hydrolysates, extracts, phospholipids, lecithin, and organic molecules. In some embodiments, a group of volatile compounds may include compounds from group 1 of volatile compounds. In some embodiments, a group of volatile compounds may be group 1 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 2 of volatile compounds. In some embodiments, a group of volatile compounds may be group 2 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 3 of volatile compounds. In some embodiments, a group of volatile compounds may be group 3 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 4 of volatile compounds. In some embodiments, a group of volatile compounds may be group 4 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 5 of volatile compounds. In some embodiments, a group of volatile compounds may be group 5 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 6 of volatile compounds. In some embodiments, a group of volatile compounds may be group 6 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 7 of volatile compounds. In some embodiments, a group of volatile compounds may be group 7 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 8 of volatile compounds. In some embodiments, a group of volatile compounds may be group 8 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 9 of volatile compounds. In some embodiments, a group of volatile compounds may be group 9 of volatile compounds. In some embodiments, a group of volatile compounds may include compounds from group 10 of volatile compounds. In some embodiments, a group of volatile compounds may be group 10 of volatile compounds.

[0228] In some embodiments, the protein composition as described herein may contain one or more isoflavones in a smaller amount than that in the source protein composition. In some cases, the isoflavone content of the protein composition may be about 90% less than the isoflavone content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some cases, the total content of daidzein, genistein, genistein, genistein, genistein, and genistein in the protein composition may be about 90% less than the total content of daidzein, genistein, genistein, genistein, genistein, and genistein in the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some cases, the total content of daidzein, genistein, and genistein in the protein composition may be about 90% less than the total content of daidzein, genistein, and genistein in the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the total content of daidzein, genistein, and genistein in the protein composition may be about 90% less than the total content of daidzein, genistein, and genistein in the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some cases, the isoflavone content is the content of isoflavones selected from the group consisting of daidzein, genistein, genistein, genistein, genistein, genistein, and any combination thereof. In some cases, the daidzein content of the protein composition may be about 90% less than the daidzein content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the daidzein content of the protein composition may be about 90% less than the daidzein content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the genistein content of the protein composition may be about 90% less than the genistein content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the genistein content of the protein composition may be about 90% less than the genistein content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the daidzein content of the protein composition may be about 90% less than the daidzein content of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less).In some cases, the genistein content of the protein composition may be about 90% less than the genistein content of the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some cases, the isoflavone content is the content of isoflavones selected from the group consisting of gentiopicrin and chickpea buds A.

[0229] In some embodiments, the protein composition as described herein may comprise one or more phospholipids in a smaller amount than that in the source protein composition. In some cases, the phospholipid content of the protein composition may be about 90% less than that of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some cases, the phosphatidylcholine-36:4 content of the protein composition may be about 90% less than that of the source protein composition (e.g., about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% less). In some embodiments, the phospholipid content is the phosphatidylcholine-36:3 content. In some embodiments, the phospholipid content is the phosphatidylethanolamine-36:4 content. In some embodiments, the phospholipid content is the phosphatidic acid-36:4 content.

[0230] In some embodiments, the protein composition as described herein may contain one or more saponins in a lesser amount than that in the source protein composition. In some cases, the saponin content of the protein composition may be less than about 90% of the saponin content of the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some cases, the daidzein content of the protein composition may be less than about 90% of the daidzein content of the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%).

[0231] In some embodiments, the protein composition as described herein may contain one or more lipids in a smaller amount than that in the source protein composition. In some cases, the lipid content of the protein composition may be less than about 90% of the lipid content of the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%).

[0232] In some embodiments, the protein composition as described herein may contain one or more phenolic acids in a lesser amount than that in the source protein composition. In some cases, the phenolic acid content of the protein composition may be less than about 90% of the phenolic acid content of the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%).

[0233] In some embodiments, the protein composition as described herein may comprise one or more flavor compounds in a smaller amount than that in the source protein composition. In some cases, the content of flavor compounds in the protein composition may be less than about 90% of the content of flavor compounds in the source protein composition (e.g., less than about 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%). In some embodiments, the flavor compounds are selected from the group consisting of aldehydes, ketones, esters, alcohols, pyrazines, pyranones, acids, sulfur compounds, terpenes, furans, alkanes, alkenes, and combinations thereof.

[0234] Flavor can refer to taste and / or aroma. The five basic tastes (i.e., sweet, bitter, sour, salty, and umami or salty) primarily respond to non-volatile compounds and can be perceived by receptors on the tongue. Aroma primarily refers to volatile compounds perceived by nasal receptors. Other effects can influence flavor, including but not limited to astringency, dryness, roughness, metallicity, pungentness, spiciness, coolness, and oiliness, as well as texture (e.g., smoothness, roughness, hardness, thickness, slipperiness, viscosity).

[0235] Unbound by any particular theory, it is believed that off-odors and their precursors may exist as protein-bound complexes in protein sources and / or may be generated during harvesting, processing, or storage. Residual phospholipids (PL) and free fatty acids (FFA) in protein compositions may be precursors to off-odors. Auto-oxidation or enzymatic oxidation of PL and FFA during storage may produce unacceptable levels of off-odor compounds. Furthermore, it is believed that even if the carbonyl compounds causing off-odors are removed from the protein composition, residual PL and FFA in the protein will continuously generate these carbonyl compounds during storage through auto-oxidation or enzymatic oxidation.

[0236] Volatile compounds that can cause off-odors may include, but are not limited to, aldehydes, ketones, esters, alcohols, pyrazines, pyranones, acids, sulfur compounds, terpenes, furans, alkanes, and alkenes. Non-limiting examples of off-odors may include beany, fatty, raw, pea-like, earthy, hay-like, grassy, ​​putrid, leafy, cardboard-like, spicy, pungent, medicinal, metallic, and broth-like flavors. Non-volatile compounds can also cause off-odors. For example, isoflavones can cause bitter off-odors, saponins can cause astringent off-odors, and phenolic acids, peptides, or amino acids can cause metallic off-odors.

[0237] The methods provided herein can also be used to prepare detoxifying protein compositions. As used herein, a “detoxifying protein composition” refers to a protein composition prepared from a source protein composition that is otherwise unsuitable for human consumption (e.g., due to the presence or amount of one or more toxins), wherein the protein composition has one or more toxins removed or reduced in amount compared to the source protein composition, making the detoxifying protein composition suitable for human consumption.

[0238] In some embodiments, a method for preparing a detoxifying protein composition includes: (a) adding an aqueous solution to a source protein composition to form a solution of dissolved proteins; (b) optionally removing solids from the solution of dissolved proteins; (c) adding an organic solvent to the solution of dissolved proteins to form a solid phase and a liquid phase; and (d) separating the solid phase and the liquid phase to form a detoxifying protein composition, wherein the detoxifying protein composition includes a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate (e.g., insects and / or arachnids) proteins, and wherein the source protein composition is not suitable for human consumption.

[0239] In some such embodiments, the source protein composition includes one or more toxins in amounts sufficient to harm humans. For example, the source protein composition may be a cottonwood-derived protein composition. In some embodiments, the source protein composition includes a toxic phenolic compound, such as gossypol. For example, the source protein composition may contain more than 450 ppm of gossypol. Therefore, in some embodiments, the detoxifying protein composition includes less than 450 ppm (e.g., less than about 300 ppm; less than about 100 ppm; less than about 50 ppm; less than about 10 ppm, less than about 5 ppm, or less than about 2 ppm). In some embodiments, the protein composition as described herein may contain one or more toxins in amounts less than those in the source protein composition. In some cases, the protein composition may have a toxin content less than about 90% (e.g., less than about 70%, 50%, 30%, or 10%) of the toxin content of the source protein composition. Non-limiting examples of toxins include gossypol (e.g., in poplar), vicine or convicine glycosides (e.g., in broad beans), cyanogenic glycosides (e.g., in cassava or bamboo), glucosinolates (e.g., in cruciferous vegetables) and glycoalkaloids (e.g., in potatoes and Solanum plants).

[0240] Various methods can be used to determine the amount of one or more toxins in the source protein composition or the detoxified protein composition (e.g., spectrophotometry, HPLC, enzyme-linked immunosorbent assay (ELISA)). In some embodiments, toxins may also contribute to the color of the protein composition, and their removal may result in a lighter color of the protein composition. For example, gossypol is typically yellow-green.

[0241] This document also provides a method for extracting small molecules from a protein source composition. In some embodiments, the method comprises: (a) adding an aqueous solution to the source protein composition to form a solution of dissolved protein; (b) optionally removing solids from the solution of dissolved protein; (c) adding an organic solvent to the solution of dissolved protein to form a solid phase and a liquid phase; and (d) separating the solid and liquid phases to form a solution rich in small molecules. For example, the source protein composition may be a soybean-derived protein composition. In some such embodiments, the small molecules to be extracted may comprise one or more isoflavones. For example, one or more isoflavones may comprise genistein and daidzein. The small molecules to be extracted may comprise isoflavones, pigments (e.g., chlorophyll, anthocyanins, carotenoids, and betaines), flavor compounds (e.g., soybean flavor compounds), saponins, toxins (e.g., gossypol), natural products (e.g., plant natural products, pharmacologically active natural products), metabolites (e.g., primary metabolites and / or secondary metabolites), and / or phospholipids (e.g., lecithin). For example, isoflavones and saponins may have medical or nutritional uses. Lecithin can be used as an emulsifier, for example, in food, or as a choline-rich nutrient source. Small molecules can have molecular weights up to 900 Daltons (e.g., up to 800 Daltons, up to 700 Daltons, up to 600 Daltons, or up to 500 Daltons). In some embodiments, the extracted small molecules can be used as supplements. In some embodiments, the extracted small molecules can be used as food ingredients (e.g., food colorings or flavor compounds). In some embodiments, the extracted small molecules can be used as chemical precursors for industrial synthesis (e.g., pharmaceutical synthesis). As non-limiting examples, isoflavones have been suggested to reduce the risk of breast cancer, prevent or inhibit the progression of prostate cancer, and reduce menopausal symptoms; soy isoflavones are sold as nutritional supplements; saponins are believed to lower blood lipids, reduce cancer risk, and reduce glycemic response, and are also sold as nutritional supplements; and soy lecithin (phospholipids) are sold as food emulsifiers, and soy lecithin is rich in choline, an essential nutrient for humans and animals.

[0242] This document also provides protein compositions. In some embodiments, the protein compositions can be produced by any of the methods described herein.

[0243] In some cases, protein compositions can be compared with commercial protein products. Non-limiting examples of commercial protein products are protein concentrates and protein isolates. In some embodiments, the comparison can be based on the agricultural origin of the protein in the protein composition. For example, a soybean protein composition as described herein can be compared with a commercial soybean protein product. In some embodiments, the comparison can be based on protein type. For example, a protein composition that is a protein isolate as described herein can be compared with a commercial protein isolate product, while a protein composition that is a protein concentrate as described herein can be compared with a commercial protein concentrate product. In some embodiments, the comparison can be based on both the agricultural origin and the protein type of the protein in the protein composition. For example, a protein composition that is a canola oil protein concentrate as described herein can be compared with a commercial canola oil protein concentrate. In some embodiments, a commercial protein product can be a soybean protein concentrate. In some embodiments, a commercial protein product can be a soybean protein isolate.

[0244] Examples of commercial protein products include, but are not limited to, commercially available soy protein isolates, commercially available pea protein isolates, and commercially available canola oil protein isolates. In some embodiments, the protein compositions provided herein may be protein concentrates (e.g., soy protein concentrates), and commercial protein products may be protein concentrates (e.g., soy protein concentrates). In some embodiments, the protein compositions provided herein may be protein isolates (e.g., soy protein isolates), and commercial protein products may be protein isolates (e.g., soy protein isolates).

[0245] In some embodiments, this document provides a protein composition comprising at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof, wherein said protein composition is a low-color protein composition. In some embodiments, the protein composition is a low-color protein composition.

[0246] In some embodiments, this document provides a protein composition comprising at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof; and less than 1.0% by dry weight of lipids.

[0247] The protein compositions described herein typically have a protein content of at least 50% (e.g., at least 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99%) based on the dry weight of the protein composition. In some embodiments, the protein compositions described herein may have a protein content of at least about 90% (e.g., at least 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 97%, or 99%) based on the dry weight of the protein composition. In some embodiments, the protein compositions described herein may have a protein content of about 60% to about 80% (e.g., about 65% to about 75%) based on the dry weight of the protein composition. The protein content of a protein composition may vary depending on whether the protein composition is a protein concentrate or a protein isolate. In some cases, the protein concentrate may have a protein content of about 55% to about 75% (e.g., about 55% to about 70%, about 55% to about 65%, about 55% to about 60%, about 60% to about 75%, about 65% to about 75%, about 70% to about 75%) based on the dry weight of the protein composition. In some cases, the protein isolate may have a protein content of about 80% to about 99% (e.g., about 80% to about 95%, about 80% to about 95%, about 80% to about 85%, about 85% to about 99%, about 90% to about 99%, or about 95% to about 99%) based on the dry weight of the protein composition. In some cases, the protein isolate may have less than about 8% (e.g., less than about 7%, 6%, 5%, 4%, 3%, 2%, or 1%) of carbohydrates (e.g., insoluble carbohydrates) based on dry weight. In some cases, protein concentrates may have at least about 8% (e.g., at least about 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20% or more) of carbohydrates (e.g., insoluble carbohydrates) on a dry weight basis.

[0248] The proteins in the protein compositions described herein can be any suitable protein. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% plant proteins. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% legume proteins. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% legume fruit proteins. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% soybean protein. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% fungal proteins. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% yeast protein. In some embodiments, the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% algal proteins.

[0249] Protein compositions can be produced using any suitable starting material (e.g., any starting material described herein) or any mixture thereof. Therefore, protein compositions as described herein can comprise a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, invertebrate (e.g., insect and / or arachnid) proteins, or combinations thereof.

[0250] In some embodiments, the protein composition as described herein comprises substantially aggregated, denatured, or both proteins. Aggregation and / or denaturation can be determined by any suitable method. In some cases, aggregation can be measured by average particle size (e.g., using dynamic light scattering (DLS)). In some embodiments, the protein composition as described herein may have an average particle size of about 1 µm to about 40 µm at its maximum size (e.g., about 5 µm to about 40 µm, about 10 µm to about 40 µm, about 20 µm to about 40 µm, about 30 µm to about 40 µm, about 1 µm to about 5 µm, about 1 µm to about 10 µm, about 1 µm to about 20 µm, about 1 µm to about 30 µm, about 10 µm to about 30 µm, or about 20 µm to about 30 µm). In some embodiments, the size and shape of the particle size distribution may be related to the conditions under which the protein composition is precipitated. In some embodiments, the particles in the protein composition as described herein may have a zeta potential of about -1.5 mV to about -4.5 mV. In some embodiments, the charge of the particles may be correlated with the conditions under which the protein composition precipitates. In some cases, the surface hydrophobicity and protein solubility of the protein composition may be tunable. In some cases, denaturation or unfolding may be measured by circular dichroism spectroscopy, differential scanning calorimetry, or fluorescent dye assay, in which a dye binds to the hydrophobic regions exposed during protein unfolding. In some cases, denaturation may be associated with the loss of one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) in a temperature-dependent manner over a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C).

[0251] In some embodiments, the protein composition as described herein has a protein dispersion index of at least about 5 (e.g., at least about 10 or at least about 15). In some embodiments, the protein composition as described herein has a sodium level of up to about 1% w / w (e.g., up to about 0.5% w / w, up to about 0.1% w / w, up to about 0.05% w / w, up to about 0.01% w / w, or up to about 0.005% w / w).

[0252] In some embodiments, the protein composition as described herein may have a solubility of at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, or at least 30%) in an aqueous solution (e.g., water). In some embodiments, the aqueous solution has a pH of about 6.0 to about 8.0, about 6.5 to about 7.5, about 7.0 to about 8.0, about 7.0, or about 8.0. In some embodiments, the aqueous solution may contain a buffer.

[0253] In some embodiments, the protein composition described herein may exhibit temperature-dependent changes in one or more mechanical properties (e.g., storage modulus, loss modulus, and / or viscosity) within a temperature range (e.g., from 25°C to 95°C, from 40°C to 95°C, from 60°C to 95°C, or from 80°C to 90°C). In some embodiments, the magnitude of the temperature-dependent change is at least 5-fold (e.g., at least 10-fold, at least 100-fold, at least 500-fold, or at least 1,000-fold). In some embodiments, the temperature-dependent change is substantially irreversible (e.g., the magnitude of the change when cooling within the same temperature range is up to 25%, up to 20%, up to 15%, up to 10%, up to 5%, up to 1%, up to 0.5%, or up to 0.1% of the magnitude of the change observed when heating). In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 90°C. In some embodiments, the energy storage modulus and / or loss modulus reaches a value of at least 1,000 Pa (e.g., at least 2,000 Pa, at least 3,000 Pa, at least 4,000 Pa, at least 5,000 Pa, at least 6,000 Pa, at least 7,000 Pa, at least 8,000 Pa, at least 9,000 Pa, or at least 10,000 Pa) at 95°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 90°C. In some embodiments, the viscosity reaches a value of at least 1,000 Pa·s (e.g., at least 2,000 Pa·s, at least 3,000 Pa·s, at least 4,000 Pa·s, at least 5,000 Pa·s, at least 6,000 Pa·s, at least 7,000 Pa·s, at least 8,000 Pa·s, at least 9,000 Pa·s, or at least 10,000 Pa·s) at 95°C.

[0254] The protein compositions described herein may comprise components other than proteins. In some cases, the protein compositions described herein may comprise carbohydrates (e.g., insoluble carbohydrates), lipids (e.g., fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, phospholipids, or combinations thereof), saponins, or combinations thereof. In some embodiments, the protein compositions described herein may comprise less than 1.5% (e.g., less than about 1.3%, 1.2%, 1.1%, 1.0%, 0.9%, 0.8%, 0.7%, 0.6%, 0.5%, 0.4%, 0.3%, 0.2%, 0.1%, or less) of the amount of lipids based on the dry weight of the protein composition. In some embodiments, the protein compositions described herein may comprise less than 1.2% (less than the amount of lipids based on the dry weight of the protein composition). In some embodiments, the protein compositions may comprise less than 1.0% (less than the amount of lipids based on the dry weight of the protein composition). In some embodiments, the protein compositions may comprise less than 0.8% (less than the amount of lipids based on the dry weight of the protein composition). In some embodiments, the protein compositions may comprise less than 0.7% (less than the amount of lipids based on the dry weight of the protein composition). In some embodiments, the protein composition may contain about 0.6% of lipids based on the dry weight of the protein composition. In some embodiments, the protein composition may contain about 0.5% of lipids based on the dry weight of the protein composition. In some embodiments, the protein composition may contain about 0.4% of lipids based on the dry weight of the protein composition. In some embodiments, the protein composition as described herein may contain about 0.5% of lipids based on the dry weight of the protein composition. In some embodiments, the protein composition as described herein may contain about 0.5% of phospholipids based on the dry weight of the protein composition (e.g., less than about 0.4%, 0.3%, 0.2%, or 0.1%) based on the dry weight of the protein composition. In some cases, phosphatidylcholine 36:4 may be used as an alternative measure of total phospholipids. In some embodiments, the protein composition as described herein may have reduced amounts of one or more of the following compared to the protein source in the protein composition: fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, or phospholipids.In some embodiments, the protein composition as described herein may have a reduced amount (e.g., a reduction of at least 5%, 10%, 20%, 25%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or more) of phospholipids (e.g., phosphatidylcholine (e.g., phosphatidylcholine-36:4, phosphatidylcholine-34:2, phosphatidylcholine-36:3), phosphatidylethanolamine (e.g., phosphatidylethanolamine-36:4), glycerophospholipids, phosphatidic acid (e.g., phosphatidic acid-36:4), phosphatidylserine, phosphatidylinositol or combinations thereof) compared to the protein source in the protein composition (or, for example, the source protein composition from which the protein composition is prepared).

[0255] Saponins can cause foaming in solutions. In some embodiments, the protein composition as described herein may have a lower saponin content than the saponin content of the protein source (or, for example, the source protein composition used to prepare the protein composition) in the composition. In some embodiments, the protein composition as described herein may have a saponin content less than 90% (e.g., less than 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10% or less) of the saponin content of the protein source (or, for example, the source protein composition used to prepare the protein composition) in the composition. In some embodiments, the protein isolate as described herein may have a lower saponin content than the saponin content of commercial protein isolates. In some embodiments, the protein isolate as described herein may have a saponin content less than 90% (e.g., less than 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10% or less) of the saponin content of commercial protein isolates.

[0256] In some embodiments, the protein composition as described herein may contain one or more isoflavones. In some cases, the protein composition may have an isoflavone content of less than about 500 ppm (e.g., less than about 400 ppm, 300 ppm, 250 ppm, 200 ppm, 150 ppm, 125 ppm, 100 ppm, 75 ppm, or 50 ppm). In some cases, the isoflavone content refers to the total content of daidzein, genistein, genistein, genistein, genistein, and genistein. In some cases, the protein composition may have a total content of less than about 250 ppm (e.g., less than about 200 ppm, 150 ppm, 125 ppm, 100 ppm, 75 ppm, or 50 ppm). In some cases, the isoflavone content refers to the total content of genistein, genistein, and genistein. In some embodiments, the protein composition may have a total content of less than about 200 ppm (e.g., less than about 150 ppm, 100 ppm, or 75 ppm) of daidzein, genistein, and genistein. In some cases, the isoflavone content refers to the total content of daidzein, genistein, and genistein. In some embodiments, the protein composition may have a total content of less than about 50 ppm (e.g., less than about 30 ppm, 20 ppm, or 10 ppm) of daidzein, genistein, and genistein. In some cases, the isoflavone content is the content of isoflavones selected from the group consisting of daidzein, daidzein, genistein, genistein, genistein, genistein, and any combination thereof. In some embodiments, the protein composition may have a daidzein content of less than about 100 ppm (e.g., less than about 75 ppm, 50 ppm, 30 ppm, 20 ppm, 10 ppm, 5 ppm, or 3 ppm). In some embodiments, the protein composition may have a genistein content of less than about 100 ppm (e.g., less than about 75 ppm, 50 ppm, 30 ppm, or 10 ppm). In some embodiments, the protein composition may have a genistein content of less than about 100 ppm (e.g., less than about 75 ppm, 50 ppm, 20 ppm, 10 ppm, 5 ppm, 3 ppm, or 1 ppm). In some embodiments, the protein composition may have a genistein content of less than about 300 ppm (e.g., less than about 200 ppm, 100 ppm, 75 ppm, 50 ppm, or 30 ppm). In some embodiments, the protein composition may have a daidzein content of less than about 30 ppm (e.g., less than about 20 ppm, 10 ppm, 5 ppm, 3 ppm, or 1 ppm).In some embodiments, the protein composition may have a content of less than about 30 ppm (e.g., less than about 20 ppm, 10 ppm, or 5 ppm) of daidzein. In some cases, the isoflavone content is the content of isoflavones selected from the group consisting of gentianin and chickpea spore extract A.

[0257] In some embodiments, the protein composition as described herein may comprise one or more phospholipids. In some cases, the protein composition may have a phospholipid content of less than about 1,000 ppm (e.g., less than about 750 ppm, 500 ppm, 250 ppm, 100 ppm, 50 ppm, 25 ppm, 10 ppm, 5 ppm, 2 ppm, or 1 ppm). In some embodiments, the phospholipid content is a phosphatidylcholine-36:4 content. In some embodiments, the protein composition may have a phosphatidylcholine-36:4 content of less than about 500 ppm (e.g., less than about 250 ppm, 100 ppm, 50 ppm, 25 ppm, 10 ppm, 5 ppm, 2 ppm, or 1 ppm). In some embodiments, the phospholipid content is a phosphatidylcholine-34:2 content. In some embodiments, the protein composition may have a phosphatidylcholine-34:2 content of less than about 750 ppm (e.g., less than about 500 ppm, 250 ppm, 100 ppm, 50 ppm, 25 ppm, 10 ppm, 5 ppm, 2 ppm, or 1 ppm). In some embodiments, the phospholipid content is a phosphatidylcholine-36:3 content. In some embodiments, the phospholipid content is a phosphatidylethanolamine-36:4 content. In some embodiments, the phospholipid content is a phosphatidic acid-36:4 content.

[0258] In some embodiments, the protein composition as described herein may contain one or more saponins. In some cases, the protein composition may have a saponin content of less than about 1000 ppm (e.g., less than about 750 ppm, 500 ppm, 250 ppm, 100 ppm, 75 ppm, 50 ppm, or 25 ppm). In some cases, the saponin content is the same as that of soybean saponins. In some cases, the protein composition may have a soybean saponin content of less than about 1000 ppm (e.g., less than about 750 ppm, 500 ppm, 250 ppm, 100 ppm, 75 ppm, 50 ppm, or 25 ppm).

[0259] In some embodiments, the protein compositions described herein may contain sodium. Without being bound by any particular theory, it is believed that various commercial processes, such as isoelectric point precipitation, can introduce sodium into protein products. In some embodiments, the protein compositions described herein may contain less sodium than commercial protein products. Figure 10 An example sodium content is shown in the figure.

[0260] In some embodiments, the protein composition (e.g., protein concentrate) as described herein may have a sodium content of about 0.0005% to about 0.01% (w / w) (e.g., about 0.0005% to about 0.001%, about 0.0005% to about 0.002%, about 0.0005% to about 0.003%, about 0.0005% to about 0.004%, about 0.0005% to about 0.005%, about 0.0005% to about 0.007%, about 0.0005% to about 0.0009%, about 0.001% to about 0.01%, about 0.002% to about 0.01%, about 0.003% to about 0.01%, about 0.004% to about 0.01%, about 0.005% to about 0.01%, about 0.007% to about 0.01%, or about 0.009% to about 0.01% (w / w)). In some embodiments, the protein composition (e.g., protein isolate) as described herein may have a sodium content of about 0.05% to about 0.3% (w / w) (e.g., about 0.05% to about 0.1%, about 0.05% to about 0.2%, about 0.1% to about 0.2%, about 0.1% to about 0.3%, or about 0.2% to about 0.3% (w / w). In some cases, the protein composition may have a sodium content of less than about 1% (w / w) (e.g., less than about 0.9%, 0.8%, 0.7%, 0.6%, 0.5%, 0.4%, 0.3%, 0.2%, or 0.1% (w / w)).

[0261] The protein compositions described herein may contain non-organic contents (sometimes referred to as "ash" in analysis). These non-organic contents may contain salts, such as sodium salts. In some embodiments, the protein compositions described herein may contain non-organic contents in an amount of about 4% to about 8% based on the dry weight of the protein composition (e.g., about 4% to about 7%, about 4% to about 6%, about 4% to about 5%, about 5% to about 8%, about 6% to about 8%, about 7% to about 8%, or about 5% to about 6%).

[0262] In some cases, protein compositions as described herein may have parameters that make them ideally suited as ingredients in food. For example, protein compositions as described herein may be one or more of the following: low color, low flavor, and detoxifying.

[0263] The color of a protein composition can be determined by any suitable measurement. In some cases, the relative lightness of the protein composition can be evaluated, where an internal white control is rated as 100 and an internal black control is rated as 0. In some embodiments, the protein composition as described herein may have a lightness of at least 85 (e.g., at least 86, 87, 88, 89, 90, 91, 92 or higher) on the relative scale. In some embodiments, the protein composition as described herein may have a lightness of at least 85 (e.g., at least 85.5, 86, 86.5, 87, 87.5, 88, 88.5, 89, 89.5, 90, 90.5, 91, 91.5, 92 or higher) on the relative scale. In some cases, the chromaticity of the protein composition (a unitless measure given herein on a scale of 0-100) can be evaluated, for example, using a colorimeter or colorimeter. In some embodiments, the protein composition as described herein may have a chromaticity value of less than 15 (e.g., less than 14, 13, 12, 11, 10, 9, 8, 7, 6, 5 or lower). In some embodiments, the protein composition as described herein may have a chromaticity value of less than 15 (e.g., less than 14.5, 14, 13.5, 13, 12.5, 12, 11.5, 11, 10.5, 10, 9.5, 9, 8.5, 8, 7.5, 7, 6.5, 6, 5.5, 5 or lower). In some embodiments, the low-color protein composition may have a lightness value of at least about 85 (e.g., at least 86, 87, 88, 89, 90, 91, 92 or higher), a chromaticity value of less than 15 (e.g., less than 14, 13, 12, 11, 10, 9, 8, 7, 6, 5 or lower), or both. In some embodiments, the low-color protein composition may have a luminance of at least about 85 (e.g., at least 85.5, 86, 86.5, 87, 87.5, 88, 88.5, 89, 89.5, 90, 90.5, 91, 91.5, 92 or higher), a chromaticity value of less than 15 (e.g., less than 14.5, 14, 13.5, 13, 12.5, 12, 11.5, 11, 10.5, 10, 9.5, 9, 8.5, 8, 7.5, 7, 6.5, 6, 5.5, 5 or lower), or both.

[0264] The flavor of a protein composition (or, for example, the protein source, source protein composition, or commercial protein product in the protein composition) can be determined using any suitable method. In some cases, the protein composition, the protein source, source protein composition, or commercial protein product in the composition may be ground into a powder prior to flavor analysis. Grinding into a powder can be performed by any suitable method. For example, a cryogenic grinder (e.g., a SPEX cryogenic grinder) or a mixer (e.g., a high-performance mixer, such as a Vitamix mixer, in which case temperature is optionally monitored) may be used. In some embodiments, the amount of one or more volatile compounds produced by the protein composition (or the protein source, source protein composition, or commercial protein product in the protein composition, for example, for the purpose of comparison with the protein composition provided herein) (e.g., as a 1% (w / v) suspension) can be evaluated without heating (e.g., without cooking). In some embodiments, the amount of one or more volatile compounds produced by cooking the protein composition (or the protein source, source protein composition, or commercial protein product in the protein composition, for example, for the purpose of comparison with the protein composition provided herein) (e.g., as a 1% (w / v) suspension) can be evaluated. In some embodiments, the protein composition (or the protein source, source protein composition, or commercial protein product in the protein composition, for example, for comparison purposes with the protein compositions provided herein) may be cooked in water (e.g., tap water). In some embodiments, the protein composition (or the protein source, source protein composition, or commercial protein product in the protein composition, for example, for comparison purposes with the protein compositions provided herein) may be cooked in a flavored broth. In some embodiments, the flavored broth comprises one or more (e.g., two or more, three or more, four or more, or five or more) flavor precursor molecules or compounds. The one or more flavor precursors may include at least one compound selected from the group consisting of: glucose, ribose, cysteine, cysteine ​​derivatives, thiamine, alanine, methionine, lysine, lysine derivatives, glutamic acid, glutamic acid derivatives, IMP, GMP, lactic acid, maltodextrin, creatine, alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, valine, linoleic acid, and mixtures thereof. Suitable flavor precursors may include sugars, sugar alcohols, sugar derivatives, oils (e.g., vegetable oils), free fatty acids, α-hydroxy acids, dicarboxylic acids, amino acids and their derivatives, nucleosides, nucleotides, vitamins, peptides, protein hydrolysates, extracts, phospholipids, lecithin, and organic molecules. In some embodiments, the flavor broth may contain reducing sugars, sulfur-containing amino acids, and heme-containing proteins.In some cases, protein isolates as described herein may produce fewer of one or more volatile compounds during cooking compared to the amount of one or more volatiles produced by cooking the protein source in a protein composition (or a source protein composition, or a commercial protein isolate, for example, for comparison with the protein isolates provided herein). In some cases, protein isolates as described herein may produce a greater amount of one or more volatiles in the meat volatiles group when cooked in flavored broths compared to the amount of one or more volatiles in the meat volatiles group produced by cooking the source protein composition in a protein composition (or a source protein composition, or a commercial protein isolate, for example, for comparison with the protein isolates provided herein). In some cases, where 1% (w / v) of the protein composition produces one or more volatile compounds related to the aroma and / or flavor of meat when cooked in a solution comprising reducing sugars, sulfur-containing amino acids, and heme-containing proteins. In some embodiments, when reducing sugars, sulfur-containing amino acids, and heme-containing proteins are cooked in the absence of a protein composition, at least one of one or more volatile compounds associated with the aroma and / or flavor of meat is produced in small amounts. In some embodiments, when reducing sugars, sulfur-containing amino acids, and heme-containing proteins are cooked in the absence of a protein composition, at least one of one or more volatile compounds associated with the aroma and / or flavor of meat is not produced. In some embodiments, the one or more volatile compounds associated with the aroma and / or flavor of meat include at least one compound selected from the group consisting of 2,3-butanedione, 2,3-pentanedione, thiazole, 2-acetylthiazole, benzaldehyde, 3-methylbutyraldehyde, 2-methylbutyraldehyde, thiophene, pyrazine, and combinations thereof. In some cases, “cooking” may mean sealing a 3 ml sample in a 20 ml GC glass vial and cooking it for 3 minutes in a heating block at 150 degrees Celsius with vigorous agitation (e.g., 750 rpm). In some cases, gas chromatography-mass spectrometry (GCMS) can be used to evaluate volatile compounds. For example, volatile compounds can be extracted from the headspace of a 1% (w / v) suspension (cooked or uncooked) using a solid-phase microextraction (SPME) fiber (e.g., DVB / CAR / PDMS) at 50 °C. Volatile compounds can be separated on a chromatographic column (e.g., on a capillary wax column with a temperature ramp of 35 °C to 255 °C). Mass spectra can be collected, for example at 10 Hz, with a mass range of 20 to 500.

[0265] In some cases, one or more volatile compounds can indicate the source of the protein in a protein composition. For example, if the protein source in a protein composition is soybean, a reduction in the amount of one or more soybean flavor compounds may be observed in some cases. Non-limiting examples of flavor compounds (e.g., soybean flavor compounds) include hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonanal, (E,Z)-2,6-nonadienal, (E,E)-2,4-decadienal, and combinations thereof. Flavor compounds (e.g., soybean flavor compounds) may contain isoflavones or saponins. Other examples of soybean flavor compounds can be found in the literature, such as in Kao, Jian-Wen, Earl G. Hammond, and Pamela J. White, “Volatile compounds produced during deodorization of soybean oil and their flavor significance,” *Journal of the American Oil Chemists' Society*, 75.12 (1998): 1103-1107; and in Solina, Marica, et al., “Volatile aroma components of soy protein isolate and acid-hydrolyzed vegetable protein,” *Food Chemistry*, 90.4 (2005): 861-873; and in Irwin, Anthony J., John D. Everard, and Robert J. Micketts. "Identification of Flavor-Active Volatiles in Soy Protein Isolate via Gas Chromatography-Olfactometry." *Chemistry, Texture, and Flavor of Soy*. American Chemical Society, 2010. 389-400; or Lei, Q, and WL.Boatright, “Compounds contributing to the odor of aqueous slurries of soy protein concentrate”. Journal of Food Science 66.9 (2001): 1306-1310. Ramasamy Ravi, Ali Taheri, Durga Khandekar, and Reneth Millas. “Rapid Profiling of Soybean Aromatic Compounds Using Electronic Nose”. Biosensors 2019, 9(2), 66, each of which is incorporated herein by reference in its entirety. Other examples of flavor compounds can be found in the literature, for example in Wibke SU Roland et al., “Flavor Aspects of Pulse Ingredients,” *Cereal Chemistry*, 2017, 94(1), 58-65, which is incorporated herein by reference in its entirety.

[0266] In some embodiments, when cooked in water (e.g., as a 1% (w / v) suspension), the protein composition as described herein may produce a smaller amount (e.g., no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of one or more compounds from a group of volatile compounds compared to the amount of one or more compounds produced by cooking the protein source (or, for example, the source protein composition used to prepare the protein composition) in the protein composition (e.g., as a 1% (w / v) suspension) in the group of volatile compounds. In some embodiments, when cooked in a flavored broth (e.g., as a 1% (w / v) suspension), the protein composition as described herein may produce a smaller amount (e.g., no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of one or more compounds from a group of volatile compounds compared to the amount of one or more compounds produced by cooking the protein source (or, for example, the source protein composition used to prepare the protein composition) in the flavored broth (e.g., as a 1% (w / v) suspension).

[0267] In some embodiments, when cooked in water (e.g., as a 1% (w / v) suspension), the protein isolate as described herein may produce a smaller amount (e.g., no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of one or more compounds from a group of volatile compounds compared to the amount produced by cooking a commercial protein isolate (e.g., as a 1% (w / v) suspension) in water. In some embodiments, when cooked in flavored broth (e.g., as a 1% (w / v) suspension), the protein isolate as described herein may produce a smaller amount (e.g., no more than 90% (e.g., no more than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10%) of one or more compounds from a group of volatile compounds compared to the amount produced by cooking a commercial protein isolate (e.g., as a 1% (w / v) suspension) in flavored broth.

[0268] In some embodiments, a group of volatile compounds may include volatile compounds in group 1. In some embodiments, a group of volatile compounds may be volatile group 1. In some embodiments, a group of volatile compounds may include compounds in volatile group 2. In some embodiments, a group of volatile compounds may be volatile group 2. In some embodiments, a group of volatile compounds may include compounds in volatile group 3. In some embodiments, a group of volatile compounds may be volatile group 3. In some embodiments, a group of volatile compounds may include compounds in volatile group 4. In some embodiments, a group of volatile compounds may be volatile group 4. In some embodiments, a group of volatile compounds may include compounds in volatile group 5. In some embodiments, a group of volatile compounds may be volatile group 5. In some embodiments, a group of volatile compounds may include compounds in volatile group 6. In some embodiments, a group of volatile compounds may be volatile group 6. In some embodiments, a group of volatile compounds may include compounds in volatile group 7. In some embodiments, a group of volatile compounds may be volatile group 7. In some embodiments, a group of volatile compounds may include compounds in volatile group 8. In some embodiments, a group of volatile compounds may be volatile group 8. In some embodiments, a group of volatile compounds may include compounds from volatile group 9. In some embodiments, a group of volatile compounds may be volatile group 9. In some embodiments, a group of volatile compounds may include compounds from volatile group 10. In some embodiments, a group of volatile compounds may be volatile group 10.

[0269] Commercial protein products can be any suitable commercial protein product, such as commercial soy protein products (e.g., soy protein isolate).

[0270] In some embodiments, the protein compositions provided herein, or foods comprising such protein compositions, can be advantageously evaluated by a group of trained tasters. In some embodiments, when evaluated by a trained descriptive panel using the Spectrum method, the protein compositions described herein are described as having low intensity of one or more of the following: oxidized / putrid flavor, cardboard flavor, astringent flavor, bitter flavor, vegetable complex flavor, and sweet fermented flavor. In some embodiments, when evaluated by a trained descriptive panel using the Spectrum method, the protein compositions described herein are described as having low intensity of one or more of the following: beany flavor, fatty flavor, raw flavor, pea flavor, earthy flavor, hay-like flavor, grassy flavor, putrid flavor, leafy flavor, cardboard flavor, spicy flavor, pungent flavor, medicinal flavor, metallic flavor, and broth flavor. In some cases, trained panel members are able to distinguish the protein compositions provided herein from different protein compositions (e.g., commercial protein products), or to distinguish foods containing them. In some embodiments, the protein composition has a discriminability index of at least 1.0 (e.g., at least 1.5, 2.0, 2.5, or 3.0) when evaluated by a trained panel.

[0271] In some embodiments, other small molecules that are part of the protein source in the protein composition are also reduced compared to the protein source in the protein composition as described herein. In some embodiments, the small molecules may have economic value outside the context of the protein composition as described herein. In some embodiments, the protein composition may contain less than 90% by weight (e.g., less than 80%, 70%, 60%, 50%, 40%, 30%, 20%, or 10% by weight) of one or more other small molecules. For example, when the protein source in the protein composition is soybean, one or more isoflavones (e.g., genistein, daidzein, genistein, or combinations thereof) may be depleted compared to soybean or defatted soy flour.

[0272] In some embodiments, the protein composition as described herein may comprise one or more added ingredients. In some cases, the added ingredients may be one or more of preservatives, antioxidants, or shelf-life extenders. Non-limiting examples of preservatives, antioxidants, or shelf-extenders include 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglycerides or diglycerides, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​hydrochloride, lecithin, lecithin citrate. Salt, Leuconostoc mesenteroides, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0273] The protein composition described herein can be in any suitable form. In some embodiments, the protein composition can be in the form of a solution, suspension, or emulsion. In some embodiments, the protein composition can be in the form of a solid or powder. In some embodiments, the protein composition is in the form of an extrudate. In some cases, the extrudate can be substantially in the form of granules. The granules can have an average maximum size of about 3 mm to about 5 mm. In some embodiments, less than about 20% (w / w) of the granules can have a maximum size of less than 1 mm. In some embodiments, less than 5% (w / w) of the granules can have a maximum size of more than 1 cm. In some embodiments, the extrudate can have a concentration of about 0.25 to about 0.4 g / cm³. 3The bulk density. In some embodiments, the extrudate may have a moisture content of about 5% to about 10%. In some embodiments, the extrudate may have a protein content of about 65% to about 100% on a dry weight basis. In some embodiments, the extrudate may have a fat content of less than about 2%. In some embodiments, the extrudate may have a sugar content of less than about 1%. In some embodiments, the extrudate may have a hydration ratio of about 2.5 to about 3 after hydration at room temperature for about 60 minutes. In some embodiments, the extrudate may have a hydration time of less than about 30 minutes. In some embodiments, the extrudate may have a pH of about 5.0 to about 7.5 when hydrated. In some embodiments, the extrudate may have a bite strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0274] This document also provides food products comprising any protein composition as described herein and / or protein compositions produced by any of the methods described herein. Food products as described herein may optionally further comprise fats (e.g., non-animal fats) and one or more flavor precursor compounds. Food products may take any suitable form, such as those described herein. In some embodiments, the food product may be a meat analogue. In some embodiments, the food product may be a beverage. In some embodiments, the food product may be a milk replica (e.g., a milk replica).

[0275] As used herein, “food” means (1) articles of food or beverages for human or other animal use, (2) chewing gum, and (3) articles of ingredients in any such articles.

[0276] As used in this article, “plant-based food” is a food in which at least 50% (e.g., at least 60%, 70%, 80%, 90% or more) of the ingredients by dry weight are derived from plants.

[0277] As used in this article, "algae-based food" is a food in which at least 50% (e.g., at least 60%, 70%, 80%, 90% or more) of the ingredients by dry weight are derived from algae.

[0278] As used herein, “fungus-based food” is a food in which at least 50% (e.g., at least 60%, 70%, 80%, 90% or more) of the ingredients by dry weight are derived from fungi.

[0279] As used herein, “invertebrate-based food” is a food in which at least 50% (e.g., at least 60%, 70%, 80%, 90% or more) of the ingredients by dry weight are derived from invertebrates (e.g., insects and / or arachnids).

[0280] The protein compositions described herein or produced by the methods described herein may be included in food in any suitable amount. For example, in some embodiments, the protein compositions described herein or produced by the methods described herein may be included in food in an amount of about 1% to about 99% (e.g., about 5% to about 80% or about 10% to about 30% based on the dry weight of the food).

[0281] In some embodiments, this document also provides a method for preparing a food comprising combining a fat, one or more optional flavor precursor compounds, and a protein composition as described herein or a protein composition prepared by the methods described herein.

[0282] In some embodiments, the food as described herein may contain less than 10% (e.g., less than 5% or less than 1%) of animal products by weight. In some embodiments, the food may not contain animal products. In some embodiments, the food may not contain animal meat. In some embodiments, the food may not contain animal blood. In some embodiments, the food may not contain animal products containing heme.

[0283] Fat can be present in food in any suitable amount. For example, fat can be present in a lower amount in lean meat analogues (e.g., chicken breast analogues) or in a higher amount in high-fat meat analogues (e.g., bacon analogues). In some embodiments, fat can be present in lean meat analogues in an amount of about 0.1% to about 5%. In some embodiments, fat can be present in adipose tissue analogues in an amount of about 85% to about 90%. In some embodiments, minced meat analogues can contain about 10% to about 25% (e.g., about 10% to about 15%, about 10% to about 20%, about 15% to about 25%, or about 20% to about 25%) of fat. In some embodiments, milk replicas can contain about 0.01% to about 5% (e.g., about 0.01% to about 0.1%, about 0.1% to about 1%, or about 1% to about 5%) of fat by weight of the milk replica.

[0284] Non-limiting examples of flavor precursor molecules include glucose, ribose, cysteine, cysteine ​​derivatives, thiamine, alanine, methionine, lysine, lysine derivatives, glutamic acid, glutamic acid derivatives, IMP, GMP, lactic acid, maltodextrin, creatine, alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, valine, linoleic acid, and mixtures thereof.

[0285] This document also provides methods for preparing food. In some embodiments, the method may comprise combining fat, one or more optional flavor precursor compounds, and any protein composition as described herein (e.g., low-flavor protein isolates or low-color protein compositions in the form of protein isolates or protein concentrates).

[0286] This document also provides methods for reducing perceived protein source flavor in foods (e.g., plant-based foods, algae-based foods, fungal-based foods, or invertebrate-based foods). The methods may comprise combining fats, one or more optional flavor precursor compounds, and any protein composition as described herein (e.g., low-flavor protein isolates or low-color protein compositions in the form of protein isolates or protein concentrates), wherein at least 5% by weight (e.g., at least 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, or more) of the protein content of the food comprises the protein composition, compared to foods with similar protein content but lacking the protein composition.

[0287] Any protein composition described herein may be included in a variety of foods, including meat replicas, dairy replicas (e.g., milk replicas or cheese replicas), and beverages (e.g., protein supplement drinks, sports drinks, protein shakes, protein pellets, energy drinks, caffeinated beverages, coffee drinks (e.g., milk coffee), milk, fermented milk, smoothies, carbonated beverages, alcoholic beverages, meal replacement drinks, or infant formula). In some cases, any protein composition described herein may be sold to consumers for use in food products at the consumer's discretion (e.g., protein supplement baked goods). Meat replicas may be formulated as, for example, ground meat (e.g., ground beef, pork, or chicken), sausages (e.g., breakfast sausages, multi-flavored sausages, or hot dogs), or slices of meat (e.g., steak, roast meat, loin, breast, thigh, leg, or wing).

[0288] Exemplary food products are described in U.S. Patent Nos. 10,039,306, 9,700,067, and 9,011,949; and U.S. Patent Application Publication Nos. US20150305361A1, US20170172169A1, US20150289541A1, and US20170188612A1 (each of which is incorporated herein by reference in its entirety).

[0289] In some embodiments, the food may be a protein supplement. For example, in some embodiments, the protein composition disclosed herein may be part of a protein powder that can be used in protein shakes, smoothies, baking, etc.

[0290] In some embodiments, the food may contain muscle replicas. In some embodiments, the food may contain fat replicas. In some embodiments, the food may contain both muscle replicas and fat replicas. In some embodiments, a food containing both muscle replicas and fat replicas may also be referred to as a meat replica.

[0291] In some embodiments, the food product may be a milk replica (e.g., a replica of milk, fermented milk, yogurt, cream, butter, cheese, custard, ice cream, gelatin, or frozen yogurt). In some embodiments, the food product may be a cheese replica. In some embodiments, the food product may be a milk replica. In some embodiments, a milk replica comprising the protein composition described herein may have one or more properties more similar to animal milk than other non-dairy milks, including, for example, a whiter color, a better mouthfeel, greater stability (e.g., greater emulsion stability, non-coagulation in hot or acidic liquids such as coffee), or combinations thereof. In some embodiments, the milk replica may have a protein content similar to or greater than that of cow's milk. In some embodiments, the milk replica may have a protein content of about 20 mg / mL to about 60 mg / mL (e.g., about 30 mg / mL to about 55 mg / mL, about 25 mg / mL to about 35 mg / mL), some or all of which may be the protein composition described herein and / or a protein composition produced by the methods described herein. For example, in some embodiments, the milk replica is stable (e.g., the emulsion does not break down) when added to a liquid at a temperature of about 70°C to about 100°C (e.g., about 80°C to about 100°C, about 80°C to about 98°C, about 70°C to about 80°C, about 70°C to about 95°C, about 70°C to about 85°C, or about 80°C to about 85°C). In some embodiments, the milk replica is stable (e.g., the emulsion does not break down) when added to a liquid with a pH of about 4.0 to about 8.0 (e.g., about 4.0 to about 7.0, about 4.5 to about 6.5, about 4.5 to about 6.0). In some embodiments, the milk replica can be used to make cheese replicas.

[0292] In some embodiments, this document provides an emulsion comprising a fat, water, and protein composition as described herein, or a milk replica comprising a protein composition produced by methods described herein. In some embodiments, fat is present in the milk replica in an amount of about 0.01% to about 5% (e.g., about 0.01% to about 0.1%, about 0.01% to about 0.5%, about 0.01% to about 1%, about 0.01% to about 2%, about 0.01% to about 3%, about 0.01% to about 4%, about 0.1% to about 5%, about 0.5% to about 5%, about 1% to about 5%, about 2% to about 5%, about 3% to about 5%, or about 4% to about 5%). In some embodiments, the fat is selected from the group consisting of corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flaxseed oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango oil, cocoa butter, wheat germ oil, rice bran oil, and combinations thereof.

[0293] In some embodiments, the food may be an egg replica. In some embodiments, the food may be a whole egg replica (e.g., where the yolk replica is separate from the white replica). In some embodiments, the food may be an egg yolk replica. In some embodiments, the food may be an egg white replica. In some embodiments, the food may be a scrambled egg replica (e.g., a mixture of egg yolk and egg white replicas).

[0294] Food products may contain one or more proteins (e.g., protein compositions as described herein, commercially available proteins, proteins purified by any method known in the art, or combinations thereof). In some embodiments, a food product may contain any protein composition as described herein. In some embodiments, a food product may contain any protein composition as described herein, in addition to commercially available proteins (e.g., soy protein concentrate, soy protein isolate, casein, whey, wheat gluten, pea lectin, or pea protein). In some embodiments, a food product may contain any protein composition as described herein, in addition to one or more proteins purified by any method known in the art.

[0295] One or more proteins (e.g., protein compositions as described herein, commercially available proteins, proteins purified by any method known in the art, or combinations thereof) may be present in the food (e.g., meat replicas, dairy replicas, or supplements) at a weight of about 0.1% to about 100% (e.g., about 0.1% to about 1%, about 1% to about 5%, about 5% to about 10%, about 1% to about 10%, about 10% to about 20%, about 20% to about 30%, about 30% to about 40%, about 40% to about 50%, about 50% to about 60%, about 60% to about 70%, about 70% to about 80%, about 80% to about 90%, about 90% to about 100%). The following amounts are present: about 10% to about 30%, about 30% to about 50%, about 50% to about 70%, about 70% to about 90%, about 0.1% to about 20%, about 20% to about 40%, about 40% to about 60%, about 60% to about 80%, about 80% to about 100%, about 0.1% to about 33%, about 33% to about 66%, about 66% to about 100%, about 0.1% to about 50%, or about 50% to about 100%.

[0296] Any food product described herein may contain iron complexes (e.g., ferrous chlorophyllin (e.g., CAS No. 69138-22-3), ferrous pheophorbide (e.g., CAS No. 15664-29-6), iron salts (e.g., ferric sulfate (e.g., any one of CAS Nos. 7720-78-7, 17375-41-6, 7782-63-0, or 10028-22-5), ferric gluconate (e.g., any one of CAS Nos. 299-29-6, 22830-45-1, or 699014-53-4), ferric citrate (e.g., CAS No. 15664-29-6), iron salts (e.g., ferric sulfate (e.g., any one of CAS Nos. 299-29-6, 22830-45-1, or 699014-53-4), iron citrate (e.g., CAS No. 15664-29-6), iron salts (e.g., ferric sulfate ... CAS No. 1566 Any of the following: 3522-50-7, 2338-05-8 or 207399-12-0; EDTA iron (e.g., CAS number 17099-81-9); or heme (e.g., heme A (e.g., CAS number 18535-39-2), heme B (e.g., CAS number 14875-96-8), heme C (e.g., CAS number 26598-29-8), heme O (e.g., CAS number 137397-56-9), heme I, heme M, heme D, heme S)); or heme-containing proteins.

[0297] In some embodiments, the food may contain heme-containing proteins. In some embodiments, the food may contain heme-containing proteins in an amount of about 0.01% to about 5% (e.g., 0.01% to about 1%, about 0.01% to about 0.5%, about 0.01% to about 0.1%, about 0.01% to about 0.05%, about 0.05% to about 5%, about 0.1% to about 5%, about 0.5% to about 5%, about 1% to about 5%, about 0.05% to about 0.5%, or about 0.1% to about 0.5%) based on the weight of the food. In some embodiments, the heme-containing protein is a globin. In some embodiments, the globin is selected from the group consisting of androgenic hemoglobin, cytoglobin, globin E, globin X, globin Y, hemoglobin, myoglobin, legumehemoglobin, hemoglobin, β-hemoglobin, α-hemoglobin, protoglobin, cyanoglobin, cytoglobin, tissue globin, neuroglobin, hemoglobin, truncated hemoglobin, truncated 2 / 2 globin, and hemoglobin 3. In some embodiments, the heme-containing protein is a non-animal heme-containing protein. In some embodiments, the heme-containing protein is a plant, fungal, algal, archaea, or bacterial protein. In some embodiments, the heme-containing protein is not naturally expressed in plant, fungal, algal, archaea, or bacterial cells. In some embodiments, the heme-containing protein comprises an amino acid sequence having at least 50% sequence identity (e.g., at least 60%, 70%, 80%, 90%, or 95% sequence identity) with the polypeptides listed in SEQ ID NOs. 1-27.

[0298] Heme-containing proteins that can be used in any of the foods described herein can be derived from mammals (e.g., farm animals such as cattle, goats, sheep, pigs, cows, or rabbits), birds, plants, algae (e.g., mutagenic Chlamydomonas reinhardtii), fungi (e.g., yeasts or filamentous fungi), ciliates, or bacteria. For example, heme-containing proteins can be derived from mammals such as livestock (e.g., dairy cows, goats, sheep, pigs, fish, bulls, or rabbits) or birds such as turkeys or chickens. Heme-containing proteins can come from plants such as tobacco (Nicotiana tabacum) or Nicotiana asylvestris; corn (Zea mays); Arabidopsis thaliana; legumes such as soybean (Glycine max); chickpea (Cicer arietinum); pea varieties such as garden pea or sugar pea; common beans such as mung bean (Phaseolus vulgaris); black bean; saffron bean; cowpea (Vigna unguiculata); mung bean (Vigna radiata); white lupin (Lupinus albus); or alfalfa (Medicago). sativa (alfalfa); Brassica napus (canola); Triticum sps. (wheat, including wheat berries and spelt wheat); upland cotton (cotton); rice (rice); Zizania sps. (wild rice); Helianthus annuus (sunflower); Beta vulgaris (sugarbeet); Pennisetum glaucum (pearl millet); Quinoa; Sesamum sp. (sesame); Linum usitatissimum (flax); or Hordeum vulgare (barley).Heme-containing proteins can be isolated from fungi such as *Saccharomyces cerevisiae*, *Pichia pastoris*, *Magnaportheoryzae*, *Fusarium graminearum*, *Aspergillus oryzae*, *Trichoderma reesei*, *Myceliopthera thermophile*, *Kluyvera lactis*, or *Fusarium oxysporum*. Heme-containing proteins can also be isolated from bacteria such as *Escherichia coli*, *Bacillus subtilis*, *Bacillus licheniformis*, *Bacillus megaterium*, *Synechocistis* sp., *Aquifex aeolicus*, *Methylacidiphiluminfernorum*, or thermophilic bacteria such as *Thermophilus*. The sequences and structures of many heme-containing proteins are known. See, for example, Reedy et al., Nucleic Acids Research, 2008, Vol. 36, Database Special Issues D307-D313 and the heme protein database available on the World Wide Web at hemeprotein.info / heme.php.

[0299] For example, non-symbiotic hemoglobin can be derived from plants selected from the following groups: soybean, sprouted soybean, alfalfa, golden flax, black bean, black-eyed bean, northern bean, chickpea, mung bean, cowpea, black and white bean, pea pod, quinoa, sesame, sunflower, wheat flour, spelt wheat, barley, wild rice, or rice.

[0300] Any of the heme-containing proteins described herein that can be used in food production may have at least 70% (e.g., at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, 99%, or 100%) sequence identity with the corresponding wild-type heme-containing protein or fragment thereof containing a heme-binding motif.For example, heme-containing proteins can have at least 70% sequence identity with an amino acid sequence, including non-symbiotic hemoglobins, such as those from mung bean (SEQ ID NO:1), barley (SEQ ID NO:5), maize (SEQ ID NO:13), rice subsp. japonica (rice) (SEQ ID NO:14), or Arabidopsis thaliana (SEQ ID NO:15); hellgospherin I, for example from extreme acidophilic methanogens (SEQ ID NO:2); yellow heme proteins, for example from *Aeromonas hydrophila* (SEQ ID NO:3); legume hemoglobin, for example from soybean (SEQ ID NO:4), pea (SEQ ID NO:16), or cowpea (SEQ ID NO:17); heme-dependent peroxidases, for example from *Bacillus oryzae* (SEQ ID NO:6) or *Fusarium oxysporum* (SEQ ID NO:7); and those from *Fusarium graminearum* (SEQ ID NO:15). Cytochrome c peroxidase from NO:8; truncated hemoglobin from Chlamydomonas moewusii (SEQ ID NO:9), Tetrahymena pyriformis (SEQ ID NO:10, Group I truncated), Paramecium caudatum (SEQ ID NO:11, Group I truncated); hemoglobin from Aspergillus niger (SEQ ID NO:12); or mammalian myoglobin proteins, such as bovine (Bos taurus) myoglobin (SEQ ID NO:18), wild boar (Sus scrofa) myoglobin (SEQ ID NO:19), and horse (Equus caballus) myoglobin (SEQ ID NO:20); from Nicotiana benthamiana (SEQ ID NO:21), Bacillus subtilis (SEQ ID NO:22), and Corynebacterium glutamicum (SEQ ID NO:8). Heme proteins from *Synechococcus* sp. (SEQ ID NO: 23), *Synechococcus* sp. (SEQ ID NO: 24), *Nostoc commune* sp. (SEQ ID NO: 25), or *Bacillus megaterium* sp. (SEQ ID NO: 27).

[0301] The percentage of identity between two amino acid sequences can be determined as follows. First, the amino acid sequences are aligned using the BLAST 2 Sequences (Bl2seq) program, a standalone version of BLASTZ containing BLASTP version 2.0.14. This standalone version of BLASTZ is available from Fish & Richardson's website (e.g., www.fr.com / blast / ) or the National Center for Biotechnology Information website (ncbi.nlm.nih.gov). Instructions on how to use the Bl2seq program can be found in the readme accompanying BLASTZ. Bl2seq uses the BLASTP algorithm to compare two amino acid sequences. To compare two amino acid sequences, the Bl2seq options are set as follows: -i is set to the file containing the first amino acid sequence to be compared (e.g., C:\seq1.txt); -j is set to the file containing the second amino acid sequence to be compared (e.g., C:\seq2.txt); -p is set to blastp; -o is set to any desired filename (e.g., C:\output.txt); and all other options remain at their default settings. For example, the following command can be used to generate an output file containing the comparison between two amino acid sequences: C:\Bl2seq –ic:\seq1.txt –jc:\seq2.txt –p blastp –oc:\output.txt. If the two sequences being compared share homology, the specified output file will present those homologous regions as the aligned sequences. If the two sequences being compared do not share homology, the specified output file will not present the aligned sequences. A similar procedure can be followed for nucleic acid sequences, except that blastn is used.

[0302] After alignment, the number of matches is determined by counting the positions of identical amino acid residues in both sequences. The identity percentage is determined by dividing the number of matches by the length of the full-length polypeptide amino acid sequence and then multiplying the result by 100. It should be noted that the identity percentage value is rounded to one decimal place. For example, 78.11, 78.12, 78.13, and 78.14 are rounded down to 78.1, while 78.15, 78.16, 78.17, 78.18, and 78.19 are rounded up to 78.2. It should also be noted that the length value will always be an integer.

[0303] It should be understood that many nucleic acids can encode polypeptides with specific amino acid sequences. The degeneracy of the genetic code is well known in the art; that is, for many amino acids, there are more than one nucleotide triplet that can act as a codon for the amino acid. For example, using an appropriate codon bias table for a specific species (e.g., bacteria or fungi), codons in the coding sequence of a given enzyme can be modified to obtain optimal expression in said species (e.g., bacteria or fungi).

[0304] In some embodiments, heme-containing proteins can be extracted from the producing organism (e.g., from animal tissue or plant, fungal, algal, or bacterial biomass, or from the supernatant of a culture containing secreted proteins) or from a combination of producing organisms (e.g., multiple plant species). Legume-based legume hemoglobin is readily available as an unused byproduct of commercial legume crops (e.g., soybean, alfalfa, or pea). In the United States, the amount of legume-based legume hemoglobin in the roots of these crops exceeds the myoglobin content of all red meat consumed in the United States.

[0305] In some embodiments, the extract of heme-containing proteins comprises one or more heme-free proteins derived from source materials (e.g., proteins from other animals, plants, fungi, algae, or bacteria) or from combinations of source materials (e.g., different animals, plants, fungi, algae, or bacteria).

[0306] In some embodiments, the heme-containing protein may be provided in food in a form that is not part of the protein composition described herein. In some embodiments, the heme-containing protein may be purified by any method known in the art.

[0307] This document also provides a method for evaluating the effect of a protein composition on the flavor of a food, the method comprising determining that the level of one or more volatile compounds of a first protein composition from a protein source is higher than the level of one or more volatile compounds of a second protein composition from a protein source; and determining that the second protein composition is superior to the first protein composition for use in the food. In some embodiments, the second protein composition is a protein composition as described herein or a protein composition produced by the methods described herein. In some embodiments, the first protein composition is neither a protein composition as described herein nor a protein composition produced by the methods described herein.

[0308] This document also provides a method for evaluating the effect of a protein composition on the flavor of a food, the method comprising determining that the level of one or more volatile compounds in a group of volatile compounds from a protein source protein composition is higher than the level of one or more volatile compounds from the protein composition itself; and determining that the protein composition is superior to the source protein composition used in the food. In some embodiments, the protein composition is a protein composition as described herein, or a protein composition produced by the methods described herein.

[0309] In some embodiments, the set of volatile compounds includes volatile compounds from any one of volatile groups 1-10. In some embodiments, the set of volatile compounds is any one of volatile groups 1-10. In some embodiments, the set of volatile compounds is selected from the group consisting of volatile groups 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, and combinations thereof. In some embodiments, the protein source is a plant, fungus, algae, bacteria, protozoa, invertebrate, or a combination thereof. In some embodiments, the protein source is soybean. In some embodiments, the set of volatile compounds includes at least one compound selected from the group consisting of hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonanal, (E,Z)-2,6-nonadienal, and (E,E)-2,4-decadienal. In some embodiments, a group of volatile compounds is hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonanal, (E,Z)-2,6-nonadienal, and (E,E)-2,4-decadienal. In some embodiments, the food is a meat replica. In some embodiments, the food is plant-based. In some embodiments, the food contains less than 10% by weight of animal products. In some embodiments, the food contains less than 5% by weight of animal products. In some embodiments, the food contains less than 1% by weight of animal products. In some embodiments, the food does not contain animal products.

[0310] This document also provides a method for reducing flavor in a protein composition, the method comprising: (a) determining the level of one or more volatile compounds in a group of volatile compounds of a first protein composition derived from a protein source; (b) preparing a second protein composition from the protein source, wherein preparing the second protein composition includes reducing the amount of one or more components of the protein source contained in the second protein composition; and (c) determining that the level of one or more volatile compounds in a group of volatile compounds of the second protein composition is lower than the level of one or more volatile compounds in a group of volatile compounds of the first protein composition.

[0311] This document also provides a method for determining the cause of flavor in a protein composition, the method comprising: (a) determining the level of one or more volatile compounds in a group of volatile compounds of a first protein composition from a protein source; (b) providing a second protein composition from the protein source, wherein the second protein composition comprises a reduced amount of one or more components of the protein source; (c) determining that the level of one or more volatile compounds in a group of volatile compounds from the second protein composition is lower than the level of one or more volatile compounds in a group of volatile compounds of the first protein composition; and (d) identifying one or more components of the protein source as the cause of flavor in the protein composition.

[0312] In some embodiments, the second protein composition may be a protein composition as described herein, or a protein composition produced by the methods described herein. In some embodiments, the set of volatile compounds includes volatile compounds from any one of volatile groups 1-10. In some embodiments, the set of volatile compounds is any one of volatile groups 1-10. In some embodiments, the set of volatile compounds is selected from the group consisting of volatile groups 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, and combinations thereof. In some embodiments, the protein source is a plant, fungus, algae, bacteria, protozoa, invertebrate, or a combination thereof. In some embodiments, the protein source is soybean. In some embodiments, the group of volatile compounds includes at least one compound selected from the group consisting of: hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonanal, (E,Z)-2,6-nonadienal, and (E,E)-2,4-decadienal. In some embodiments, the group of volatile compounds is hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonanal, (E,Z)-2,6-nonadienal, and (E,E)-2,4-decadienal. In some embodiments, the components reduced in the protein source include lipids. In some embodiments, the components reduced in the protein source include fatty acids, waxes, sterols, monoglycerides, diglycerides, triglycerides, sphingolipids, phospholipids, or combinations thereof. In some embodiments, the components reduced in the protein source include phospholipids. In some embodiments, the amount of reduction of one or more components of the protein source in the second protein composition is at least 10% (e.g., at least 30%, 50%, 70%, or 90%) compared to the first protein composition.

[0313] Exemplary embodiments

[0314] Example 1 is a protein composition comprising:

[0315] At least 50% by dry weight of various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0316] The protein composition described therein is a low-color protein composition.

[0317] Example 2 is a protein composition comprising:

[0318] At least 50% by dry weight of various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof;

[0319] Lipids less than 1.0% on a dry weight basis.

[0320] Example 3 is a protein composition produced by a method comprising the following steps:

[0321] (a) Adding an aqueous solution to the source protein composition to form a solution of dissolved protein;

[0322] (b) Optionally, remove the solid from the solution of the dissolved protein;

[0323] (c) Optionally, heat the solution of the dissolved protein;

[0324] (d) Optionally, the pH of the solution of the dissolved protein is adjusted to about 4.0 to about 9.0;

[0325] (e) Optionally, the solution of the dissolved protein is cooled to about 0°C to about 10°C;

[0326] (f) Add an organic solvent to the solution of the dissolved protein to form a solid phase and a liquid phase;

[0327] (g) Separating the solid phase from the liquid phase to form the protein composition;

[0328] (h) Optionally, the protein composition is washed with a washing solvent; and

[0329] (I) Optionally, the protein composition is treated.

[0330] The protein composition therein comprises at least 50% by dry weight of a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0331] Example 4 is a protein composition described in any of Examples 2-3, wherein the protein composition is a low-color protein composition.

[0332] Example 5 is a protein composition described in any of Examples 1-4, wherein the protein composition comprises at least about 90% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0333] Example 6 is a protein composition described in any of Examples 1-4, wherein the protein composition comprises at least about 91% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0334] Example 7 is a protein composition described in any of Examples 1-4, wherein the protein composition comprises at least about 93% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0335] Example 8 is a protein composition described in any of Examples 5-7, wherein the protein composition is a protein isolate.

[0336] Example 9 is the protein composition described in Example 8, wherein the protein composition comprises less than 8% insoluble carbohydrates on a dry weight basis.

[0337] Example 10 is a protein composition described in any of Examples 8-9, wherein the protein composition is a low-flavor protein composition.

[0338] Example 11 is a protein composition described in any of Examples 8-10, wherein the protein composition has an isoflavone content of less than about 150 ppm.

[0339] Example 12 is a protein composition described in any of Examples 8-11, wherein the protein composition has an isoflavone content of less than about 125 ppm.

[0340] Example 13 is a protein composition described in any of Examples 8-12, wherein the protein composition has an isoflavone content of less than about 100 ppm.

[0341] Example 14 is a protein composition described in any of Examples 8-13, wherein the protein composition has an isoflavone content of less than about 75 ppm.

[0342] Example 15 is a protein composition described in any of Examples 8-14, wherein the protein composition has a saponin content of less than about 75 ppm.

[0343] Example 16 is a protein composition described in any of Examples 8-15, wherein the protein composition has a saponin content of less than about 50 ppm.

[0344] Example 17 is a protein composition described in any of Examples 8-16, wherein the protein composition has a saponin content of less than about 25 ppm.

[0345] Example 18 is a protein composition described in any of Examples 8-17, wherein the protein composition has a phospholipid content of less than about 500 ppm.

[0346] Example 19 is a protein composition described in any of Examples 8-18, wherein the protein composition has a phospholipid content of less than about 250 ppm.

[0347] Example 20 is a protein composition described in any of Examples 8-19, wherein the protein composition has a phospholipid content of less than about 100 ppm.

[0348] Example 21 is a protein composition described in any of Examples 8-20, wherein the protein composition has a phospholipid content of less than about 50 ppm.

[0349] Example 22 is a protein composition described in any of Examples 8-21, wherein the protein composition has a phospholipid content of less than about 25 ppm.

[0350] Example 23 is a protein composition described in any of Examples 8-22, wherein the protein composition has a phospholipid content of less than about 10 ppm.

[0351] Example 24 is a protein composition described in any of Examples 8-23, wherein the protein composition has a phospholipid content of less than about 5 ppm.

[0352] Example 25 is a protein composition described in any of Examples 8-24, wherein the protein composition has a phospholipid content of less than about 2 ppm.

[0353] Example 26 is a protein composition described in any of Examples 8-25, wherein the protein composition has a phospholipid content of less than about 1 ppm.

[0354] Example 27 is a protein composition described in any of Examples 1-5, wherein the protein composition comprises about 60% to about 80% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0355] Example 28 is the protein composition described in Example 27, wherein the protein composition comprises about 65% to about 75% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

[0356] Example 29 is the protein composition described in Example 27 or Example 28, wherein the protein composition is a protein concentrate.

[0357] Example 30 is the protein composition described in Example 29, wherein the protein composition comprises at least 9% insoluble carbohydrates on a dry weight basis.

[0358] Example 31 is a protein composition described in any of Examples 1-30, wherein the protein composition comprises less than 0.8% lipids on a dry weight basis.

[0359] Example 32 is a protein composition described in any of Examples 1-31, wherein the protein composition comprises less than 0.6% lipids on a dry weight basis.

[0360] Example 33 is a protein composition described in any of Examples 1-32, wherein the protein composition comprises less than 0.4% lipids on a dry weight basis.

[0361] Example 34 is a protein composition described in any of Examples 1-33, wherein the protein composition has a brightness of at least 86 on a scale from 0 (black control value) to 100 (white control value).

[0362] Example 35 is a protein composition described in any of Examples 1-34, wherein the protein composition has a brightness of at least 88 on a scale from 0 (black control value) to 100 (white control value).

[0363] Example 36 is a protein composition described in any of Examples 1-35, wherein the protein composition has a brightness of at least 90 on a scale from 0 (black control value) to 100 (white control value).

[0364] Example 37 is a protein composition described in any of Examples 1-36, wherein the protein composition has a colorimetric value of less than 14.

[0365] Example 38 is a protein composition described in any of Examples 1-37, wherein the protein composition has a colorimetric value of less than 12.

[0366] Example 39 is a protein composition described in any of Examples 1-38, wherein the protein composition has a colorimetric value of less than 10.

[0367] Example 40 is a protein composition described in any of Examples 1-39, wherein the protein composition has a colorimetric value of less than 8.

[0368] Example 41 is a protein composition described in any of Examples 1-40, wherein the protein composition has a colorimetric value of less than 6.

[0369] Example 42 is a protein composition described in any of Examples 1-41, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% plant proteins.

[0370] Example 43 is a protein composition described in any of Examples 1-41, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% legume proteins.

[0371] Example 44 is a protein composition described in any of Examples 1-41, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% legume or fruit proteins.

[0372] Example 45 is a protein composition described in any of Examples 1-41, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% soybean protein.

[0373] Example 46 is a protein composition described in any of Examples 1-41, wherein a variety of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% fungal proteins.

[0374] Example 47 is a protein composition described in any of Examples 1-41, wherein the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise at least 90% algal proteins.

[0375] Example 48 is a protein composition according to any one of the embodiments of claims 1-47, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof are substantially denatured, aggregated, or both.

[0376] Example 49 is a protein composition described in any of Examples 1-48, wherein when cooked in a solution of a protein comprising reducing sugars, sulfur-containing amino acids and heme, 1% (w / v) of the protein composition produces one or more volatile compounds associated with the aroma and / or flavor of meat.

[0377] Example 50 is the protein composition described in Example 49, wherein when the reducing sugar, the sulfur-containing amino acid, and the heme-containing protein are cooked in the absence of the protein composition, at least one of the one or more volatile compounds associated with the aroma and / or flavor of meat is produced in a smaller amount.

[0378] Example 51 is the protein composition described in Example 49, wherein when the reducing sugar, the sulfur-containing amino acid, and the heme-containing protein are cooked in the absence of the protein composition, at least one of the one or more volatile compounds associated with the aroma and / or flavor of meat is not produced.

[0379] Example 52 is a protein composition described in any of Examples 49-51, wherein the one or more volatile compounds associated with the aroma and / or flavor of meat include at least one compound selected from the group consisting of 2,3-butanedione, 2,3-pentanedione, thiazole, 2-acetylthiazole, benzaldehyde, 3-methylbutyraldehyde, 2-methylbutyraldehyde, thiophene, pyrazine, and combinations thereof.

[0380] Example 53 is a protein composition described in any of Examples 1-52, wherein, when evaluated by a trained descriptive team using the Spectrum method, the protein composition is described as having a low intensity of one or more of the following: oxidative / putrid flavor, cardboard flavor, astringent flavor, bitter flavor, vegetable complex flavor, and sweet fermented flavor.

[0381] Example 54 is a protein composition described in any of Examples 1-52, wherein, when evaluated by a trained descriptive team using the Spectrum method, the protein composition is described as having a low intensity of one or more of the following: beany flavor, fatty flavor, raw flavor, pea flavor, earthy flavor, hay-like flavor, grassy flavor, putrid flavor, leafy flavor, cardboard flavor, spicy flavor, pungent flavor, medicinal flavor, metallic flavor, and broth flavor.

[0382] Example 55 is a protein composition described in any of Examples 1-54, wherein the protein composition has a discrimination index of at least 1.0 when evaluated by a trained panel.

[0383] Example 56 is a protein composition described in any of Examples 1-55, wherein the protein composition has a discrimination index of at least 1.5 when evaluated by a trained panel.

[0384] Example 57 is a protein composition described in any of Examples 1-56, wherein the protein composition has a discrimination index of at least 2.0 when evaluated by a trained panel.

[0385] Example 58 is a protein composition described in any of Examples 1-57, wherein the protein composition has a discrimination index of at least 2.5 when evaluated by a trained panel.

[0386] Example 59 is a protein composition described in any of Examples 1-58, wherein the protein composition has a discrimination index of at least 3.0 when evaluated by a trained panel.

[0387] Example 60 is a protein composition described in any of Examples 1-59, wherein the protein composition comprises less than about 0.5% phospholipids on a dry weight basis.

[0388] Example 61 is a protein composition described in any of Examples 1-60, wherein the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof constitute at least 90% soybean protein on a dry weight basis.

[0389] Example 62 is a protein composition described in any of Examples 1-61, further comprising at least one of a preservative, an antioxidant, or a shelf-life extender.

[0390] Example 63 is the protein composition described in Example 62, wherein the preservative, antioxidant, or shelf-life extender comprises at least one of the following: 4-hexylresorcinol, acetic acid, ascorbic acid, ascorbyl palmitate, ascorbyl stearate, benzoic acid, butylated hydroxyanisole (a mixture of 2-tert-butyl-4-hydroxyanisole and 3-tert-butyl-4-hydroxyanisole), butylated hydroxytoluene (3,5-di-tert-butyl-4-hydroxytoluene), calcium ascorbate, calcium propionate, calcium sorbate, Clostridium botulinum M35, Clostridium maltose cb1, Leuconostoc 4010, citric acid, citrate of monoglyceride or diglyceride, dimethyl carbonate, isoascorbic acid, ethyl lauroyl arginine, guaiac gum, isoascorbic acid, L-cysteine, L-cysteine ​​salt Salts, lecithin, lecithin citrate, Leuconostoc mesenteroides, methylparaben, methylparaben, glyceryl monocitrate, isopropyl citrate, natamycin, nisin, potassium acetate, potassium benzoate, potassium bisulfite, potassium diacetate, potassium lactate, sodium metabisulfite, potassium nitrate, potassium nitrite, potassium sorbate, propionic acid, propyl gallate, propylparaben, propylparaben, sodium acetate, sodium ascorbate, sodium benzoate, sodium bisulfite, sodium diacetate, sodium dithionite, sodium isoascorbate, sodium isoascorbate, sodium lactate, sodium metabisulfite, sodium nitrate, sodium nitrite, sodium propionate, sodium salt of methylparaben, sodium salt of propylparaben, sodium sorbate, sodium sulfite, sorbic acid, sulfurous acid, tartaric acid, tert-butylhydroquinone or tocopherol.

[0391] Example 64 is a protein composition described in any of Examples 1-63, wherein the protein composition is in the form of a solution, suspension or emulsion.

[0392] Example 65 is a protein composition described in any of Examples 1-63, wherein the protein composition is in solid or powder form.

[0393] Example 66 is the protein composition described in Example 65, wherein the protein composition has an average particle size of about 5 µm to about 40 µm at its maximum size.

[0394] Example 67 is a protein composition of Example 65, wherein the protein composition has an average particle size of about 10 µm to about 40 µm at the maximum size.

[0395] Example 68 is the protein composition described in Example 65, wherein the protein composition has an average particle size of about 10 µm to about 30 µm at its maximum size.

[0396] Example 69 is the protein composition described in Example 65, wherein the protein composition has an average particle size of about 10 µm to about 20 µm at its maximum size.

[0397] Example 70 is a protein composition described in any of Examples 1-69, wherein the protein composition is in the form of an extrusion.

[0398] Example 71 is the protein composition described in Example 70, wherein the extrudate is substantially in granular form.

[0399] Example 72 is the protein composition described in Example 71, wherein the particles have an average maximum size of about 3 mm to about 5 mm.

[0400] Example 73 is the protein composition described in Example 71 or Example 72, wherein less than about 20% (w / w) of the particles have a maximum size of less than 1 mm.

[0401] Example 74 is a protein composition described in any of Examples 71-73, wherein less than about 5% (w / w) of the particles have a maximum size of more than 1 cm.

[0402] Example 75 is a protein composition described in any of Examples 70-74, wherein the extrudate has a content of about 0.25 to about 0.4 g / cm³. 3 The packing density.

[0403] Example 76 is a protein composition described in any of Examples 70-75, wherein the extrudate has a moisture content of about 5% to about 10%.

[0404] Example 77 is a protein composition described in any of Examples 70-76, wherein the extrudate has a protein content of about 65% to about 100% on a dry weight basis.

[0405] Example 78 is a protein composition described in any of Examples 70-77, wherein the extrudate has a fat content of less than about 1.0%.

[0406] Example 79 is a protein composition described in any of Examples 70-78, wherein the extrudate has a sugar content of less than about 1%.

[0407] Example 80 is a protein composition described in any of Examples 70-79, wherein the extrudate has a hydration ratio of about 2.5 to about 3 after about 60 minutes of hydration at room temperature.

[0408] Example 81 is a protein composition described in any of Examples 70-80, wherein the extrudate has a hydration time of less than about 30 minutes.

[0409] Example 82 is a protein composition described in any of Examples 70-81, wherein the extrudate has a pH of about 5.0 to about 7.5 when hydrated.

[0410] Example 83 is a protein composition described in any of Examples 70-82, wherein the extrudate has an occlusive strength of about 2000 g to about 4000 g at a hydration ratio of about 3.

[0411] Example 84 is the protein composition described in Example 3 or any of Examples 4-83 which are subordinate to Example 3, wherein step (a) is performed at a pH of about 7.0 to about 10.0.

[0412] Example 85 is the protein composition described in Example 3 or any of Examples 4-84 which are subordinate to Example 3, wherein step (a) is performed at a pH of about 6.0 to about 9.0.

[0413] Example 86 is the protein composition described in Example 3 or any of Examples 4-85 which are subordinate to Example 3, wherein step (a) is carried out at a pH of about 7.5 to about 8.5.

[0414] Example 87 is a protein composition described in Example 3 or any of Examples 4-86 which are subordinate to Example 3, wherein step (b) includes centrifugation, filtration or a combination thereof.

[0415] Example 88 is a protein composition described in Example 3 or any of Examples 4-87 which are subordinate to Example 3, wherein step (d) includes adjusting the pH of the solution of the dissolved protein to about 4.0 to about 6.0.

[0416] Example 89 is a protein composition described in Example 3 or any of Examples 4-88 which are subordinate to Example 3, wherein step (d) includes adjusting the pH of the solution of the dissolved protein to about 6.0 to about 7.0.

[0417] Example 90 is a protein composition described in Example 3 or any of Examples 4-89 which are subordinate to Example 3, wherein step (f) includes adding an organic solvent to a final concentration of about 5% to about 70% (v / v).

[0418] Example 91 is a protein composition described in Example 3 or any of Examples 4-90 which are subordinate to Example 3, wherein step (f) includes adding an organic solvent to a final concentration of about 10% to about 50% (v / v).

[0419] Example 92 is a protein composition described in Example 3 or any of Examples 4-90 which are subordinate to Example 3, wherein step (f) includes adding an organic solvent to a final concentration of about 40% to about 70% (v / v).

[0420] Example 93 is a protein composition described in Example 3 or any of Examples 4-92 which are subordinate to Example 3, wherein at the beginning of step (f), the organic solvent has a temperature of about -20°C to about 10°C.

[0421] Example 94 is a protein composition described in Example 3 or any of Examples 4-93 which are subordinate to Example 3, wherein at the beginning of step (f), the organic solvent has a temperature of about -20°C to about 0°C.

[0422] Example 95 is a protein composition described in Example 3 or any of Examples 4-93 which are subordinate to Example 3, wherein at the beginning of step (f), the organic solvent has a temperature of about 0°C to about 4°C.

[0423] Example 96 is a protein composition described in Example 3 or any of Examples 4-92 which are subordinate to Example 3, wherein at the beginning of step (f), the organic solvent has a temperature of about 10°C to about 25°C.

[0424] Example 97 is a protein composition described in Example 3 or any of Examples 4-96 which are subordinate to Example 3, wherein step (e) includes cooling the solution of the dissolved protein to a temperature of about 0°C to about 4°C.

[0425] Example 98 is the protein composition described in Example 3 or any of Examples 4-96 which are subordinate to Example 3, wherein at the beginning of step (f), the solution of the dissolved protein has a temperature of about 10°C to about 25°C.

[0426] Example 99 is the protein composition described in Example 3 or any of Examples 4-98 which are subordinate to Example 3, wherein step (c) includes heating the solution of the dissolved protein for a period of about 10 seconds to about 30 minutes.

[0427] Example 100 is the protein composition described in Example 3 or any of Examples 4-99 which are subordinate to Example 3, wherein step (c) includes heating the solution of the dissolved protein for a period of about 1 minute to about 20 minutes.

[0428] Example 101 is a protein composition described in Example 3 or any of Examples 4-100 which are subordinate to Example 3, wherein step (c) includes heating the solution of the dissolved protein at a temperature of about 70°C to about 100°C.

[0429] Example 102 is a protein composition described in Example 3 or any of Examples 4-101 which are subordinate to Example 3, wherein step (c) includes heating the solution of the dissolved protein at a temperature of about 85°C to about 95°C.

[0430] Example 103 is a protein composition described in Example 3 or any of Examples 4-102 which are subordinate to Example 3, wherein step (g) includes centrifugation, filtration or a combination thereof.

[0431] Example 104 is a protein composition described in Example 3 or any of Examples 4-103 which are subordinate to Example 3, wherein the organic solvent is selected from the group consisting of ethanol, methanol, propanol, isopropanol and acetone.

[0432] Example 105 is the protein composition described in Example 3 or any of Examples 4-104 which are subordinate to Example 3, wherein the organic solvent is ethanol.

[0433] Example 106 is the protein composition described in Example 3 or any of Examples 4-105 which are subordinate to Example 3, wherein the washing solvent is an organic washing solvent.

[0434] Example 107 is the protein composition described in Example 106, wherein the organic washing solvent is the same as the organic solvent in step (f).

[0435] Example 108 is the protein composition described in Example 106, wherein the organic washing solvent is selected from the group consisting of ethanol, methanol, propanol, isopropanol and acetone.

[0436] Example 109 is the protein composition described in Example 106, wherein the organic washing solvent is ethanol.

[0437] Example 110 is the protein composition described in Example 3 or any of Examples 4-105 which are subordinate to Example 3, wherein the washing solvent is an aqueous solution.

[0438] Example 111 is the protein composition described in Example 3 or any of Examples 4-105, wherein the washing solvent is a mixture of an aqueous solution and an organic washing solvent.

[0439] Example 112 is the protein composition described in Example 111, wherein the washing solvent comprises about 1% (v / v) to about 30% (v / v) of an organic washing solvent.

[0440] Example 113 is the protein composition described in Example 111, wherein the washing solvent comprises about 30% (v / v) to about 80% (v / v) of an organic washing solvent.

[0441] Example 114 is the protein composition described in Example 111, wherein the washing solvent comprises about 80% (v / v) to about 99% (v / v) of an organic washing solvent.

[0442] Example 115 is the protein composition described in any of Examples 111-114, wherein the organic washing solvent is ethanol.

[0443] Example 116 is the protein composition described in any of Examples 111-114, wherein the organic washing solvent in step (h) is the same as the organic solvent in step (f).

[0444] Example 117 is a protein composition described in Example 3 or any of Examples 4-116 which are subordinate to Example 3, wherein the treatment includes resolving the protein composition to a concentration of about 1.5 to about 50 mg / mL.

[0445] Example 118 is a protein composition described in Example 3 or any of Examples 4-117 which are subordinate to Example 3, wherein the treatment includes resolving the protein composition to a concentration of about 2 mg / mL to about 4 mg / mL.

[0446] Example 119 is a protein composition described in Example 3 or any of Examples 4-117 which are subordinate to Example 3, wherein the treatment includes resolving the protein composition to a concentration of about 20 mg / mL to about 40 mg / mL.

[0447] Example 120 is a protein composition described in Example 3 or any of Examples 4-119 which are dependent on Example 3, wherein the treatment includes redissolving at least a portion of the protein composition at a pH of at least 8.0.

[0448] Example 121 is the protein composition described in Example 120, wherein the treatment includes redissolving at least a portion of the protein composition at a pH of at least 9.0.

[0449] Example 122 is the protein composition of Example 121, wherein the treatment includes redissolving at least a portion of the protein composition at a pH of at least 10.0.

[0450] Example 123 is a protein composition described in any of Examples 120-122, further comprising neutralizing or acidifying the protein composition.

[0451] Example 124 is a protein composition described in Example 3 or any of Examples 4-123 which are subordinate to Example 3, wherein the treatment includes re-dissolving at least a portion of the protein composition using an enzyme.

[0452] Example 125 is the protein composition described in Example 121, wherein the enzyme is a protein deamidase.

[0453] Example 126 is the protein composition described in Example 121, wherein the enzyme is protein glutaminase.

[0454] Example 127 is the protein composition described in Example 121, wherein the enzyme is protein asparaginase.

[0455] Example 128 is a protein composition described in Example 3 or any of Examples 4-127 which are subordinate to Example 3, including steps (a), (b), (f) and (g).

[0456] Example 129 is the protein composition described in Example 3 or any of Examples 4-128 which are subordinate to Example 3, including steps (a), (b), (c), (f) and (g).

[0457] Example 130 is the protein composition described in Example 129, wherein step (c) is after step (b).

[0458] Example 131 is the protein composition described in Example 129, wherein step (b) is after step (c).

[0459] Example 132 is a protein composition described in Example 3 or any of Examples 4-131 which are subordinate to Example 3, including steps (a), (b), (d), (f) and (g).

[0460] Example 133 is the protein composition described in Example 132, wherein step (d) is after step (b).

[0461] Example 134 is the protein composition described in Example 3 or any of Examples 4-133 which are subordinate to Example 3, including steps (a), (b), (e), (f) and (g).

[0462] Example 135 is the protein composition described in Example 134, wherein step (e) occurs after step (b).

[0463] Example 136 is the protein composition described in Example 134, wherein step (b) is after step (e).

[0464] Example 137 is the protein composition described in Example 3 or any of Examples 4-136 which are subordinate to Example 3, including steps (a), (b), (c), (d), (f), and (g).

[0465] Example 138 is the protein composition described in Example 137, wherein steps (b), (c) and (d) are performed in the order of (b), (c), and (d).

[0466] Example 139 is the protein composition described in Example 137, wherein steps (b), (c), and (d) are performed in the order of (c), (b), and (d).

[0467] Example 140 is the protein composition described in Example 137, wherein steps (b), (c) and (d) are performed in the order of (b), (d), and (c).

[0468] Example 141 is a protein composition described in Example 3 or any of Examples 4-140 which are subordinate to Example 3, including steps (a), (b), (c), (e), (f) and (g).

[0469] Example 142 is the protein composition described in Example 141, wherein steps (b), (c) and (e) are performed in the order of (b), (c), and (e).

[0470] Example 143 is the protein composition described in Example 141, wherein steps (b), (c) and (e) are performed in the order of (c), (b), and (e).

[0471] Example 144 is the protein composition described in Example 141, wherein steps (b), (c) and (e) are performed in the order of (b), (e), and (c).

[0472] Example 145 is the protein composition described in Example 3 or any of Examples 4-144 which are subordinate to Example 3, including steps (a), (b), (c), (d), (e), (f) and (g).

[0473] Example 146 is the protein composition described in Example 146, wherein steps (b), (c), (d) and (e) are performed in the order of (b), (c), (d), and (e).

[0474] Example 147 is the protein composition described in Example 146, wherein steps (b), (c), (d), and (e) are performed in the order of (c), (b), (d), and (e).

[0475] Example 148 is the protein composition described in Example 146, wherein steps (b), (c), (d), and (e) are performed in the order of (b), (d), (e), and (c).

[0476] Example 149 is the protein composition described in Example 146, wherein steps (b), (c), (d), and (e) are performed in the order of (b), (d), (c), and (e).

[0477] Example 150 is the protein composition described in Example 3 or any of Examples 4-149 which are subordinate to Example 3, including steps (a), (c), (f) and (g).

[0478] Example 151 is a protein composition described in Example 3 or any of Examples 4-149 which are subordinate to Example 3, including steps (a), (c), (d), (f) and (g).

[0479] Example 152 is the protein composition described in Example 151, wherein step (c) is performed prior to step (d).

[0480] Example 153 is the protein composition described in Example 151, wherein step (d) is performed prior to step (c).

[0481] Example 154 is the protein composition described in Example 3 or any of Examples 4-153 which are subordinate to Example 3, including steps (a), (c), (d), (e), (f) and (g).

[0482] Example 155 is the protein composition described in Example 154, wherein steps (c), (d), and (e) are performed in the order of (c), (d), and (e).

[0483] Example 156 is the protein composition described in Example 154, wherein steps (c), (d), and (e) are performed in the order of (d), (e), and (c).

[0484] Example 157 is the protein composition described in Example 154, wherein steps (c), (d), and (e) are performed in the order of (d), (c), and (e).

[0485] Example 158 is a protein composition described in Example 3 or any of Examples 4-157 which are subordinate to Example 3, including steps (a), (d), (f) and (g).

[0486] Example 159 is a protein composition described in Example 3 or any of Examples 4-158 which are subordinate to Example 3, including steps (a), (d), (e), (f) and (g).

[0487] Example 160 is the protein composition described in Example 3, wherein step (d) is performed prior to step (e).

[0488] Example 161 is a protein composition described in Example 3 or any of Examples 4-160 which are subordinate to Example 3, including steps (a), (e), (f) and (g).

[0489] Example 162 is a protein composition described in Example 3 or any of Examples 4-161 which are subordinate to Example 3, including step (h).

[0490] Example 163 is the protein composition described in Example 162, further comprising repeating step (h).

[0491] Example 164 is the protein composition described in Example 163, wherein in a repetition of step (h), the washing solvent is the same as that in the first step (h).

[0492] Example 165 is the protein composition described in Example 163, wherein the washing solvent in the repetition of step (h) is different from that in the first step (h).

[0493] Example 166 is a protein composition described in Example 3 or any of Examples 4-165 which are subordinate to Example 3, including step (i).

[0494] Example 167 is a protein composition described in Example 3 or any of Examples 4-166 which are subordinate to Example 3, further comprising drying the protein composition.

[0495] Example 168 is the protein composition described in Example 167, including spray drying, pad drying, freeze drying, or oven drying.

[0496] Example 169 is a protein composition described in Example 3 or any of Examples 4-168 which are subordinate to Example 3, wherein the source protein composition is based on a portion or derivative of any plant, algae, fungus, bacteria, protozoa, invertebrate, or any combination thereof, with a dry weight of at least 90%.

[0497] Example 170 is the protein composition described in Example 169, wherein the source protein composition is based on defatted soy flour, defatted pea flour, or a combination thereof, with a dry weight of at least 90%.

[0498] Example 171 is a protein composition described in Example 3 or any of Examples 4-170 which are subordinate to Example 3, wherein the source protein composition is a soybean protein composition and the isoflavone content of the protein composition is based on less than 90% of the isoflavone content of the source protein composition by dry weight.

[0499] Example 172 is a protein composition described in Example 3 or any of Examples 4-171 which are subordinate to Example 3, wherein the source protein composition is a soybean protein composition and the isoflavone content of the protein composition is based on less than 70% of the isoflavone content of the source protein composition by dry weight.

[0500] Example 173 is a protein composition described in Example 3 or any of Examples 4-172 which are subordinate to Example 3, wherein the source protein composition is a soybean protein composition and the isoflavone content of the protein composition is based on less than 50% of the isoflavone content of the source protein composition by dry weight.

[0501] Example 174 is a protein composition described in Example 3 or any of Examples 4-173 which are subordinate to Example 3, wherein the source protein composition is a soybean protein composition and the isoflavone content of the protein composition is less than 30% of the isoflavone content of the source protein composition based on a dry weight.

[0502] Example 175 is a protein composition described in Example 3 or any of Examples 4-174 which are subordinate to Example 3, wherein the source protein composition is a soybean protein composition and the isoflavone content of the protein composition is based on less than 10% of the isoflavone content of the source protein composition by dry weight.

[0503] Example 176 is a protein composition described in Example 3 or any of Examples 4-175 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 90% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0504] Example 177 is a protein composition described in Example 3 or any of Examples 4-176 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 70% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0505] Example 178 is a protein composition described in Example 3 or any of Examples 4-177 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 50% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0506] Example 179 is a protein composition described in Example 3 or any of Examples 4-178 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 30% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0507] Example 180 is a protein composition described in Example 3 or any of Examples 4-179 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition based on the dry weight of the protein composition produces no more than 10% of the amount of one or more soy flavor compounds, said one or more soy flavor compounds being produced by cooking a 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0508] Example 181 is a protein composition described in any of Examples 176-180, wherein the one or more soybean flavor compounds include at least one compound selected from the group consisting of hexanal, pentanal, 2-pentylfuran, 1-octen-3-ol, 1-octen-3-one, 1-hexanol, (E)-2-nonenal, (E,Z)-2,6-nonadienal and (E,E)-2,4-decadienal.

[0509] Example 182 is a protein composition described in Example 3 or any of Examples 4-181 which are subordinate to Example 3, wherein when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 90% of the amount of one or more volatile compounds from a group of volatile compounds produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0510] Example 183 is a protein composition described in Example 3 or any of Examples 4-182 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 70% of the amount of one or more volatile compounds from a group of volatile compounds, said volatile compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0511] Example 184 is a protein composition described in Example 3 or any of Examples 4-183 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 50% of the amount of one or more volatile compounds from a group of volatile compounds, said volatile compounds being produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0512] Example 185 is a protein composition described in Example 3 or any of Examples 4-184 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 30% of the amount of one or more volatile compounds from a group of volatile compounds, which are produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0513] Example 186 is a protein composition described in Example 3 or any of Examples 4-185 which are subordinate to Example 3, wherein, when cooked in water, a 1% (w / v) suspension of the protein composition, based on the dry weight of the protein composition, produces no more than 10% of the amount of one or more volatile compounds from a group of volatile compounds, which are produced by cooking the 1% (w / v) suspension of the source protein composition (based on the dry weight of the source protein composition).

[0514] Example 187 is a protein composition described in Example 3 or any of Examples 4-186 which are subordinate to Example 3, wherein the protein composition produces no more than 90% of the amount of one or more volatile compounds from a group of volatile compounds produced from the source protein composition by solvent-assisted flavor extraction (SAFE).

[0515] Example 188 is a protein composition described in Example 3 or any of Examples 4-187 which are subordinate to Example 3, wherein the protein composition produces no more than 70% of the amount of one or more volatile compounds from a group of volatile compounds produced by the source protein composition via SAFE.

[0516] Example 189 is a protein composition described in Example 3 or any of Examples 4-188 which are subordinate to Example 3, wherein the protein composition produces no more than 50% of the amount of one or more volatile compounds from a group of volatile compounds produced by the source protein composition via SAFE.

[0517] Example 190 is a protein composition described in Example 3 or any of Examples 4-189 which are subordinate to Example 3, wherein the protein composition produces no more than 30% of the amount of one or more volatile compounds from a group of volatile compounds produced by the source protein composition via SAFE.

[0518] Example 191 is a protein composition described in Example 3 or any of Examples 4-190 which are subordinate to Example 3, wherein the protein composition produces no more than 10% of the amount of one or more volatile compounds from a group of volatile compounds produced by the source protein composition via SAFE.

[0519] Example 192 is a protein composition described in any of Examples 182-191, wherein the group of ...

Claims

1. A protein composition produced by a method comprising: (a) Adding an aqueous solution to the source protein composition to form a solution of dissolved protein; (b) Optionally, remove the solid from the solution of the dissolved protein; (c) Heating the solution of the dissolved protein; (d) Optionally, the pH of the solution of the dissolved protein is adjusted to about 4.0 to about 9.0; (e) Cool the solution of the dissolved protein to about 0°C to about 10°C; (f) An organic solvent is added to the solution of the dissolved protein to form a solid phase and a liquid phase, wherein the organic solvent is cooled to a temperature of about -20 °C to about 10 °C; (g) Separating the solid phase from the liquid phase to form the protein composition; (h) Optionally, the protein composition is washed with a washing solvent; and (i) Optionally, the protein composition is treated. The protein composition comprises at least 50% by dry weight of various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof, and The protein composition therein contains less than 0.8% lipids on a dry weight basis.

2. The protein composition according to claim 1, wherein the protein composition comprises at least about 90% by dry weight of the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

3. The protein composition of claim 2, wherein the protein composition is a protein isolate, wherein the protein composition comprises less than 8% by dry weight insoluble carbohydrates, or both.

4. The protein composition according to claim 3, wherein the protein composition comprises one or more of the following: (a) Isoflavone content less than approximately 125 ppm, (b) Saponin content less than about 75 ppm, and (c) Phospholipid content less than about 500 ppm.

5. The protein composition according to claim 1, wherein the protein composition comprises about 60% to about 80% by dry weight of the various plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof.

6. The protein composition of claim 1, wherein the protein composition comprises less than 0.4% lipids on a dry weight basis.

7. The protein composition of claim 1, wherein the protein composition has a lightness value of at least 86 and a chromaticity value of less than 14 on a scale from 0 (black control value) to 100 (white control value), or both.

8. The protein composition according to claim 1, wherein the plurality of plant proteins, fungal proteins, algal proteins, bacterial proteins, protozoan proteins, invertebrate proteins, or combinations thereof comprise: (a) At least 90% plant protein, (b) At least 90% of fungal proteins, and (c) At least 90% algal protein.

9. The protein composition according to claim 1, wherein when cooked in a solution comprising reducing sugars, sulfur-containing amino acids and heme-containing proteins, 1% (w / v) of the protein composition produces one or more volatile compounds associated with the aroma and / or flavor of meat.

10. The protein composition according to claim 1, wherein the protein composition is a solution, suspension, emulsion, solid or powder.

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