Use of ionic polymers for hydrolysis of proteins and protein-containing raw materials

Abstract

The present invention relates to the use of ionic polymers (IPs) consisting of an anion- and cation-containing polymer backbone in the hydrolysis of proteins and protein-containing materials to produce protein hydrolysates.

Description

[Technical Field]

[0001] The present invention relates to the use of an ionic polymer (IP) comprising an anion and a cation-containing polymer backbone in the hydrolysis of proteins and protein-containing raw materials to produce protein hydrolysates. [Background technology]

[0002] Proteins make up all the organs of the body and are necessary for the proper functioning of organ systems. While all proteins are composed of amino acids, differences in the composition and sequence of these amino acids distinguish how proteins function. The body uses amino acids to build specific proteins for specific functions in maintaining organ health. However, the body does not have novel pathways for the synthesis of many necessary amino acids; therefore, these essential amino acids must be obtained from dietary proteins. The body must consistently digest, absorb, and metabolize appropriate dietary proteins to supply the organs with the specific proteins needed to function.

[0003] Dietary proteins can be more easily digested and absorbed by ingesting smaller peptide subunits of proteins or even mixtures of amino acids. Peptides and amino acids can be obtained by hydrolyzing proteins, which are often derived from sources that are plants, animals, fungi, or microorganisms. Peptides and amino acids are usually obtained by acidic hydrolysis, alkaline hydrolysis, or enzymatic hydrolysis of proteins. The alkaline hydrolysis process results in the complete destruction of most amino acids (almost 100% loss). The acidic hydrolysis process offers the advantage of low cost. However, this process results in the complete destruction of tryptophan, partial loss of methionine, and the conversion of glutamine to glutamate and asparagine to aspartate. The main drawback of enzymatic hydrolysis of proteins is that the pH and temperature range that optimizes enzyme activity tends to maximize protein folding. High steric hindrance results in poorly hydrolyzable proteins, which negatively affects solubility, absorption, potency, sensory properties, and interaction stability. Furthermore, enzymatic hydrolysis of proteins involves relatively high costs and the possibility of enzyme inhibitors being present in the raw protein material.

[0004] Industrial processes for hydrolyzing proteins to produce protein hydrolysates containing oligopeptides, peptides, and / or amino acids primarily rely on suboptimal enzyme mixtures, and therefore require expensive purification steps to produce peptide mixtures with suboptimal size distributions.

[0005] Therefore, there is still a need for simple and safe methods to hydrolyze proteins from various sources to produce protein hydrolysates with high digestibility, high absorption properties, and high benefits. [Overview of the Initiative] [Means for solving the problem]

[0006] One aspect of the present invention is a method for hydrolyzing a protein and / or protein-containing raw material to a protein hydrolysate, a) A step of providing protein and / or protein-containing raw materials, b) Optionally, a step of determining the protein content in the protein-containing raw material, c) Optionally, a step of pre-treating the above protein-containing raw material, d) Optionally, a step of isolating the protein from the protein-containing raw material and forming a protein concentrate, e) A step of contacting the above-mentioned protein, protein concentrate and / or protein-containing raw material with a catalyst to form a reaction mixture, wherein the catalyst is an ionic polymer or a combination of ionic polymers, an ionic polymer network, a solid-supported ionic polymer, and / or a polymer film incorporating an ionic polymer. f) A step of decomposing the protein, protein concentrate and / or protein-containing raw material in the above reaction mixture to produce a liquid phase and a solid phase, wherein the liquid phase contains protein hydrolysates and the solid phase contains residual substances, g) A step of isolating at least a portion of the liquid phase from the solid phase, h) A step of recovering the above protein hydrolysate from the isolated liquid phase. Includes, The above ionic polymer (IP) consists of the monomer of formula I, [ka] Alternatively, the first monomer of formula I [ka] and, [ka] It consists of at least one second monomer selected from the group comprising, In the above formula, n and m are independently selected from 1, 2, 3, 4, 5, and 6. z and w are each independently selected from 0, 1, 2, 3, Z1, Z2 and Z3 are each independently, [Chemical formula] a cation selected from the group consisting of R1, R2, R3, R4, R5, R6 and R7 are each independently a bond, H, C1-C6 alkyl, C1-C6 allyl, CH3-(CH2)p-O-(CH2)q-CH3, C1-C6 alkoxy, C1-C6 alkoxyalkyl, benzyl, -SO3H, -(CH2)q-SO3H, provided that two of R1, R2, R3, R4, R5, R6 and R7 are each a bond, p and q are each independently selected from 0, 1, 2, 3, 4, 5, 6, L is an optional linker, and when present, each occurrence of L is independently H, substituted or unsubstituted C1-C - , - , , - , - , - , - , - , - , , - alkylene, C1-C 20 alkenylene, C1-C 20 alkynylene and substituted or unsubstituted C5-C 10 aryl, and the substituents are selected from the group consisting of H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], A is an optional acidic group, and when present, each occurrence of A is independently H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], -CH2-COOH, provided that when z and w are 0, A is present in formula IV, X - is F - , Cl - , Br - , I - , ClO4 - , BF4 - , PF6 - , AsF6 - , SbF6- NO2 - NO3 - HSO4 - SO4 2- , PO4 3- HPO4 2- CF3CO2 - CF3CO3 - CO3 2- CF3SO3 - , C1~C6 carboxylates, CN - SCN - OCN - , CNO - , N3 - Selected from the group including tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate. Ra is C1~C 24 It is alkyl, Rb and Rc are independently selected from the group containing H and CH3, or are absent. Rd is C1~C 24 C1-C may be substituted with alkyl groups. 24 Alkylene and C1~C 24 It is alkyl, Re and Rf are independently C1~C 24 It is alkyl, Y is either N or O, however, if Y is O, then Rc does not exist. R is C1~C 24 Alkyl and C5~C 10 Selected from the group containing aryls, or if none exist. The above ionic polymer network comprises one or more crosslinked ionic polymers (IP), The above solid support has at least one surface comprising one or more of the above ionic polymers (IP) or the above ionic polymer network, The polymer film incorporates one or more of the above ionic polymers (IPs) or the above ionic polymer networks. Provide a method.

[0007] Another aspect of the present invention provides a protein hydrolysate obtained by a method of hydrolyzing the protein and / or protein-containing raw material of the present invention.

[0008] Another aspect of the present invention provides a protein hydrolysate comprising peptides and free amino acids, wherein the protein hydrolysate is water-soluble, has improved solubility and a degree of hydrolysis greater than 2.5%, and the peptides are oligopeptides and polypeptides having a molecular weight of less than 10,000 Da, which may be linked to carbohydrates.

[0009] Another aspect of the present invention provides the use of the protein hydrolysates of the present invention in the manufacture of food, animal feed products and cosmetics.

[0010] Another aspect of the present invention provides a food product comprising an edible material and a protein hydrolysate of the present invention.

[0011] Another aspect of the present invention is the first monomer of formula I. [ka] and, [ka] An ionic polymer (IP) comprising at least one second monomer selected from the group consisting of, However, at least the second monomer of formula V or at least the second monomer of formula VI is present in the ionic polymer (IP), In the above formula, n and m are independently selected from 1, 2, 3, 4, 5, and 6. z and w are independently selected from 0, 1, 2, and 3. Z1, Z2, and Z3 are each independent of each other. [ka] A cation selected from the group including, R1, R2, R3, R4, R5, R6, and R7 are each independently selected from the group containing a bond, H, C1-C6 alkyl, C1-C6 allyl, CH3-(CH2)pO-(CH2)q-CH3, C1-C6 alkoxy, C1-C6 alkoxyalkyl, benzyl, -SO3H, and -(CH2)q-SO3H, provided that two of R1, R2, R3, R4, R5, R6, and R7 are each a bond. p and q are independently selected from 0, 1, 2, 3, 4, 5, and 6. L is an optional linker, and if present, each occurrence of L independently corresponds to H, the substituted or unsubstituted C1-C 20 Alkylene, C1~C 20 Alkenylene, C1~C 20 Alkynylene and substituted or unsubstituted C5-C 10 Selected from aryls, the substituents are selected from the group including H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], A is an optional acidic group, and if present, each occurrence of A is independently selected from the group including H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], and -CH2-COOH, except when z and w are 0, A exists in formula IV. X - is, F - Cl - , Br - , I - ClO4 - BF4 - PF6 - AsF6 - SbF6 - NO2 - NO3 - HSO4 - SO4 2- , PO4 3- HPO4 2- CF3CO2- CF3CO3 - CO3 2- CF3SO3 - , C1~C6 carboxylates, CN - SCN - OCN - , CNO - , N3 - Selected from the group including tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate, Ra is C1~C 24 It is alkyl, Rb and Rc are independently selected from the group containing H and CH3, or are absent. Rd is C1~C 24 C1-C may be substituted with alkyl groups. 24 Alkylene and C1~C 24 It is alkyl, Re and Rf are independently C1~C 24 It is alkyl, Y is either N or O, however, if Y is O, then Rc does not exist. R is C1~C 24 Alkyl and C5~C 10 Selected from the group containing aryls, or not present. We provide ionic polymers (IP). [Brief explanation of the drawing]

[0012] [Figure 1] Figure 1 shows MS(+) chromatograms of the hydrolyzed gluten mixture (top) and the resulting peptide profile (bottom). [Figure 2] Figure 2 shows the MS(+) chromatogram of the hydrolyzed albumin mixture. [Figure 3] Figure 3 shows the MS(+) chromatogram of hydrolyzed used barley mixture. [Figure 4]Figure 4 shows the growth of Lactobacillus X strain in the presence of Prembion, a composition containing glucose, FOS, XOS, and the protein hydrolysate of the present invention. The number of colonies is shown as a function of growth time for Lactobacillus X strain, which has been reported to be partially involved in human and animal intestinal health. All additives were added at a 1% (total sugar basis) level. [Figure 5] Figure 5 shows the growth of Bifidobacterium X strain in the presence of Prembion, a composition containing glucose, FOS, XOS, and the protein hydrolysate of the present invention. The number of colonies is shown as a function of growth time for Bifidobacterium X strain, which has been reported to be partially involved in human and animal gut health. All additives were added at a 1% (total sugar basis) level. [Modes for carrying out the invention]

[0013] All published documents, patent applications, patents, and other references referred to herein are incorporated in their entirety by reference. The published documents and applications discussed herein are provided only for those disclosures prior to the filing date of this application. Nothing in this specification is intended to be construed as acknowledging that the present invention does not have prior rights to such publications on the grounds that they are prior inventions. Furthermore, the materials, methods, and examples are for illustrative purposes only and are not intended to limit the scope of this invention.

[0014] In case of any conflict, this specification, including definitions, shall prevail. Unless otherwise specified, all technical and scientific terms used herein have the same meaning as those generally understood by those skilled in the art in the field to which the subject matter of this invention pertains. For the purpose of facilitating the understanding of this invention when used herein, the following definitions are given:

[0015] The term “comprise” is generally used in the sense of “include,” meaning to allow the presence of one or more features or components. Furthermore, as used herein and in the claims, the phrase “comprising” may encompass similar embodiments described by the phrases “consisting of” and / or “consisting essentially of.”

[0016] As used herein and in the claims, the singular forms "a," "an," and "the" refer to multiple subjects unless they are clearly inconsistent with the context.

[0017] As used in this specification and in the claims, the term "and / or" as used in phrases such as "A and / or B" in this specification includes "A and B", "A or B", "A", and "B".

[0018] The "allyl" group is a substituent with the structural formula H2C=CH-CH2R, where R is the remainder of the molecule.

[0019] The term "monomer" refers to a molecule that can undergo polymerization or copolymerization, thereby contributing its constituent units to the essential structure of a polymer.

[0020] As used herein, “crosslinking” refers to the bonding of two or more monomers, oligomers, or longer polymer chains by crosslinking with a crosslinking agent, such as an element, molecular group, compound, or another oligomer or polymer. Crosslinking can result in a polymer network (which may be two-dimensional or three-dimensional) in which polymer subunits are interconnected by multiple crosslinking agents and without free ends. Crosslinking may occur upon exposure to stimuli such as heat or light. As a result, some crosslinking processes occur at elevated temperatures, while some can occur at room temperature or lower. As the crosslinking density increases, the properties of the material can change from thermoplastic to thermosetting.

[0021] As used herein, the terms “peptide” or “oligopeptide” are defined as a chain of at least two amino acids linked together by peptide bonds. The terms “peptide” and “oligopeptide” may be used interchangeably depending on the context.

[0022] Proteins consist of one or more chains containing more than 30 amino acid residues (polypeptides) linked together by peptide bonds.

[0023] As used herein, "protein hydrolysate" (or "hydrolysate" or "hydrolyzed protein") refers to a product formed by the hydrolysis of protein peptide bonds between amino acids, and means a mixture of amino acids and peptides of different chain lengths. A concentrated hydrolysate is a fraction of a protein hydrolysate, for example, in which selected peptides are concentrated, or in which a portion of a peptide or polypeptide has been removed from the hydrolysate. Therefore, a concentrated hydrolysate is preferably a mixture of peptides or a peptide mixture.

[0024] As used herein, the term “food” means any food or feed suitable for consumption by humans, non-ruminants, or ruminants. “Food” may be prepared and packaged food (e.g., mayonnaise, salad dressing, bread, or cheese food) or animal feed (e.g., extruded and pelletized animal feed or crude feed).

[0025] As used herein, the term "functional food" refers to a food to which a biologically active supplement, such as the protein hydrolysate of the present invention, has been added.

[0026] As used herein, the term “dietary supplement” refers to a dietary supplement or a food product formulated as a dietary supplement, intended for use as part of a meal.

[0027] One aspect of the present invention provides a method for hydrolyzing proteins and / or protein-containing raw materials (feedstock) into protein hydrolysates.

[0028] In one embodiment, the present invention is a method for hydrolyzing a protein and / or protein-containing raw material to a protein hydrolysate, a) A step of providing protein and / or protein-containing raw materials, b) Optionally, a step of determining the protein content in the protein-containing raw material, c) Optionally, a step of pre-treating the above protein-containing raw material, d) Optionally, a step of isolating the protein from the protein-containing raw material and forming a protein concentrate, e) A step of contacting the above-mentioned protein, protein concentrate and / or protein-containing raw material with a catalyst to form a reaction mixture, wherein the catalyst is an ionic polymer or a combination of ionic polymers, an ionic polymer network, a solid-supported ionic polymer, and / or a polymer film incorporating an ionic polymer. f) A step of decomposing the protein, protein concentrate and / or protein-containing raw material in the above reaction mixture to produce a liquid phase and a solid phase, wherein the liquid phase contains protein hydrolysates and the solid phase contains residual substances, g) A step of isolating at least a portion of the liquid phase from the solid phase, h) A step of recovering the above protein hydrolysate from the isolated liquid phase. This provides a method that includes [something].

[0029] In one embodiment, step e) forming a reaction mixture by contacting the protein, protein concentrate, and / or protein-containing raw material with a catalyst comprises adding water or a suitable organic solvent and an effective amount of catalyst to the protein, protein concentrate, and / or protein-containing raw material to form a reaction mixture, wherein the catalyst is the ionic polymer of the present invention or a combination of the ionic polymers of the present invention, the ionic polymer network of the present invention, a membrane incorporating the ionic polymer of the present invention, and / or an ionic polymer supported on a solid of the present invention. Decomposition step f) comprises heating the reaction mixture from step e) for a suitable time, followed by cooling to room temperature (typically 20-25°C). In some embodiments, the heating is 50°C-170°C or 100°C-160°C or 110°C-150°C or 140°C-160°C or 100°C-170°C. In some other embodiments, the heating is up to 50°C or up to 100°C or up to 170°C. In other embodiments, the suitable time is typically 0.5-3 hours. The reaction temperature and time depend on the origin of the protein or protein-containing raw material.

[0030] In some embodiments of the present invention's method for hydrolyzing proteins and protein-containing raw materials to protein hydrolysates, the method further includes applying pressure of N2 or CO2 during the decomposition step f). The pressure may be in the range of 20 bar to 300 bar, preferably 20 to 150 bar.

[0031] As used herein, the term "protein" refers to any protein from any animal, plant, or microorganism.

[0032] As used herein, the term “protein-containing raw material” refers to living or dead biological material that can be used in the method for producing protein hydrolysates of the present invention. In some embodiments, the protein-containing raw material is selected from the group including plant-based proteins, single-cell proteins, in vitro meat (meat in a test tube, cellular meat), yeast extract, spent yeast or yeast slurry, spent barley, insects, soybeans, peas, rapeseed, whey, casein, wheat, canola, corn, jatropha (a plant of the genus Jatropha), palm, peanuts, sunflower, coconut, mustard, cottonseed, palm kernel, olive, safflower, sesame, flaxseed, algae, crustaceans, fish meal, meat meal and bone meal, molasses, germinated cereals and legumes, collagen, and other major commercial categories of protein isolates.

[0033] Optionally, prior to any use, the protein content in the protein-containing raw material may be determined according to the Bradford protein assay, the Kjeldahl method, or the Lowry method.

[0034] Optional pretreatment of protein-containing raw materials used in the methods described herein may involve one or more methods selected from the group consisting of washing, solvent extraction, solvent swelling, grinding, milling, steam pretreatment, explosive steam pretreatment, dilute acid pretreatment, hot water pretreatment, alkali pretreatment, lime pretreatment, wet oxidation, wet explosion, ammonia fiber explosion, organic solvent pretreatment, biological pretreatment, ammonia percolation, ultrasound, electroporation, microwave, supercritical CO2, supercritical H2O, ozone, and gamma ray irradiation. Optional pretreatment of protein-containing raw materials may include, for example, milling of the protein-containing raw material.

[0035] The steps used in the methods described herein for isolating proteins from optional protein-containing raw materials to form protein concentrates utilize one or more selective precipitation methods selected from the group consisting of salting out, isoelectric focusing, organic cosolvent precipitation, two-carbon (C2) organic cosolvent precipitation of proteins, C4 and C5 organic cosolvent precipitation, protein phase partitioning and extraction, protein exclusion and condensation agents (neutral polymers) and osmotic regulators (osmolites), precipitation with synthetic and semi-synthetic polymer electrolytes, metal and polyphenol heteropolyanion precipitation, hydrophobic ion pairing (HIP) entanglement ligands, matrix stacking ligand coprecipitation; and divalent and trivalent metal cation precipitation.

[0036] Some ionic polymers used in the method of the present invention for hydrolyzing proteins and protein-containing raw materials into protein hydrolysates consist of an anion and a polymer backbone containing a cation, as disclosed in International Publication No. 2019 / 058270A1, which is incorporated in whole by reference. Specifically, the ionic polymers (IPs) used in the method of the present invention for hydrolyzing proteins and protein-containing raw materials into protein hydrolysates consist of monomers of formula I, [ka] Alternatively, the first monomer of formula I [ka] and, [ka] It consists of at least one second monomer selected from the group comprising, In the above formula, n and m are independently selected from 1, 2, 3, 4, 5, and 6, preferably n and m are independently selected from 1, 2, and 3, most preferably n is 2 and m is 1 or 2. z and w are independently selected from 0, 1, 2, and 3, preferably z and w are independently selected from 0 and 1, and most preferably z and w are 0 or 1. Z1, Z2, and Z3 are each independent of each other. [ka] A cation selected from the group including, Preferably, Z1, Z2 and Z3 are each independently [ka] A cation selected from the group including, Most preferably, Z1, Z2, and Z3 are each independently, [ka] A cation selected from the group including, R1, R2, R3, R4, R5, R6, and R7 are each independently selected from the group comprising a bond, H, C1-C6 alkyl, C1-C6 allyl, CH3-(CH2)pO-(CH2)q-CH3, C1-C6 alkoxy, C1-C6 alkoxyalkyl, benzyl, -SO3H, and -(CH2)q-SO3H, wherein two of R1, R2, R3, R4, R5, R6, and R7 are each a bond, preferably R1 and R2. R3, R4, R5, R6, and R7 are each independently selected from the group containing a bond, H, and C1-C6 alkyl, provided that two of R1, R2, R3, R4, R5, R6, and R7 are each a bond, and most preferably R1, R2, R3, R4, R5, R6, and R7 are each independently selected from the group containing a bond and H, provided that two of R1, R2, R3, R4, R5, R6, and R7 are each a bond. p and q are independently selected from 0, 1, 2, 3, 4, 5, and 6. L is an optional linker, and if present, each occurrence of L independently corresponds to H, the substituted or unsubstituted C1-C 20 Alkylene, C1~C 20 Alkenylene, C1~C 20 Alkynylene and substituted or unsubstituted C5-C 10Selected from aryl, the substituents are selected from the group consisting of H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], preferably L does not exist, A is an optional acidic group, and when present, each occurrence of A is independently selected from the group consisting of H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], -CH2-COOH, provided that when z and w are 0, A is present in Formula IV, preferably when present, each occurrence of A is independently selected from the group consisting of H, -SO3H, -COOH, -O-COOH, -CH2-COOH, provided that when z and w are 0, A is present in Formula IV, most preferably A does not exist or when present, the occurrences of A are independently selected from the group consisting of H, -COOH, -CH2-COOH, provided that when z and w are 0, A is present in Formula IV, X - is F - 、Cl - 、Br - 、I - 、ClO4 - 、BF4 - 、PF6 - 、AsF6 - 、SbF6 - 、NO2 - 、NO3 - 、HSO4 - 、SO4 2- 、PO4 3- 、HPO4 2- 、CF3CO2 - 、CF3CO3 - 、CO3 2- 、CF3SO3 - 、C1-C6 carboxylate, CN - 、SCN - 、OCN - 、CNO - 、N3 -Selected from the group including tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate, preferably X - is, F - Cl - HSO4 - SO4 2- , PO4 3- HPO4 2- CF3CO2 - CF3CO3 - CF3SO3 - A selection from the group including X is most preferably X - Cl - HSO4 - SO4 2- CF3SO3 - Selected from the group including, Ra is C1~C 24 It is alkyl, Rb and Rc are each independently selected from the group including H and CH3, or are absent, preferably Rc is absent. Rd is C1~C 24 C1-C may be substituted with alkyl groups. 24 Alkylene and C1~C 24 Alkyl, preferably C1-C2 alkylene or C1-C2 alkyl, Re and Rf are independently C1~C 24 Alkyl, preferably CH3, Y is either N or O, however, if Y is O, then Rc does not exist. R is C1~C 24 Alkyl and C5~C 10 Either selected from the group containing aryls, or none exist.

[0037] In some embodiments of the ionic polymer (IP) of the present invention, the second monomer of formula VI is [ka] That is the case.

[0038] In some embodiments of the ionic polymer of the present invention, the (first) monomer of formula I is [ka] That is the case.

[0039] In some embodiments of the ionic polymer of the present invention, Z1 and Z2 are the same (identical). In other embodiments, Z1 and Z2 are different.

[0040] In some embodiments of the ionic polymer of the present invention, Z1 and Z2 are [ka] In this case, R2 and R5 are bonds, R1, R3 and R4 are H, and n is not 4.

[0041] In other embodiments of the ionic polymer of the present invention, Z1 and Z2 are [ka] If this is the case, then R2 and R5 are bonded, n is 4, and at least one of R1, R3, and R4 is not H.

[0042] In some preferred embodiments of the ionic polymer of the present invention, the C1-C6 carboxylate is selected from the group including formates, acetates, propionates, butyrates, hexanoates, maleates, fumarates, oxalates, lactates, and pirubates.

[0043] The ratio of different monomers in the ionic polymer of the present invention, comprising the first monomer and the second monomer, may be any preferred ratio and may vary depending on the protein-containing raw material being processed. In some embodiments, the first and second monomers are present in a 1:1 ratio.

[0044] According to some embodiments, the present invention provides monomers relating to formula I, selected from the group including the following: [ka]

[0045] According to further embodiments, the present invention provides monomers relating to formula I, selected from the group including the following: [ka]

[0046] According to some embodiments, the present invention provides a monomer according to formula II. [ka]

[0047] According to some embodiments, the present invention provides ionic polymers selected from the group including the following: [ka] [ka] x and y are integers independently selected within the range of 1 to 1000, preferably 1 to 500 or 1 to 200, more preferably 1 to 100 or 1 to 50.

[0048] According to other embodiments, the present invention provides ionic polymers selected from the group including the following: [ka] x and y are integers independently selected within the range of 1 to 1000, preferably 1 to 500 or 1 to 200, more preferably 1 to 100 or 1 to 50.

[0049] Another aspect of the present invention is the first monomer of formula I. [ka] and, [ka] An ionic polymer (IP) comprising at least one second monomer selected from the group consisting of, However, at least the second monomer of formula V or at least the second monomer of formula VI is present in the ionic polymer (IP), In the above formula, n and m are independently selected from 1, 2, 3, 4, 5, and 6, preferably n and m are independently selected from 1, 2, and 3, most preferably n is 2 and m is 1 or 2. z and w are independently selected from 0, 1, 2, and 3, preferably z and w are independently selected from 0 and 1, and most preferably z and w are 0 or 1. Z1, Z2, and Z3 are each independent of each other. [ka] A cation selected from the group including, Preferably, Z1, Z2 and Z3 are each independently [ka] A cation selected from the group including, Most preferably, Z1, Z2, and Z3 are each independently, [ka] A cation selected from the group including, R1, R2, R3, R4, R5, R6, and R7 are each independently selected from the group comprising a bond, H, C1-C6 alkyl, C1-C6 allyl, CH3-(CH2)pO-(CH2)q-CH3, C1-C6 alkoxy, C1-C6 alkoxyalkyl, benzyl, -SO3H, and -(CH2)q-SO3H, wherein two of R1, R2, R3, R4, R5, R6, and R7 are each a bond, preferably R1 and R2. R3, R4, R5, R6, and R7 are each independently selected from the group containing a bond, H, and C1-C6 alkyl, provided that two of R1, R2, R3, R4, R5, R6, and R7 are each a bond, and most preferably R1, R2, R3, R4, R5, R6, and R7 are each independently selected from the group containing a bond and H, provided that two of R1, R2, R3, R4, R5, R6, and R7 are each a bond. p and q are independently selected from 0, 1, 2, 3, 4, 5, and 6. L is an optional linker, and if present, each occurrence of L independently corresponds to H, the substituted or unsubstituted C1-C 20 Alkylene, C1~C 20 Alkenylene, C1~C 20 Alkynylene and substituted or unsubstituted C5-C 10 The substituent is selected from aryls, and the substituent is selected from the group including H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], preferably without L. A is an optional acidic group, and if present, each occurrence of A is independently selected from the group including H, -SO3H, -COOH, -[P(=O)(OH)2], -[P(=O)(OH)], -O-SO3H, -O-COOH, -O-[P(=O)(OH)2], -O-[P(=O)(OH)], -CH2-COOH, however, if z and w are 0, A is present in formula IV, preferably if present, each occurrence of A is independently selected from the group including H, -SO3H, -COOH, -O-COOH, -CH2-COOH, however, if z and w are 0, A is present in formula IV, most preferably A is absent, or if present, each occurrence of A is independently selected from the group including H, -COOH, -CH2-COOH, however, if z and w are 0, A is present in formula IV, X - is, F - Cl - , Br - , I - ClO4 - BF4 - PF6 - AsF6 - SbF6 - NO2 - NO3 - HSO4 - SO4 2- , PO4 3- HPO4 2- CF3CO2 - CF3CO3 - CO3 2- CF3SO3 - , C1~C6 carboxylates, CN - SCN - OCN - , CNO - , N3 - Selected from the group comprising tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate, preferably X - is, F - Cl - HSO4 - SO4 2- , PO43- HPO4 2- CF3CO2 - CF3CO3 - CF3SO3 - A selection from the group including X - Cl - HSO4 - SO4 2- CF3SO3 - Selected from the group including, Ra is C1~C 24 It is alkyl, Rb and Rc are each independently selected from the group including H and CH3, or are absent, preferably Rc is absent. Rd is C1~C 24 C1-C may be substituted with alkyl groups. 24 Alkylene and C1~C 24 It is alkyl, preferably C1-C2 alkylene or C1-C2 alkyl, Re and Rf are independently C1~C 24 Alkyl, preferably CH3, Y is either N or O, however, if Y is O, then Rc does not exist. R is C1~C 24 Alkyl and C5~C 10 Selected from the group containing aryls, or not present. We provide ionic polymers (IP).

[0050] In some embodiments of the ionic polymer (IP) of the present invention, the second monomer of formula VI is [ka] That is the case.

[0051] In some embodiments of the ionic polymer of the present invention, the first monomer of formula I is [ka] That is the case.

[0052] In some embodiments of the ionic polymer of the present invention, Z1 and Z2 are the same (identical). In other embodiments, Z1 and Z2 are different.

[0053] In some embodiments of the ionic polymer of the present invention, Z1 and Z2 are [ka] In this case, R2 and R5 are bonds, R1, R3 and R4 are H, and n is not 4.

[0054] In other embodiments of the ionic polymer of the present invention, Z1 and Z2 are [ka] If this is the case, then R2 and R5 are bonded, n is 4, and at least one of R1, R3, and R4 is not H.

[0055] The ionic polymers (IPs) of the present invention can be synthesized by several methods, including but not limited to direct polymerization of suitable ionic species in different solvents (water, acetonitrile, alcohols (methanol, ethanol, propanol, etc.), toluene, THF), and chemical modification of non-IPs (see examples). Polymerization may include different approaches, e.g., free radical polymerization, living / controlled radical polymerization, reversible addition-cleavage chain transfer, ionic polymerization, and coordination polymerization. The anionic structure can be designed before or after polymerization as preferred. The resulting ionic polymers (IPs) combine the general properties of ionic monomers with the effective properties of solid catalysts due to the presence of specific functional groups. In one embodiment of the present invention, the salt is prepared using a cation and anion, both of which contain a vinyl group that can be polymerized using AIBN or other initiators. This is an essentially very simple method, and the ionic polymer is purified by removing excess AIBN by washing and filtration. In certain embodiments of the present invention, a salt composed of 1-(1-vinylimidazolium)ethyl-3-vinylimidazolium [dichloride]) is prepared. This salt, as a pure compound, is then polymerized using the radical initiator AIBN. This ionic polymer is purified by removing excess AIBN by washing and filtration. As an alternative to the dichloride anion, a ditriflate anion can be obtained via anion exchange reaction before polymerization.

[0056] The present invention also provides an ionic polymer network comprising one or more crosslinked ionic polymers of the present invention.

[0057] In some embodiments, the ionic polymer network of the present invention further comprises itaconic acid, citric acid, and / or 1,4-butanediol.

[0058] In other embodiments, the ionic polymer network of the present invention further comprises one or more metal catalysts. In some embodiments, this metal catalyst is a metal salt. In preferred embodiments, the anion in the metal salt is F -Cl - , Br - , I - ClO4 - BF4 - PF6 - AsF6 - SbF6 - NO2 - NO3 - HSO4 - SO4 2- , PO4 3- HPO4 2- CF3CO2 - CF3CO3 - CO3 2- CF3SO3 - , C1~C6 carboxylates, CN - SCN - OCN - , CNO - , N3 - The group is selected from tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate, and the metal ion is selected from the group including Na, Ba, Sr, Ca, Cd, Sn, Pb, Fe, Cu, Zn, Zr, Mn, Co, Ni, Li, Al, Cr, Mg, Mo, Hg, Ag, Au, Pt, Rh, Re, Ti, Pb, Bi, Ga, In, Sn, Ir, La, Hf, Ta, W, and Os.

[0059] In some preferred embodiments, the C1-C6 carboxylates are selected from the group including formates, acetates, propionates, butyrates, hexanoates, maleates, fumarates, oxalates, lactates, and pirubates.

[0060] The ionic polymer network of the present invention, which includes one or more metal catalysts, provides better stability and reusability of the ionic polymer-metal combination.

[0061] The preparation of the ionic polymer network of the present invention having one or more metal catalysts typically involves mixing or refluxing the ionic polymer network and metal salts overnight in water / organic solvent. See, for example, J.Am.Chem.Soc., 2012, 134, 11852-11855; Chem.Cat.Chem., 2016, 8, 2508-2515; J.Org.Chem., 2011, 76(24), pp. 10140-10147; Inorg.Chem., 2006, 45, 6396-6403.

[0062] The ionic polymer of the present invention can be incorporated into a film or attached to and bonded to a solid support.

[0063] Another aspect of the present invention provides a film composed of the ionic polymer of the present invention. In some embodiments, the present invention provides a polymer film comprising one or more of the ionic polymers of the present invention. A polymer film can be produced by adding a suitable copolymer (e.g., acrylic acid) to the salt used in the preparation of the ionic polymer of the present invention, and then polymerizing the mixture. The approach for film formation is based on a template-free method by simple ionic complexing (see Taeuber K. et al., Polym. Chem., 2015, 6, 4855-4858; Taeuber K. et al., ACS Macro Lett., 2015, 4(1), 39-42; Zhang S. et al., Chem. Sci., 2015, 6, 3684-3691) when the ionic monomer is copolymerized with a suitable organic acid / acid derivative. As an example, the ionic monomer was dissolved in DMSO and stirred at 60°C for 2 hours. This clear solution was then poured onto a glass plate and the solvent was evaporated in an oven at 80°C. Next, the resulting non-porous, dry polymer film was immersed overnight in aqueous ammonia (0.2 wt%) for pore formation and electrostatic composite formation. The film was easily removed from the glass plate and washed several times with water.

[0064] Another aspect of the present invention provides a solid-supported ionic polymer. In some embodiments, the present invention provides a solid support having at least one surface containing one or more of the ionic polymers of the present invention. The supported ionic polymer can be immobilized on a variety of materials as a support: silicon or carbon (nanotube, wire) sources, graphene or graphene oxide, zeolites, metals / metal alloys or metal / metal alloy oxides. For example, FeO x The support was oxidized in an oven in the presence of oxygen at a high temperature (500°C), and then its surface was modified with a mixture of silanes dissolved in ethanol in the presence of HCl. After drying at room temperature, the support was uniformly impregnated with a methanol solution of the ionic polymer and AIBN. After drying at room temperature, the resulting material was placed in an oven at 95°C for 2 hours. By repeating this impregnation process, the desired polymer filling amount may be achieved. Another example is a stainless steel film containing the ionic polymer of the present invention. A mixture containing ionic monomers (0.2-0.5 molar ratio), acrylic acid (0.1-0.6 molar ratio), and benzoin ethyl ether (1 wt% as a photoinitiator) was dissolved in methanol to obtain a homogeneous solution. This was then dispersed by wetting a stainless steel film and photocrosslinked at room temperature by irradiation with UV light at a wavelength of 250 nm.

[0065] The attachment of ionic polymers can also be achieved by surface grafting, which requires activation of the support by UV or O3, O2, H2, or air plasma. Surface grafting involves the generation of reactive sites (radicals) on the polymer surface, followed by covalent bonding of the pre-formed polymer, or more generally, polymerization of monomers from these radical sites (see Alves P. et al., Colloids and Surfaces B: Biointerfaces, Vol. 82, No. 2, February 1, 2011, 371-377; Barbey R. et al., Chem. Rev., 2009, 109(11), 5437-5527). Another copolymer or polymerization initiator can also be used during the polymerization process (as in the case of film formation).

[0066] In some embodiments of the present invention, a method for hydrolyzing proteins and protein-containing raw materials to protein hydrolysates, the organic solvent is selected from the group including alcohols (e.g., methanol, ethanol, butanol, ethylene glycol, etc.), ethers (e.g., dimethoxyethane, diglyme, butyl methyl ether, etc.), ketones (e.g., methyl isobutyl ketone, N-methyl-2-pyrrolidone, etc.), and eutectic solvents (e.g., glycerol-choline chloride, octanoic acid-tetrabutylammonium chloride, poly(ethylene glycol)-choline chloride, lactic acid-glycine).

[0067] In some embodiments of the method of the present invention, the recovery of protein hydrolysates can be carried out by any technique known in the art, such as filtration, centrifugation, or gravity sedimentation.

[0068] The effective amount of the ionic polymer or combination thereof used in the methods described herein may depend on several factors, including, for example, the type of protein or protein-containing raw material, the amount of protein-containing raw material, the protein content in the protein-containing raw material, the type and number of pretreatments applied to the protein-containing raw material, and the reaction conditions (temperature and time, etc.). The effective amount of the ionic polymer of the present invention refers to an amount sufficient to decompose the protein or protein-containing raw material into the protein hydrolysate of the present invention. In some embodiments, the effective amount of the ionic polymer of the present invention is typically 0.05:1 w / w to 10:1 w / w, 0.5:1 w / w to 10:1 w / w, 1:1 w / w to 1:5 w / w, preferably 0.1:1 w / w to 1:5 w / w, relative to the protein content in the protein-containing raw material.

[0069] The ratio of protein-containing raw material to water used in the methods described herein may depend on several factors, including, for example, the type and amount of protein-containing raw material. In some embodiments, the ratio of protein-containing raw material to water or organic solvent (alcohol, ether, ketone, eutectic solvent, etc.) used in the methods described herein is in the range of 1:100 w / v to 1:1 w / v, preferably 1:50 w / v to 1:10 w / v.

[0070] The preferred temperature profile for heating used in the methods described herein also depends on the protein-containing raw material used and the intended protein hydrolysate to be produced. The heating temperature should preferably be maintained at a maximum of 200°C, and in some embodiments at a maximum of 170°C or 160°C. In some embodiments, the heating temperature is 100°C to 200°C, or 100°C to 170°C, or 100°C to 160°C, or 110°C to 150°C, preferably 120°C to 170°C or 120°C to 140°C. Preferably, for small-scale applications, heating is carried out in a high-pressure autoclave reactor, which is sealed and then heated for an appropriate reaction time and temperature.

[0071] The protein hydrolysate production method of the present invention is carried out at moderate temperatures, typically below 170°C, 160°C, or 50°C, whereas conventional methods require temperatures above 170°C. In addition, the protein hydrolysate production method of the present invention produces fewer by-products, which facilitates the recovery of the target product.

[0072] In some embodiments, the appropriate reaction time in the method described herein is, for example, 10 minutes to 10 hours, preferably 0.5 hours to 5 hours or 1 hour to 3 hours, depending on the type and amount of protein-containing raw materials.

[0073] A key advantage of the use of the ionic polymer or combination thereof of the present invention, a membrane incorporating the ionic polymer and / or solid-supported ionic polymer of the present invention, and its use for the hydrolysis, disintegration, or degradation of proteins and protein-containing raw materials is its use in a one-pot system for the disintegration of protein-containing raw materials and the selective extraction of the aforementioned protein hydrolysates from the protein-containing raw materials. Furthermore, the ionic polymer of the present invention is insoluble and therefore does not mix with the protein hydrolysates of the present invention.

[0074] According to the present invention, in order to make proteins into more attractive food substitutes with improved digestibility, absorption, and benefits, large natural proteins are hydrolyzed into smaller protein fragments called protein hydrolysates, such as peptides and / or amino acids, using ionic polymers disclosed herein.

[0075] Another aspect of the present invention provides a protein hydrolysate obtained by a method of hydrolyzing the protein and / or protein-containing raw material of the present invention. In some embodiments, the protein hydrolysate obtained by the method of the present invention comprises peptides and free amino acids, the protein hydrolysate is water-soluble and has improved solubility and a degree of hydrolysis greater than 2.5%, and the peptides are oligopeptides and polypeptides which may be linked to carbohydrates and have a molecular weight of less than 10,000 Da.

[0076] Another aspect of the present invention provides protein hydrolysates containing peptides such as oligopeptides and polypeptides, as well as free amino acids. In some embodiments, the peptides present in the protein hydrolysates of the present invention are glycopeptides and / or peptides linked to carbohydrates.

[0077] In some embodiments, the oligopeptides and / or polypeptides in the protein hydrolysate have a molecular weight of less than 10,000 Da, preferably 500 to 8,000 Da.

[0078] The above peptide typically contains 2 to 20 or more amino acids. This peptide may also be biologically active. The protein hydrolysate of the present invention is water-soluble and has improved solubility and a degree of hydrolysis greater than 2.5%.

[0079] In some embodiments, the protein hydrolysate of the present invention comprises peptides and free amino acids, the protein hydrolysate is water-soluble, has improved solubility and a degree of hydrolysis greater than 2.5%, and the peptides are oligopeptides and polypeptides which may be linked to carbohydrates and have a molecular weight of less than 10,000 Da.

[0080] In other embodiments, the protein hydrolysate of the present invention comprises peptides and free amino acids, the protein hydrolysate is water-soluble, has improved solubility and a degree of hydrolysis greater than 2.5%, and the peptides are oligopeptides and polypeptides which may be linked to carbohydrates and have a molecular weight of less than 10,000 Da.

[0081] In some embodiments, the protein hydrolysate is obtained by a method of hydrolyzing the protein and / or protein-containing raw material of the present invention.

[0082] The protein hydrolysates of the present invention can act as physiological modulators of metabolism and may possess a wide range of biological activities, including immunomodulators, anticancer agents, antihypertensive agents, antioxidants, anti-inflammatory agents, mineral binders, opioid agents, antihypertensive agents, antibacterial / antimicrobial agents, antifungal and antiviral agents, anticoagulants, fever-generating agents, anti-osteoporosis agents (bone protectants), modulators of cell proliferation and repair, angiotensin-converting enzyme (ACE) inhibitors, and, in addition, biological signaling mediators involved in countless signaling functions that affect recovery, lipid metabolism, carbohydrate metabolism, immune function, cardiovascular and bone health, nervous system and brain function, optimization of muscle performance during exercise, digestive satiety, and weight management.

[0083] In addition to biological activity, the protein hydrolysates of the present invention possess a variety of physicochemical properties, including solubility, lipid binding, foaming, and emulsifying properties, depending on their composition, sequence, and length. In fact, the protein hydrolysates of the present invention can have beneficial effects on improving the morphology, function, and resistance to infectious diseases of the intestines in humans and animals (e.g., pigs, calves, chickens, companion animals, and fish), thereby enhancing their health and well-being, as well as their growth performance and feed efficiency. This provides a cost-effective approach to converting protein-containing raw materials such as animal by-products, brewery by-products, or plant feeds into high-quality protein hydrolysate components, and to providing human nutritional supplements and animal feed formulations. Furthermore, the protein hydrolysates of the present invention may have applications in textiles, including plywood adhesives; applications in aquaculture and agriculture, including promoting plant rooting, germination, growth, and life extension; applications in cosmetic formulations; applications in biological and absorbable hydrogel formulations; applications in functional food and beverage formulations; applications in enteric-coated formulations and nutritional supplements; applications in infant and child nutritional product formulations; applications in animal feed formulations; applications in cell culture and growth media and fermentation processes; and applications in baking ingredients to improve freeze resistance and desirable texture;

[0084] The protein hydrolysates of the present invention can be used in a variety of applications selected from the group including pharmaceuticals, preventive hygiene, nutritional supplements, functional foods and beverages, pediatric nutrition, food additives, animal feed, fertilizers, antioxidants, antibacterial agents, cosmetics, and surfactants.

[0085] Preferably, the protein hydrolysates of the present invention are used in the manufacture of foods, functional foods, nutritional supplements, animal feed products and / or cosmetics.

[0086] In another embodiment, the present invention provides a method for producing food, functional food, nutritional supplement, animal feed product and / or cosmetic, comprising the use of the protein hydrolysate of the present invention.

[0087] Another aspect of the present invention provides foods, functional foods, nutritional supplements, animal feed products and / or cosmetics containing the protein hydrolysate of the present invention.

[0088] In some embodiments of the present invention, the food comprises an edible material and a protein hydrolysate of the present invention. The selection of a specific protein hydrolysate to be combined with the edible material may and will vary depending on the desired food. The selection of an appropriate edible material will also vary depending on the desired food. The edible material may be a plant-derived material (e.g., vegetable juice, cereal products, etc.), an animal-derived material (e.g., dairy products, egg products, etc.), or a biomaterial isolated from a plant-derived or animal-derived material (e.g., protein, carbohydrate, lipid, etc.).

[0089] The foods of the present invention may include, for example, hot or cold cereals (grains), bars, baked foods, beverages, yogurt, desserts, snacks, pasta, and meat (including poultry and seafood).

[0090] The protein hydrolysates of the present invention can be combined with all kinds of ingredients, such as oils, fats, emulsifiers, carbohydrates, fruit concentrates, flavorings, colorings, alcohols, carbon dioxide, thickeners, acidulants, antioxidants, herbs or herbal extracts, vitamins or bioactive compounds, and other health-promoting compounds, to formulate products that meet market needs.

[0091] Those skilled in the art will understand that modifications and alterations other than those specifically described are possible with respect to the invention described herein. It should be understood that the present invention includes all such modifications and alterations that do not depart from its spirit or essential features. The present invention also includes all of the steps, features, compositions and compounds referenced or indicated herein, individually or collectively, and any and all combinations or any two or more of the above steps or features. Therefore, this disclosure should be considered in all exemplary, non-limiting embodiments, the scope of the present invention is indicated by the appended claims, and all modifications that fall within the meaning and scope of equivalents are intended to be incorporated into the present invention.

[0092] The above description will be better understood by referring to the following examples. However, such examples are illustrative of ways of carrying out the present invention and are not intended to limit the application and scope of the present invention. [Examples]

[0093] Preparation of monomers of formula VI To prepare cationic DMAEMAQ, 30 mmol of DMAEMA is dissolved in an appropriate amount of solvent (the solvent may be THF, acetonitrile, DCM, chloroform, diethyl ether, etc.), followed by 36 mmol of RX (wherein X is a halide, HSO4) in the same solution. - or SO4 2- A (where R is alkyl or aryl) was carefully added. The reaction mixture was stirred at room temperature for 12 hours. The precipitate was then filtered and washed with cold hexane. Finally, the resulting product was dried under vacuum for 8 hours to obtain a crystalline solid of the corresponding DMAEMAQ monomer. [ka]

[0094] Preparation of protein hydrolysates from whey gluten 5 g of whey gluten suspended in 75 ml of water with 65 mg of IP1 was stirred at 140°C for 1 hour. After the reaction, the mixture was cooled to room temperature, filtered, the solid phase was dried, and the liquid phase was subjected to QTOF-ESI(+) analysis. A 35% weight conversion rate was measured. Interpretation of the obtained data revealed a mixture of oligopeptides and polypeptides with a mass range of 500–7000 daltons. See Figure 1.

[0095] Preparation of protein hydrolysates from bovine albumin 100 mg of bovine albumin suspended in 1.5 ml of water with 4 mg of IP1 was stirred at 140°C for 1 hour. After the reaction, the mixture was cooled to room temperature, filtered, and the liquid phase was subjected to QTOF-ESI(+) analysis. Interpretation of the obtained data revealed a mixture of oligopeptides and polypeptides with a mass range of 500–8000 Da. See Figure 2.

[0096] Preparation of protein hydrolysates from used barley 200 g of used barley suspended in 1.5 L of water with 3 g of IP1 was stirred at 140°C for 1 hour. After the reaction, the mixture was cooled to room temperature, filtered, and the liquid phase was subjected to QTOF-ESI(+) analysis. Interpretation of the obtained data revealed the presence of peptides linked to carbohydrates. See Figure 3.

[0097] Preparation of protein hydrolysates from yeast slurry 67 g of yeast slurry (dry base) suspended in 0.666 L of water with 0.22 g of IP3 was stirred at 145°C for 1.5 hours. After the reaction, the mixture was cooled to room temperature, filtered, and the liquid phase was dried using a spray dryer. The resulting dried product was analyzed for protein content using the Kjeldahl method, and 45% by weight was measured as hydrolyzed protein.

[0098] Examples of physicochemical improvements to proteins Okara has high nutritional value due to its high-quality protein (15.2–33.4%), fat (8.3–10.9%), carbohydrates, and fiber (30–58%). Due to the technical process, okara residue mainly contains insoluble or poorly extractable proteins. Okara protein isolates contain all essential amino acids and have a higher protein efficiency index than soy milk (2.71 vs. 2.11) and even higher than tofu, but have low water solubility. It has also been found that the protein fraction of okara can withstand complete digestion by gastrointestinal enzymes, pepsin, and pancreatin (the latter mainly consisting of trypsin, amylopsin, and stearpsin). However, the undesirable flavor of okara, referred to as "bean" flavor in its study, has been a major challenge to its application and production of okara-based foods. To address these challenges, hydrolysis treatment may be applied to increase the soluble fiber and soluble protein content, thereby improving nutritional quality and processing characteristics.

[0099] Preparation of okara hydrolysate I: 10 g of okara (dry base) suspended in 100 ml of water with the ionic polymer catalyst IP3 was stirred at 120°C for 1 hour. After the reaction, the mixture was cooled to room temperature, filtered, and the liquid phase was dried using a spray dryer.

[0100] Preparation of Okara Hydrolyzate II: 10 g of okara (dry base) suspended in 100 ml of water with the ionic polymer catalyst IP3 was stirred at 130°C for 1 hour. After the reaction, the mixture was cooled to room temperature, filtered, and the liquid phase was dried using a spray dryer.

[0101] [Table 1]

[0102] Examples of beneficial effects against specific bacterial growth Macronutrients and micronutrients can regulate the gut microbiota. The overall balance of macronutrients, such as proteins, carbohydrates, and fats, is known to influence the composition and functional potential of the gut microbiota. The efficacy of used barley hydrolysate (Prembion, a composition containing the protein hydrolysate of the present invention) was compared with glucose, commercially available XOS and FOS products, and the growth curves of Bifidobacterium X and Lactobacillus X bacterial strains were measured. The activity of these bacteria is associated with improved gut health in animals and humans.

[0103] Figures 4 and 5 show how two different strains function in vitro when different nutrient sources are supplemented in the culture medium. Compared to pure FOS and XOS, the complex product derived from spent barley and containing hydrolyzed proteins showed superior preferential growth of the Bifidobacterium strain (Figure 5) and relative growth of the Lactobacillus strain (Figure 4).

Claims

[Claim 1] A method for hydrolyzing proteins and / or protein-containing raw materials into protein hydrolysates, a) A step of providing protein and / or protein-containing raw materials, e) A step of contacting the protein and / or the protein-containing raw material with a catalyst to form a reaction reaction, wherein the catalyst is an ionic polymer or a combination of ionic polymers, an ionic polymer network, a solid-supported ionic polymer, and / or a polymer film incorporating an ionic polymer, f) A step of decomposing the protein and / or the protein-containing raw material in the reaction mixture to produce a liquid phase and a solid phase, wherein the liquid phase contains the protein hydrolysate and the solid phase contains residual material, g) A step of isolating at least a portion of the liquid phase from the solid phase, h) A step of recovering the protein hydrolysate from the isolated liquid phase. Includes, The ionic polymer (IP) is the first monomer of formula I. 【Chemistry 1】 It consists of the second monomer of formula II below, 【Chemistry 2】 In the above formula, n and m are independently selected from 1, 2, 3, 4, 5, and 6. z and w are independently selected from 0, 1, 2, and 3. Z １ Z ２ and Z ３ Each of them operates independently. 【Transformation 3】 A cation selected from the group including, R1, R2, R3, R4, R5, and R6 are each independently a bond, H, C １ ~C ６ alkyl, C １ ~C ６ allyl, CH ３ -(CH ２ )p-O-(CH ２ )q-CH ３ , C １ ~C ６ alkoxy, C １ ~C ６ alkoxyalkyl, benzyl, -SO ３ H, -(CH ２ )q-SO ３ H, and are selected from the group consisting of, provided that two of R1, R2, R3, R4, R5, and R6 are each a bond p and q are independently selected from 0, 1, 2, 3, 4, 5, and 6. L is an optional linker, and if present, each occurrence of L independently corresponds to H, a substituted or unsubstituted C. １ ~C ２０ Alkylene, C １ ~C ２０ Alkenylene, C １ ~C ２０ Alkynylene and substituted or unsubstituted C ５ ~C １０ Selected from aryls, the substituents are H, -SO ３ H, -COOH, -[P(=O)(OH) ２ ], -[P(=O)(OH)], -O-SO ３ H, -O-COOH, -O-[P(=O)(OH) ２ Selected from the group including ], -O-[P(=O)(OH)], A is an optional acidic group, and if present, each occurrence of A is independently -SO ３ H, -COOH, -[P(=O)(OH) ２ ], -[P(=O)(OH)], -O-SO ３ H, -O-COOH, -O-[P(=O)(OH) ２ ], -O-[P(=O)(OH)], -CH ２ - Selected from the group containing COOH, X － is F － , Cl － , Br － , I － , ClO ４ － BF ４ － , PF ６ － AsF ６ － SbF ６ － NO ２ － NO ３ － HSO ４ － SO ４ ２－ , PO ４ ３－ HPO ４ ２－ CF ３ CO ２ － CF ３ CO ３ － CO ３ ２－ CF ３ SO ３ － , C １ ~C ６ Carboxylate, CN － SCN － OCN － , CNO － , N ３ － Selected from the group including tosylate, mesylate, trifluoromethanesulfonate, trifluoroethanesulfonate, di-trifluoromethanesulfonylamino, doxate, and xylenesulfonate. The ionic polymer network comprises one or more crosslinked ionic polymers (IP), The solid support has at least one surface comprising one or more of the ionic polymers (IPs) or the ionic polymer network, The polymer film is a method of incorporating one or more ionic polymers (IPs) or an ionic polymer network.

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