Meat-like food composition

Abstract

To provide a meat-like food composition that exhibits excellent real-meat likeness.SOLUTION: A meat-like food composition comprising at least one raw material selected from the group consisting of a meat raw material and a meat substitute composition raw material, and a sheet containing a purified protein.SELECTED DRAWING: None

Description

[Technical Field]

[0001] The present invention relates to a meat-like food composition. [Background technology]

[0002] Formed meat is made by softening fine scraps of meat and organ meat with a tenderizer, solidifying them with a binder, and shaping them, and is used as artificial steak meat, etc. Formed meat is advantageous from the viewpoint of cost compared to natural meat products. On the other hand, since formed meat uses a binder to bind the fine pieces of meat, the joints are easily separated, making it difficult to produce the texture of steak meat.

[0003] Meanwhile, active efforts are being made around the world to develop meat substitute compositions that artificially reproduce the taste and texture of real meat. Non-animal-derived meat substitute compositions are attracting attention for their low calorie and high protein content, which allows them to address food issues and be provided as vegan foods. Known meat substitute compositions include, for example, cultured meat, which is produced by culturing cells collected from animals, and meat substitutes made from plant proteins such as soybeans, peas, and wheat (e.g., Patent Documents 1 and 2). [Prior art documents] [Patent documents]

[0004] [Patent Document 1] Japanese Patent Application Laid-Open No. 2017-517273 [Patent Document 2] Japanese Patent Application Laid-Open No. 2009-537178 Summary of the Invention [Problem to be solved by the invention]

[0005] Most meat substitute compositions are used to make so-called "minced meat." In most plant-based meat substitute compositions, the plant protein fibers are aligned in one direction and in a single plane, which makes them easily and quickly degraded during chewing and prevents them from providing the chewing sensation of meat.

[0006] To artificially create a three-dimensional meat-like structure, for example, in the case of cultured meat, technology is being developed to transform muscle cells into elongated structures, place a scaffold (muscle tissue substitute) to which the cells can attach in a culture medium, layer aggregates of muscle cells, create three-dimensional muscle tissue, and produce the texture and mouthfeel of real meat, like steak. However, it will likely take some time before scaffold materials can be mass-produced cheaply and stably, just like culture medium.

[0007] Currently, several meat-like food compositions, such as artificial steak meat and artificial block meat, using meat or plant proteins, have been put to practical use. However, these meat-like food compositions still lack the "realistic feel" that combines texture (e.g., appearance) and sensory properties (e.g., texture, juiciness, tenderness).

[0008] An object of the present invention is to provide a meat-like food composition that is highly realistic. [Means for solving the problem]

[0009] The present inventors have found that by further incorporating a sheet containing purified protein into a meat-like food composition containing a meat ingredient and / or a meat substitute ingredient, the "authenticity" of the food, which is a combination of texture (appearance) and sensory properties (feel, juiciness, tenderness), is improved. The present invention is based on this finding.

[0010] The present invention relates to, for example, the following inventions. [1] A meat-like food composition comprising at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients, and a sheet containing purified protein. [2] The meat-like food composition according to [1], wherein the protein is a structural protein. [3] The meat-like food composition according to [1] or [2], wherein the protein has an alanine residue content of 10 to 40% and a glycine residue content of 10 to 55%. [4] The meat-like food composition according to any one of [1] to [3], wherein the protein is fibroin. [5] The meat-like food composition according to any one of [1] to [4], wherein the sheet is made of spun protein fibers. [6] The meat-like food composition according to any one of [1] to [5], which does not contain animal protein. [7] The meat-like food composition according to any one of [1] to [6], which does not contain any animal-derived ingredients. [8] The meat-like food composition according to any one of [1] to [7], which is formed into the shape of steak meat. [9] The meat-like food composition according to [8], wherein layers containing at least one ingredient selected from the group consisting of the meat ingredients and meat substitute composition ingredients and the sheets are arranged alternately.

[10] The sheet includes a layer formed on at least one surface of the sheet, the layer containing at least one ingredient selected from the group consisting of the meat ingredient and the meat substitute composition ingredient, The meat-like food composition according to any one of [1] to [9], wherein the sheet on which the layer is formed has been subjected to at least one treatment selected from the group consisting of stitching, weaving, braiding, knitting, and needle punching.

[11] 1. A method for enhancing the authenticity of a meat-like food composition, comprising: The method comprises attaching at least one ingredient selected from the group consisting of a meat ingredient and a meat substitute composition ingredient to at least one surface of a sheet containing purified protein.

[12] The method according to

[11] , further comprising adding a protein cross-linking agent to at least one ingredient selected from the group consisting of the meat ingredients and meat substitute composition ingredients.

[13]

[12] The method according to

[12] , wherein the protein cross-linking agent is transglutaminase. [Effects of the Invention]

[0011] According to the present invention, it is possible to provide a meat-like food composition that is superior in realism compared to conventional meat-like food compositions. [Brief explanation of the drawings]

[0012] [Figure 1] FIG. 1 is an explanatory diagram schematically illustrating an example of a spinning apparatus for producing protein fibers. [Figure 2] 1 is a photograph showing the artificial steak meat compositions of Example 1 and Comparative Example 1. [Figure 3] 3 is a photograph showing the artificial steak meat compositions of Example 2 and Comparative Example 2. [Figure 4] 1 is a photograph showing the artificial steak meat composition of Example 5. [Figure 5] 1 is a photograph showing the artificial steak meat composition of Example 6. [Figure 6] 1 is a graph showing the results of measuring the hardness of cooked artificial steak meat compositions of Examples 7 to 13, as measured by TPA. [Figure 7] 1 is a graph showing the results of measurement of hardness (Hardness) of cooked artificial steak meat compositions of Examples 7 to 13, measured by SSF. [Figure 8] 1 is a graph showing the results of measuring the cohesiveness of the cooked artificial steak meat compositions of Examples 7 to 13 using TPA. [Figure 9] 1 is a graph showing the results of measuring the springiness (springiness) of cooked artificial steak meat compositions of Examples 7 to 13 using TPA. [Figure 10]1 is a graph showing the results of measurement of hardness (Hardness) of cooked artificial steak meat compositions of Examples 14 to 20, measured by SSF. [Figure 11] 1 is a graph showing the results of measuring the springiness (Springiness) of cooked artificial steak meat compositions of Examples 14 to 20, measured by SSF. [Figure 12] 1 is a graph showing the results of measuring the cohesiveness of the cooked artificial steak meat compositions of Examples 14 to 20, as measured by SSF. [Figure 13] 1 is a graph showing the results of measuring the hardness (Hardness) of cooked artificial steak meat compositions of Examples 14 and 21 using TPA. [Figure 14] 1 is a graph showing the results of measuring the hardness (Hardness) of cooked artificial steak meat compositions of Examples 14 and 21, measured by SSF. [Figure 15] 1 is a graph showing the results of measuring the cohesiveness of cooked artificial steak meat compositions of Examples 14 and 21, as measured by SSF. [Figure 16] 1 is a graph showing the results of measuring the springiness (Springiness) of cooked artificial steak meat compositions of Examples 14 and 21, measured by SSF. [Figure 17] 1 is a graph showing the results of measuring the chewiness (Chewiness) of cooked artificial steak meat compositions of Examples 14 and 21 using an SSF. DETAILED DESCRIPTION OF THE INVENTION

[0013] DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS The following describes in detail the embodiments of the present invention, but the present invention is not limited to the following embodiments.

[0014] The meat-like food composition of this embodiment comprises at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients, and a sheet containing purified protein. Because the meat-like food composition of this embodiment has this configuration, when cooked (for example, cooked with heat), it has improved "authenticity," which is a combination of texture (appearance) and sensory properties (texture, juiciness, tenderness), compared to conventional meat-like food compositions.

[0015] As used herein, the term "meat-like food composition" refers to a food composition that primarily contains meat ingredients and / or meat substitute composition ingredients and is obtained by forming the composition into a desired shape. The term "meat-like food composition" as used herein also includes so-called formed meat, but does not include meat that is simply cut from natural meat. Examples of the shape of a meat-like food composition include steak meat (e.g., whole steak, chops, etc.), block meat (e.g., cubes, rectangular prisms, etc.), and thinly sliced ​​meat.

[0016] As used herein, the term "artificial steak meat composition" refers to a meat-like food composition formed into the shape of steak meat.

[0017] As used herein, "meat" refers to meat from livestock and poultry that is edible. Specific examples of meat include beef, pork, chicken, horse meat, mutton, goat meat, and duck meat. "Meat ingredients" include, for example, meat that has been cut into small pieces by processing such as cutting, slicing, or mincing. As the meat ingredient used in the meat-like food composition, ground meat (minced meat) is preferred, as this more significantly exhibits the effects of the present invention. The meat ingredient may be one type of meat or a combination of two or more types.

[0018] As used herein, the term "meat substitute composition" refers to a meat substitute that artificially reproduces the chemical properties (nutritional composition, etc.) or quality (taste, flavor, texture, appearance, etc.) of meat without relying on meat derived from livestock or poultry. Meat substitute compositions also include so-called cultured meat and meat substitutes. "Cultured meat," which is produced in a lab by extracting tissues or cells from animals and culturing those cells, is also called "lab-meat," "in vitro meat," "clean meat," etc. "Meat substitutes" made from non-animal-derived ingredients such as plants are also called "imitation meat," "fake meat," "vegan meat," "plant-based meat," "artificial meat," etc. "Meat substitute composition raw material" refers to the primary protein source in the meat substitute composition, and includes, for example, proteins derived from non-animal sources such as cultured cells (such as animal cells), soybeans, peas, wheat, oats, rye, barley, canola, sunflower, sorghum, rice, amaranth, potato, tapioca, arrowroot, canna, lupin, rapeseed, algae, edible filamentous fungi, and mixtures thereof. Note that meat-like food compositions that do not contain animal-derived components (such as animal proteins) fall under the category of meat substitute compositions.

[0019] A sheet containing a purified protein (hereinafter simply referred to as a "sheet") contains a purified protein as a main component and is formed into a sheet shape. The sheet according to this embodiment may be made of a purified protein.

[0020] The type of protein contained in the sheet according to this embodiment is not particularly limited and may be, for example, a protein derived from a plant, fungus, algae, animal, or microorganism. The protein may be a recombinant protein. A recombinant protein refers to a protein produced using genetic recombination technology. A recombinant protein may be, for example, one isolated from a non-animal genetically modified organism.

[0021] The protein contained in the sheet according to this embodiment may be derived from a non-plant source. Specifically, for example, it may be a protein purified from a non-plant, or it may be a protein produced using genetic recombination technology from a gene isolated from a non-plant. Similarly, the protein contained in the sheet according to this embodiment may be derived from a non-animal source. Specifically, for example, it may be a protein purified from a non-animal, or it may be a protein produced using genetic recombination technology from a gene isolated from a non-animal.

[0022] The protein contained in the sheet according to this embodiment may be either a hydrophilic protein or a hydrophobic protein. The protein contained in the sheet according to this embodiment is preferably one whose average HI, calculated by summing the hydrophobicity indices (HI) of all amino acid residues constituting the protein and then dividing this sum by the total number of amino acid residues (hereinafter also referred to as "hydrophobicity"), is 1.0 or less. The hydrophobicity index of amino acid residues is determined using a known index (Hydropathy index: Kyte J, & Doolittle R (1982) "A simple method for displaying the hydropathic character of a protein", J. Mol. Biol., 157, pp. 105-132). Specifically, the hydrophobicity index of each amino acid is as shown in Table 1 below. [Table 1]

[0023] The hydrophobicity of the protein contained in the sheet according to this embodiment may be -1.0 or more, -0.9 or more, or -0.8 or more, or may be 1.0 or less, 0.9 or less, 0.8 or less, 0.7 or less, 0.6 or less, 0.5 or less, 0.4 or less, 0.3 or less, 0.2 or less, 0.1 or less, -0.1 or less, -0.2 or less, -0.3 or less, -0.4 or less, -0.5 or less, -0.6 or less, or -0.7 or less. A hydrophobicity of 0.5 or less increases the affinity with aqueous components, further improving the texture (appearance) and sensory properties (texture, juiciness, tenderness) of the meat-like food composition.

[0024] The protein contained in the sheet according to this embodiment may have 50 or more amino acid residues. The number of amino acid residues may be, for example, 100 or more or 150 or more, 200 or more or 250 or more, and is preferably 300 or more, 350 or more, 400 or more, 450 or more, or 500 or more.

[0025] The protein contained in the sheet according to this embodiment may be, for example, a structural protein. A structural protein refers to a protein involved in the structure of a living organism, a protein that constitutes a structure produced by a living organism, or a protein derived therefrom. A structural protein also refers to a protein that self-aggregates under certain conditions to form structures such as fibers, films, resins, gels, micelles, and nanoparticles, and examples of natural structural proteins include fibroin, keratin, collagen, elastin, and resilin.

[0026] The protein contained in the sheet according to this embodiment may be, for example, a globular protein. Globular proteins are folded into a spherical shape with complex tertiary and quaternary structures. They are typically water-soluble due to the hydrophobic side chains located at the center of the protein structure. Examples of globular proteins include enzymes, hemoglobin, myoglobin, globulin, fibrin, and albumin.

[0027] The protein contained in the sheet according to this embodiment preferably contains a high proportion of amino acid residues such as glycine, alanine, and serine. This is because amino acid residues with smaller side chains are more likely to form hydrogen bonds and thus form stronger sheets. Furthermore, alanine and glycine residues are amino acids with nonpolar side chains, and therefore are positioned so that they face inward during the folding process in protein synthesis, making them more likely to adopt an α-helix or β-sheet structure.

[0028] In one embodiment, the protein contained in the sheet according to this embodiment preferably has an alanine residue content of 10 to 40% and a glycine residue content of 10 to 55%. As used herein, the "alanine residue content" is a value expressed by the following formula: Alanine residue content = (number of alanine residues in protein / total number of amino acid residues in protein) x 100 (%) In addition, in this specification, the terms "glycine residue content," "serine residue content," "threonine residue content," "proline residue content," "tyrosine residue," "glutamine residue," and "lysine residue content" have the same meaning as those obtained by replacing the alanine residue in the above formula with "glycine residue," "serine residue," "threonine residue," "proline residue," "tyrosine residue," "glutamine residue," and "lysine residue," respectively.

[0029] The alanine residue content of the protein contained in the sheet according to this embodiment may be, for example, 12 to 40%, 15 to 40%, 18 to 40%, 20 to 40%, or 22 to 40%, and the glycine residue content may be, for example, 11 to 55%, 13 to 55%, 15 to 55%, 18 to 55%, 20 to 55%, 22 to 55%, or 25 to 55%.

[0030] From the viewpoint of improving processability into sheets, it is important to inhibit strong intermolecular hydrogen bonds during processing. From this viewpoint, it is desirable that amino acids with large side chains or flexible amino acids are uniformly contained to a certain extent throughout the entire sequence. For example, when a protein is divided into units of consecutive amino acid sequences of a predetermined number of amino acid residues, the total content of tyrosine residues, threonine residues, and proline residues contained in each unit may be equal to or greater than a predetermined value. Specifically, for example, among any consecutive 20 amino acid residues, the total content of proline residues, threonine residues, and tyrosine residues may be 5% or more, 10% or more, or 15% or more, or 50% or less, 40% or less, 30% or less, or 20% or less.

[0031] The protein contained in the sheet according to this embodiment may have a total serine residue content, threonine residue content, and tyrosine residue content of 4% or more, 4.5% or more, 5% or more, 5.5% or more, 6% or more, 6.5% or more, or 7% or more. The total serine residue content, threonine residue content, and tyrosine residue content may be, for example, 35% or less, 33% or less, 30% or less, 25% or less, or 20% or less.

[0032] The protein contained in the sheet according to this embodiment may contain glutamine residues and / or lysine residues. By containing glutamine residues and / or lysine residues, intramolecular or intermolecular crosslinks are formed in the protein in the presence of an edible crosslinking agent such as transglutaminase. The glutamine residue content may be, for example, 0% to 30%, 0% to 25%, 0% to 20%, 5% to 20%, 10% to 20%, or 15% to 20%. The lysine residue content may be, for example, 5% or more, 10% or more, 25% or less, 20% or less, 15% or less, or 10% or less.

[0033] The protein contained in the sheet according to this embodiment may have a repeat sequence. That is, the protein contained in the sheet according to this embodiment may have a plurality of amino acid sequences (repeat sequence units) with high sequence identity within the protein. The number of amino acid residues in the repeat sequence unit is preferably 6 to 200. Furthermore, the sequence identity between the repeat sequence units may be, for example, 85% or more, 90% or more, 95% or more, 96% or more, 97% or more, 98% or more, or 99% or more.

[0034] The protein contained in the sheet according to this embodiment is (A) n In the present specification, (A) n The motif refers to an amino acid sequence consisting mainly of alanine residues. (A) n The number of amino acid residues in the motif may be 2 to 27, or may be an integer of 2 to 20, 2 to 16, or 2 to 12. n The ratio of the number of alanine residues to the total number of amino acid residues in the motif may be 40% or more, and may be 60% or more, 70% or more, 80% or more, 83% or more, 85% or more, 86% or more, 90% or more, 95% or more, or 100% (meaning that it is composed only of alanine residues).

[0035] The protein contained in the sheet according to this embodiment is preferably fibroin. Examples of fibroin include naturally occurring fibroin and artificial fibroin.

[0036] Naturally occurring fibroin includes, for example, fibroin produced by insects or arachnids.

[0037] Examples of fibroin produced by insects include silk proteins produced by silkworms such as Bombyx mori, Bombyx mandarina, Antheraea yamamai, Antheraea pernyi, Eriogyna pyretorum, Pilosamia Cynthia ricini, Samia cynthia, Caligura japonica, Antheraea mylitta, and Antheraea assama, as well as hornet silk proteins excreted by larvae of the Japanese hornet (Vespa simillima xanthoptera).

[0038] A more specific example of fibroin produced by insects is silkworm fibroin L chain (GenBank accession numbers M76430 (nucleotide sequence), AAA27840.1 (amino acid sequence)).

[0039] Examples of fibroin produced by spiders include spiders belonging to the Araneus genus, such as the orb spider, the garden spider, the red orb spider, the green orb spider, and the bean spider; spiders belonging to the Neoscona genus, such as the mountain orb spider, the house spider, the dun orb spider, and the Satsuma spider; spiders belonging to the Pronus genus, such as the little orb spider; spiders belonging to the Cyrtarachne genus, such as the Japanese orb spider and the large orb spider; spiders of the genus Gasteracantha such as the Japanese bush spider and the Japanese bush spider; spiders of the genus Ordgarius such as the Japanese bush spider and the Japanese bush spider; spiders of the genus Argiope such as the orb-weaver spider, the orb-weaver spider and the long-jawed orb-weaver spider; spiders of the genus Arachnura such as the Japanese bush spider; spiders of the genus Acusilas such as the scraping spider; spiders of the genus C such as the orb-weaver spider, the orb-weaver spider and the Japanese bush spider; spider silk proteins produced by spiders belonging to the genus Poltys (such as the house spider), spiders belonging to the genus Cyclosa (such as the house spider, the four-headed house spider, the common house spider, and the black house spider), and spiders belonging to the genus Chorizopes (such as the Japanese canary spider), as well as spiders belonging to the genus Tetragnatha (such as the long-legged spider, the long-legged spider, the common house spider, and the scaly house spider), spiders belonging to the genus Tetragnatha (such as the long-legged spider, the common house spider, the large-legged spider), and ... spiders belonging to the genus Leucauge such as orb spiders and white orb spiders, spiders belonging to the genus Nephila such as orb spiders and giant orb spiders, spiders belonging to the genus Menosira such as golden spiders, spiders belonging to the genus Dyschiriognatha such as small red widow spiders, spiders belonging to the genus Latrodectus such as black widow spiders, redback spiders, gray widow spiders and three-spotted widow spiders,Examples of spider silk proteins include spider silk proteins produced by spiders belonging to the family Tetragnathidae, such as spiders belonging to the genus Euprosthenops. Examples of spider silk proteins include dragline proteins such as MaSp (MaSp1 and MaSp2) and ADF (ADF3 and ADF4), and MiSp (MiSp1 and MiSp2).

[0040] More specific examples of fibroins produced by spiders include fibroin-3 (adf-3) [derived from Araneus diadematus] (GenBank accession numbers AAC47010 (amino acid sequence), U47855 (nucleotide sequence)), fibroin-4 (adf-4) [derived from Araneus diadematus] (GenBank accession numbers AAC47011 (amino acid sequence), U47856 (nucleotide sequence)), dragline silk protein spidroin 1 [derived from Nephila clavipes] (GenBank accession numbers AAC04504 (amino acid sequence), U37520 (nucleotide sequence)), major anguillate spidroin 1 [derived from Latrodectus hesperus] (GenBank accession numbers ABR68856 (amino acid sequence), EF595246 (nucleotide sequence)), and dragline silk protein spidroin 2 [derived from Nephila clavata] (GenBank accession numbers AAL32472 (amino acid sequence), AF441245 (nucleotide sequence)), major ampullate spidroin 1 [Euprosthenops australis] (GenBank accession numbers CAJ00428 (amino acid sequence), AJ973155 (nucleotide sequence)), and major ampullate spidroin 2 [Euprosthenops australis] (GenBank accession numbers CAM32249.1 (amino acid sequence), AM490169 (nucleotide sequence)), minor ampullate silk protein 1 [Nephila clavipes] (GenBank accession number AAC14589.1 (amino acid sequence)), minor ampullate silk protein 2 [Nephila clavipes] (GenBank accession number AAC14591.1 (amino acid sequence)), minor ampullate spidroin-like protein [Nephila clavipes] cruentata] (GenBank accession number ABR37278.1 (amino acid sequence) and the like.

[0041] More specific examples of naturally occurring fibroins include those whose sequence information is registered in NCBI GenBank. For example, these can be confirmed by extracting, from among the sequences registered in NCBI GenBank that contain INV as the division, sequences with spidroin, ampullate, fibroin, "silk and polypeptide," or "silk and protein" as keywords in the definition, sequences with a specific product character string in the CDS, and sequences with a specific character string in the tissue type field in the source.

[0042] As used herein, "artificial fibroin" refers to artificially produced fibroin (man-made fibroin). Artificial fibroin may be a fibroin with an amino acid sequence different from that of naturally occurring fibroin, or may be a fibroin with an amino acid sequence identical to that of naturally occurring fibroin.

[0043] Artificial fibroin may be a fibrous protein having a structure similar to that of naturally occurring fibroin, or may be a fibroin having a sequence similar to the repetitive sequence of naturally occurring fibroin. The "similar sequence to the repetitive sequence of fibroin" may be a sequence actually found in naturally occurring fibroin, or a sequence similar thereto.

[0044] Artificial fibroin may be, for example, a naturally occurring fibroin whose amino acid sequence has been modified (e.g., an amino acid sequence modified by modifying the gene sequence of a cloned naturally occurring fibroin), or an artificially designed amino acid sequence that is not based on naturally occurring fibroin (e.g., an artificially designed amino acid sequence obtained by chemically synthesizing a nucleic acid that encodes the designed amino acid sequence).

[0045] Examples of artificial fibroins include artificial silk fibroin (a silk protein produced by silkworms with a modified amino acid sequence), and artificial spider silk fibroin (a spider silk protein produced by spiders with a modified amino acid sequence), etc. The artificial fibroin preferably contains artificial spider silk fibroin, and more preferably consists of artificial spider silk fibroin, because it is easily fibrillated and has high fiber-forming ability.

[0046] The artificial fibroin may be, for example, a polymer represented by the formula 1: [(A) n Motif-REP] m , or Formula 2: [(A) n Motif-REP] m -(A) n The artificial fibroin may be a protein containing a domain sequence represented by a motif. The artificial fibroin may have further amino acid sequences (N-terminal sequence and C-terminal sequence) added to either or both of the N-terminal and C-terminal sides of the domain sequence. The N-terminal sequence and C-terminal sequence are typically, but not limited to, regions that do not have repeats of the amino acid motif characteristic of fibroin and consist of about 100 amino acid residues.

[0047] As used herein, the term "domain sequence" refers to a crystalline region specific to fibroin (typically, the amino acid sequence (A) n It is an amino acid sequence that generates a region (corresponding to a motif) and an amorphous region (typically corresponding to an REP in an amino acid sequence), and is represented by formula 1: [(A) n Motif-REP] m , or Formula 2: [(A) n Motif-REP] m -(A) n The amino acid sequence represented by the motif (A) n The motif shows an amino acid sequence mainly consisting of alanine residues, and the number of amino acid residues is 2 to 27. (A) n The number of amino acid residues in the motif may be an integer of 2 to 20, 4 to 27, 4 to 20, 8 to 20, 10 to 20, 4 to 16, 8 to 16, or 10 to 16. nThe ratio of the number of alanine residues to the total number of amino acid residues in the motif may be 40% or more, and may be 60% or more, 70% or more, 80% or more, 83% or more, 85% or more, 86% or more, 90% or more, 95% or more, or 100% (meaning that the motif is composed of only alanine residues). n At least seven of the motifs may be composed of only alanine residues. REP represents an amino acid sequence composed of 2 to 200 amino acid residues. REP may also be an amino acid sequence composed of 10 to 200 amino acid residues. m represents an integer of 2 to 300, and may be an integer of 10 to 300. (A) n The motifs may have the same or different amino acid sequences, and the REPs present in multiple instances may have the same or different amino acid sequences.

[0048] Specific examples of artificial fibroins include those shown in Table 2 below.

[0049] [Table 2]

[0050] The protein contained in the sheet according to this embodiment is preferably collagen. Examples of collagen include naturally occurring collagen and artificial collagen. Examples of collagen (collagen or a protein derived therefrom) that can be used in the present invention include, for example, collagen represented by Formula 3: [REP2] p (wherein, in formula 3, p represents an integer of 5 to 300. REP2 represents an amino acid sequence consisting of Gly-X-Y, where X and Y represent any amino acid residues other than Gly. Multiple REP2s may have the same amino acid sequence or different amino acid sequences.)

[0051] The protein contained in the sheet according to this embodiment can be obtained, for example, by recombinant expression according to standard methods, followed by isolation and purification according to standard methods. The purified protein preferably contains only the protein, but may contain unavoidable impurities. In one embodiment, from the viewpoint of the mechanical properties and moldability of the sheet, the purification purity of the purified protein is preferably 60% or more.

[0052] The protein contained in the sheet according to the present embodiment may have antibacterial properties. Specific examples of proteins with antibacterial properties include proteins having an antibacterial amino acid sequence and proteins having an antibacterial protein motif. The antibacterial properties of the protein contained in the sheet according to the present embodiment allow the meat-like food composition according to the present embodiment to have a long shelf life, and can be stored or transported, particularly at room temperature.

[0053] The protein contained in the sheet according to this embodiment may have antioxidant properties. Specific examples of proteins with antioxidant properties include proteins with amino acid compositions that have antioxidant properties and proteins with protein motifs that have antioxidant properties. The antioxidant properties of the protein contained in the sheet according to this embodiment can prevent browning, discoloration, and a decrease in nutritional value of the meat-like food composition according to this embodiment.

[0054] The proteins contained in the sheet according to the present embodiment may have prebiotic, postbiotic, and / or paraprobiotic functionality. Specific examples of proteins with prebiotic, postbiotic, and / or paraprobiotic functionality include proteins having amino acid sequences with prebiotic, postbiotic, and / or paraprobiotic functionality, and proteins having protein motifs with prebiotic, postbiotic, and / or paraprobiotic functionality. By having the proteins contained in the sheet according to the present embodiment have prebiotic, postbiotic, and / or paraprobiotic functionality, the meat-like food composition according to the present embodiment is expected to provide several health benefits by regulating the intestinal microflora.

[0055] The sheet according to this embodiment may contain one kind of the above-mentioned purified protein alone, or may contain two or more kinds of the above-mentioned purified protein.

[0056] When the sheet according to the present embodiment contains two or more of the purified proteins described above, the sheet can be obtained, for example, by producing a sheet using a protein solution or fibers containing two or more of the purified proteins. The sheet can also be produced by producing a sheet using two or more protein solutions or fibers. Furthermore, the sheet can be produced by producing a sheet using two or more protein fibers that differ in at least one characteristic selected from the group consisting of diameter, length, density, and crimping method.

[0057] The sheet according to the present embodiment can be obtained, for example, by a method of using a dope solution containing the purified protein described above and molding it into a sheet shape such as a film, or by a method of using the dope solution to spin protein fibers and then molding the protein fibers into a sheet shape such as a woven fabric, knitted fabric, nonwoven fabric, web, or mesh.

[0058] The dope solution can be prepared, for example, by adding the purified protein described above to a solvent or solution such as water, a lower alcohol, dimethyl sulfoxide (DMSO), N,N-dimethylformamide (DMF), hydrochloric acid, sodium hydroxide, formic acid, or hexafluoroisopronol (HFIP) together with an inorganic salt as a dissolution promoter, and dissolving the protein.

[0059] A sheet-shaped film can be produced, for example, as follows. First, the dope liquid is applied to a substrate surface to a predetermined thickness (for example, to a thickness of 1 to 1000 μm after drying and / or desolvation). The substrate may be a resin substrate, a glass substrate, a metal substrate, or the like. The substrate is preferably a resin substrate from the viewpoint of easy peeling of the film after cast molding. Examples of the resin substrate include a polyethylene terephthalate (PET) film, a fluororesin film such as polytetrafluoroethylene, a polypropylene (PP) film, or a release film having a silicone compound immobilized on the surface of such a film. Drying and / or desolvation is carried out by at least one method selected from vacuum drying, hot air drying, air drying, and immersion in a liquid. The unstretched film after drying and / or desolvation can also be uniaxially or biaxially stretched in water.

[0060] The protein fiber may be a long fiber or a short fiber. The protein fiber may be a filament yarn (multifilament, monofilament, etc.), a spun yarn, a twisted yarn, a false-twisted yarn, a textured yarn, a blended yarn, a mixed yarn, etc.

[0061] The protein fibers can be produced by a known spinning method. That is, the dope solution prepared by the above-mentioned method can be spun by a known spinning method such as wet spinning, dry spinning, dry-wet spinning, or melt spinning to obtain the protein fibers.

[0062] Fig. 1 is an explanatory diagram schematically illustrating an example of a spinning apparatus for producing protein fibers. The spinning apparatus 10 shown in Fig. 1 is an example of a spinning apparatus for dry / wet spinning, and includes an extrusion apparatus 1, an undrawn yarn production apparatus 2, a wet heat drawing apparatus 3, and a drying apparatus 4.

[0063] A spinning method using a spinning apparatus 10 will be described. First, a dope solution 6 stored in a storage tank 7 is extruded from a spinneret 9 by a gear pump 8. Next, the extruded dope solution 6 passes through an air gap 19 and is supplied into a coagulation liquid 11 in a coagulation liquid tank 20, where the solvent is removed and the polypeptide is coagulated to form a fibrous coagulate. Next, the fibrous coagulate is supplied into warm water 12 in a drawing bath 21 and drawn. The drawing ratio is determined by the speed ratio between a supply nip roller 13 and a take-up nip roller 14. Thereafter, the drawn fibrous coagulate is supplied to a drying device 4 and dried in a yarn path 22, where protein fibers 36 are obtained as a wound yarn 5. Reference numerals 18a to 18g denote yarn guides.

[0064] The coagulation liquid 11 may be any solvent or solution that can be desolvated, and examples thereof include lower alcohols having 1 to 5 carbon atoms, such as methanol, ethanol, and 2-propanol, as well as acetone, sodium hydroxide, sodium carbonate, and sodium bicarbonate. The coagulation liquid 11 may contain water as appropriate. The temperature of the coagulation liquid 11 is preferably 0 to 30°C. When a syringe pump having a nozzle with a diameter of 0.1 to 0.6 mm is used as the spinneret 9, the extrusion rate is preferably 0.2 to 6.0 ml / hour per hole, and more preferably 1.4 to 4.0 ml / hour per hole. The distance over which the coagulated protein passes through the coagulation liquid 11 (effectively the distance from the yarn guide 18a to the yarn guide 18b) may be any length that allows efficient desolvation, and is, for example, 200 to 500 mm. The take-up speed of the undrawn yarn may be, for example, 1 to 20 m / min, and preferably 1 to 3 m / min. The residence time in the coagulation liquid 11 may be, for example, 0.01 to 3 minutes, and preferably 0.05 to 0.15 minutes. Furthermore, stretching (pre-stretching) may be performed in the coagulation liquid 11. The coagulation liquid tank 20 may be provided in multiple stages, and stretching may be performed in each stage or in a specific stage as necessary.

[0065] The stretching performed when obtaining protein fibers includes, for example, the above-described pre-stretching performed in the coagulation liquid bath 20 and wet heat stretching performed in the stretching bath 21, as well as dry heat stretching.

[0066] The wet heat drawing can be carried out in warm water, in a solution of warm water with an organic solvent added, or under steam heating. The temperature may be, for example, 50 to 90° C., and preferably 75 to 85° C. In the wet heat drawing, the undrawn yarn (or pre-drawn yarn) can be drawn, for example, 1 to 10 times, and preferably 2 to 8 times.

[0067] Hot drawing can be carried out using an electric tubular furnace, a hot plate, etc. The temperature may be, for example, 140°C to 270°C, and preferably 160°C to 230°C. In hot drawing, the undrawn yarn (or pre-drawn yarn) can be drawn, for example, 0.5 to 8 times, and preferably 1 to 4 times.

[0068] The wet heat stretching and the dry heat stretching may be carried out independently, or may be carried out in multiple stages or in combination. That is, the wet heat stretching and the dry heat stretching may be appropriately combined, for example, by carrying out wet heat stretching in the first stage and dry heat stretching in the second stage, or by carrying out wet heat stretching in the first stage, wet heat stretching in the second stage, and dry heat stretching in the third stage.

[0069] The lower limit of the final draw ratio relative to the undrawn yarn (or pre-drawn yarn) is preferably any one of more than 1, 2 or more, 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, or 9 or more, and the upper limit is preferably 40 or less, 30 or less, 20 or less, 15 or less, 14 or less, 13 or less, 12 or less, 11 or less, or 10 or less. Drawn yarns can exhibit higher strength, and therefore can exhibit the effects of the present invention more significantly.

[0070] The protein fibers may be dried, which allows the sheets or uncooked meat-like food compositions of the present invention to have a long shelf life, particularly when stored or transported at room temperature.

[0071] The protein fibers may have a stress of 0.5 gf / d or more. The stress is preferably 0.8 gf / d or more, and more preferably 1 gf / d or more. The stress of the protein fibers may be 1 to 10 gf / d, preferably 1 to 5 gf / d, and more preferably 1 to 3 gf / d. When the stress is within this range, the effect of further improving the yield in the production of the meat-like food composition is obtained. The strength is a value determined by a standard tensile test of multifilament yarn.

[0072] The protein fibers may have a diameter of less than 50 μm. The diameter of the protein fibers is, for example, preferably less than 45 μm or less than 40 μm, more preferably 35 μm or less, 32 μm or less, or 30 μm or less, and even more preferably 15 μm or less or 10 μm or less. The use of protein fibers with a smaller diameter improves the authenticity of the meat-like food composition, resulting in a mouthfeel and texture closer to the real thing. The diameter of the protein fibers may be, for example, 5 μm or more, 10 μm or more, 15 μm or more, 18 μm or more, 20 μm or more, 22 μm or more, 25 μm or more, 30 μm or more, 32 μm or more, 35 μm or more, 40 μm or more, or 45 μm or more. The diameter of the protein fibers may be, for example, 5 to 50 μm, 10 to 50 μm, 15 to 50 μm, 5 to 45 μm, 5 to 40 μm, 5 to 35 μm, 5 to 32 μm, 5 to 50 μm, 10 to 45 μm, 10 to 40 μm, 10 to 35 μm, 10 to 32 μm, or 10 to 30 μm.

[0073] The production of woven fabrics, knitted fabrics, nonwoven fabrics, webs, meshes, etc. using protein fibers can be carried out according to conventional methods.

[0074] Woven and knitted fabrics can be obtained by weaving or knitting raw yarns containing protein fibers. Known methods can be used for weaving and knitting. Examples of knitting machines that can be used include circular knitting machines, warp knitting machines, and flat knitting machines, with circular knitting machines being preferred from the standpoint of productivity. Flat knitting machines include molding knitting machines and seamless knitting machines, but seamless knitting machines are more preferred, particularly because they allow the production of knitted fabrics in the form of final products. Examples of looms that can be used include shuttle looms and shuttleless looms such as gripper looms, rapier looms, water jet looms, and air jet looms.

[0075] Nonwoven fabrics can be produced by known production methods using, for example, fibers containing protein fibers. Specifically, for example, a web (including a single-layer web and a laminated web) can be formed from fibers containing protein fibers by a dry method, a wet method, an air-laid method, or the like, and then the fibers of the web can be bonded by a chemical bonding method (a dipping method, a spray method, or the like) or a needle punch method, to obtain a nonwoven fabric. 3D printed nonwoven fabrics can also be used.

[0076] The sheet according to this embodiment may be a shredded sheet. If necessary, the sheet may be cut into small pieces.

[0077] The sheet according to this embodiment has a sheet density of 10 to 100 g / m 2 The sheet density may be 10 to 30 g / m 2 and may be 10 to 50 g / m 2 and may be 10 to 70 g / m 2 and may be 30 g to 70 g / m 2 and may be 30 g to 100 g / m 2 It may be 50 to 100 g / m 2 It is preferable that the thickness is 70 to 100 g / m 2 It is more preferable that the sheet density is a value obtained by dividing the weight of the sheet by the area of ​​the sheet.

[0078] The sheet according to this embodiment may have a thickness of 0.1 to 2 mm. The thickness is preferably 0.1 to 1 mm, and more preferably 0.1 to 0.5 mm. When the thickness is within this range, the realism is enhanced, and a mouthfeel and texture closer to the real thing can be obtained.

[0079] When the sheet according to the present embodiment is a woven fabric, knitted fabric, nonwoven fabric, web, mesh, or the like, using protein fibers, the diameter of the protein fibers contained in the sheet may be less than 50 μm. The diameter of the protein fibers is, for example, preferably less than 45 μm or less than 40 μm, more preferably 35 μm or less, 32 μm or less, or 30 μm or less, and even more preferably 15 μm or less or 10 μm or less. The use of protein fibers with a smaller diameter results in a more realistic appearance and a mouthfeel and texture closer to the real thing. Protein fibers with even smaller diameters can be obtained, for example, by electrospinning. By using electrospinning, the diameter of the protein fibers can be adjusted to a range of approximately 10 nm to 10 μm. The average diameter of the protein fibers is preferably in the range of 10 nm to 1 μm, and more preferably in the range of 10 nm to 500 nm. Note that the diameter of the protein fibers here refers to the major axis of the cross section of the protein fiber.

[0080] The present invention may also include chemical or mechanical treatments to incorporate the sheets of the present invention into meat-like food compositions, allowing the sheets of the present invention to maintain the structural integrity of the meat-like food composition, both before and after cooking, and without size limitations, providing meat-like food compositions with desirable mechanical properties.

[0081] The properties of the protein fibers in the sheets of the present invention can be further modified by protease treatment. Proteolysis and hydrolysis of protein fibers can weaken or alter the overall mechanical properties of the protein fibers. Incorporating protease-treated protein fibers into meat-like food compositions can further modify the texture and mouthfeel of the final product. Depending on the amino acid sequence of the protein fibers and the cleavage sites of various proteases, various proteases can be used to treat the protein fibers. Examples of suitable proteases include, but are not limited to, papain, bromelain, keratinase, ficin, trypsin, α-chymotrypsin, rennin, pepsin, collagenase, elastase, alcalase, neutrase, protease XIV, proteinase K, and fungal proteases.

[0082] The content of the sheet in the meat-like food composition according to this embodiment may be, for example, 0.1% by weight or more, 0.2% by weight or more, 0.3% by weight or more, 0.4% by weight or more, 0.5% by weight or more, 1.0% by weight or more, or 2.0% by weight or more, based on the total amount of the meat-like food composition. The content of the sheet in the meat-like food composition according to this embodiment may be, for example, 5% by weight or less, 4% by weight or less, 3% by weight or less, 2% by weight or less, 1% by weight or less, 0.5% by weight or less, 0.4% by weight or less, or 0.3% by weight or less, based on the total amount of the meat-like food composition.

[0083] The protein content of the meat-like food composition according to this embodiment may be, for example, 0.5% by weight or more, 1% by weight or more, 2% by weight or more, 3% by weight or more, 4% by weight or more, 5% by weight or more, 6% by weight or more, 7% by weight or more, 8% by weight or more, 9% by weight or more, 10% by weight or more, 20% by weight or more, 30% by weight or more, 40% by weight or more, or 50% by weight or more, based on the total weight of the meat-like food composition. The protein content of the meat-like food composition according to this embodiment may be, for example, 90% by weight or less, 80% by weight or less, 70% by weight or less, 60% by weight or less, 50% by weight or less, 40% by weight or less, 30% by weight or less, 20% by weight or less, or 10% by weight or less, based on the total weight of the meat-like food composition.

[0084] The protein component in the meat-like food composition according to this embodiment may be an animal protein (a protein derived from an animal source) or a non-animal protein (e.g., a protein derived from a non-animal source, such as a plant protein or a microbial protein). The meat-like food composition according to this embodiment may not contain an animal protein as a protein component. Animal proteins include proteins obtained from animals and proteins recombinantly expressed using genes encoding animal proteins.

[0085] The meat-like food composition of this embodiment may contain at least one selected from a binder, a cross-linking agent (protein cross-linking agent), and a gelling agent. Examples of binders include starch obtained from potatoes, tapioca, etc. Cross-linking agents include food-grade chemical cross-linkers, transglutaminase, tyrosinase, laccase, peroxidase, and sulfhydryl oxidase. Examples of gelling agents include hydrocolloids such as gellan gum, xanthan gum, guar gum, gum arabic, tragacanth gum, locust bean gum, konjac glucomannan, sodium alginate, propylene glycol alginate, carrageenan, agar, dextran, pectin, microcrystalline cellulose, carboxymethylcellulose, and methylcellulose, as well as proteins such as fibrinogen / thrombin, blood proteins, plasma proteins, egg albumin, whey protein, and gelatin.

[0086] The meat-like food composition of this embodiment may further contain other food-acceptable ingredients. These ingredients include, for example, fats and oils, seasonings, herbs, flavorings, proteins other than those contained in the meat and meat substitute composition ingredients (including concentrates and isolates), emulsifiers, functional ingredients, and nutritional supplements. Examples of fats and oils include corn oil, olive oil, soybean oil, peanut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, hemp oil, palm oil, walnut oil, algae lipids, coconut oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, and oils and lipids derived from microorganisms (including bacteria, algae, archaea, and genetically modified bacteria, algae, and archaea). Saturated fats are preferably used to mimic the melting temperature profile and texture of animal fats. Alternatives to fat include the use of edible oleogel or microencapsulated lipids. The use of edible oleogel or microencapsulated lipids can minimize the migration of fat droplets. The sheets and lipids of the present invention can be used to recreate adipose tissue. For example, an adipose tissue replica can be prepared by impregnating the sheets of the present invention with lipids. The sheets of the present invention can create a layered structure of adipose tissue replicas prepared from lipids and protein fiber sheets, thereby creating a marbled effect in the meat-like food composition of the present invention. The meat-like food composition prepared from lipids and the sheets of the present invention can be made chewy and juicy. Examples of seasonings and herbs include rosemary, oregano, cumin, sage, pepper, thyme, basil, and curry powder. Examples of flavorings include spice extracts, spice oils, natural liquid smoke, yeast extract, mushroom extract, onion extract, garlic extract, and herb extract. Examples of emulsifiers include lecithin, mono- and diglycerides, monoglyceride derivatives, and fatty acid derivatives.Examples of functional ingredients include antioxidants such as polyphenols, immunostimulants such as lactoferrin, and substances for improving the intestinal environment such as probiotics, prebiotics, and biogenics. Examples of nutritional supplements include dietary fiber (inulin, methylcellulose, psyllium, wheat dextrin, etc.), vitamins and minerals (folic acid, vitamin B12 and other vitamin B, vitamin C, vitamin D, vitamin A, calcium, zinc, iron, iodine, etc.).

[0087] The meat-like food composition according to this embodiment may be free of animal-derived components, for example, so that it can be provided as a vegan diet. Animal-derived components are components obtained from animals (e.g., the other components described above), including animal proteins. The meat-like food composition according to this embodiment may contain cultured cells. For example, it may contain a cell composition and extracellular matrix that form three-dimensional tissue in vivo. The cell composition and extracellular matrix may be bioprinted.

[0088] The meat-like food composition of this embodiment can be produced, for example, by mixing at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients, a sheet containing purified protein, and optionally at least one selected from a binder, a crosslinking agent (protein crosslinking agent), and a gelling agent, and optionally other ingredients acceptable for foods (mixture obtaining step 1), followed by a step of molding the resulting mixture into a desired shape (molding step). This production method may further include, for example, a step of sterilizing the meat-like food composition, a step of packaging the meat-like food composition, etc.

[0089] The meat-like food composition of this embodiment can also be produced by, for example, a step of mixing at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients, optionally at least one selected from a binder, a crosslinking agent (protein crosslinking agent), and a gelling agent, and optionally other ingredients acceptable for foods, to obtain a mixture (mixture obtaining step 2), a step of attaching the mixture obtained in the previous step to at least one surface of a sheet containing purified protein (attaching step), and a step of molding the sheet with the attached mixture into a desired shape (molding step). This production method may further include, for example, a step of sterilizing the meat-like food composition, a step of packaging the meat-like food composition, etc.

[0090] The meat-like food composition according to this embodiment may be formed by alternating layers containing at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients and sheets. The meat-like food composition can be produced, for example, by obtaining a sheet on which an ingredient-containing layer is formed in the above-mentioned adhesion step, and then spirally winding the sheet to obtain a roll in which the ingredient-containing layers and sheets are alternately arranged. Alternatively, the meat-like food composition can be produced by repeating the above-mentioned adhesion step to alternately stack the ingredient-containing layers and sheets to obtain a laminate. By alternately arranging the ingredient-containing layers and sheets, the "authenticity" of the food composition, which is a combination of texture (appearance) and sensory characteristics (texture, juiciness, tenderness), can be further improved.

[0091] The meat-like food composition of this embodiment may be subjected to a treatment to strengthen mechanical entanglement. That is, the meat-like food composition of this embodiment may be produced by, after the above-mentioned attachment step, subjecting a sheet having a layer containing ingredients formed on at least one surface of the sheet to a three-dimensional forming process such as stitching, weaving, braiding, knitting, or needle punching. The three-dimensional forming process may be performed alone or in combination of two or more. Furthermore, the meat-like food composition may be produced by, for example, obtaining a sheet having a layer containing ingredients formed on it in the above-mentioned attachment step, and then subjecting the sheet to a process that allows the sheet and ingredients to be interwoven. Needle punching is preferred in this process. Needle punching can, for example, attach fiber layers to each other using fibers carried by hooked needles (the hooks are designed to remain at the location where the fibers were carried when the needles leave the preform). Needle punching can be performed using, for example, an injector, a meat tenderizer, a meat hammer, or a meat mallet. For example, the meat-like food composition can be prepared by obtaining a sheet having a layer containing ingredients formed thereon in the above-mentioned adhesion step, and then applying felt needles to the fiber sheet to drive the fibers into the ingredient layer so that the sheet and the ingredient are interwoven. The needle-punching process may be performed at high or low speed as needed. Multiple needle-punching processes may be performed. Needle-punching may be performed from multiple directions. The needle-punching process may be performed uniformly on the ingredient-containing layer sheet, or may be performed unevenly depending on the required texture for the application. By interweaving the ingredient-containing layer and the sheet, the "authenticity" of the product, which is a combination of texture (appearance) and sensory characteristics (texture, juiciness, tenderness), is further improved.

[0092] The meat-like food composition may be produced by a lamination process in which ingredient-containing layers and sheets are alternately laminated, followed by a process of processing the laminate using a three-dimensional forming technique such as stitching, weaving, braiding, knitting, or needle punching. The ingredient-containing layers and sheets may be alternately arranged to connect multiple layers, providing greater structural integrity. The meat-like food composition may be produced by a process in which an ingredient-containing layer is formed on a sheet in the above-mentioned attachment process, followed by a three-dimensional forming technique such as stitching, weaving, braiding, knitting, or needle punching, followed by a lamination process in which ingredient-containing layers and sheets are alternately laminated, followed by a three-dimensional forming technique such as stitching, weaving, braiding, knitting, or needle punching. By interweaving the ingredient-containing layers and sheets, the "authenticity" of the product, which combines texture (appearance) and sensory characteristics (feel, juiciness, tenderness), is further improved.

[0093] The present invention also relates to artificial meat products comprising the meat-like food composition of the present invention or processed products thereof. Processed meat-like food compositions include, for example, heat-treated meat-like food compositions, seasoned meat-like food compositions, and meat-like food compositions cooked with other ingredients (including cooked and semi-cooked products) as needed. The meat-like food compositions can be processed into various foods for either human or animal consumption. For example, the final product can be a meat-like food composition for human consumption or processed products thereof that imitates a ground meat product, steak product, sirloin tip product, kebab product, bacon product, jerky product, sausage product, shredded product, diced meat product, or nugget product. Any of the above products can be placed on a tray and covered with a package, vacuum-packed, placed in a retort can or bag, or frozen.

[0094] The present invention also relates to a method for producing an artificial meat dish, comprising the step of cooking the meat-like food composition or a processed product thereof, or an artificial meat product according to the present invention. Cooking the meat-like food composition or a processed product thereof, or the artificial meat product can be carried out according to a conventional method.

[0095] The present invention described above can also be understood as a method for improving the authenticity of a meat-like food composition, comprising attaching at least one ingredient selected from the group consisting of meat raw materials and meat substitute composition ingredients to at least one surface of a sheet containing purified protein. Preferably, the method further comprises adding a protein cross-linking agent (e.g., transglutaminase) to the at least one ingredient selected from the group consisting of meat raw materials and meat substitute composition ingredients. This further improves the authenticity. The above-mentioned embodiments can be applied to specific aspects of the method without limitation. [Example]

[0096] The present invention will be described in more detail below based on test examples, although the present invention is not limited to the following test examples.

[0097] Test Example 1: Production and Evaluation of Meat-Like Food Composition <Material> (Meat ingredients and meat substitute composition ingredients) Three types of meat ingredients or meat substitute composition ingredients were prepared: a beef / pork ground meat mixture (6 / 4), Beyond Beef (registered trademark) (manufactured by Beyond Meat), and OmniPork (manufactured by OmniFoods). Beyond Beef® Ingredient List: Water, Pea Protein, Expeller-Pressed Canola Oil, Refined Coconut Oil, Rice Protein, Natural Flavor, Cocoa Butter, Mung Bean Protein, Methylcellulose, Potato Starch, Apple Extract, Pomegranate Extract, Salt, Potassium Chloride, Vinegar, Lemon Juice Concentrate, Sunflower Lecithin, Beet Juice Extract (for Color). OmniPork Ingredient List: Water, Protein Blend (Soy Protein Concentrate, Soy Protein Isolate, Shiitake Fermented Pea & Rice Protein), Thickeners (Methylcellulose, Maltodextrin), Yeast Extract, Palm Oil, Potato Starch, Cane Sugar, Salt, Natural Flavors (Canola and Sunflower Oil), Barley Malt Extract, Color (Beet Red), Dextrose, Anti-Caking Agent (Silicon Dioxide).

[0098] (Protein crosslinker) As protein cross-linking agents, Ajinomoto Co., Inc.'s Activa (registered trademark) microbial transglutaminase KS-CT (1% transglutaminase, 99% maltitol) and TG-K (1% transglutaminase, 75% calcium caseinate, 24% dextrin) were prepared.

[0099] (Sheet containing purified protein) The sheet containing the purified protein was prepared by the following procedure.

[0100] The nucleotide and amino acid sequences of Nephila clavipes fibroin (GenBank accession number: P46804.1, GI: 1174415) were obtained from the GenBank web database, and then amino acid substitutions, insertions, and deletions were performed to improve productivity. Furthermore, a tag sequence and a hinge sequence were added to the N-terminus to design artificial fibroins with the amino acid sequences shown in SEQ ID NO: 2 and SEQ ID NO: 1 (hereinafter referred to as "PRT966" and "PRT799," respectively). The hydrophobicity index of PRT966 is 0.47, and that of PRT799 is -0.80.

[0101] Nucleic acids encoding the designed artificial fibroins having the amino acid sequences shown in SEQ ID NO: 2 and SEQ ID NO: 1 were synthesized. An NdeI site was added to the 5' end of the nucleic acid, and an EcoRI site was added downstream of the stop codon. These two types of nucleic acids were cloned into a cloning vector (pUC118), and then the nucleic acids were excised by restriction enzyme treatment with NdeI and EcoRI, and then recombined with the protein expression vector pET-22b(+) to obtain an expression vector.

[0102] The resulting expression vector was used to transform E. coli BLR (DE3). The transformed E. coli was cultured in 2 mL of LB medium containing ampicillin for 15 hours. The culture was then transferred to 100 mL of seed culture medium (Table 3) containing ampicillin at OD . 600 The culture temperature was kept at 30°C, and the OD 600 The flask culture was continued until the fertilization rate reached 5 (about 15 hours), and a seed culture solution was obtained.

[0103] [Table 3]

[0104] The seed culture solution was added to a jar fermenter containing 500 ml of production medium (Table 4) and the OD 600 The culture temperature was maintained at 37°C and the pH was controlled to be constant at 6.9. The dissolved oxygen concentration in the culture medium was maintained at 20% of the dissolved oxygen saturation concentration.

[0105] [Table 4]

[0106] Immediately after the glucose in the production medium was completely consumed, a feed solution (455 g glucose / 1 L, 120 g yeast extract / 1 L) was added at a rate of 1 mL / min. The culture temperature was maintained at 37°C, and the pH was controlled to a constant 6.7. The dissolved oxygen concentration in the culture medium was maintained at 20% of the dissolved oxygen saturation concentration, and the culture was continued for 20 hours.

[0107] Subsequently, a 1M aqueous solution of isopropyl-β-thiogalactopyranoside (IPTG) was added to the culture medium to a final concentration of 1 mM to induce expression of the desired artificial fibroin. 20 hours after the addition of IPTG, the culture medium was centrifuged and the cells were collected. SDS-PAGE was performed using cells prepared from the culture medium before and after the addition of IPTG, and the appearance of a band of the size corresponding to the desired artificial fibroin, which was dependent on the addition of IPTG, confirmed the expression of the desired artificial fibroin.

[0108] The cells were harvested 24 hours after the addition of IPTG and washed with 20 mM Tris-HCl buffer (pH 7.4). The washed cells were suspended in 20 mM Tris-HCl buffer (pH 7.4) containing approximately 1 mM phenylmethylsulfonyl fluoride (PMSF) and disrupted three times using a high-pressure homogenizer (Panda Plus 2000, GEA Niro Saovi). The disrupted cells were centrifuged in a centrifuge (Model 7000, Kubota) at 11,000 g for 10 minutes at room temperature to obtain a precipitate. The resulting precipitate was washed with 20 mM Tris-HCl buffer (pH 7.4) or 3% SDS buffer (pH 3.0) until highly purified. The washed precipitate was diluted to a concentration of 100 mg / mL with 8 M guanidine buffer (8 M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM The protein was suspended in Tris-HCl (pH 7.0) and stirred at 60°C for 30 minutes to dissolve. After dissolution, the protein was dialyzed against water using a dialysis tube (Cellulose tube 36 / 32 manufactured by Sanko Junyaku Co., Ltd.). The white aggregated protein obtained after dialysis was recovered by centrifugation and the water was removed using a freeze-dryer to obtain a freeze-dried powder of artificial fibroin.

[0109] A spinning solution (dope solution) was prepared using the freeze-dried artificial fibroin powder obtained above. 99% formic acid was added to the freeze-dried artificial fibroin PRT966 powder so that the concentration of the freeze-dried artificial fibroin PRT966 powder was 28% by mass. After dissolving for 14 hours on a rotator, dust and bubbles were removed. This was designated as spinning solution 1 (dope solution 1).

[0110] Similarly, the freeze-dried powder of artificial fibroin PRT799 obtained above was added to formic acid (manufactured by Asahi Chemical Co., Ltd.) to a concentration of 26% by mass, and then dissolved at 70° C. for 1 hour. After that, dust and bubbles were removed, and spinning solution 2 (dope solution 2) was obtained.

[0111] Using the spinning apparatus shown in Figure 1, dope solution 1 or dope solution 2 was extruded into the coagulation liquid (methanol) using a nitrogen air pump. The wet spinning conditions were as shown below. As a result, each artificial fibroin fiber was obtained. -Wet spinning conditions- Dope temperature: 25℃ Coagulation liquid (methanol) 1 Temperature: 5℃ Coagulation liquid (methanol) 2 Temperature: 25℃ Water bath stretching tank temperature: 25℃ Hot roller (HR) temperature: 60℃

[0112] Using a small warping machine (SW550, manufactured by CCI TECH INC.), several hundred 3.6 m long fibers were obtained from a bobbin (derived from artificial fibroin). The obtained long fibers were cut using a tabletop high-power fiber cutter (NP-300, manufactured by INTEC CO. LTD.) to obtain artificial fibroin short fibers with a length of 50 mm.

[0113] The resulting artificial fibroin short fibers were dispersed in sodium bicarbonate water for 10 minutes, filtered, and then washed several times with ion-exchanged water.

[0114] Thereafter, carding was carried out using a known carding machine to obtain a sheet (hereinafter also referred to as "fiber sheet") containing purified protein PRT966 (artificial fibroin PRT966) as a web consisting of entangled artificial fibroin PRT966 short fibers.

[0115] Example 1 3.5 parts by weight of transglutaminase TG-K was added to 96.4 parts by weight of a beef / pork ground meat mixture (6 / 4), and the mixture was kneaded for several minutes to uniformly disperse the enzyme (transglutaminase). This mixture was spread to a uniform thickness on one side of a fiber sheet (equivalent to 0.1 part by weight), resulting in a sheet with a meat layer formed on the fiber sheet. The resulting sheet was then spirally wound to obtain a roll with alternating meat layers and fiber sheets. The resulting roll was vacuum-sealed and stored at 4°C for 18 hours to complete the enzyme reaction. The roll was then sliced ​​to obtain discs approximately 2 cm thick, which were formed into the shape of steak meat to obtain a meat-like food composition (artificial steak meat composition). The resulting artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0116] <Comparative Example 1> To 96.4 parts by weight of ground beef / pork (6 / 4), 3.5 parts by weight of transglutaminase TG-K was added and kneaded for several minutes to uniformly disperse the enzyme (transglutaminase). This was formed into a cylindrical shape, vacuum sealed, and stored at 4°C for 18 hours to complete the enzyme reaction. Next, the cylinder was sliced ​​to obtain a disk approximately 2 cm thick with a shape similar to that of Example 1, and a steak-shaped meat-like food composition (artificial steak meat composition) was obtained. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0117] <Example 2> An artificial steak meat composition was obtained in the same manner as in Example 1, except that 96.3 parts by mass of Beyond Beef (registered trademark) was used instead of 96.4 parts by weight of beef / pork ground meat (6 / 4), transglutaminase KS-CT was used instead of transglutaminase TG-K, and 0.2 parts by mass of a fiber sheet was used. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0118] <Comparative Example 2> An artificial steak meat composition was obtained in the same manner as in Comparative Example 1, except that 96.3 parts by mass of Beyond Beef (registered trademark) was used instead of 96.4 parts by weight of the beef / pork ground meat mixture (6 / 4), and that transglutaminase KS-CT was used instead of transglutaminase TG-K. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0119] Example 3 An artificial steak meat (artificial pork chop) composition was obtained in the same manner as in Example 1, except that 96.0 parts by mass of OmniPork was used instead of 96.4 parts by mass of ground beef / pork (6 / 4), transglutaminase KS-CT was used instead of transglutaminase TG-K, and 0.5 parts by mass of a fiber sheet was used. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0120] <Comparative Example 3> An artificial steak meat (artificial pork chop) composition was obtained in the same manner as in Comparative Example 1, except that 96.0 parts by mass of OmniPork was used instead of 96.4 parts by weight of the beef / pork ground meat (6 / 4), and transglutaminase KS-CT was used instead of transglutaminase TG-K. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0121] <Sensory evaluation> Sensory evaluation was carried out on the artificial steak meat compositions (cooked) of Examples 1 to 3 and Comparative Examples 1 to 3, with evaluation items including overall appearance, overall texture, juiciness, tenderness, and authenticity (steak / pork chop likeness). The sensory evaluation was carried out by a panel of 3 to 4 members, and each evaluation item was rated on a 9-point scale from 1 to 9 (1 being the worst and 9 being the best).

[0122] "Overall appearance" was judged as "better" the closer the appearance was to real meat when visually observed. "Overall texture" was judged as "better" the closer the texture was to real meat when chewed. "Juicy" was judged as "better" the more juice felt when chewed. "Tenderness" was judged as "better" the softer it was when chewed. "Realism" was judged as "better" the closer the texture (appearance) and sensory characteristics (texture, juiciness, tenderness) were combined to be closer to real meat (steak / pork chop). The results (average scores of 3-4 panelists) are shown in Tables 5-7.

[0123] [Table 5]

[0124] [Table 6]

[0125] [Table 7]

[0126] The artificial steak meat compositions of Examples 1 to 3 were prepared by adding a fiber sheet to the artificial steak meat compositions of Comparative Examples 1 to 3. As shown in Tables 4 to 6, the addition of the fiber sheet tended to improve the overall appearance, overall texture, juiciness, and tenderness, and the overall realism (steak-likeness / pork chop-likeness) of these properties was improved.

[0127] Figure 2 is a photograph showing the artificial steak meat compositions of Example 1 and Comparative Example 1. In Figure 2, (1a), (1d), and (1f) are the artificial steak meat compositions of Example 1, and (1b), (1c), and (1e) are the artificial steak meat compositions of Comparative Example 1. Also in Figure 2, (1a) and (1b) are the artificial steak meat compositions before cooking, and (1c), (1d), (1e), and (1f) are the artificial steak meat compositions after cooking.

[0128] Figure 3 is a photograph showing the artificial steak meat compositions of Example 2 and Comparative Example 2. In Figure 3, (2a), (2d), and (2e) are the artificial steak meat compositions of Example 2, and (2b), (2c), and (2f) are the artificial steak meat compositions of Comparative Example 2. Also in Figure 3, (2a) and (2b) are the artificial steak meat compositions before cooking, and (2c), (2d), (2e), and (2f) are the artificial steak meat compositions after cooking.

[0129] Test Example 2: Production and evaluation of meat-like food compositions Example 4 Two parts by mass of transglutaminase KS-CT were added to 96.9 parts by weight of a beef / pork ground meat mixture (6 / 4), and the mixture was kneaded for several minutes to uniformly disperse the enzyme (transglutaminase). This mixture was spread to a uniform thickness on one side of a fiber sheet (equivalent to 1.1 parts by weight), resulting in a sheet with a meat layer formed on the fiber sheet. Next, a felt needle was applied to the fiber sheet to interweave the sheet and the ground meat, and the fibers were punched into the ground meat layer. Up to six layers of fiber sheet and ground meat were stacked. Then, needle punching was performed again from the back side using a felt needle, vacuum sealed, and stored at 4°C for 18 hours to complete the enzyme reaction, yielding an artificial steak meat composition. The resulting artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0130] <Comparative Example 4> An artificial steak meat composition was obtained in the same manner as in Example 4, except that needle punching with a felt needle was not performed. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70° C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation.

[0131] <Example 5> To tailor the texture of the artificial steak meat composition, proteinaceous fibrous sheets were prepared from two purified proteins that differ in hydrophobicity and mechanical properties.

[0132] As with the fiber sheets used in Examples 1 to 4 above, carding was carried out using a known carding machine to obtain a mixed sheet (hereinafter also referred to as a "mixed fiber sheet") containing purified proteins PRT966 (artificial fibroin PRT966) and PRT799 (artificial fibroin PRT799) as a web of entangled short fibers in which artificial fibroin PRT966 short fibers and artificial fibroin PRT799 short fibers were mixed in a ratio of 7:3.

[0133] An artificial steak meat composition was obtained in the same manner as in Example 4, except that a mixed fiber sheet was used instead of the fiber sheet. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation. Figure 4 is a photograph showing the appearance and cross section of the artificial steak after cooking.

[0134] Example 6 An artificial steak meat composition was obtained in the same manner as in Example 5, except that 97.5 parts by mass of Beyond Beef (registered trademark) was used instead of 96.9 parts by mass of beef / pork ground meat (6 / 4), transglutaminase KS-CT was used, 0.5 parts by mass of a mixed fiber sheet was used, and up to four layers of fiber sheets and Beyond Beef (registered trademark) were stacked. Up to six layers of fiber sheets and ground meat were stacked. The obtained artificial steak meat composition was cooked at medium temperature until the internal temperature reached 70°C. After cooking, the artificial steak meat composition was immediately subjected to sensory evaluation. Figure 5 is a photograph showing the appearance and cross-section of the artificial steak after cooking.

[0135] <Sensory evaluation> Sensory evaluation was carried out on the artificial steak meat compositions (cooked) of Example 4, Example 5, and Comparative Example 4 for the evaluation items of overall appearance, overall texture, juiciness, tenderness, and realness (steak-likeness). The sensory evaluation was carried out by four panelists, and each evaluation item was rated on a 9-point scale from 1 to 9 (1 being the worst and 9 being the best). Sensory evaluation was carried out on the artificial steak meat composition (cooked) of Example 6 for the evaluation items of overall appearance, overall texture, juiciness, tenderness, and realness (steak-likeness). The sensory evaluation was carried out by two panelists, and each evaluation item was rated on a 9-point scale from 1 to 9 (1 being the worst and 9 being the best).

[0136] "Overall appearance" was judged as "better" the closer the appearance was to real meat when visually observed. "Overall texture" was judged as "better" the closer the texture was to real meat when chewed. "Juicy" was judged as "better" the more juice felt when chewed. "Tenderness" was judged as "better" the softer it was when chewed. "Realism" was judged as "better" the closer the texture (appearance) and sensory characteristics (texture, juiciness, tenderness) were combined to resemble real meat (steak meat). The results (average scores of four or two panels) are shown in Table 8.

[0137] The needlepunched artificial steak meat composition was perceived as having a firmer texture and was rated as more similar to beef steak compared to the non-needlepunched sample.

[0138] An artificial steak meat sample prepared by needle punching using two proteins with different hydrophobicity and mechanical properties was rated as more tender and similar to beef steak compared to a sample prepared using only one highly hydrophobic protein. [Table 8]

[0139] Test Example 3: Production and evaluation of meat-like food compositions (Fiber sheet containing purified protein) A fibrous sheet containing purified protein was prepared by the following procedure.

[0140] Using a small warper (SW550, manufactured by CCI TECH INC.), several hundred 3.6 m long fibers were obtained from a bobbin (derived from artificial fibroin PRT966. The PRT966 fiber diameter was 10.7 ± 0.3 μm). The obtained long fibers were cut to a fixed length (see Table 9) using a bench-top high-power fiber cutter (NP-300, manufactured by INTEC CO. LTD.) at a speed of 20 m / min to obtain approximately 20 g of staple fibers. The staple fibers were crimped using water at 90°C and air-dried overnight.

[0141] The resulting fiber sheet 2 was then carded using a known carding machine to obtain a web of entangled short fibers of the artificial fibroin PRT966, containing the purified protein PRT966 (hereinafter also referred to as "fiber sheet 2"). The density of the resulting fiber sheet 2 was measured, and the fiber sheet 2 was cut to a predetermined size for preparing meat samples.

[0142] As another sheet containing purified protein, a fiber sheet was obtained in the same manner as above using commercially available gelatin fibers (manufactured by GelaCell). The fiber diameter of the gelatin fibers was 4 μm.

[0143] <Examples 7 to 21> 160 g of OmniPork® meat base was spread into a thin rectangular layer measuring 20 cm x 30 cm using a pin roller, and the fiber sheet 2 of the same size was placed on top of it. Using a roller cutter, the meat layer combined with the card web was cut into 10 cm x 10 cm squares, and up to six layers were stacked to obtain a "preform." A felting needle was then applied to the fiber sheet 2 to punch the fibers into the meat layer so that the sheet and OmniPork® were interwoven. The needle-punching process was repeated from the opposite side of the preform, and then needle-punched again from the back side using a felting needle to increase the degree of fiber interlacing within the preform. The needle-punched preform was wrapped in plastic wrap and stored in a refrigerator at 4°C until cooking, obtaining an artificial steak meat composition.

[0144] The resulting artificial steak meat composition was cooked on a cooking sheet for 7 minutes on each side using an electric grill set at 200° C. Samples of the cooked artificial steak meat composition were prepared for Slice Shear Force (SSF) testing (20° C., 60% humidity) and Texture Profile Analysis (TPA) (20° C., 60% humidity) as described below. SSF sample size: L4cm x W2cm x H~1.5cm TPA sample size: 2cm x 2cm x ~1.5cm

[0145] SSF was measured in quadruplicate using a Universal Testing Instrument EZ Test (Shimadzu Corporation). Cooked samples were cut into 4 cm x 2 cm x ~1.5 cm (original height) and sliced ​​using a 3 mm thick, 45° angle shear blade attached to a 500 N load cell. The cutting time was across the entire thickness of the sample until the sample was cut in half. The crosshead speed was 200 mm / min. SSF is the maximum force required to generate the "slicing shear force" in Newtons (hereafter also referred to as "hardness") and to cut the sample. This is a texture parameter that quantifies the consumer's "first bite" experience.

[0146] TPA of whole muscle meat samples prepared with proteinaceous fiber was performed eight times for each treatment using a Universal Testing Instrument EZ Test (Shimadzu Corporation). Cooked samples were cut into 2 cm x 2 cm x ~1.5 cm (original height) and compressed to 50% of their original height using a compression plate (size φ11.5 cm) with a 500 N load cell. The crosshead speed was 200 mm / min, and the time interval between two compressions was 2 seconds. TPA parameters were springiness (the ratio of the time required to reach maximum force in the second compression to the first compression), cohesiveness (the work done during the second compression to the first compression), and chewability (hardness × springiness × cohesiveness).

[0147] [Table 9]

[0148] Figure 6 is a graph showing the results of measuring the hardness (Hardness) of the cooked artificial steak meat compositions of Examples 7 to 13 using TPA. As a control, the results of measuring the hardness (Hardness) of a cooked artificial steak meat composition made only from Omnipork are also shown. The values ​​shown in Figure 7 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the hardness (Hardness) of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) using TPA are also shown.

[0149] Figure 7 is a graph showing the results of measuring the hardness (Hardness) of the cooked artificial steak meat compositions of Examples 7 to 13 using SSF. As a control, the results of measuring the hardness using SSF of a cooked artificial steak meat composition made only from Omnipork are also shown. The values ​​shown in Figure 7 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the hardness using SSF of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) are also shown.

[0150] As shown in Figures 6 and 7, samples containing needle-punched fiber sheets (Examples 7-13) had significantly higher firmness measured by TPA and SSF compared to the OmniPork-only control (Figures 6 and 7). Furthermore, increasing the density of the fiber sheet when the staple fiber length was fixed at 30 mm (Examples 11-13) resulted in a gradual increase in both TPA and SSF firmness. Increasing the density of the fiber sheet when the staple fiber length was fixed at 52 mm (Examples 7-10) also resulted in a gradual increase in SSF firmness. Notably, the SSF firmness of many samples containing needle-punched fiber sheets was in the same range as the SSF firmness of animal-based pork (Reference Examples 1 and 2). This means that the "first bite experience" of restructured OmniPork is similar to that of its animal counterpart.

[0151] Figure 8 is a graph showing the results of measuring the cohesiveness (cohesiveness) of the cooked artificial steak meat compositions of Examples 7 to 13 using TPA. As a control, the results of measuring the cohesiveness (cohesiveness) of a cooked artificial steak meat composition made only from Omnipork are also shown. The values ​​shown in Figure 8 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the cohesiveness (cohesiveness) of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) using TPA are also shown.

[0152] Figure 9 is a graph showing the results of measuring the springiness (springiness) of the cooked artificial steak meat compositions of Examples 7 to 13 using TPA. As a control, the results of measuring the springiness of a cooked artificial steak meat composition made only from Omnipork using TPA are also shown. The values ​​shown in Figure 9 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the springiness of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) using TPA are also shown.

[0153] As shown in Figures 8 and 9, the samples containing needle-punched fiber sheets (Examples 7-13) had significantly higher cohesion and resilience compared to the OmniPork-only control. Increasing the density of the fiber sheet increased cohesion. Increasing the staple fiber length from 30 mm to 52 mm increased the cohesion at a specific density (29 g / m 2 ) has been shown to increase elasticity (Examples 10 and 13). Cohesiveness is not significantly affected by staple fiber length, so different mouthfeels can be created with different staple fiber lengths while maintaining the cohesiveness of the final product. Notably, many of the treated samples had cohesiveness and elasticity in the same range as animal-based pork (Reference Examples 1 and 2).

[0154] Figure 10 is a graph showing the results of measuring the hardness (Hardness) of the cooked artificial steak meat compositions of Examples 14 to 20, as measured by SSF. As a control, the results of measuring the hardness, as measured by SSF, of a cooked artificial steak meat composition made only from Omnipork are also shown. The values ​​shown in Figure 10 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the hardness, as measured by SSF, of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) are also shown.

[0155] As shown in Figure 10, the firmness measured by SSF can be increased by shortening the staple fiber length of the fiber sheet, allowing the texture of meat products containing fiber sheets to be fine-tuned depending on the product type.

[0156] Figure 11 is a graph showing the results of measuring the springiness (Springiness) of the cooked artificial steak meat compositions of Examples 14 to 20 using an SSF. As a control, the results of measuring the springiness of a cooked artificial steak meat composition made only from Omnipork using an SSF are also shown. The values ​​shown in Figure 11 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the springiness of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2) using an SSF are also shown.

[0157] As shown in Figure 11, for a given fiber sheet density, increasing the length of the staple fibers can increase the elasticity value, similar to the results shown in Figure 9.

[0158] Figure 12 is a graph showing the results of measuring the cohesiveness (Cohesiveness) of the cooked artificial steak meat compositions of Examples 14 to 20, as measured by SSF. As a control, the results of measuring the cohesiveness (Cohesiveness) of a cooked artificial steak meat composition made only from Omnipork, as measured by SSF, are also shown. The values ​​shown in Figure 12 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the cohesiveness (Cohesiveness) of a cooked pork thigh steak (Reference Example 1) and a cooked pork tenderloin steak (Reference Example 2), as measured by SSF, are also shown.

[0159] As shown in Figure 12, it is further demonstrated that cohesion is not significantly affected by staple fiber length, but can be manipulated by varying the density of the fiber sheet.

[0160] Figure 13 is a graph showing the results of measuring the hardness (Hardness) of the cooked artificial steak meat compositions of Examples 14 and 21, as measured by TPA. As a control, the results of measuring the hardness of a cooked artificial steak meat composition made only from Omnipork, as measured by TPA, are also shown. The values ​​shown in Figure 13 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the hardness of a cooked pork sirloin steak (Reference Example 3) and a cooked ground pork steak (Reference Example 4), as measured by TPA, are also shown.

[0161] Figure 14 is a graph showing the results of measuring the hardness (Hardness) of the cooked artificial steak meat compositions of Examples 14 and 21, as measured by SSF. As a control, the results of measuring the hardness, as measured by SSF, of a cooked artificial steak meat composition made only from Omnipork are also shown. The values ​​shown in Figure 14 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the hardness, as measured by SSF, of a cooked pork sirloin steak (Reference Example 3) and a cooked pork mince steak (Reference Example 4) are also shown.

[0162] Figure 15 is a graph showing the results of measuring the cohesiveness (Cohesiveness) of the cooked artificial steak meat compositions of Examples 14 and 21, as measured by SSF. As a control, the results of measuring the cohesiveness (Cohesiveness) of a cooked artificial steak meat composition made only from Omnipork, as measured by SSF, are also shown. The values ​​shown in Figure 15 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the cohesiveness (Cohesiveness) of a cooked pork sirloin steak (Reference Example 3) and a cooked ground pork steak (Reference Example 4), as measured by SSF, are also shown.

[0163] Figure 16 is a graph showing the results of measuring the springiness (Springiness) of the cooked artificial steak meat compositions of Examples 14 and 21 using an SSF. As a control, the results of measuring the springiness of a cooked artificial steak meat composition made only from Omnipork using an SSF are also shown. The values ​​shown in Figure 16 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the springiness of a cooked pork sirloin steak (Reference Example 3) and a cooked ground pork steak (Reference Example 4) using an SSF are also shown.

[0164] Figure 17 is a graph showing the results of measuring the chewiness (Chewiness) of the cooked artificial steak meat compositions of Examples 14 and 21 using an SSF. As a control, the results of measuring the chewiness of a cooked artificial steak meat composition made only from Omnipork using an SSF are also shown. The values ​​shown in Figure 17 are relative values, with the measurement result of the control taken as 100 (%). For reference, the results of measuring the chewiness of a cooked pork sirloin steak (Reference Example 3) and a cooked ground pork steak (Reference Example 4) using an SSF are also shown.

[0165] As shown in Figures 13-17, the gelatin fiber sheet (Example 21) was able to increase the cohesion of the treated samples. Because gelatin is an excellent binder even in powder form, it was concluded that the fiber web was not the contributing factor to the increased cohesion, but rather the inherent binding strength of the gelatin protein. This binding effect was also observed in the firmness measured by SSF. With larger fiber diameters and staple fiber lengths, gelatin fiber sheets may prove effective in further improving the textural properties of the treated samples. Furthermore, because the structural integrity and mechanical properties of gelatin fiber sheets decrease upon contact with moisture, gelatin fiber sheets with higher mechanical properties (e.g., higher sheet density) may improve the textural properties of samples treated with gelatin fiber sheets. [Explanation of symbols]

[0166] 1...extrusion device, 2...undrawn yarn manufacturing device, 3...moist heat drawing device, 4...drying device, 6...dope liquid, 10...spinning device, 20...coagulation liquid tank, 21...drawing bath, 36...protein fiber

Claims

[Claim 1] A meat-like food composition comprising at least one ingredient selected from the group consisting of meat ingredients and meat substitute composition ingredients, and a sheet containing purified protein.

Images