Dough, three-dimensionally shaped dough and its manufacturing method

Abstract

The present invention aims to provide a fabric that can easily and inexpensively form a desired 3D shape. This fabric has a surface comprising: a section A that includes an artificial protein fiber containing protein and shrinks at a prescribed shrinkage rate upon contact with water; and a section B that has a lower shrinkage rate upon contact with water than section A.

Description

[Technical field]

[0001] The present invention relates to a dough, a three-dimensionally shaped dough, and a method for producing the same. [Background technology]

[0002] Generally, fabrics used for clothing and bedding are given various colors and patterns by dyeing, printing, etc. Some clothing items have desired three-dimensional shapes formed by smocking or the like in addition to flat patterns formed by dyeing, printing, etc.

[0003] For example, Patent Document 1 discloses a woven fabric having a three-dimensional shape, the woven fabric having a plurality of warp threads and a plurality of weft threads intersecting with the plurality of warp threads, some of the plurality of warp threads being shrinkable warp threads that shrink in the length direction more than the other warp threads when a specific treatment is applied, the shrinkable warp threads having a first skip portion that skips over a first predetermined number of adjacent weft threads at at least one point in the length direction, the plurality of first skip portions being arranged in a predetermined first pattern, some of the plurality of weft threads being shrinkable weft threads that shrink in the length direction more than the other weft threads when the specific treatment is applied, the shrinkable weft threads having a first skip portion that skips over a first predetermined number of adjacent weft threads at at least one point in the length direction, the plurality of first skip portions being arranged in a predetermined first pattern, The disclosed woven fabric has a second skip portion that skips a second predetermined number of adjacent warp threads at a location, and a plurality of the second skip portions are arranged in a predetermined second pattern, and when the specific treatment is applied to the shrinkable warp thread, it shrinks in the length direction more than other warp threads to form a constant first shrinkage portion, and when the specific treatment is applied to the shrinkable weft thread, it shrinks in the length direction more than other weft threads to form a constant second shrinkage portion, and a first fold line portion formed along the weft direction by arranging a plurality of the first shrinkage portions in succession, and a second fold line portion formed along the warp direction by arranging a plurality of the second shrinkage portions in succession is formed. [Prior art documents] [Patent documents]

[0004] [Patent Document 1] JP 2015-218426 A Summary of the Invention [Problem to be solved by the invention]

[0005] The woven fabric disclosed in Patent Document 1 is woven by combining shrinkable warp yarns and shrinkable weft yarns with normal yarns to form a desired pattern, and then shrinking the shrinkable warp yarns and shrinkable weft yarns to form a desired three-dimensional shape. The method described in Patent Document 1 has problems such as the inability to change the pattern after weaving and the need for advanced design and advanced weaving technology to form the pattern.

[0006] An object of the present invention is to provide a fabric that can be easily and inexpensively formed into a desired three-dimensional shape.Another object of the present invention is to provide a three-dimensionally shaped fabric that can be easily and inexpensively formed into a desired three-dimensional shape.A further object of the present invention is to provide a method for easily and inexpensively producing the three-dimensionally shaped fabric. [Means for solving the problem]

[0007] The present invention relates to, for example, the following inventions. [1] Artificial protein fibers containing proteins, A fabric having a surface including a portion A which shrinks at a predetermined shrinkage rate on contact with water, and a portion B which shrinks at a smaller shrinkage rate on contact with water than the portion A. [2] The fabric described in [1], wherein the part B does not shrink upon contact with water. [3] The fabric described in [1] or [2], in which the above-mentioned part A exists in plurality. [4] A substrate containing the above-mentioned artificial protein fiber and a water-repellent or waterproof coating that partially covers a surface of the substrate, The fabric according to any one of [1] to [3], wherein the portion B is constituted by a portion covered by the coating film, and the portion A is constituted by a portion not covered. [5] The fabric according to any one of [1] to [3], wherein the part A contains an artificial protein fiber that shrinks at a predetermined shrinkage rate upon contact with water, while the part B contains a fiber having a smaller shrinkage rate than the artificial protein fiber contained in the part A. [6] The fabric described in [5], wherein the part B contains artificial protein fibers having a smaller shrinkage rate than the artificial protein fibers contained in the part A. [7] The fabric according to any one of [1] to [6], wherein at least the artificial protein fiber contained in the portion A has a dry shrinkage rate defined by the following formula I of more than 7%. Dry shrinkage rate = {1 - (length of dried artificial protein fiber / length of artificial protein fiber after spinning and before contact with water)} x 100 (%) ... (Formula I) [8] The fabric according to any one of [1] to [7], wherein the protein is a modified fibroin. [9] The fabric has a surface consisting of a part C containing fibers that shrink at a predetermined shrinkage rate in response to an external stimulus, and a part D containing fibers whose shrinkage rate due to the external stimulus is smaller than that of the fibers contained in part C, and the shrinkage rate due to the external stimulus of part D is smaller than that of part C.

[10] The fabric described in [9] comprises a woven fabric woven with yarns extending in one direction and yarns extending in a direction intersecting the one direction, the yarns extending in the one direction being part C including fibers that shrink at a predetermined shrinkage rate in response to an external stimulus, while the yarns extending in a direction intersecting the one direction being part D including fibers whose shrinkage rate in response to the external stimulus is smaller than that of the fibers included in part C.

[11] Artificial protein fibers containing proteins, The three-dimensionally shaped fabric comprises a part E which shrinks at a predetermined shrinkage rate when contacted with water, and a part F which shrinks at a shrinkage rate smaller than that of the part E when contacted with water or which does not shrink even when contacted with water, and has a surface on which a three-dimensional shape is formed due to the difference in shrinkage rate between the part E and the part F.

[12] The three-dimensional shaped fabric described in

[11] , wherein the portion F does not shrink even when contacted with water.

[13] The three-dimensionally shaped fabric is composed of a part G which shrinks at a predetermined shrinkage rate in response to an external stimulus, and a part H which shrinks at a shrinkage rate smaller than that of the part G due to the external stimulus or which does not shrink even due to the external stimulus, and has a surface on which a three-dimensional shape is formed due to the difference in shrinkage rate between the part G and the part H.

[14] A method for producing a three-dimensionally shaped fabric, comprising a step of subjecting the fabric according to any one of [1] to [8] to a shrinkage treatment, which includes contacting the fabric with water.

[15] A method for producing a three-dimensionally shaped fabric, comprising a step of subjecting the fabric described in [9] or

[10] to a shrinkage process that includes applying an external stimulus to the fabric. Effect of the Invention

[0008] According to the present invention, it is possible to provide fabric that can be easily and inexpensively formed into a desired three-dimensional shape, to provide fabric with a three-dimensional shape in which a desired three-dimensional shape is easily and inexpensively formed, and to provide a manufacturing method by which the fabric with a three-dimensional shape can be easily and inexpensively produced. [Brief description of the drawings]

[0009] [Figure 1] FIG. 2 is a schematic cross-sectional view of a fabric according to one embodiment. [Diagram 2] FIG. 2 is a schematic cross-sectional view of a fabric according to one embodiment. [Diagram 3] FIG. 2 is a schematic diagram of a fabric according to an embodiment. [Figure 4] 1 is a photograph of the fabric produced in Test Example 5. [Diagram 5]1 is a photograph of the three-dimensionally shaped dough produced in Test Example 6. [Figure 6] FIG. 2 is a schematic diagram showing an example of a domain sequence of a modified fibroin. [Figure 7] FIG. 1 shows the distribution of z / w (%) values ​​of naturally derived fibroin. [Figure 8] FIG. 1 shows the distribution of x / y (%) values ​​of naturally derived fibroin. [Figure 9] FIG. 2 is a schematic diagram showing an example of a domain sequence of a modified fibroin. [Figure 10] FIG. 2 is a schematic diagram showing an example of a domain sequence of a modified fibroin. [Figure 11] 1 is a photograph of the three-dimensionally shaped dough produced in Test Example 7. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0010] Hereinafter, the embodiments of the present invention will be described in detail with reference to the drawings. For convenience, substantially the same elements are given the same reference numerals, and the description thereof may be omitted. Note that the present invention is not limited to the following embodiments.

[0011] 〔material〕 One aspect of the fabric according to this embodiment includes artificial protein fibers containing proteins, and has a surface consisting of part A that shrinks at a predetermined shrinkage rate upon contact with water, and part B that shrinks at a smaller shrinkage rate than part A upon contact with water.

[0012] The fabric according to this embodiment utilizes the property of artificial protein fibers to shrink when in contact with water, and can form a three-dimensional shape by contacting with water, an easy and inexpensive method, whereby part A shrinks more than part B. For example, part B within an area formed by connecting multiple shrunken parts A (whose area it occupies is reduced) with straight lines shrinks less than part A and occupies a relatively large area, forming a convex portion on the front or back surface of the fabric (see, for example, FIG. 5).

[0013] The artificial protein fibers contained in the fabric according to this embodiment may be, for example, fibers (a) before contact with water after spinning (having no history of contact with water after spinning) and fibers (b) that have shrunk upon contact with water after spinning and have zero or limited shrinkage upon further contact with water, either alone or in appropriate combination. When using artificial protein fibers (b), two or more types of fibers having different shrinkage rates upon further contact with water may be used. The combination of the artificial protein fibers (a) and (b) is not particularly limited as long as part A and part B can be formed as described below.

[0014] After spinning, the artificial protein fiber (A) before contact with water is irreversibly shrunk by contact with water. In addition, the fiber (B) that has shrunk by contact with water and is suppressed from shrinking by further contact with water also shrinks irreversibly, although not to the same extent as the fiber (A). These irreversible shrinkages have a large shrinkage rate, making it easier to form a three-dimensional shape. Furthermore, between fibers that have shrunk by contact with water after spinning and have different shrinkage rates by further contact with water, the irreversible shrinkage rates by contact with water are different, so the three-dimensional shapes formed by shrinkage are also different from each other. Therefore, the fabric according to this embodiment is preferably configured to be capable of forming a three-dimensional shape by utilizing this irreversible shrinkage. In addition, the irreversible shrinkage of the artificial protein fiber is thought to occur, for example, for the following reasons. That is, one reason is thought to be due to the secondary structure or tertiary structure of the artificial protein fiber, and another reason is thought to occur, for example, in an artificial protein fiber having residual stress due to stretching or the like in the manufacturing process, when the residual stress is relaxed. The shrinkage rate of such irreversible shrinkage of the artificial protein fiber can be appropriately adjusted, for example, by the contact time of the artificial protein fiber with water, the temperature of the water, or the tensile force applied to the artificial protein fiber during contact with water or during subsequent drying, etc. In this way, artificial protein fibers with different shrinkage rates due to contact with water can be obtained.

[0015] Part B can be formed, for example, by subjecting at least a portion of a substrate (e.g., a woven or knitted fabric, nonwoven fabric, etc.) containing artificial protein fibers to a water-repellent or waterproofing treatment. The area to be water-repellent or waterproofed can be designed as desired, so the area of ​​part B can also be set as desired (the area of ​​part A is also set at the same time), thereby making it possible to obtain a fabric capable of forming any three-dimensional shape. In addition, since a normal woven or knitted fabric can be used as the substrate, the pattern of the three-dimensional shape can also be easily changed. When part B is formed by subjecting it to a water-repellent or waterproofing treatment, the above-mentioned fiber (A) before contact with water is generally used as the artificial protein fiber contained in part B and part A that has not been water-repellent or waterproofed.

[0016] Furthermore, the portion B can be formed by including fibers having a smaller shrinkage rate in contact with water than the artificial protein fibers contained in the portion A. This can be realized, for example, by forming the portion B by including the artificial protein fibers (B) described above, while forming the portion A by including the artificial protein fibers (A). It can also be realized by forming both the portion B and the portion A by including the artificial protein fibers (B), and selecting a fiber contained in the portion B that has a smaller shrinkage rate in contact with water than the fiber contained in the portion A. In addition, it can also be realized, for example, by forming the portion B by including the artificial protein fibers (B), while forming the portion A using the fibers (A) and the fibers (B) having a larger shrinkage rate in contact with water than the fibers (B) contained in the portion B, or by forming the portion A by including two or more different types of fibers (B) that have a larger shrinkage rate in contact with water than the fibers (B) contained in the portion B. When the portion A is formed by including two or more types of fibers (B) that have different shrinkage rates in contact with water, it becomes possible to more easily form a more complicated shape or a more varied shape on the fabric.

[0017] When the fabric according to this embodiment is a woven fabric, the above-mentioned artificial protein fiber (A) may be used for either the weft or warp threads, and at least a part of the fabric consisting of either the weft or warp threads may be part A, while the other of the weft or warp threads may be made of the above-mentioned artificial protein fiber (B) or a fiber other than the artificial protein fiber that does not shrink upon contact with water, and at least a part of the fabric consisting of either the weft or warp threads may be part B. In this way, by bringing the fabric into contact with water, part A can be shrunk in the extension direction of the threads consisting of the artificial protein fiber (A) among the weft and warp threads. In addition, it is possible to impart a three-dimensional shape corresponding to this to the fabric.

[0018] The fabric according to the present embodiment may have a plurality of parts A and parts B. The shape of part A is not particularly limited, and may be any shape such as a circle, an ellipse, a regular polygon (e.g., an equilateral triangle, a regular square, a regular pentagon, a regular hexagon, etc.), a polygon (e.g., a triangle, a square, a pentagon, a hexagon), etc., or may be a strip shape extending in one direction or in multiple directions such as the width direction or length direction of the fabric. When there are a plurality of parts A and parts B, the shapes of each part may be the same or different. By designing the arrangement of a plurality of parts A and parts B and the shapes of each part, it is possible to control the resulting three-dimensional shape. By controlling the resulting three-dimensional shape, it is possible to form a three-dimensional pattern on the fabric, squeeze the fabric, or impart a desired shape (such as an uneven shape) to a part or the entire fabric. In addition, for example, when making a garment using a fabric to which an uneven shape has been imparted, an uneven shape that fits along the shape of the body can be imparted to the parts of the garment that correspond to the positions of the shoulders, elbows, knees, waist, and other waists when worn.

[0019] In addition, in another aspect of the fabric according to this embodiment, the fabric has a surface consisting of a portion C containing fibers that shrink at a predetermined shrinkage rate in response to an external stimulus, and a portion D containing fibers whose shrinkage rate in response to the external stimulus is smaller than that of the fibers contained in portion C, and the shrinkage rate in response to the external stimulus of portion D is smaller than that of portion C.

[0020] In this embodiment, the property of the fibers contained in the fabric to shrink in response to various external stimuli is utilized, and a three-dimensional shape can be formed by reacting to the external stimuli in a simple and inexpensive manner, causing part C to shrink more than part D.

[0021] In the fabric according to this embodiment, for example, a fiber (c) that has not shrunk before receiving an external stimulus and a fiber (d) that has shrunk in response to an external stimulus and has zero or reduced shrinkage due to a further external stimulus are used alone or in appropriate combination. In addition, when using such a fiber (d), two or more types of fibers with different shrinkage rates due to a further external stimulus may be used. The combination of the fibers (c) and (d) is not particularly limited as long as the part C and the part D can be formed as described below. The external stimulus referred to here is not limited in any way as long as it can irreversibly shrink the fiber (c), and examples of such external stimulus include contact with water, heating, irradiation with light, contact with various chemical substances consisting of liquids, gases, and solids, etc. In addition, examples of such fibers that shrink irreversibly due to an external stimulus include artificial protein fibers, natural fibers such as cotton, and regenerated fibers such as rayon that shrink when contacted with water, as well as synthetic fibers such as artificial protein fibers and acrylic fibers that shrink when heated.

[0022] When the fabric according to this embodiment is a woven fabric, the above-mentioned fiber (C) may be used for either the weft or warp threads to define at least a part of the fabric consisting of either the weft or warp thread as part C, while the above-mentioned fiber (D) may be used for the other of the weft or warp threads to define at least a part of the fabric consisting of either the weft or warp thread as part D. In this way, by applying an external stimulus to the fabric, part C can be contracted in the direction in which the weft and warp threads consisting of fiber (C) extend. In addition, it is possible to impart a three-dimensional shape to the fabric accordingly.

[0023] In the fabric according to this embodiment, the shrinkage rate of the fiber that has shrunk in response to an external stimulus is increased, making it easier to form a three-dimensional shape. In addition, between fibers that have shrunk due to an external stimulus and have different shrinkage rates due to a further external stimulus, the shrinkage rates due to the external stimulus are different from each other, so that the three-dimensional shapes formed by the shrinkage are also different from each other. Therefore, it is preferable that the fabric according to this embodiment is configured to be able to form a three-dimensional shape by utilizing this irreversible shrinkage. The shrinkage rate of such fibers that shrink due to an external stimulus can be appropriately adjusted, for example, depending on the strength of the external stimulus, the reaction time, etc.

[0024] In the fabric according to this embodiment, the portion D can be formed by including a fiber having a smaller shrinkage rate in response to an external stimulus than the fiber contained in the portion C. This can be realized, for example, by forming the portion D by including the above-mentioned fiber (d) and forming the portion C by including the above-mentioned fiber (c). It can also be realized by forming both the portion D and the portion C by including the fiber (d) and selecting a fiber contained in the portion D that has a smaller shrinkage rate in response to an external stimulus than the fiber contained in the portion C. In addition, it can also be realized, for example, by forming the portion D by including the above-mentioned fiber (d) and forming the portion C by using the fiber (c) and the fiber (d) that has a larger shrinkage rate in contact with water than the fiber (d) contained in the portion D, or by forming the portion C by including two or more different types of fibers (d) that have a larger shrinkage rate in response to an external stimulus than the fiber (d) contained in the portion D. It should be noted that when the portion C is formed by including two or more types of fibers (d) that have different shrinkage rates in response to an external stimulus, it becomes possible to more easily form a more complicated shape or a more varied shape on the fabric.

[0025] In the fabric according to this embodiment, the number and shape of the parts C and D are the same as the number and shape of the parts A and C provided in the fabric according to this embodiment. The effects obtained by selecting the number and shape are similar to those achieved in the fabric according to this embodiment.

[0026] (Artificial protein fiber) Artificial protein fibers are fibers obtained by spinning raw materials containing proteins. Artificial protein fibers can be obtained, for example, by dissolving raw materials containing proteins in a solvent capable of dissolving proteins to prepare a dope solution, and spinning the solution by a known spinning method such as wet spinning, dry spinning, dry-wet spinning, or melt spinning. Examples of solvents capable of dissolving proteins include dimethyl sulfoxide (DMSO), N,N-dimethylformamide (DMF), formic acid, and hexafluoroisopropanol (HFIP). Inorganic salts may be added to the solvent as a dissolution promoter.

[0027] There is no particular limitation on the protein used as the raw material for the artificial protein fiber, and any protein can be used. Examples of the protein include natural proteins and recombinant proteins (artificial proteins). Examples of the recombinant protein include any protein that can be produced on an industrial scale, such as proteins that can be used for industrial purposes, proteins that can be used for medical purposes, and structural proteins. Specific examples of proteins that can be used for industrial or medical purposes include enzymes, regulatory proteins, receptors, peptide hormones, cytokines, membrane or transport proteins, antigens used in vaccinations, vaccines, antigen-binding proteins, immunostimulating proteins, allergens, full-length antibodies, or antibody fragments or derivatives. Specific examples of structural proteins include spider silk, silkworm silk, keratin, collagen, elastin, and resilin, as well as proteins derived therefrom. The protein used is preferably modified fibroin, and more preferably modified spider silk fibroin, because it can impart a sufficient shrinkage rate to the base material containing the artificial protein fiber, thereby making it possible to sufficiently increase the difference between the shrinkage rate of part A and the shrinkage rate of part B that has been subjected to a water-repellent or waterproofing treatment. A preferred embodiment of the modified fibroin will be described later.

[0028] The artificial protein fiber may have a dry shrinkage rate of more than 7%. The dry shrinkage rate may be 15% or more, 25% or more, 32% or more, 40% or more, 48% or more, 56% or more, 64% or more, or 72% or more. The upper limit of the dry shrinkage rate is usually 80% or less. The dry shrinkage rate is defined by the following formula I. Dry shrinkage rate = {1 - (length of dried artificial protein fiber / length of artificial protein fiber after spinning and before contact with water)} x 100 (%) ... (Formula I) The "dried artificial protein fiber" referred to here is an artificial protein fiber that has a history of contact with water and has been dried after spinning.

[0029] The artificial protein fiber may have a wet shrinkage rate of 2% or more. The wet shrinkage rate may be 4% or more, 6% or more, 8% or more, 10% or more, 15% or more, 20% or more, 25% or more, or 30% or more. The upper limit of the wet shrinkage rate is usually 80% or less. The wet shrinkage rate is defined by the following formula II. Wet shrinkage rate = {1 - (length of artificial protein fiber wetted by contact with water / length of artificial protein fiber after spinning and before contact with water)} x 100 (%) ... (Formula II)

[0030] (base material) The type of the base material of the fabric according to the present embodiment is not particularly limited. Specific examples of the base material include knitted or woven fabrics and nonwoven fabrics.

[0031] The knitted fabric is a general term for knitted fabrics and woven fabrics. The knitted fabric may be any of knitted fabrics having a weft knit structure such as flat knit, circular knit, plain knit, or plaid plain knit (also simply referred to as "weft knit"), and knitted fabrics having a warp knit structure such as tricot or raschel (also simply referred to as "warp knit"). The woven fabric may be any of plain weave, twill weave, satin weave, or other known weave structures.

[0032] The knitted or woven body can be obtained by knitting or weaving raw yarn. Known methods can be used as the knitting method and weaving method. Examples of the knitting machine that can be used include a circular knitting machine, a warp knitting machine, and a flat knitting machine, and from the viewpoint of productivity, the use of a circular knitting machine is preferable. Examples of the flat knitting machine include a molded knitting machine and a seamless knitting machine, and the use of a seamless knitting machine is more preferable, especially since the knitted fabric can be produced in the form of a final product. Examples of the loom that can be used include a shuttle loom and a shuttleless loom such as a gripper loom, a rapier loom, a water jet loom, and an air jet loom.

[0033] The raw material yarn may be a single yarn, a composite yarn (e.g., blended yarn, mixed fiber yarn, covering yarn, etc.), or a combination of these. The single yarn and the composite yarn may be a spun yarn made of twisted short fibers, or a filament yarn made of twisted long fibers.

[0034] In addition to the artificial protein fiber, the raw yarn may contain other fibers as long as the effect of the present invention is not impaired. Examples of other fibers include synthetic fibers such as nylon, polyester, and polytetrafluoroethylene, regenerated fibers such as cupra, rayon, and lyocell, and natural fibers such as cotton, hemp, and silk. In addition, a raw yarn containing a fiber that contracts in response to an external stimulus can be made of another fiber that does not contain artificial protein fiber.

[0035] The nonwoven fabric can be manufactured by a known manufacturing method using fibers containing artificial protein fibers or other fibers. Specifically, for example, a web (including a single-layer web and a laminated web) can be formed from fibers containing artificial protein fibers by a dry method, a wet method, an air-laid method, etc., and then the fibers of the web can be bonded to each other by a chemical bonding method (dipping method, spray method, etc.) and a needle punch method, etc., to obtain a nonwoven fabric.

[0036] The nonwoven fabric can also be produced by, for example, adding and dissolving a protein in a solvent such as dimethyl sulfoxide (DMSO), N,N-dimethylformamide (DMF), formic acid, or hexafluoroisopropanol (HFIP) together with an inorganic salt as a dissolution promoter, if necessary, to prepare a dope solution, and then spinning the dope solution by electrospinning (electrostatic spinning). In the electrospinning method, a voltage is applied between a supply electrode (which can also be used as a spinneret) and a collection electrode (for example, a metal roll or a metal net), and the dope solution extruded from the spinneret is charged and blown to the collection electrode. At this time, the dope solution is stretched to form fibers. The applied voltage is usually 5 to 100 kV, preferably 10 to 50 kV. The distance between the electrodes is usually 1 to 25 cm, preferably 2 to 20 cm. The average fiber diameter (average fiber diameter) of the artificial protein fibers obtained by the electrospinning method is usually 1000 nm or less, and may be 100 nm to 1000 nm, 200 nm to 900 nm, or 300 nm to 800 nm. The fiber diameter of the artificial protein fibers may vary between 100 nm and 1000 nm (1 μm).

[0037] The fiber density (basis weight), void ratio, bulk density, etc. of the nonwoven fabric can be adjusted, for example, by increasing or decreasing the amount of fiber constituting the web, or, in the case of a layered web, by increasing or decreasing the number of layers.

[0038] The substrate according to the present embodiment may contain known additives as necessary, such as colorants, smoothing agents, antioxidants, UV absorbers, dyes, matting agents, and leveling agents.

[0039] Among the substrates according to the present embodiment, the nonwoven fabric in particular may have a fiber density increase rate of 20% or more. The fiber density increase rate may be 30% or more, 40% or more, 50% or more, or 100% or more. The fiber density increase rate is a value defined by the following formula III. Fiber density increase rate = {(fiber density of substrate after shrinkage processing / fiber density of substrate before shrinkage processing) - 1} x 100 (%) ... (Formula III)

[0040] (Formation of Part A and Part B) <Water-repellent or waterproof finish> The water-repellent or waterproofing treatment of the substrate can be carried out, for example, by a method (first method) of bonding a hydrophobic polymer such as a fluorine-based polymer or a silicone-based polymer to the region set as part B, or a method (second method) of forming a photocurable resin layer in the region set as part B. In addition, any of various methods used to form a water-repellent or waterproof coating on any part of the substrate can be adopted as the water-repellent or waterproofing treatment method of the substrate.

[0041] The first method may include, for example, a step of irradiating a substrate with plasma while the substrate is in contact with a hydrophobic polymer such as a fluorine-based polymer or a silicone-based polymer, or a precursor (monomer) of the hydrophobic polymer, to covalently bond the substrate to the hydrophobic polymer in a region set as part B. Even when a precursor (monomer) is used, the precursor (monomer) is polymerized by plasma irradiation to form a hydrophobic polymer, so that a substrate to which the hydrophobic polymer is bonded can be obtained.

[0042] The fluorine-based polymer is not particularly limited as long as it is a polymer containing fluorine. The fluorine-based polymer may be, for example, a polymer obtained by polymerizing an olefin containing fluorine. Examples of the fluorine-based polymer include polytetrafluoroethylene, polytrifluoroethylene, polychlorotrifluoroethylene, polyvinyl fluoride, polyvinylidene fluoride, polyperfluoroalkylvinyl ether, polyperfluoropropylene, polytetrafluoroethylene-perfluoropropylene copolymer, tetrafluoroethylene-ethylene copolymer, and polyvinyl fluoride-ethylene copolymer. The fluorine-based polymer may be a copolymer (including a random copolymer, a block copolymer, or an alternating copolymer) obtained by polymerizing two or more kinds of monomers constituting the exemplified polymers.

[0043] The silicone polymer is not particularly limited as long as it is a polymer having a polysiloxane structure in the main chain. The silicone polymer may be, for example, a homopolymer or copolymer (including random copolymer, block copolymer, or alternating copolymer) obtained by polymerizing one or more monomers having a siloxane structural unit. The silicone polymer may be a copolymer (including random copolymer, block copolymer, or alternating copolymer) obtained by polymerizing one or more monomers having a siloxane structural unit and one or more monomers not having a siloxane structural unit.

[0044] The plasma to be irradiated may be appropriately set depending on the type of the substrate and the hydrophobic polymer (or its precursor). The flow rate of the discharge gas may be, for example, in the range of 0.1 L / min to 10 L / min. The plasma density of the generated plasma may be, for example, 1×10 13 cm -3 More than 1×10 15 cm -3 It may be within the following ranges: The discharge gas may be, for example, a rare gas such as helium, neon, argon, oxygen, nitrogen, etc. Air may also be used as the discharge gas.

[0045] Plasma irradiation can be performed using a known plasma irradiation device, such as a plasma treatment device manufactured by Europlasma.

[0046] In the first method, for example, by controlling the parts to be irradiated with plasma and the parts not to be irradiated with plasma, part B may be formed in the parts to be irradiated with plasma and part A may be formed in the parts not to be irradiated with plasma. In the first method, part A and part B may also be formed by masking the parts not to be irradiated with plasma (corresponding to part A) and then irradiating the substrate with plasma.

[0047] The second method may include, for example, a step of contacting a monomer composition of a photocurable resin with a substrate and curing the monomer composition by irradiating the monomer composition with light energy such as ultraviolet light or an electron beam, thereby forming a photocurable resin layer in an area set as part B.

[0048] The monomer composition includes a photopolymerizable monomer. The photopolymerizable monomer may be, for example, a component that is polymerized and cured by irradiation with light energy such as ultraviolet light. The photopolymerizable monomer is not particularly limited, and conventionally known ones can be used alone or in combination of two or more. Examples of the photopolymerizable monomer include radical polymerizable monomers having one or more radical polymerizable groups such as (meth)acryloyl groups and vinyl groups. Specific examples of the photopolymerizable monomer include (meth)acrylate monomers having (meth)acryloyl groups, such as monofunctional (meth)acrylates such as isobornyl (meth)acrylate and benzyl (meth)acrylate, bifunctional (meth)acrylates such as hexamethylene di(meth)acrylate, and trifunctional (meth)acrylates such as trimethylisopropane tri(meth)acrylate. It is preferable to use two or more monomers having different numbers of radical polymerizable groups in combination as the photopolymerizable monomer. In this specification, the term "(meth)acryloyl" includes "methacryloyl" and "acryloyl", and the term "(meth)acrylate" includes "methacrylate" and "acrylate".

[0049] The monomer composition may contain components other than the photopolymerizable monomer, such as a photopolymerization initiator, a pigment, a dye, a colorant, a polymerization inhibitor, a radical scavenger, an antioxidant, an ultraviolet absorber, a plasticizer, a surfactant, a leveling agent, a thickener, a dispersant, an antifoaming agent, a preservative, and a solvent.

[0050] The photopolymerization initiator is a component that can be decomposed by irradiation with light energy such as ultraviolet light or an electron beam to generate active species such as radicals and initiate a polymerization reaction of a photopolymerizable monomer. The photopolymerization initiator is not particularly limited, and conventionally known photopolymerization initiators can be used alone or in combination of two or more.

[0051] The second method can be carried out, for example, by using a UV printer (e.g., VersaUV LEF2-200, manufactured by Roland DG Corporation). The ink of the UV printer contains a photopolymerizable monomer capable of forming a photocurable resin layer, and after arranging the ink in a desired pattern, the photocurable resin layer can be formed by irradiating UV light. In addition, by using a UV printer, a desired pattern (arrangement of part A and part B) can be easily and inexpensively printed on a substrate. Furthermore, a desired ink pattern that functions as a water-repellent coating can be easily and reliably formed with a sufficient thickness on the fabric while suppressing bleeding on the fabric. In addition, a desired color design can be easily realized by changing the color of the ink pattern in various ways.

[0052] <Use of artificial protein fibers with different shrinkage rates when in contact with water> As described above, the part A and the part B of the fabric according to the present embodiment can be formed by using artificial protein fibers having different shrinkage rates when contacted with water. Such a fabric having the part A and the part B can be obtained in a form in which the part A and the part B are continuously and integrally formed, for example, by changing (switching) the artificial protein fiber used during the production process. In this case, when the fabric is a woven fabric, a known method that can switch the fibers without connecting the fibers during the weaving process is advantageously adopted. Alternatively, the part A and the part B can be produced separately, and then the part A and the part B can be joined like a patchwork to obtain a fabric having the part A and the part B. In addition, the joining of the part A and the part B is generally appropriately performed by a known method depending on the form of the substrate. For example, when the substrate is a knitted or woven body, the part A and the part B are joined by sewing each other at their respective peripheral portions or by bonding with an adhesive or the like. Furthermore, when the substrate is a nonwoven fabric, the parts A and B are joined together by entangling their respective peripheral portions with each other or by bonding with an adhesive or the like.

[0053] <Use of fibers with different shrinkage rates in response to external stimuli> As described above, the parts C and D of the fabric according to this embodiment can be formed by using artificial protein fibers having different shrinkage rates due to external stimuli such as contact with water, heating, and light irradiation. Such a fabric having parts C and D can be obtained in a form in which parts C and D are continuously and integrally formed, for example, by changing (switching) the artificial protein fiber used during the production process. In this case, when the fabric is a woven fabric, a known method that can switch fibers without connecting the fibers during the weaving process is advantageously adopted. Alternatively, parts C and D can be produced separately, and then parts C and D can be joined like a patchwork to obtain a fabric having parts C and D. In addition, the joining of parts C and D is generally performed by a known method appropriately depending on the form of the substrate. For example, when the substrate is a knitted or woven body, parts C and D are joined by sewing each other at their respective peripheral portions or by bonding with an adhesive or the like. Furthermore, when the substrate is a nonwoven fabric, the portions C and D are joined together by entangling their respective peripheral portions with each other or by bonding with an adhesive or the like.

[0054] When the parts A, B and parts C, D are formed using fibers with different shrinkage rates due to contact with water or external stimuli, the parts A to D can be formed in the woven fabric as follows. For example, a thread extending in one direction of the fabric made of the woven fabric, i.e., for example, one of the warp and weft threads, may be made of a fiber that shrinks in contact with water or due to external stimuli, and the parts A and C may be formed with the one thread, while a thread extending in a direction intersecting the one direction, i.e., the other of the warp and weft threads, may be made of a fiber with a smaller shrinkage rate than the fiber constituting the one thread, and the parts B and D may be formed with the other thread. In addition, when the woven fabric is formed by, for example, triaxial weaving, one of the parts A, C and the parts B, D is formed with a thread extending in one or two of the three directions in which the thread extends, and the other of the parts A, C and the parts B, D is formed with a thread extending in the remaining one direction.

[0055] The shrinkage rate of part A and part C of the fabric according to this embodiment (shrinkage rate when contracted by contact with water or external stimuli) may be, for example, more than 7%, 10% or more, 15% or more, 20% or more, or 25% or more. The shrinkage rate of part A is a value defined by the following formula when a square area within part A is specified. Shrinkage rate (%) = {1-(average length of each side after contact with water or reaction to external stimuli / average length of each side before contact with water or reaction to external stimuli)} x 100

[0056] The shrinkage percentages of parts B and D of the fabric according to this embodiment (the shrinkage percentages when contracted due to contact with water or an external stimulus) are not particularly limited as long as they are smaller than the shrinkage percentages of parts A and C, and may be, for example, 20% or less, 15% or less, 10% or less, 7% or less, 5% or less, 3% or less, 1% or less, or 0% (no shrinkage). The shrinkage percentages of parts B and D are values ​​defined in the same way as the shrinkage percentages of parts A and C.

[0057] Fig. 1 is a schematic cross-sectional view of a fabric according to one embodiment. The fabric 10 shown in Fig. 1 comprises a substrate 1 and a water-repellent or waterproof coating 2 that partially covers the surface of the substrate 1. The surface of the fabric 10 has a portion B that is made up of the water-repellent or waterproof coating 2 and a portion A that is made up of the uncoated surface of the substrate 1. When water is brought into contact with the surface of the fabric 10, portion A shrinks at a higher shrinkage rate than portion B, forming a three-dimensional shape. Part B may be a portion that does not shrink when contacted with water.

[0058] Fig. 2 is a schematic cross-sectional view of a fabric according to another embodiment. The fabric 20 shown in Fig. 2 comprises a substrate 1 and a water-repellent or waterproof coating 2 partially covering the surfaces (both sides) of the substrate 1. Since the fabric 20 has the water-repellent or waterproof coating 2 on both sides of the substrate 1, it can be subjected to a shrinkage process, for example, by immersion in water.

[0059] Fig. 3 is a schematic diagram of a fabric according to one embodiment. Fabric 30 shown in Fig. 3 has a pattern in which circular portions A are repeatedly arranged at the vertices and center of a regular hexagon (corresponding to the fabric of Test Example 5, see Fig. 4). By subjecting fabric 30 to shrink processing, a three-dimensional fabric having an uneven shape as shown in Fig. 5 is obtained.

[0060] Although not shown, a fabric according to another embodiment has a longitudinal rectangular shape, with both end regions in the longitudinal direction being designated as part B. Furthermore, part A is formed in the longitudinal middle region so as to extend continuously across the entire width. Here, for example, part B is formed containing artificial protein fibers that have already been shrunk by contact with water after spinning. Furthermore, part A is formed containing artificial protein fibers that have not had a history of contact with water. In such a fabric, both side edges in the width direction are joined together to form a tube, and then a shrinking process is performed to form a three-dimensional fabric with a constricted portion formed in the middle of the height direction of the tube.

[0061] Although not shown, a fabric according to yet another embodiment has a ring-shaped portion A. In this fabric 50, for example, portion B is formed containing artificial protein fibers that have already been shrunk by contact with water after spinning, while portion A is formed containing artificial protein fibers that have not had a history of contact with water after spinning. By subjecting such a fabric to a shrinking process, a three-dimensionally shaped fabric is obtained in which a convex shape is formed in a circular portion B surrounded by the ring-shaped portion A. Then, by using this three-dimensionally shaped fabric as a fabric for clothing, for example, clothing is obtained in which convex shapes are formed in portions that correspond to the shoulders, elbows, knees, etc. when worn.

[0062] Although not shown, a fabric according to another embodiment is a knitted fabric in which a plain knitted portion knitted by a laying plain knit is interposed between a plurality of plain knitted portions knitted by plain knitting, in other words, a knitted fabric in which plain knitted portions and plain knitted portions are alternately provided. In this fabric, the entire back side of the plain knitted portion is part A, while the entire front side is part B. This fabric is produced, for example, by using a yarn containing artificial protein fiber that has not had a history of contact with water after spinning as the back yarn that provides the back side of the plain knitted portion, and a yarn containing artificial protein fiber that has already been shrunk by contact with water after spinning as the front yarn that provides the front side of the plain knitted portion. By subjecting such a fabric to a shrinking process, a three-dimensionally shaped fabric in which a special three-dimensional shape is formed in the plain knitted portion is obtained.

[0063] Although not shown, a fabric according to yet another embodiment is a woven fabric of a substantially elongated rectangular shape that provides the front body of pants. In the fabric, two triangular regions are provided in the longitudinal middle portion that is located at the knee when worn, with the vertices in the height direction butting against each other at the center in the width direction of the fabric and the bases being located at both side edges in the width direction. The warp threads extending in the longitudinal direction of the fabric (the longitudinal direction of the pants) included in each of the triangular regions are made of fibers that shrink when heated (e.g., acrylic fibers), while the weft threads are made of fibers that do not shrink when heated (e.g., fibers other than acrylic fibers). That is, in the fabric of this embodiment, part C is formed by some of the warp threads in the longitudinal middle portion, while part D is formed by some of the weft threads. By applying an external stimulus of heat to such fabric, shrinkage due to shrinkage of part C is formed in the longitudinal middle portion. If pants are made using this three-dimensionally shaped fabric, the parts that correspond to the sides of the knees will shrink, which can effectively prevent a feeling of tightness from occurring when the knees are bent and stretched. That is, for example, it is possible to create trousers that fit the body perfectly without performing three-dimensional cutting.

[0064] [Fabric with three-dimensional shapes] One aspect of the three-dimensionally shaped fabric according to this embodiment comprises artificial protein fibers containing proteins, and is composed of part E that shrinks at a predetermined shrinkage rate upon contact with water, and part F that shrinks at a smaller shrinkage rate than part E upon contact with water or does not shrink even upon contact with water, and has a surface on which a three-dimensional shape is formed due to the difference in shrinkage rates between part E and part F.

[0065] The three-dimensionally shaped fabric according to this embodiment is obtained, for example, by subjecting the fabric according to this embodiment described above to a shrinkage process due to contact with water. In this case, part E corresponds to part A that has shrunk due to contact with water, and part F corresponds to part B that has not shrunk even in contact with water, or part B that has shrunk due to contact with water at a smaller shrinkage rate than part A.

[0066] Another aspect of the three-dimensionally shaped fabric according to this embodiment includes fibers that shrink in response to an external stimulus, and is composed of part G that shrinks in response to the external stimulus at a predetermined shrinkage rate, and part H that shrinks in response to the external stimulus at a shrinkage rate smaller than part E or does not shrink even in response to the external stimulus, and has a surface on which a three-dimensional shape is formed due to the difference in the shrinkage rates of part G and part H.

[0067] The three-dimensionally shaped fabric according to this embodiment is obtained by, for example, subjecting the fabric according to this embodiment described above to a shrinking process due to an external stimulus. In this case, part G corresponds to part C that has shrunk due to the external stimulus, and part H corresponds to part D that has not shrunk due to the external stimulus, or part D that has shrunk due to the external stimulus at a smaller shrinkage rate than part C.

[0068] The fiber density (weight per unit area) of part E and part G is, for example, 0.04 g / cm 2 or more, 0.045 g / cm 2 or more, and 2 or more, and 2 The fiber density (weight per unit area) is a value defined as the weight per unit area.

[0069] [Method for manufacturing three-dimensional shaped fabric] One aspect of the method for producing a three-dimensionally shaped fabric according to this embodiment includes a step of performing a shrinkage process including contacting the fabric according to this embodiment with water (shrinkage process). The shrinkage process causes the artificial protein fibers to irreversibly shrink and form a three-dimensional shape. It is preferable that the fabric to be subjected to the shrinkage process contains artificial protein fibers before contact with water after spinning (i.e., artificial protein fibers that have no history of shrinkage due to contact with water).

[0070] In the shrinking process, the artificial protein fiber shrinks due to contact with water without the application of an external force. The water to be brought into contact may be in either a liquid or gaseous state. The method of bringing the artificial protein fiber into contact with water is not particularly limited, and examples thereof include a method of immersing the fabric according to this embodiment (including the artificial protein fiber) in water, a method of spraying water at room temperature or in a state of heated steam or the like onto the fabric according to this embodiment, and a method of exposing the fabric according to this embodiment to a high humidity environment filled with water vapor. Among these methods, the method of immersing the fabric according to this embodiment in water is preferred because it can effectively shorten the shrinkage time and can simplify the processing equipment. Specific examples of the method of immersing the fabric according to this embodiment in water include a method of putting the fabric according to this embodiment in a container containing water at a predetermined temperature and bringing it into contact with water.

[0071] The temperature of the water brought into contact with the fabric according to the present embodiment is not particularly limited, but is preferably, for example, below the boiling point. Such a temperature improves the handling property and the workability of the shrinking process. The upper limit of the water temperature is preferably 90°C or less, more preferably 80°C or less. The lower limit of the water temperature is preferably 10°C or more, more preferably 40°C or more, and even more preferably 70°C or more. The temperature of the water brought into contact with the fabric according to the present embodiment can be adjusted according to the fibers constituting the artificial protein fibers contained in the fabric according to the present embodiment. The temperature of the water may be constant during the contact of the water with the fabric according to the present embodiment, or may be varied to a predetermined temperature.

[0072] The time for contacting the fabric according to the present embodiment with water is not particularly limited, and may be, for example, 10 seconds or more. The time may be 30 seconds or more, 1 minute or more, 1 minute 30 seconds or more, 2 minutes or more, 10 minutes or more, 20 minutes or more, or 30 minutes or more. There is no particular limit to the upper limit of the time, but from the viewpoint of shortening the time of the manufacturing process and eliminating the risk of hydrolysis of the artificial protein fiber, it may be, for example, 120 minutes or less, 90 minutes or less, or 60 minutes or less.

[0073] The shrinking process may further include a step of drying the fabric according to this embodiment after contacting it with water (drying step).

[0074] The drying method in the drying step is not particularly limited, and may be, for example, natural drying or forced drying using drying equipment. The drying temperature is not particularly limited as long as it is lower than the temperature at which the protein is thermally damaged, but is generally in the range of 20 to 150°C, may be in the range of 40 to 120°C, or may be in the range of 60 to 100°C. Within such a temperature range, the fabric according to the present embodiment can be dried more quickly and efficiently without causing thermal damage to the protein. The drying temperature may also be room temperature or may be ambient temperature. The drying time is appropriately selected depending on the drying temperature, etc., and, for example, a time that can eliminate the influence of overdrying of the artificial protein fiber on the quality and physical properties of the fabric is adopted.

[0075] Another aspect of the method for producing a three-dimensionally shaped fabric according to the present embodiment includes a step of performing a shrinkage process including applying an external stimulus to the fabric according to the present embodiment described above (shrinkage process). The shrinkage process causes the fibers to shrink irreversibly, forming a three-dimensional shape. It is preferable that the fabric to be subjected to the shrinkage process contains fibers before being subjected to an external stimulus after spinning (i.e., fibers that have no history of shrinkage due to an external stimulus).

[0076] In the shrinking process, the fibers shrink due to an external stimulus without any external force. As described above, the external stimulus may be contact with water, heating, light irradiation, contact with various chemical substances consisting of liquids, gases, or solids, etc. Any known method may be used to apply the external stimulus to the fabric.

[0077] [Modified fibroin] The modified fibroin according to this embodiment is represented by the formula 1: [(A) n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n The modified fibroin is a protein containing a domain sequence represented by a motif. The modified 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 the C-terminal sequence are typically, but not limited to, regions that do not have repetitions of amino acid motifs characteristic of fibroin and consist of about 100 amino acid residues.

[0078] As used herein, the term "modified fibroin" refers to artificially produced fibroin (artificial fibroin). The modified fibroin may be a fibroin whose domain sequence is different from the amino acid sequence of naturally occurring fibroin, or may be a fibroin whose domain sequence is identical to the amino acid sequence of naturally occurring fibroin. The "naturally occurring fibroin" referred to in this specification is also a fibroin represented by the formula 1: [(A) n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n A protein containing a domain sequence represented by a motif.

[0079] A "modified fibroin" may be one that uses the amino acid sequence of naturally occurring fibroin as is, or one that has had its amino acid sequence modified based on the amino acid sequence of naturally occurring fibroin (for example, one that has had its amino acid sequence modified by modifying the gene sequence of a cloned naturally occurring fibroin), or one that has been artificially designed and synthesized independent of naturally occurring fibroin (for example, one having a desired amino acid sequence obtained by chemically synthesizing a nucleic acid that codes for a designed amino acid sequence).

[0080] As used herein, the term "domain sequence" refers to a crystalline region specific to fibroin (typically, the (A) n A motif) and an amorphous region (typically corresponding to REP of an amino acid sequence), and the amino acid sequence is represented by the 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 composed 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. 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 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 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) nThe motifs may be identical to each other or different from each other in amino acid sequence, and the REPs present in multiple locations may be identical to each other or different from each other in amino acid sequence.

[0081] The modified fibroin according to the present embodiment can be obtained, for example, by modifying the amino acid sequence of the cloned gene sequence of naturally occurring fibroin by, for example, substituting, deleting, inserting, and / or adding one or more amino acid residues. Substitution, deletion, insertion, and / or addition of amino acid residues can be performed by methods well known to those skilled in the art, such as site-specific mutagenesis. Specifically, it can be performed according to the methods described in literature, such as Nucleic Acid Res. 10, 6487 (1982) and Methods in Enzymology, 100, 448 (1983).

[0082] Naturally occurring fibroin has the formula 1: [(A)n motif-REP]m, or the formula 2: [(A n Motif-REP] m -(A) n A protein containing a domain sequence represented by a motif, specifically, for example, fibroin produced by insects or arachnids.

[0083] 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, and silk proteins produced by wasps such as Vespa One example is the hornet silk protein excreted by the larvae of the silkworm moth (Hornet simillima xanthoptera).

[0084] A more specific example of fibroin produced by an insect is, for example, silkworm fibroin L chain (GenBank accession numbers M76430 (nucleotide sequence) and AAA27840.1 (amino acid sequence)).

[0085] Examples of fibroin produced by spiders include spider silk proteins produced by spiders belonging to the order Araneae. More specifically, spiders belonging to the genus Araneus, such as the Japanese orb spider, the Japanese garden orb spider, the red orb spider, the green orb spider, and the like; spiders belonging to the genus Neoscona, such as the Japanese orb spider, the Japanese house orb spider, and the Japanese orb spider; spiders belonging to the genus Pronus, such as the Japanese orb spider; spiders belonging to the genus Cyrtarachne, such as the Japanese orb spider and the Japanese orb spider; spiders belonging to the genus Togegumo and the Japanese orb spider; Spiders of the genus Gasteracantha, spiders of the genus Ordgarius such as the Orbweaver Spider and the Orbweaver Spider, spiders of the genus Argiope such as the Orbweaver Spider, the Orbweaver Spider and the Orbweaver Spider, spiders of the genus Arachnura such as the Orbweaver Spider, spiders of the genus Acusilas such as the Breeding Spider, the Orbweaver Spider and the Orbweaver Spider, spiders of the genus Cytophorus such as the Orbweaver Spider, the Orbweaver Spider and the Orbweaver Spider, spider silk proteins produced by spiders belonging to the genus Poltys such as the Poltys spider, spiders belonging to the genus Cyclosa such as the Japanese bush spider, the four-headed bush spider, the round bush spider and the black bush spider, and spiders belonging to the genus Chorizopes such as the Japanese bush spider, as well as spiders belonging to the genus Tetragnatha such as the long-legged spider, the long-legged spider, the Japanese bush spider and the scaled long-legged spider, spiders belonging to the genus Orbweaver spider, Spiders of the genus Leucauge, such as the medium-sized orb-weaver spider and the small orb-weaver spider; spiders of the genus Nephila, such as the orb-weaver spider and the giant orb-weaver spider; spiders of the genus Menosira, such as the golden spider; spiders of the genus Dyschiriognatha, such as the long-legged spider; spiders of the genus Latrodectus, such as the black widow spider, the redback spider, the gray widow spider, and the three-spotted widow spider;and 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), MiSp (MiSp1 and MiSp2), AcSp, PySp, Flag, etc.

[0086] More specific examples of spider silk proteins 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 ampullate spidroin 1 [derived from Latrodectus hesperus] (GenBank accession numbers ABR68856 (amino acid sequence), EF595246 (nucleotide sequence)), 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 [Nephilengys cruentata] (GenBank accession number ABR37278.1 (amino acid sequence) and the like.

[0087] More specific examples of naturally derived fibroins include fibroins whose sequence information is registered in NCBI GenBank. For example, from among the sequence information registered in NCBI GenBank, sequences that include INV as DIVISION can be confirmed by extracting sequences with spidroin, ampullate, fibroin, "silk and polypeptide," or "silk and protein" as keywords in DEFINITION, sequences with a specific product character string in CDS, and sequences with a specific character string in TISSUE TYPE in SOURCE.

[0088] The modified fibroin in this embodiment may be modified silk fibroin (a silk protein produced by silkworms with a modified amino acid sequence) or modified spider silk fibroin (a spider silk protein produced by spiders with a modified amino acid sequence).

[0089] Specific examples of modified fibroins include a modified fibroin derived from the major ampullate gland protein of spiders (first modified fibroin), a modified fibroin having a domain sequence with a reduced content of glycine residues (second modified fibroin), (A) n A modified fibroin having a domain sequence with a reduced content of motifs (third modified fibroin), the content of glycine residues, and (A) n These include a modified fibroin with a reduced motif content (the fourth modified fibroin), a modified fibroin with a domain sequence that includes a region of high local hydrophobicity index (the fifth modified fibroin), and a modified fibroin with a domain sequence with a reduced content of glutamine residues (the sixth modified fibroin).

[0090] The first modified fibroin is represented by the formula 1: [(A) n Motif-REP] mIn the first modified fibroin, a protein having a domain sequence represented by the formula: n The number of amino acid residues in the motif is preferably an integer of 3 to 20, more preferably an integer of 4 to 20, even more preferably an integer of 8 to 20, even more preferably an integer of 10 to 20, even more preferably an integer of 4 to 16, particularly preferably an integer of 8 to 16, and most preferably an integer of 10 to 16. The first modified fibroin has a number of amino acid residues constituting REP in formula 1 of preferably 10 to 200 residues, more preferably 10 to 150 residues, even more preferably 20 to 100 residues, and even more preferably 20 to 75 residues. The first modified fibroin has a number of amino acid residues constituting REP in formula 1: [(A) n Motif-REP] m The total number of glycine residues, serine residues and alanine residues contained in the amino acid sequence represented by the formula (I) is preferably 40% or more, more preferably 60% or more, and even more preferably 70% or more, based on the total number of amino acid residues.

[0091] The first modified fibroin has the formula 1: [(A) n Motif-REP] m and the C-terminal sequence is an amino acid sequence shown in any one of SEQ ID NOs: 1 to 3 or an amino acid sequence having 90% or more homology to the amino acid sequence shown in any one of SEQ ID NOs: 1 to 3.

[0092] The amino acid sequence shown in SEQ ID NO:1 is identical to the amino acid sequence consisting of 50 amino acid residues at the C-terminus of the amino acid sequence of ADF3 (GI:1263287, NCBI), the amino acid sequence shown in SEQ ID NO:2 is identical to the amino acid sequence obtained by removing 20 residues from the C-terminus of the amino acid sequence shown in SEQ ID NO:1, and the amino acid sequence shown in SEQ ID NO:3 is identical to the amino acid sequence obtained by removing 29 residues from the C-terminus of the amino acid sequence shown in SEQ ID NO:1.

[0093] A more specific example of the first modified fibroin is (1-i) a modified fibroin comprising an amino acid sequence shown in SEQ ID NO: 4 (recombinant spider silk protein ADF3KaiLargeNRSH1), or (1-ii) an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 4. The sequence identity is preferably 95% or more.

[0094] The amino acid sequence shown in SEQ ID NO:4 is an amino acid sequence of ADF3 with an amino acid sequence (SEQ ID NO:5) consisting of an initiation codon, a His10 tag, and an HRV3C protease (Human rhinovirus 3C protease) recognition site added to the N-terminus, in which the repeat region at positions 1 to 13 is increased approximately twice and mutated so that translation terminates at amino acid residue 1154. The amino acid sequence at the C-terminus of the amino acid sequence shown in SEQ ID NO:4 is identical to the amino acid sequence shown in SEQ ID NO:3.

[0095] The modified fibroin of (1-i) may consist of the amino acid sequence shown in SEQ ID NO:4.

[0096] The second modified fibroin has an amino acid sequence in which the domain sequence has a reduced content of glycine residues compared to naturally-derived fibroin. It can be said that the second modified fibroin has an amino acid sequence in which at least one or more glycine residues in REP have been replaced with another amino acid residue compared to naturally-derived fibroin.

[0097] The second modified fibroin may have an amino acid sequence in which, compared to a naturally occurring fibroin, at least one glycine residue in at least one motif sequence selected from GGX and GPGXX (wherein G represents a glycine residue, P represents a proline residue, and X represents an amino acid residue other than glycine) in REP is replaced with another amino acid residue in at least one or more of the motif sequences.

[0098] In the second modified fibroin, the proportion of the motif sequence in which the above-mentioned glycine residue is replaced with another amino acid residue may be 10% or more relative to the total motif sequence.

[0099] The second modified fibroin has the formula 1: [(A) n Motif-REP] m (A) is located at the most C-terminal side of the domain sequence. n The total number of amino acid residues in the amino acid sequence consisting of XGX (where X represents an amino acid residue other than glycine) contained in all REPs in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence is z, and the amino acid sequence located at the most C-terminus side from the domain sequence is (A). n When the total number of amino acid residues in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence is w, the z / w ratio may be 30% or more, 40% or more, 50% or more, or 50.9% or more. (A) n The number of alanine residues relative to the total number of amino acid residues in the motif may be 83% or more, but is preferably 86% or more, more preferably 90% or more, even more preferably 95% or more, and even more preferably 100% (meaning that it is composed only of alanine residues).

[0100] The second modified fibroin is preferably one in which one glycine residue of the GGX motif is replaced with another amino acid residue to increase the content of the amino acid sequence consisting of XGX. The second modified fibroin preferably has a content of the amino acid sequence consisting of GGX in the domain sequence of 30% or less, more preferably 20% or less, even more preferably 10% or less, even more preferably 6% or less, even more preferably 4% or less, and particularly preferably 2% or less. The content of the amino acid sequence consisting of GGX in the domain sequence can be calculated by the same method as the calculation method for the content (z / w) of the amino acid sequence consisting of XGX below.

[0101] The method for calculating z / w will be described in more detail. First, the formula 1: [(A) n Motif-REP] m In a fibroin (modified fibroin or naturally-occurring fibroin) containing a domain sequence represented by the formula: n An amino acid sequence consisting of XGX is extracted from all REPs contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence. The total number of amino acid residues constituting XGX is z. For example, if 50 amino acid sequences consisting of XGX are extracted (no overlaps), z is 50×3=150. In addition, for example, in the case of an amino acid sequence consisting of XGXGX, if there is an X (a central X) contained in two XGXs, the overlaps are subtracted from the calculation (in the case of XGXGX, it is 5 amino acid residues). w is the total number of amino acid residues contained in the sequence excluding the sequence from the (A)n motif located at the most C-terminus side to the C-terminus of the domain sequence from the domain sequence. For example, in the case of the domain sequence shown in FIG. 6, w is 4+50+4+100+4+10+4+20+4+30=230 (the (A)n motif located at the most C-terminus side). n (The motif is excluded.) Next, z / w (%) can be calculated by dividing z by w.

[0102] Here, z / w in naturally derived fibroin will be explained. First, as described above, fibroins whose amino acid sequence information is registered in NCBI GenBank were confirmed by the method exemplified, and 663 types of fibroin (of which, 415 types are spider-derived fibroin) were extracted. From all the extracted fibroins, z / w was calculated by the above-mentioned calculation method from the amino acid sequence of naturally derived fibroin that contains a domain sequence represented by formula 1: [(A)n motif-REP]m and has an amino acid sequence content of GGX in the fibroin of 6% or less. The results are shown in FIG. 7. The horizontal axis of FIG. 7 indicates z / w (%), and the vertical axis indicates frequency. As is clear from FIG. 7, z / w in all naturally derived fibroins is less than 50.9% (the highest is 50.86%).

[0103] In the second modified fibroin, z / w is preferably 50.9% or more, more preferably 56.1% or more, even more preferably 58.7% or more, even more preferably 70% or more, and even more preferably 80% or more. There is no particular upper limit to z / w, but it may be, for example, 95% or less.

[0104] The second modified fibroin can be obtained, for example, by modifying the gene sequence of a cloned naturally-derived fibroin by substituting at least a part of the base sequence encoding a glycine residue to encode another amino acid residue. In this case, one glycine residue in the GGX motif and the GPGXX motif may be selected as the glycine residue to be modified, or may be substituted so that z / w is 50.9% or more. Alternatively, for example, an amino acid sequence satisfying the above-mentioned aspects may be designed from the amino acid sequence of a naturally-derived fibroin, and a nucleic acid encoding the designed amino acid sequence may be chemically synthesized to obtain the second modified fibroin. In either case, in addition to the modification equivalent to substituting the glycine residue in REP with another amino acid residue from the amino acid sequence of a naturally-derived fibroin, the amino acid sequence may be modified by substituting, deleting, inserting and / or adding one or more amino acid residues.

[0105] The other amino acid residue is not particularly limited as long as it is an amino acid residue other than a glycine residue, but is preferably a hydrophobic amino acid residue such as a valine (V) residue, a leucine (L) residue, an isoleucine (I) residue, a methionine (M) residue, a proline (P) residue, a phenylalanine (F) residue, or a tryptophan (W) residue, or a hydrophilic amino acid residue such as a glutamine (Q) residue, an asparagine (N) residue, a serine (S) residue, a lysine (K) residue, or a glutamic acid (E) residue, more preferably a valine (V) residue, a leucine (L) residue, an isoleucine (I) residue, a phenylalanine (F) residue, or a glutamine (Q) residue, and even more preferably a glutamine (Q) residue.

[0106] More specific examples of the second modified fibroin include (2-i) a modified fibroin comprising an amino acid sequence shown in SEQ ID NO: 6 (Met-PRT380), SEQ ID NO: 7 (Met-PRT410), SEQ ID NO: 8 (Met-PRT525) or SEQ ID NO: 9 (Met-PRT799), or (2-ii) an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9.

[0107] The modified fibroin (2-i) will be described. The amino acid sequence shown in SEQ ID NO:6 is obtained by replacing all GGX in the REP of the amino acid sequence shown in SEQ ID NO:10 (Met-PRT313) corresponding to naturally-occurring fibroin with GQX. The amino acid sequence shown in SEQ ID NO:7 is obtained by replacing every third amino acid (A) from the N-terminus to the C-terminus of the amino acid sequence shown in SEQ ID NO:6. n The motif was deleted, and the C-terminal sequence was further amplified with [(A) n The amino acid sequence shown in SEQ ID NO:8 is a sequence in which each of (A) of the amino acid sequence shown in SEQ ID NO:7 is inserted. n Two alanine residues were inserted at the C-terminus of the motif, and some glutamine (Q) residues were further replaced with serine (S) residues, with some amino acids deleted at the C-terminus to have approximately the same molecular weight as SEQ ID NO: 7. The amino acid sequence shown in SEQ ID NO: 9 has a predetermined hinge sequence and His tag sequence added to the C-terminus of a sequence in which the 20 domain sequence regions present in the amino acid sequence shown in SEQ ID NO: 7 (with the exception that several amino acid residues at the C-terminus of said regions have been replaced) are repeated four times.

[0108] The z / w value in the amino acid sequence shown in SEQ ID NO: 10 (corresponding to naturally derived fibroin) is 46.8%. The z / w values ​​in the amino acid sequence shown in SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, and SEQ ID NO: 9 are 58.7%, 70.1%, 66.1%, and 70.0%, respectively. Furthermore, the x / y values ​​in the jagged ratio (described later) of 1:1.8 to 11.3 in the amino acid sequences shown in SEQ ID NO: 10, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, and SEQ ID NO: 9 are 15.0%, 15.0%, 93.4%, 92.7%, and 89.8%, respectively.

[0109] The modified fibroin (2-i) may consist of the amino acid sequence shown in SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NO:9.

[0110] The modified fibroin of (2-ii) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9. The modified fibroin of (2-ii) also ... n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0111] The modified fibroin (2-ii) preferably has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NO:9, and has a z / w ratio of 50.9% or more, where z is the total number of amino acid residues in the amino acid sequence consisting of XGX (wherein X represents an amino acid residue other than glycine) contained in REP, and w is the total number of amino acid residues in REP in the domain sequence.

[0112] The second modified fibroin may contain a tag sequence at either or both of the N-terminus and C-terminus, which allows for isolation, immobilization, detection, visualization, etc. of the modified fibroin.

[0113] An example of a tag sequence is an affinity tag that utilizes specific affinity (binding ability, affinity) with other molecules. A specific example of an affinity tag is a histidine tag (His tag). The His tag is a short peptide consisting of about 4 to 10 histidine residues lined up, and has the property of specifically binding to metal ions such as nickel, and can be used to isolate modified fibroin by metal chelating chromatography. A specific example of a tag sequence is the amino acid sequence shown in SEQ ID NO: 11 (an amino acid sequence including a His tag sequence and a hinge sequence).

[0114] Furthermore, tag sequences such as glutathione-S-transferase (GST) that specifically binds to glutathione, and maltose-binding protein (MBP) that specifically binds to maltose can also be used.

[0115] Furthermore, an "epitope tag" utilizing an antigen-antibody reaction can also be used. By adding an antigenic peptide (epitope) as a tag sequence, an antibody against the epitope can be bound. Examples of epitope tags include HA (peptide sequence of influenza virus hemagglutinin) tag, myc tag, and FLAG tag. By using an epitope tag, the modified fibroin can be easily purified with high specificity.

[0116] Furthermore, a tag sequence that can be cleaved with a specific protease can also be used. By treating the protein adsorbed via the tag sequence with the protease, the modified fibroin from which the tag sequence has been cleaved can be recovered.

[0117] More specific examples of modified fibroins containing a tag sequence include (2-iii) modified fibroins containing an amino acid sequence shown in SEQ ID NO: 12 (PRT380), SEQ ID NO: 13 (PRT410), SEQ ID NO: 14 (PRT525) or SEQ ID NO: 15 (PRT799), or (2-iv) an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14 or SEQ ID NO: 15.

[0118] The amino acid sequences shown in SEQ ID NO:16 (PRT313), SEQ ID NO:12, SEQ ID NO:13, SEQ ID NO:14 and SEQ ID NO:15 are obtained by adding the amino acid sequence shown in SEQ ID NO:11 (including the His tag sequence and hinge sequence) to the N-terminus of the amino acid sequences shown in SEQ ID NO:10, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 and SEQ ID NO:9, respectively.

[0119] The modified fibroin (2-iii) may consist of the amino acid sequence shown in SEQ ID NO:12, SEQ ID NO:13, SEQ ID NO:14 or SEQ ID NO:15.

[0120] The modified fibroin of (2-iv) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15. The modified fibroin of (2-iv) also ... n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0121] The modified fibroin (2-iv) has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14 or SEQ ID NO: 15, and preferably has a z / w ratio of 50.9% or more, where z is the total number of amino acid residues in the amino acid sequence consisting of XGX (wherein X represents an amino acid residue other than glycine) contained in REP, and w is the total number of amino acid residues in REP in the domain sequence.

[0122] The second modified fibroin may contain a secretion signal for releasing the protein produced in the recombinant protein production system to the outside of the host. The sequence of the secretion signal can be appropriately set depending on the type of the host.

[0123] The third modified fibroin has a domain sequence different from that of naturally occurring fibroin, as follows: (A) n The third modified fibroin domain sequence has an amino acid sequence with a reduced content of motifs compared to naturally occurring fibroin. n It can be said that it has an amino acid sequence corresponding to the deletion of the motif.

[0124] The third modified fibroin was derived from naturally occurring fibroin (A). n It may have an amino acid sequence corresponding to a 10 to 40% deletion of the motif.

[0125] The third modified fibroin has a domain sequence that is different from that of naturally-occurring fibroin in that it has at least one to three (A) n One (A) per motif n It may have an amino acid sequence corresponding to the deletion of the motif.

[0126] The third modified fibroin has a domain sequence that is at least two consecutive domains from the N-terminus to the C-terminus, as compared with naturally occurring fibroin (A). n Deletion of the motif and one (A) n It may have an amino acid sequence corresponding to repeated deletion of the motif in this order.

[0127] The third modified fibroin has a domain sequence in which at least every third domain from the N-terminus to the C-terminus is (A) n It may have an amino acid sequence corresponding to the deletion of the motif.

[0128] The third modified fibroin has the formula 1: [(A) n Motif-REP] m The domain sequence is represented by the following two adjacent sequences from the N-terminus to the C-terminus: n The number of amino acid residues in the REP of the motif-REP] unit is compared in sequence. When the number of amino acid residues in the REP with the smaller number of amino acid residues is set to 1, the ratio of the number of amino acid residues in the other REP is 1.8 to 11.3 in two adjacent [(A) n When the maximum sum of the numbers of amino acid residues in the motif-REP units is x and the total number of amino acid residues in the domain sequence is y, the amino acid sequence may have an x / y ratio of 20% or more, 30% or more, 40% or more, or 50% or more. (A) n The number of alanine residues relative to the total number of amino acid residues in the motif may be 83% or more, but is preferably 86% or more, more preferably 90% or more, even more preferably 95% or more, and even more preferably 100% (meaning that it is composed only of alanine residues).

[0129] The method of calculating x / y will be described in more detail with reference to Fig. 6. Fig. 6 shows the domain sequence of the modified fibroin excluding the N-terminal sequence and the C-terminal sequence. The domain sequence is as follows from the N-terminal side (left side): (A) n Motif-First REP (50 amino acid residues)-(A) n Motif-Second REP (100 amino acid residues)-(A) n Motif-3 REP (10 amino acid residues)-(A) n Motif-4th REP (20 amino acid residues)-(A) n Motif-5 REP (30 amino acid residues)-(A) n It has a sequence called a motif.

[0130] Two adjacent [(A) n The motif-REP] units are selected sequentially from the N-terminus to the C-terminus, without overlapping. nA motif-REP] unit may be present. FIG. 6 shows pattern 1 (comparison of the first REP with the second REP, and comparison of the third REP with the fourth REP), pattern 2 (comparison of the first REP with the second REP, and comparison of the fourth REP with the fifth REP), pattern 3 (comparison of the second REP with the third REP, and comparison of the fourth REP with the fifth REP), and pattern 4 (comparison of the first REP with the second REP). There are other selection methods.

[0131] Next, for each pattern, select two adjacent [(A) n The number of amino acid residues of each REP in the motif-REP unit is compared. The comparison is performed by determining the ratio of the number of amino acid residues of the other REP to the number of amino acid residues of the one with fewer amino acid residues set as 1. For example, when comparing the first REP (50 amino acid residues) with the second REP (100 amino acid residues), the ratio of the number of amino acid residues of the second REP is 100 / 50=2 when the number of amino acid residues of the first REP with fewer amino acid residues is set as 1. Similarly, when comparing the fourth REP (20 amino acid residues) with the fifth REP (30 amino acid residues), the ratio of the number of amino acid residues of the fifth REP is 30 / 20=1.5 when the number of amino acid residues of the fourth REP with fewer amino acid residues is set as 1.

[0132] In FIG. 6, when the number of amino acid residues of the one with fewer amino acid residues is set to 1, the ratio of the number of amino acid residues of the other one is 1.8 to 11.3 [(A) n The combination of motif-REP] units is shown by a solid line. In this specification, this ratio is called the "Jagged ratio." When the one with the fewer amino acid residues is set to 1, the ratio of the other amino acid residue number is less than 1.8 or more than 11.3 [(A) n The motif-REP] unit pairs are indicated by dashed lines.

[0133] In each pattern, the two adjacent [(A) nThe numbers of all amino acid residues in the motif-REP unit are added together (not only the numbers of amino acid residues in REP, but also in the (A)n motif). The sums are then compared, and the sum of the pattern with the largest sum (the maximum sum) is designated as x. In the example shown in FIG. 6, the sum of pattern 1 is the largest.

[0134] Next, x / y (%) can be calculated by dividing x by the total number of amino acid residues, y, in the domain sequence.

[0135] In the third modified fibroin, x / y is preferably 50% or more, more preferably 60% or more, even more preferably 65% ​​or more, even more preferably 70% or more, even more preferably 75% or more, and particularly preferably 80% or more. There is no particular upper limit for x / y, and it may be, for example, 100% or less. When the knurling ratio is 1:1.9 to 11.3, x / y is preferably 89.6% or more, when the knurling ratio is 1:1.8 to 3.4, x / y is preferably 77.1% or more, when the knurling ratio is 1:1.9 to 8.4, x / y is preferably 75.9% or more, and when the knurling ratio is 1:1.9 to 4.1, x / y is preferably 64.2% or more.

[0136] The third modified fibroin is present multiple times in the domain sequence (A). n In the case of a modified fibroin in which at least seven of the motifs are composed only of alanine residues, x / y is preferably 46.4% or more, more preferably 50% or more, even more preferably 55% or more, even more preferably 60% or more, even more preferably 70% or more, and particularly preferably 80% or more. There is no particular upper limit to x / y, and it is sufficient as long as it is 100% or less.

[0137] Here, we will explain the x / y ratio of naturally occurring fibroin. First, as mentioned above, NCBI When fibroins with amino acid sequence information registered in GenBank were identified using the method described above, 663 types of fibroins (of which 415 were spider-derived fibroins) were extracted. Of all the extracted fibroins, those with the formula 1: [(A) n Motif-REP] m The ratio x / y was calculated by the above-mentioned calculation method from the amino acid sequence of naturally-occurring fibroin composed of the domain sequence represented by the following formula: The results when the jaggedness ratio was 1:1.9 to 4.1 are shown in FIG.

[0138] The horizontal axis of Fig. 8 indicates x / y (%), and the vertical axis indicates frequency. As is clear from Fig. 8, x / y in all naturally derived fibroins is less than 64.2% (the highest is 64.14%).

[0139] The third modified fibroin is, for example, (A) such that x / y is 64.2% or more based on the gene sequence of a cloned naturally occurring fibroin. n For example, one or more of the sequences encoding the motifs (A) may be deleted from the amino acid sequence of naturally occurring fibroin such that x / y is 64.2% or more. n Alternatively, the amino acid sequence corresponding to the deletion of the motif may be designed and a nucleic acid encoding the designed amino acid sequence may be chemically synthesized. In either case, the amino acid sequence of the naturally occurring fibroin may be selected from (A) n In addition to modifications corresponding to the deletion of a motif, further modifications to the amino acid sequence corresponding to the substitution, deletion, insertion and / or addition of one or more amino acid residues may be made.

[0140] More specific examples of the third modified fibroin include (3-i) a modified fibroin comprising an amino acid sequence shown in SEQ ID NO: 17 (Met-PRT399), SEQ ID NO: 7 (Met-PRT410), SEQ ID NO: 8 (Met-PRT525) or SEQ ID NO: 9 (Met-PRT799), or (3-ii) an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 17, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9.

[0141] The modified fibroin (3-i) will be described. The amino acid sequence shown in SEQ ID NO: 17 is a sequence of the amino acid sequence shown in SEQ ID NO: 10 (Met-PRT313) corresponding to naturally-occurring fibroin, which is obtained by subtracting every third amino acid from the N-terminus to the C-terminus. n The motif was deleted, and the C-terminal sequence was further amplified with [(A) n The amino acid sequence shown in SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9 is as described in the second modified fibroin.

[0142] The value of x / y in the jagged ratio of 1:1.8-11.3 of the amino acid sequence shown in SEQ ID NO:10 (corresponding to naturally derived fibroin) is 15.0%. The values ​​of x / y in the amino acid sequence shown in SEQ ID NO:17 and the amino acid sequence shown in SEQ ID NO:7 are both 93.4%. The value of x / y in the amino acid sequence shown in SEQ ID NO:8 is 92.7%. The value of x / y in the amino acid sequence shown in SEQ ID NO:9 is 89.8%. The values ​​of z / w in the amino acid sequences shown in SEQ ID NO:10, SEQ ID NO:17, SEQ ID NO:7, SEQ ID NO:8 and SEQ ID NO:9 are 46.8%, 56.2%, 70.1%, 66.1% and 70.0%, respectively.

[0143] The modified fibroin (3-i) may consist of the amino acid sequence shown in SEQ ID NO: 17, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9.

[0144] The modified fibroin of (3-ii) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 17, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9. The modified fibroin of (3-ii) also ... n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0145] The modified fibroin (3-ii) has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO: 17, SEQ ID NO: 7, SEQ ID NO: 8 or SEQ ID NO: 9, and has two adjacent amino acids [(A) n The number of amino acid residues in the REP of the motif-REP] unit is compared in sequence. When the number of amino acid residues in the REP with the fewer amino acid residues is set to 1, the ratio of the number of amino acid residues in the other REP is 1.8 to 11.3 (the jagged ratio is 1:1.8 to 11.3) between two adjacent [(A) n When the maximum sum of the numbers of amino acid residues in the motif-REP units is x and the total number of amino acid residues in the domain sequence is y, it is preferable that x / y is 64.2% or more.

[0146] The third modified fibroin may contain the above-mentioned tag sequence at either or both of the N-terminus and C-terminus.

[0147] More specific examples of modified fibroins containing a tag sequence include (3-iii) modified fibroins containing an amino acid sequence shown in SEQ ID NO: 18 (PRT399), SEQ ID NO: 13 (PRT410), SEQ ID NO: 14 (PRT525) or SEQ ID NO: 15 (PRT799), or (3-iv) an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 18, SEQ ID NO: 13, SEQ ID NO: 14 or SEQ ID NO: 15.

[0148] The amino acid sequences shown in SEQ ID NO:18, SEQ ID NO:13, SEQ ID NO:14 and SEQ ID NO:15 are obtained by adding the amino acid sequence shown in SEQ ID NO:11 (including a His tag sequence and a hinge sequence) to the N-terminus of the amino acid sequences shown in SEQ ID NO:17, SEQ ID NO:7, SEQ ID NO:8 and SEQ ID NO:9, respectively.

[0149] The modified fibroin (3-iii) may consist of the amino acid sequence shown in SEQ ID NO:18, SEQ ID NO:13, SEQ ID NO:14 or SEQ ID NO:15.

[0150] The modified fibroin of (3-iv) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 18, SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15. The modified fibroin of (3-iv) also ... n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0151] The modified fibroin (3-iv) has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO: 18, SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15, and has two adjacent amino acids [(A) n The number of amino acid residues in the REP of the motif-REP] unit is compared in sequence. When the number of amino acid residues in the REP with the smaller number of amino acid residues is set to 1, the ratio of the number of amino acid residues in the other REP is 1.8 to 11.3 in two adjacent [(A) n When the maximum sum of the numbers of amino acid residues in the motif-REP units is x and the total number of amino acid residues in the domain sequence is y, it is preferable that x / y is 64.2% or more.

[0152] The third modified fibroin may contain a secretion signal for releasing the protein produced in the recombinant protein production system to the outside of the host. The sequence of the secretion signal can be appropriately set depending on the type of the host.

[0153] The fourth modified fibroin has a domain sequence different from that of naturally occurring fibroin, as follows: (A) n In addition to the reduced content of the motif, the fourth modified fibroin has an amino acid sequence with a reduced content of glycine residues. The fourth modified fibroin domain sequence has at least one or more (A) n In addition to the deletion of the motif, the fourth modified fibroin has an amino acid sequence in which at least one or more glycine residues in REP have been replaced with another amino acid residue. That is, the fourth modified fibroin is a modified fibroin having both the characteristics of the second modified fibroin and the third modified fibroin described above. Specific aspects are as described for the second modified fibroin and the third modified fibroin.

[0154] More specific examples of the fourth modified fibroin include (4-i) modified fibroin containing an amino acid sequence shown in SEQ ID NO: 7 (Met-PRT410), SEQ ID NO: 8 (Met-PRT525), SEQ ID NO: 9 (Met-PRT799), SEQ ID NO: 13 (PRT410), SEQ ID NO: 14 (PRT525) or SEQ ID NO: 15 (PRT799), or (4-ii) modified fibroin containing an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 13, SEQ ID NO: 14 or SEQ ID NO: 15. Specific embodiments of modified fibroin containing the amino acid sequence shown in SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 13, SEQ ID NO: 14 or SEQ ID NO: 15 are as described above.

[0155] The fifth modified fibroin may have an amino acid sequence whose domain sequence includes a localized region of high hydrophobicity index, corresponding to the replacement of one or more amino acid residues in REP with amino acid residues with a high hydrophobicity index and / or the insertion of one or more amino acid residues with a high hydrophobicity index into REP, compared to naturally occurring fibroin.

[0156] The region with a locally high hydrophobicity index is preferably composed of 2 to 4 consecutive amino acid residues.

[0157] The amino acid residue with a high hydrophobicity index is more preferably an amino acid residue selected from isoleucine (I), valine (V), leucine (L), phenylalanine (F), cysteine ​​(C), methionine (M) and alanine (A).

[0158] The fifth modified fibroin may, in addition to modifications corresponding to the replacement of one or more amino acid residues in REP with amino acid residues having a high hydrophobicity index and / or the insertion of one or more amino acid residues having a high hydrophobicity index into REP, have further modifications in the amino acid sequence corresponding to the substitution, deletion, insertion and / or addition of one or more amino acid residues compared to the naturally occurring fibroin.

[0159] The fifth modified fibroin can be obtained, for example, by substituting one or more hydrophilic amino acid residues (e.g., amino acid residues with a negative hydrophobicity index) in REP from the gene sequence of cloned naturally-derived fibroin with hydrophobic amino acid residues (e.g., amino acid residues with a positive hydrophobicity index) and / or by inserting one or more hydrophobic amino acid residues into REP. Alternatively, for example, it can be obtained by designing an amino acid sequence corresponding to the substitution of one or more hydrophilic amino acid residues in REP with hydrophobic amino acid residues from the amino acid sequence of naturally-derived fibroin and / or the insertion of one or more hydrophobic amino acid residues into REP, and chemically synthesizing a nucleic acid encoding the designed amino acid sequence. In either case, in addition to the modification corresponding to the substitution of one or more hydrophilic amino acid residues in REP with hydrophobic amino acid residues from the amino acid sequence of naturally-derived fibroin and / or the insertion of one or more hydrophobic amino acid residues into REP, the amino acid sequence may be modified by further substituting, deleting, inserting and / or adding one or more amino acid residues.

[0160] The fifth modified fibroin has the formula 1: [(A) n Motif-REP] m and (A) is located at the most C-terminal end. n In all REPs contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence, the total number of amino acid residues contained in a region in which the average hydrophobicity index of four consecutive amino acid residues is 2.6 or more is defined as p, and the region located most C-terminally is defined as (A). n The domain may have an amino acid sequence in which p / q is 6.2% or more, where q is the total number of amino acid residues contained in the domain sequence excluding the sequence from the motif to the C-terminus of the domain sequence.

[0161] The hydrophobicity index of amino acid residues is determined by 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 (hereinafter also referred to as "HI") of each amino acid is as shown in Table 1 below.

[0162] [Table 1]

[0163] The method of calculating p / q will be described in more detail. The calculation is carried out using the formula 1: [(A) n Motif-REP] m (A) is located at the C-terminal end of the domain sequence represented by nA sequence excluding the sequence from the motif to the C-terminus of the domain sequence (hereinafter referred to as "sequence A") is used. First, the average value of the hydrophobicity index of four consecutive amino acid residues is calculated for all REPs included in sequence A. The average value of the hydrophobicity index is calculated by dividing the sum of the HI of each amino acid residue included in the four consecutive amino acid residues by 4 (the number of amino acid residues). The average value of the hydrophobicity index is calculated for all four consecutive amino acid residues (each amino acid residue is used to calculate the average value 1 to 4 times). Next, a region in which the average value of the hydrophobicity index of the four consecutive amino acid residues is 2.6 or more is specified. Even if a certain amino acid residue corresponds to a plurality of "four consecutive amino acid residues with an average value of the hydrophobicity index of 2.6 or more", it is included as one amino acid residue in the region. The total number of amino acid residues included in the region is p. The total number of amino acid residues included in sequence A is q.

[0164] For example, if 20 "sequential four amino acid residues with an average hydrophobicity index of 2.6 or more" are extracted (without overlaps), the region in which the average hydrophobicity index of the consecutive four amino acid residues is 2.6 or more contains 20 consecutive four amino acid residues (without overlaps), and p is 20×4=80. Also, for example, if two "sequential four amino acid residues with an average hydrophobicity index of 2.6 or more" overlap by one amino acid residue, the region in which the average hydrophobicity index of the consecutive four amino acid residues is 2.6 or more contains seven amino acid residues (p=2×4-1=7, where "-1" is the deduction of the overlap). For example, in the case of the domain sequence shown in FIG. 9, there are seven "sequential four amino acid residues with an average hydrophobicity index of 2.6 or more" without overlaps, and p is 7×4=28. For example, in the case of the domain sequence shown in FIG. 9, q is 4+50+4+40+4+10+4+20+4+30=170 ((A) at the end of the C-terminus). n (The motif is not included.) Next, p / q (%) can be calculated by dividing p by q. In the case of Figure 9, it is 28 / 170 = 16.47%.

[0165] In the fifth modified fibroin, p / q is preferably 6.2% or more, more preferably 7% or more, even more preferably 10% or more, even more preferably 20% or more, and even more preferably 30% or more. The upper limit of p / q is not particularly limited, but may be, for example, 45% or less.

[0166] The fifth modified fibroin can be obtained, for example, by modifying the amino acid sequence of a cloned naturally-derived fibroin to include a region with a high hydrophobic index locally by substituting one or more hydrophilic amino acid residues (e.g., amino acid residues with a negative hydrophobic index) in the REP with hydrophobic amino acid residues (e.g., amino acid residues with a positive hydrophobic index) and / or inserting one or more hydrophobic amino acid residues into the REP so as to satisfy the above-mentioned p / q condition. Alternatively, for example, the fifth modified fibroin can be obtained by designing an amino acid sequence that satisfies the above-mentioned p / q condition from the amino acid sequence of a naturally-derived fibroin and chemically synthesizing a nucleic acid encoding the designed amino acid sequence. In either case, in addition to the modification corresponding to the substitution of one or more amino acid residues in the REP with amino acid residues with a high hydrophobic index and / or the insertion of one or more amino acid residues with a high hydrophobic index into the REP, modifications corresponding to the substitution, deletion, insertion and / or addition of one or more amino acid residues may be performed.

[0167] The amino acid residues having a high hydrophobicity index are not particularly limited, but are preferably isoleucine (I), valine (V), leucine (L), phenylalanine (F), cysteine ​​(C), methionine (M) and alanine (A), and more preferably valine (V), leucine (L) and isoleucine (I).

[0168] A more specific example of the fifth modified fibroin includes (5-i) a modified fibroin comprising an amino acid sequence shown in SEQ ID NO: 19 (Met-PRT720), SEQ ID NO: 20 (Met-PRT665) or SEQ ID NO: 21 (Met-PRT666), or (5-ii) an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 19, SEQ ID NO: 20 or SEQ ID NO: 21.

[0169] The modified fibroin of (5-i) will be described. The amino acid sequence shown in SEQ ID NO: 19 is obtained by inserting an amino acid sequence (VLI) consisting of three amino acid residues at every other REP at two positions, excluding the domain sequence at the C-terminus, and further substituting some glutamine (Q) residues with serine (S) residues, and deleting some amino acids at the C-terminus, in the amino acid sequence shown in SEQ ID NO: 7 (Met-PRT410). The amino acid sequence shown in SEQ ID NO: 20 is obtained by inserting an amino acid sequence (VLI) consisting of three amino acid residues at every other REP at one position, in the amino acid sequence shown in SEQ ID NO: 8 (Met-PRT525). The amino acid sequence shown in SEQ ID NO: 21 is obtained by inserting an amino acid sequence (VLI) consisting of three amino acid residues at every other REP at two positions, in the amino acid sequence shown in SEQ ID NO: 8.

[0170] The modified fibroin (5-i) may consist of the amino acid sequence shown in SEQ ID NO:19, SEQ ID NO:20 or SEQ ID NO:21.

[0171] The modified fibroin of (5-ii) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 19, SEQ ID NO: 20, or SEQ ID NO: 21. The modified fibroin of (5-ii) also ... n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0172] The modified fibroin (5-ii) has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO: 19, SEQ ID NO: 20, or SEQ ID NO: 21 and is located at the most C-terminal side (A). n In all REPs contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence, the total number of amino acid residues contained in the region in which the average hydrophobicity index of four consecutive amino acid residues is 2.6 or more is defined as p, and the region located most C-terminally is defined as (A). n When the total number of amino acid residues contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence is defined as q, it is preferable that p / q is 6.2% or more.

[0173] The fifth modified fibroin may contain a tag sequence at either or both of the N-terminus and C-terminus.

[0174] More specific examples of modified fibroins containing a tag sequence include (5-iii) modified fibroins containing an amino acid sequence shown in SEQ ID NO: 22 (PRT720), SEQ ID NO: 23 (PRT665) or SEQ ID NO: 24 (PRT666), or (5-iv) an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 22, SEQ ID NO: 23 or SEQ ID NO: 24.

[0175] The amino acid sequences shown in SEQ ID NO: 22, SEQ ID NO: 23 and SEQ ID NO: 24 are obtained by adding the amino acid sequence shown in SEQ ID NO: 11 (including the His tag sequence and hinge sequence) to the N-terminus of the amino acid sequences shown in SEQ ID NO: 19, SEQ ID NO: 20 and SEQ ID NO: 21, respectively.

[0176] The modified fibroin (5-iii) may consist of the amino acid sequence shown in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:24.

[0177] The modified fibroin (5-iv) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 22, SEQ ID NO: 23, or SEQ ID NO: 24. The modified fibroin (5-iv) also contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 22, SEQ ID NO: 23, or SEQ ID NO: 24. The modified fibroin (5- n Motif-REP] m It is a protein comprising a domain sequence represented by the following formula: The sequence identity is preferably 95% or more.

[0178] The modified fibroin (5-iv) has a sequence identity of 90% or more with the amino acid sequence shown in SEQ ID NO: 22, SEQ ID NO: 23, or SEQ ID NO: 24 and is located at the most C-terminal side (A). n In all REPs contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence, the total number of amino acid residues contained in the region in which the average hydrophobicity index of four consecutive amino acid residues is 2.6 or more is defined as p, and the region located most C-terminally is defined as (A). n When the total number of amino acid residues contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence is defined as q, it is preferable that p / q is 6.2% or more.

[0179] The fifth modified fibroin may contain a secretion signal for releasing the protein produced in the recombinant protein production system to the outside of the host. The sequence of the secretion signal can be appropriately set depending on the type of the host.

[0180] The sixth modified fibroin has an amino acid sequence with a reduced content of glutamine residues compared to naturally occurring fibroin.

[0181] It is preferable that the sixth modified fibroin contains at least one motif selected from the GGX motif and the GPGXX motif in the amino acid sequence of REP.

[0182] When the sixth modified fibroin contains a GPGXX motif in the REP, the GPGXX motif content is usually 1% or more, may be 5% or more, and is preferably 10% or more. There is no particular upper limit to the GPGXX motif content, and it may be 50% or less, or may be 30% or less.

[0183] As used herein, the "GPGXX motif content" is a value calculated by the following method. Formula 1: [(A) n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n In a fibroin (modified fibroin or naturally-occurring fibroin) containing a domain sequence represented by the motif, (A) is located at the most C-terminal side. n For all REPs contained in the sequence excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence, the total number of GPGXX motifs contained in that region is multiplied by three (i.e., the total number of G and P in the GPGXX motif), and the number s is the number located at the most C-terminus side (A). n The sequence from the motif to the C-terminus of the domain sequence is removed from the domain sequence, and further (A) n When the total number of amino acid residues of all REPs excluding the motif is t, the GPGXX motif content is calculated as s / t.

[0184] In calculating the GPGXX motif content, the most C-terminal (A) n The target sequence is the sequence excluding the sequence from the motif to the C-terminus of the domain sequence, which is the sequence located at the most C-terminus (A). nThe "sequence from the motif to the C-terminus of the domain sequence" (sequence corresponding to REP) may contain sequences with low correlation with sequences characteristic of fibroin, and when m is small (i.e., when the domain sequence is short), this affects the calculation results of the GPGXX motif content, so this is to eliminate this influence. Note that when the "GPGXX motif" is located at the C-terminus of REP, even if "XX" is, for example, "AA", it is treated as a "GPGXX motif".

[0185] FIG. 10 is a schematic diagram showing the domain sequence of a modified fibroin. A method for calculating the GPGXX motif content will be specifically described with reference to FIG. 10. First, the domain sequence of the modified fibroin shown in FIG. n Motif-REP] m -(A) n In the 1990s, all REPs were located at the C-terminus (A) n Since the number of GPGXX motifs is 7, s is 7 × 3 = 21. Similarly, all REPs are included in the "domain sequence excluding the sequence from the motif to the C-terminus of the domain sequence" (the sequence shown as "Region A" in Figure 10). n Since the domain sequence is excluded from the sequence from the motif to the C-terminus of the domain sequence (the sequence shown as "Region A" in FIG. 10), the sequence is further divided into (A) n The total number of amino acid residues of all REPs excluding motifs, t, is 50 + 40 + 10 + 20 + 30 = 150. Next, s / t (%) can be calculated by dividing s by t, which is 21 / 150 = 14.0% in the case of the modified fibroin in Figure 10.

[0186] The sixth modified fibroin preferably has a glutamine residue content of 9% or less, more preferably 7% or less, even more preferably 4% or less, and particularly preferably 0%.

[0187] In this specification, the "glutamine residue content" is a value calculated by the following method. Formula 1: [(A) n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n In a fibroin (modified fibroin or naturally-occurring fibroin) containing a domain sequence represented by the motif, (A) is located at the most C-terminal side. n In all REPs contained in the sequence obtained by removing the sequence from the motif to the C-terminus of the domain sequence (the sequence corresponding to "Region A" in Figure 10), the total number of glutamine residues contained in the region is defined as u, and the region located most C-terminally is (A) n The sequence from the motif to the C-terminus of the domain sequence is removed from the domain sequence, and further (A) n When the total number of amino acid residues of all REPs excluding the motif is t, the glutamine residue content is calculated as u / t. n The reason for targeting "the sequence obtained by excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence" is the same as that mentioned above.

[0188] The sixth modified fibroin may have an amino acid sequence whose domain sequence corresponds to the deletion or substitution of one or more glutamine residues in the REP, compared to a naturally occurring fibroin.

[0189] The "other amino acid residue" may be any amino acid residue other than glutamine residue, but is preferably an amino acid residue with a higher hydrophobicity index than glutamine residue. The hydrophobicity indexes of amino acid residues are shown in Table 1.

[0190] As shown in Table 1, examples of amino acid residues having a higher hydrophobicity index than glutamine residues include amino acid residues selected from isoleucine (I), valine (V), leucine (L), phenylalanine (F), cysteine ​​(C), methionine (M), alanine (A), glycine (G), threonine (T), serine (S), tryptophan (W), tyrosine (Y), proline (P) and histidine (H). Among these, amino acid residues selected from isoleucine (I), valine (V), leucine (L), phenylalanine (F), cysteine ​​(C), methionine (M) and alanine (A) are more preferred, and amino acid residues selected from isoleucine (I), valine (V), leucine (L) and phenylalanine (F) are even more preferred.

[0191] In the sixth modified fibroin, the hydrophobicity of REP is preferably -0.8 or more, more preferably -0.7 or more, even more preferably 0 or more, even more preferably 0.3 or more, and particularly preferably 0.4 or more. There is no particular upper limit to the hydrophobicity of REP, and it may be 1.0 or less, or 0.7 or less.

[0192] In this specification, the "hydrophobicity of REP" is a value calculated by the following method. Formula 1: [(A) n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n In a fibroin (modified fibroin or naturally-occurring fibroin) containing a domain sequence represented by the motif, (A) is located at the most C-terminal side. n For all REPs contained in the sequence obtained by removing the sequence from the motif to the C-terminus of the domain sequence (the sequence corresponding to "Region A" in Figure 10), the sum of the hydrophobicity indexes of each amino acid residue in that region is v, and the REP located at the most C-terminus side (A) n The sequence from the motif to the C-terminus of the domain sequence is removed from the domain sequence, and further (A) nWhen the total number of amino acid residues of all REPs excluding the motif is t, the hydrophobicity of the REP is calculated as v / t. n The reason for targeting "the sequence obtained by excluding the sequence from the motif to the C-terminus of the domain sequence from the domain sequence" is the same as that mentioned above.

[0193] The sixth modified fibroin may have a domain sequence that, compared to a naturally occurring fibroin, is modified by the deletion of one or more glutamine residues in the REP and / or the replacement of one or more glutamine residues in the REP with other amino acid residues, and may also have an amino acid sequence modification that is equivalent to the substitution, deletion, insertion and / or addition of one or more amino acid residues.

[0194] The sixth modified fibroin can be obtained, for example, by deleting one or more glutamine residues in REP from the gene sequence of a cloned naturally-occurring fibroin and / or substituting one or more glutamine residues in REP with other amino acid residues. It can also be obtained, for example, by designing an amino acid sequence corresponding to the deletion of one or more glutamine residues in REP from the amino acid sequence of a naturally-occurring fibroin and / or the substitution of one or more glutamine residues in REP with other amino acid residues, and chemically synthesizing a nucleic acid encoding the designed amino acid sequence.

[0195] More specific examples of the sixth modified fibroin include (6-i) modified fibroin having an amino acid sequence shown in SEQ ID NO: 25 (Met-PRT888), SEQ ID NO: 26 (Met-PRT965), SEQ ID NO: 27 (Met-PRT889), SEQ ID NO: 28 (Met-PRT916), SEQ ID NO: 29 (Met-PRT918), SEQ ID NO: 30 (Met-PRT699), SEQ ID NO: 31 (Met-PRT698), SEQ ID NO: 32 (Met-PRT966), SEQ ID NO: 41 (Met-PRT917) or SEQ ID NO: 42 (Met-PRT1028), or (6-ii) modified fibroin having an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 41 or SEQ ID NO: 42.

[0196] The modified fibroin (6-i) will be described. The amino acid sequence shown in SEQ ID NO: 25 is obtained by substituting all QQ in the amino acid sequence shown in SEQ ID NO: 7 (Met-PRT410) with VL. The amino acid sequence shown in SEQ ID NO: 26 is obtained by substituting all QQ in the amino acid sequence shown in SEQ ID NO: 7 with TS, and substituting the remaining Q with A. The amino acid sequence shown in SEQ ID NO: 27 is obtained by substituting all QQ in the amino acid sequence shown in SEQ ID NO: 7 with VL, and substituting the remaining Q with I. The amino acid sequence shown in SEQ ID NO: 28 is obtained by substituting all QQ in the amino acid sequence shown in SEQ ID NO: 7 with VI, and substituting the remaining Q with L. The amino acid sequence shown in SEQ ID NO: 29 is obtained by substituting all QQ in the amino acid sequence shown in SEQ ID NO: 7 with VF, and substituting the remaining Q with I.

[0197] The amino acid sequence shown in SEQ ID NO: 30 is the amino acid sequence shown in SEQ ID NO: 8 (Met-PRT525) in which all QQ are replaced with VL. The amino acid sequence shown in SEQ ID NO: 31 is the amino acid sequence shown in SEQ ID NO: 8 in which all QQ are replaced with VL and the remaining Q is replaced with I.

[0198] The amino acid sequence shown in SEQ ID NO:32 is a sequence in which the 20 domain sequence region present in the amino acid sequence shown in SEQ ID NO:7 (Met-PRT410) is repeated twice, with all QQs replaced with VF and the remaining Qs replaced with I.

[0199] The amino acid sequence shown in SEQ ID NO:41 (Met-PRT917) is obtained by replacing all QQ in the amino acid sequence shown in SEQ ID NO:7 with LI and the remaining Q with V. The amino acid sequence shown in SEQ ID NO:42 (Met-PRT1028) is obtained by replacing all QQ in the amino acid sequence shown in SEQ ID NO:7 with IF and the remaining Q with T.

[0200] The amino acid sequences shown in SEQ ID NO:25, SEQ ID NO:26, SEQ ID NO:27, SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:30, SEQ ID NO:31, SEQ ID NO:32, SEQ ID NO:41 and SEQ ID NO:42 all have a glutamine residue content of 9% or less (Table 2).

[0201] [Table 2]

[0202] The modified fibroin (6-i) may consist of the amino acid sequence shown in SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 41 or SEQ ID NO: 42.

[0203] The modified fibroin of (6-ii) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 41, or SEQ ID NO: 42. The modified fibroin of (6-ii) also contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 41, or SEQ ID NO: 42. The modified fibroin of (6 n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) nIt is a protein containing a domain sequence represented by the motif. The sequence identity is preferably 95% or more.

[0204] The modified fibroin (6-ii) preferably has a glutamine residue content of 9% or less, and the modified fibroin (6-ii) preferably has a GPGXX motif content of 10% or more.

[0205] The sixth modified fibroin may contain a tag sequence at either or both of the N-terminus and C-terminus, which allows the modified fibroin to be isolated, immobilized, detected, visualized, and the like.

[0206] More specific examples of modified fibroins containing a tag sequence include (6-iii) modified fibroins containing the amino acid sequence shown in SEQ ID NO: 33 (PRT888), SEQ ID NO: 34 (PRT965), SEQ ID NO: 35 (PRT889), SEQ ID NO: 36 (PRT916), SEQ ID NO: 37 (PRT918), SEQ ID NO: 38 (PRT699), SEQ ID NO: 39 (PRT698), SEQ ID NO: 40 (PRT966), SEQ ID NO: 43 (PRT917) or SEQ ID NO: 44 (PRT1028), or (6-iv) modified fibroins containing an amino acid sequence having 90% or more sequence identity to the amino acid sequence shown in SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 43 or SEQ ID NO: 44.

[0207] The amino acid sequences shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37, SEQ ID NO:38, SEQ ID NO:39, SEQ ID NO:40, SEQ ID NO:43 and SEQ ID NO:44 are obtained by adding the amino acid sequence shown in SEQ ID NO:11 (including a His tag sequence and a hinge sequence) to the N-terminus of the amino acid sequences shown in SEQ ID NO:25, SEQ ID NO:26, SEQ ID NO:27, SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:30, SEQ ID NO:31, SEQ ID NO:32, SEQ ID NO:41 and SEQ ID NO:42, respectively. Since only a tag sequence is added to the N-terminus, there is no change in the glutamine residue content, and the amino acid sequences shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37, SEQ ID NO:38, SEQ ID NO:39, SEQ ID NO:40, SEQ ID NO:43 and SEQ ID NO:44 all have a glutamine residue content of 9% or less (Table 3).

[0208] [Table 3]

[0209] The modified fibroin (6-iii) may consist of the amino acid sequence shown in SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 43 or SEQ ID NO: 44.

[0210] The modified fibroin of (6-iv) contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 43, or SEQ ID NO: 44. The modified fibroin of (6-iv) also contains an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 43, or SEQ ID NO: 44. The modified fibroin of (6 n Motif-REP] m Or formula 2: [(A) n Motif-REP] m -(A) n It is a protein containing a domain sequence represented by the motif. The sequence identity is preferably 95% or more.

[0211] The modified fibroin (6-iv) preferably has a glutamine residue content of 9% or less, and the modified fibroin (6-iv) preferably has a GPGXX motif content of 10% or more.

[0212] The sixth modified fibroin may contain a secretion signal for releasing the protein produced in the recombinant protein production system to the outside of the host. The sequence of the secretion signal can be appropriately selected depending on the type of the host.

[0213] The modified fibroin may be a modified fibroin having at least two or more of the characteristics of the first modified fibroin, the second modified fibroin, the third modified fibroin, the fourth modified fibroin, the fifth modified fibroin, and the sixth modified fibroin.

[0214] The modified fibroin may be either hydrophilic or hydrophobic. In this specification, the term "hydrophilic modified fibroin" refers to modified fibroin in which the sum of the hydrophobicity index (HI) of all amino acid residues constituting the modified fibroin is calculated and then the sum is divided by the total number of amino acid residues, resulting in an average HI of 0 or less. The hydrophobicity index is as shown in Table 1. The term "hydrophobic modified fibroin" refers to modified fibroin in which the average HI is greater than 0. The hydrophilic modified fibroin is particularly excellent in flame retardancy. The hydrophobic modified fibroin is particularly excellent in hygroscopic heat generation and heat retention.

[0215] Examples of hydrophilic modified fibroins include modified fibroins containing the amino acid sequence shown in SEQ ID NO:4, the amino acid sequence shown in SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NO:9, the amino acid sequence shown in SEQ ID NO:13, SEQ ID NO:11, SEQ ID NO:14 or SEQ ID NO:15, the amino acid sequence shown in SEQ ID NO:18, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NO:9, the amino acid sequence shown in SEQ ID NO:17, SEQ ID NO:11, SEQ ID NO:14 or SEQ ID NO:15, the amino acid sequence shown in SEQ ID NO:19, SEQ ID NO:20 or SEQ ID NO:21.

[0216] Examples of hydrophobic modified fibroins include modified fibroins having the amino acid sequence shown in SEQ ID NO:27, SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:30, SEQ ID NO:31, SEQ ID NO:32, SEQ ID NO:33 or SEQ ID NO:43, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:38, SEQ ID NO:39, SEQ ID NO:40, SEQ ID NO:41 or SEQ ID NO:44. EXAMPLES

[0217] The present invention will be described in more detail below based on test examples, etc. However, the present invention is not limited to the following test examples.

[0218] [Test Example 1: Production of modified fibroin] Modified spider silk fibroin (PRT399) having the amino acid sequence shown in SEQ ID NO: 18, modified spider silk fibroin (PRT380) having the amino acid sequence shown in SEQ ID NO: 12, modified spider silk fibroin (PRT410) having the amino acid sequence shown in SEQ ID NO: 13, modified fibroin (PRT918) having the amino acid sequence shown in SEQ ID NO: 37, modified fibroin (PRT966) having the amino acid sequence shown in SEQ ID NO: 40, and modified fibroin (PRT799) having the amino acid sequence shown in SEQ ID NO: 15 were designed. A nucleic acid encoding the designed modified fibroin was 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. This nucleic acid was cloned into a cloning vector (pUC118). The nucleic acid was then excised by restriction enzyme treatment with NdeI and EcoRI, and then recombined into the protein expression vector pET-22b(+) to obtain an expression vector.

[0219] 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 transferred to 100 mL of seed culture medium (Table 4) containing ampicillin at OD 200. 600The culture temperature was kept at 30°C, and the OD 600 The flask culture was continued until the number of cells reached 5 (about 15 hours), and a seed culture solution was obtained.

[0220] [Table 4]

[0221] The seed culture solution was transferred to a jar fermenter containing 500 mL of production medium (Table 5) and the OD 600 The culture temperature was kept at 37°C and the pH was controlled to be constant at 6.9. The dissolved oxygen concentration in the culture was maintained at 20% of the dissolved oxygen saturation concentration.

[0222] [Table 5]

[0223] Immediately after the glucose in the production medium was completely consumed, the feed solution (glucose 455g / 1L, yeast extract 120g / 1L) was added at a rate of 1mL / min. The culture temperature was kept at 37°C and the culture was controlled to a constant pH of 6.9. The dissolved oxygen concentration in the culture was maintained at 20% of the dissolved oxygen saturation concentration, and the culture was continued for 20 hours. Then, 1M isopropyl-β-thiogalactopyranoside (IPTG) was added to the culture solution to a final concentration of 1mM to induce the expression of the modified fibroin. After 20 hours had passed after the addition of IPTG, the culture solution was centrifuged and the cells were collected. SDS-PAGE was performed using the cells prepared from the culture solution before and after the addition of IPTG, and the expression of the modified fibroin of interest was confirmed by the appearance of a band of the desired modified fibroin size depending on the addition of IPTG.

[0224] The cells harvested 2 hours after the addition of IPTG were 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 PMSF, and the cells were disrupted using a high-pressure homogenizer (GEA Niro Soavi). The disrupted cells were centrifuged to obtain a precipitate. The resulting precipitate was washed with 20 mM Tris-HCl buffer (pH 7.4) until it reached a high purity. The washed precipitate was diluted with 8 M guanidine buffer (8 M) to a concentration of 100 mg / mL. The protein was suspended in 10 mM guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0, and stirred at 60°C for 30 minutes with a stirrer 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 collected by centrifugation, water was removed using a freeze-dryer, and the freeze-dried powder was collected to obtain modified fibroins (PRT399, PRT380, PRT410, PRT918, PRT966, and PRT799).

[0225] [Test Example 2: Production of modified fibroin fiber (artificial protein fiber) and evaluation of contractility] Dimethyl sulfoxide (DMSO) in which LiCl was dissolved to a concentration of 4.0% by mass was prepared as a solvent, and freeze-dried powder of modified fibroin (PRT399, PRT380, PRT410, or PRT799) was added to the solvent to a concentration of 18% by mass or 24% by mass, and dissolved for 3 hours using a shaker. Insoluble matter and bubbles were then removed to obtain a modified fibroin solution.

[0226] The obtained modified fibroin solution was used as a dope solution (spinning stock solution), and the modified fibroin fiber (modified spider silk fibroin fiber) was produced by spinning and drawing through dry-wet spinning under the following conditions. Extrusion nozzle diameter: 0.2mm Coagulation bath temperature: 2~15℃ Total stretch ratio: 1 to 4 times Drying temperature: 60℃

[0227] (Contraction Evaluation) The resulting modified fibroin fibers (Production Examples 1 to 19) were evaluated for shrinkage. That is, each modified fibroin fiber (fibers after spinning and before contact with water) was subjected to a shrinkage process in which the fiber was brought into a wet state by contact with water (contact step) and then dried (drying step), and the shrinkage rates of the wet modified fibroin fibers and those of the wet and then dried modified fibroin fibers were determined.

[0228] <Contact Step> From each of the wound modified fibroin fibers, a plurality of modified fibroin fibers for testing, each having a length of 30 cm, were cut out. The plurality of modified fibroin fibers were bundled together to obtain a modified fibroin fiber bundle having a fineness of 150 denier. A 0.8 g lead weight was attached to each modified fibroin fiber bundle, and in that state, each modified fibroin fiber bundle was immersed in water at the temperatures shown in Tables 6 to 9 for 10 minutes. The length of each modified fibroin fiber bundle was then measured in water. The measurement was performed while the 0.8 g lead weight was attached to the modified fibroin fiber bundle in order to eliminate crimping of the modified fibroin fiber bundle. Next, the shrinkage rate of the modified fibroin fiber in a wet state (shrinkage rate when wet) was calculated according to the following formula V. In formula V, L0 indicates the length (30 cm) of the modified fibroin fiber bundle before immersion in water, and Lw indicates the length of the modified fibroin fiber bundle immersed in water and wet. Wet shrinkage (%) = {1-(Lw / L0)} x 100 ... (Formula V)

[0229] <Drying step> After the contact step, the modified fibroin fiber bundle was removed from the water. The removed modified fibroin fiber bundle was left to dry at room temperature for 2 hours with a 0.8 g lead weight still attached. After drying, the length of each modified fibroin fiber bundle was measured. Next, the shrinkage rate (shrinkage rate when dried) of the modified fibroin fiber that had been moistened and then dried was calculated according to the following formula VI. In formula VI, L0 indicates the length (30 cm) of the modified fibroin fiber bundle before immersion in water, and Lwd indicates the length of the modified fibroin fiber bundle that had been moistened by immersion in water and then dried. Shrinkage rate during drying (%)={1-(Lwd / L0)}×100(%) …(Formula VI)

[0230] The results are shown in Tables 6 to 9. In Tables 6 to 9, "total draw ratio" indicates the total draw ratio in the spinning process.

[0231] [Table 6]

[0232] [Table 7]

[0233] [Table 8]

[0234] [Table 9]

[0235] As shown in Tables 6 to 9, the artificial protein fiber (modified fibroin fiber) has a high shrinkage percentage when wet and when dry, and it can be seen that it is suitable as a fiber constituting the base material of the fabric according to the present invention.

[0236] [Test Example 3: Production of substrate and water-repellent treatment of substrate surface] (1) Preparation of spinning solution (dope solution) DMSO in which lithium chloride was dissolved to a concentration of 4% by mass was used as a solvent, and the freeze-dried powder of the modified fibroin (PRT799) produced above was added to the solvent to a concentration of 24% by mass. After dissolving for 1 hour in an aluminum block heater at 90°C, insoluble matter and bubbles were removed to obtain a spinning solution (dope solution).

[0237] (2) Spinning The spinning solution was filled into a reserve tank and discharged from a monohole nozzle with a diameter of 0.1 or 0.2 mm into a 100% by mass methanol coagulation bath using a gear pump. The discharge rate was adjusted to 0.01 to 0.08 mL / min. After coagulation, washing and drawing were performed in a 100% by mass methanol washing bath. After washing and drawing, the fiber was dried using a dry heat plate, and the obtained raw yarn (modified fibroin fiber) was wound up.

[0238] (3) Manufacturing of base material (woven fabric) The modified fibroin fibers were then used to make ply-ply yarns, which were then plain woven to obtain woven fabrics.

[0239] (4) Attachment of hydrophobic polymers to substrates (woven fabrics) The obtained woven fabric was coated with a fluorine-based coating monomer and subjected to plasma treatment using a plasma treatment device (manufactured by Europlasma). The plasma treatment resulted in a woven fabric to which a fluorine-based polymer (water resistance imparting substance) formed by polymerization of the fluorine-based coating monomer was covalently bonded. Nanofics110 (Example 1) and Nanofics120 (Example 2) (both manufactured by Europlasma) were used as the fluorine-based coating monomer.

[0240] (5) Water repellency evaluation A water repellency test (spray test) was carried out on the plasma-treated woven fabrics of Examples 1 and 2, and on the non-plasma-treated woven fabric (Comparative Example 1). The water repellency test (spray test) was carried out in accordance with ISO4920:2012. Judgment was carried out visually according to the following 6-level evaluation criteria (score 0 to 5). Score 5: No wetting or water droplets on the surface. Score 4: The surface is not wetted, but water droplets are attached. Score 3: There is a small amount of wetting on the surface. Score 2: The infiltration is widespread and some are connected to each other. Score 1: indicates complete wetting of the area hit by the water. Score 0: The entire surface is wet.

[0241] The results are shown in Table 10. The woven fabric of Comparative Example 1, which was not subjected to plasma treatment, received a score of 0, whereas the woven fabrics of Examples 1 and 2, which were subjected to plasma treatment, both received a score of 4, indicating that they were imparted with water resistance (water repellency).

[0242] [Table 10]

[0243] (6) Evaluation of texture and shrinkage Square test pieces with sides of 5 cm were cut out from the woven fabrics of Examples 1 and 2 and Comparative Example 1. Four vertices of a square with sides of 30 mm were marked with a pencil on one surface of the test pieces. Each test piece was immersed in water at 40°C for 10 minutes, and then vacuum dried at room temperature. This process was repeated five times. The vacuum drying was performed for 30 minutes at a set pressure of -0.1 MPa using a vacuum constant temperature dryer (VOS-310C, manufactured by Tokyo Rikakikai Co., Ltd.). In addition, at the end of each cycle, the tactile sensation was evaluated and the shrinkage rate was evaluated by measuring the distance between the four marked points.

[0244] The texture was evaluated according to the following criteria. The results are shown in Table 11. The woven fabrics of Examples 1 and 2, which were subjected to plasma treatment, showed less deterioration in texture than the woven fabric of Comparative Example 1, which was not subjected to plasma treatment. Score 5: As good as the original. Score 4: Good, but slightly inferior to the original. Score 3: Not bad, but a bit hard. Score 2: Poor and stiff, but bendable. Score 1: Very bad, stiff and inflexible.

[0245] [Table 11]

[0246] The shrinkage rate was calculated according to the following formula: The "average length of each side" is the sum of the lengths of each side of the rectangle formed by the four marked points divided by four. Shrinkage rate (%) = {1-(average length of each side (mm) / 30mm)} x 100 The results are shown in Table 12. The woven fabrics of Examples 1 and 2, which were subjected to plasma treatment, both had smaller shrinkage rates than the woven fabric of Comparative Example 1, which was not subjected to plasma treatment.

[0247] [Table 12]

[0248] [Test Example 4: Production of substrate and water-repellent treatment of substrate surface] (1) Preparation of spinning solution (dope solution) DMSO in which lithium chloride was dissolved to a concentration of 4% by mass was used as a solvent, and the freeze-dried powder of the modified fibroin (PRT918) produced above was added to the solvent to a concentration of 24% by mass. After dissolving for 1 hour in an aluminum block heater at 90°C, insoluble matter and bubbles were removed to obtain a spinning solution (dope solution).

[0249] (2) Spinning The spinning solution was filled into a reserve tank and discharged from a monohole nozzle with a diameter of 0.1 or 0.2 mm into a 100% by mass methanol coagulation bath using a gear pump. The discharge rate was adjusted to 0.01 to 0.08 mL / min. After coagulation, washing and drawing were performed in a 100% by mass methanol washing bath. After washing and drawing, the fiber was dried using a dry heat plate, and the obtained raw yarn (modified fibroin fiber) was wound up.

[0250] (3) Manufacturing of base material (knitted fabric) The modified fibroin fibers obtained were cut to produce modified fibroin staples. The modified fibroin staples thus produced were opened and then spun using a known spinning device to produce spun yarn. The spun yarn was knitted using a whole garment flat knitting machine (MACH2XS, manufactured by Shima Seiki Co., Ltd.) to produce a knitted fabric.

[0251] (4) Bonding of hydrophobic polymers to substrates (knitted fabrics) The obtained knitted fabric was coated with a fluorine-based coating monomer and subjected to plasma treatment using a plasma treatment device (manufactured by Europlasma). The plasma treatment resulted in a knitted fabric having a fluorine-based polymer (water resistance imparting substance) covalently bonded thereto, which was the polymerized fluorine-based coating monomer (Example 3). Nanofics120 (manufactured by Europlasma) was used as the fluorine-based coating monomer.

[0252] (5) Water repellency evaluation A water repellency test (spray test) was carried out on the plasma-treated knitted fabric of Example 3 and the non-plasma-treated knitted fabric (Comparative Example 2) in the same manner as in Test Example 1. The results are shown in Table 13. The non-plasma-treated knitted fabric of Comparative Example 2 received a score of 0, whereas the plasma-treated knitted fabric of Example 3 received a score of 5, indicating that it was imparted with water resistance (water repellency). [Table 13]

[0253] (6) Evaluation of texture and shrinkage Square test pieces with sides of 5 cm were cut out from the knitted fabrics of Example 3 and Comparative Example 2. Four vertices of a square with sides of 30 mm were marked with a pencil on one surface of the test pieces. As a preliminary treatment, each test piece was immersed in water at 40°C for 10 minutes, and then vacuum dried at room temperature. This process was repeated five times. The vacuum drying was performed for 30 minutes using a vacuum constant temperature dryer (VOS-310C, manufactured by Tokyo Rikakikai Co., Ltd.) at a set pressure of -0.1 MPa.

[0254] Next, the test piece that had undergone the preliminary treatment was subjected to five cycles of washing, drying, water immersion, and drying in this order. In the washing process, a Panasonic washing machine (NA-VG1100L) was used, and the test piece was washed for five minutes using a Lion detergent (Top Clear Liquid), rinsed twice, and then dehydrated for one minute. In the drying process, a vacuum constant temperature dryer (VOS-310C, Tokyo Rikakikai Co., Ltd.) was used to dry the test piece at room temperature for 30 minutes at a set pressure of -0.1 MPa. In the water immersion process, the test piece was immersed in water at 40°C for 10 minutes. At the end of each cycle, the tactile sensation was evaluated using the same criteria as in Test Example 1, and the shrinkage rate was evaluated by measuring the distance between the four marked points.

[0255] The sensory evaluation results for the tactile sensation are shown in Table 14. Note that "at the start" is the evaluation result after the preliminary treatment and before the cycle was started. The knitted fabric of Example 3, which was subjected to plasma treatment, showed less deterioration in tactile sensation than the knitted fabric of Comparative Example 2, which was not subjected to plasma treatment. [Table 14]

[0256] The evaluation results of the shrinkage percentage are shown in Table 15. The knitted fabric of Example 3, which was subjected to the plasma treatment, had a smaller shrinkage percentage than the knitted fabric of Comparative Example 2, which was not subjected to the plasma treatment. [Table 15]

[0257] From the results of Test Examples 3 and 4, it can be understood that part B can be formed by bonding a hydrophobic polymer to the surface of a substrate (woven or knitted fabric) by plasma treatment (and therefore the area other than part B is formed as part A).

[0258] [Test Example 5: Fabric Production] (1) Preparation of spinning solution (dope solution) DMSO in which lithium chloride was dissolved to a concentration of 4% by mass was used as a solvent, and the freeze-dried powder of the modified fibroin (PRT799) produced above was added to the solvent to a concentration of 24% by mass. After dissolving for 1 hour in an aluminum block heater at 90°C, insoluble matter and bubbles were removed to obtain a spinning solution (dope solution).

[0259] (2) Spinning The spinning solution was filled into a reserve tank and discharged from a monohole nozzle with a diameter of 0.1 or 0.2 mm into a 100% by mass methanol coagulation bath using a gear pump. The discharge rate was adjusted to 0.01 to 0.08 mL / min. After coagulation, washing and drawing were performed in a 100% by mass methanol washing bath. After washing and drawing, the fiber was dried using a dry heat plate, and the obtained raw yarn (modified fibroin fiber) was wound up.

[0260] (3) Manufacturing of base material (woven fabric) The modified fibroin fibers were then used to make ply-ply yarns, which were then plain woven to obtain woven fabrics.

[0261] (4) UV printing on the surface of the substrate (woven fabric) A UV printer (VersaUV LEF2-200, manufactured by Roland DG Corporation) was used to print a pattern on the obtained woven fabric, according to the pattern shown in Figure 3, so that the ink was fixed to the area corresponding to part B, and the ink was not fixed to the area corresponding to part A. The ink used was a mixture of equal amounts of the following six types of ink. A photograph of the obtained fabric is shown in Figure 4. EUV-CY Ver.2, manufactured by Roland DG Corporation EUV-MG Ver.2, manufactured by Roland DG Corporation EUV-YE Ver.2, manufactured by Roland DG Corporation EUV-BK Ver.2, manufactured by Roland DG Corporation EUV-WH Ver.2, manufactured by Roland DG Corporation EUV-GL Ver.2, manufactured by Roland DG Corporation The diameter of portion A (circular shape) was 1.5 cm, and the distance between portions A was 1.5 cm.

[0262] [Test Example 6: Production of three-dimensionally shaped fabric 6] The fabric obtained in Test Example 5 (see FIG. 4) was immersed in 70°C water for 1 minute and brought into contact with water. After immersion, the fabric was immediately removed, placed on a dry towel, and dried by applying hot air from a hair dryer. Next, the fabric was flattened by applying steam and pressure using an iron, to obtain a three-dimensionally shaped fabric 6. A photograph of the obtained three-dimensionally shaped fabric 6 is shown in FIG. 5.

[0263] As shown in Figure 5, upon contact with water, only part A, where the ink is not adhered, shrinks, forming folds between parts A, and the area of ​​part B sandwiched between the folds forms a convex portion (which appears as a concave portion when viewed from behind), forming a three-dimensional shape.

[0264] [Test Example 7: Production of three-dimensionally shaped fabric 7] Except for the pattern printed on the substrate, the same method as for the three-dimensionally shaped fabric 6 was carried out to produce the three-dimensionally shaped fabric 7, which has a different three-dimensional pattern from the three-dimensionally shaped fabric 6. A photograph of the produced three-dimensionally shaped fabric 7 is shown in FIG.

[0265] As shown in FIG. 11, it can be seen that by changing the printing pattern, it is possible to produce fabrics with various three-dimensional shapes. [Explanation of symbols]

[0266] 1...base material, 2...water-repellent or waterproof coating, 10, 20, 30, 40, 50...fabric.

Claims

1. The present invention comprises a substrate including artificial protein fibers containing proteins, and a water-repellent or waterproof coating that partially covers a surface of the substrate, a surface including a portion A which shrinks at a predetermined shrinkage rate when in contact with water and a portion B which shrinks at a smaller shrinkage rate when in contact with water than said portion A; The fabric, wherein the portion B is constituted by a portion covered by the coating film, and the portion A is constituted by a portion not covered by the coating film.

2. The fabric according to claim 1 , wherein the portion B is a portion that does not shrink upon contact with water.

3. The fabric according to claim 1 or 2, wherein a plurality of portions A are present.

4. The fabric according to any one of claims 1 to 3, wherein the portion A contains an artificial protein fiber that shrinks at a predetermined shrinkage rate upon contact with the water, while the portion B contains a fiber having a smaller shrinkage rate than the artificial protein fiber contained in the portion A.

5. The fabric according to claim 4 , wherein the portion B contains artificial protein fibers having a smaller shrinkage rate than the artificial protein fibers contained in the portion A.

6. At least the artificial protein fiber contained in the portion A has a dry shrinkage rate defined by the following formula I of more than 7%. The fabric according to any one of claims 1 to 5. Dry shrinkage rate={1-(length of dried artificial protein fiber / length of artificial protein fiber after spinning and before contact with water)}×100(%) (Formula I)

7. The fabric according to any one of claims 1 to 6, wherein the protein is a modified fibroin.

8. The present invention comprises a substrate including artificial protein fibers containing proteins, and a water-repellent or waterproof coating that partially covers a surface of the substrate, The present invention has a surface including a portion E which shrinks at a predetermined shrinkage rate upon contact with water, and a portion F which shrinks at a shrinkage rate smaller than that of the portion E upon contact with water or which does not shrink even upon contact with water, and on which a three-dimensional shape is formed due to the difference in shrinkage rate between the portion E and the portion F, The three-dimensionally shaped fabric, wherein the portion F is constituted by a portion covered by the coating film, and the portion E is constituted by a portion not covered by the coating film.

9. The three-dimensional shaped fabric according to claim 8, wherein the portion F is a portion that does not shrink even when contacted with water.

10. A method for producing a three-dimensionally shaped fabric, comprising a step of subjecting the fabric according to any one of claims 1 to 7 to a shrinkage treatment, the shrinkage treatment comprising contacting the fabric with water.

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