WO2019065735A1 - Procédé de production de fibre ou de tissu - Google Patents

Procédé de production de fibre ou de tissu Download PDF

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Publication number
WO2019065735A1
WO2019065735A1 PCT/JP2018/035698 JP2018035698W WO2019065735A1 WO 2019065735 A1 WO2019065735 A1 WO 2019065735A1 JP 2018035698 W JP2018035698 W JP 2018035698W WO 2019065735 A1 WO2019065735 A1 WO 2019065735A1
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Prior art keywords
fiber
protein
fabric
raw material
container
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PCT/JP2018/035698
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English (en)
Japanese (ja)
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紘介 田山
成樹 荻野
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Ｓｐｉｂｅｒ株式会社
スーパーレジン工業株式会社
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Priority to JP2019545569A priority Critical patent/JPWO2019065735A1/ja
Publication of WO2019065735A1 publication Critical patent/WO2019065735A1/fr

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    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F4/00—Monocomponent artificial filaments or the like of proteins; Manufacture thereof
    • D01F4/02—Monocomponent artificial filaments or the like of proteins; Manufacture thereof from fibroin
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06B—TREATING TEXTILE MATERIALS USING LIQUIDS, GASES OR VAPOURS
    • D06B1/00—Applying liquids, gases or vapours onto textile materials to effect treatment, e.g. washing, dyeing, bleaching, sizing or impregnating
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06B—TREATING TEXTILE MATERIALS USING LIQUIDS, GASES OR VAPOURS
    • D06B23/00—Component parts, details, or accessories of apparatus or machines, specially adapted for the treating of textile materials, not restricted to a particular kind of apparatus, provided for in groups D06B1/00 - D06B21/00
    • D06B23/14—Containers, e.g. vats

Definitions

  • the present invention relates to a method of producing fibers or fabrics.
  • Protein fibers are expected to be substitutes for fibers such as glass fibers and carbon fibers used in composite materials such as fiber reinforced plastics (FRP) from the recent increase in environmental protection awareness. It is desirable that the protein fiber used in the composite material be more excellent in strength (in particular, tensile strength).
  • Patent Document 1 discloses a fiber strength improvement method characterized in that the surface of a treated fiber is treated with a fiber strength improver containing neutral glucomannan as an active ingredient.
  • Patent Document 2 discloses a silk sock knitted by using silk fiber having an antibacterial treatment on the surface, wherein the antibacterial treatment is performed by a treatment solution containing an astringent component and a resin compound. Is disclosed.
  • Patent Documents 1 and 2 are not necessarily simple methods because they use a fiber treatment agent such as a fiber strength improver or a treatment liquid.
  • an object of this invention is to provide the method of improving the tensile strength of the fiber or fabric containing protein fiber, without using a special fiber processing agent.
  • Another object of the present invention is to provide a method for producing a fiber or fabric containing a protein fiber excellent in tensile strength without using a special fiber treatment agent.
  • the present invention relates to, for example, the following inventions.
  • a first step of preparing a raw material fiber or raw material fabric containing protein fiber A second step of containing the raw material fiber or the raw material fabric in a deformable container and reducing the pressure in the container; A third step of heating and pressing the raw material fiber or the raw material fabric from the outside of the container under reduced pressure;
  • a method of producing a fiber or fabric comprising [2] The method for producing a fiber or fabric according to [1], wherein the deformable container is a bag material. [3] The method for producing a fiber or fabric according to [1] or [2], wherein the protein fiber comprises a structural protein fiber.
  • the present invention it is possible to provide a method for improving the tensile strength of a fiber or fabric containing protein fibers without using a special fiber treatment agent. According to the present invention, it is also possible to provide a method for producing a fiber or fabric containing protein fibers excellent in tensile strength, without using a special fiber treatment agent.
  • FIG. 1 is a schematic view showing an example of a spinning apparatus for producing protein fibers.
  • FIG. 2 is a diagram showing the results of the tensile test in Example 1.
  • FIG. 3 is a view showing the results of the tensile test in Comparative Example 1.
  • FIG. 4 is a view showing the results of the tensile test in Comparative Example 2.
  • a first step of preparing a raw material fiber or fabric containing protein fibers, the raw material fibers or the raw material fabric is accommodated in a deformable container, and the pressure in the container is reduced.
  • a raw material fiber or raw material fabric containing a protein fiber is prepared (first step).
  • the raw material fiber is a fiber containing protein fiber, preferably a fiber consisting of protein fiber.
  • the raw material fabric is a fabric containing protein fibers, preferably a fabric made of protein fibers.
  • the protein fiber which concerns on this embodiment can mention the fiber which spun the protein mentioned later, for example.
  • the protein fiber is preferably a fiber into which a structural protein is spun (structural protein fiber), more preferably a fiber into which a fibroin-like protein is spun (fibroin-like protein fiber), particularly preferably a fiber into which a spider silk fibroin-like protein is spun ( Spider silk fibroin-like protein fiber).
  • the protein fibers may be short fibers or long fibers. Also, protein fibers may be used alone or in combination with other fibers. That is, when preparing a raw material fiber containing a protein fiber, a single yarn made of only a protein fiber or a composite yarn made of a combination of a protein fiber and another fiber may be prepared individually, or A combination of yarns or the above composite yarns may be prepared.
  • the single yarn and the composite yarn may be a spun yarn in which short fibers are twisted together, or may be a filament yarn in which long fibers are twisted together.
  • the single yarn and the composite yarn are preferably filament yarns.
  • the single yarn is preferably a twisted yarn.
  • the twisted yarn may be a Z-twisted yarn or an S-twisted yarn.
  • Composite yarns include, for example, blended yarns, mixed yarns, covering yarns and the like.
  • the other fibers are fibers that do not contain protein.
  • Other fibers include, for example, synthetic fibers such as nylon and polyester, regenerated fibers such as cupra and rayon, and natural fibers such as cotton and hemp.
  • the content of protein fiber is preferably 5% by mass or more, more preferably 20% by mass or more, based on the total amount of the raw material fiber including protein fiber. Preferably it is 50 mass% or more.
  • the type of raw material fabric containing protein fiber is not particularly limited.
  • the fabric may be, for example, a woven fabric, a knitted fabric, and a non-woven fabric.
  • the fabric is preferably a woven fabric.
  • the woven structure may be, for example, plain weave, twill weave, satin weave, and the like.
  • the knit may be a warp knit such as tricot and russell, or a weft knit such as a weft knit and a circular knit.
  • a structural protein refers to a protein that forms a biological structure or a protein derived therefrom. That is, the structural protein may be a naturally occurring structural protein, and is a modified protein in which a portion (for example, 10% or less of the amino acid sequence) of the amino acid sequence is altered based on the amino acid sequence of the naturally occurring structural protein. It may be.
  • structural proteins include fibroin (eg, spider silk, silkworm silk, etc.), collagen, resilin, elastin and keratin, and proteins derived therefrom.
  • fibroin-like proteins examples include, for example, proteins containing a domain sequence represented by the formula 1: [(A) n motif-REP1] m .
  • A represents an alanine residue
  • n is preferably an integer of 2 to 27, an integer of 4 to 20, an integer of 8 to 20, or 10 to 20. It may be an integer, an integer of 4 to 16, an integer of 8 to 16, or an integer of 10 to 16.
  • the number of alanine residues relative to the total number of amino acid residues in (A) n motif may be 40% or more, 60% or more, 70% or more, 80% or more, 90% or more, or 100% (Meaning composed of only alanine residues).
  • REP1 shows an amino acid sequence composed of 10 to 200 amino acid residues. m represents an integer of 10 to 300.
  • the plurality of (A) n motifs may be identical to each other or different from each other.
  • the plurality of REP1 may have the same or different amino acid sequences.
  • a fibroin-like protein for example, a protein comprising the amino acid sequence shown by SEQ ID NO: 1 can be mentioned.
  • collagen-like proteins examples include, for example, proteins containing a domain sequence represented by Formula 2: [REP2] p .
  • p represents an integer of 5 to 300.
  • REP2 represents an amino acid sequence composed of Gly-XY, and X and Y represent any amino acid residues other than Gly.
  • the plurality of REP2 may be identical to each other or different from each other.
  • the protein containing the amino acid sequence shown by sequence number 2 can be mentioned, for example.
  • amino acid sequence shown by SEQ ID NO: 2 is a repeat portion and motif of a partial sequence of human collagen type 4 (GenBank accession numbers of NCBI: CAA56335.1, GI: 3702452) obtained from the NCBI database.
  • the amino acid sequence (tag sequence and hinge sequence) shown in SEQ ID NO: 6 is added to the N-terminus of the amino acid sequence from residue 301 to residue 540 corresponding to
  • resilin-like proteins examples include, for example, proteins containing a domain sequence represented by Formula 3: [REP3] q .
  • q represents an integer of 4 to 300.
  • REP3 shows an amino acid sequence composed of Ser-J-J-Tyr-Gly-U-Pro.
  • J is any amino acid residue, preferably an amino acid residue selected from the group consisting of Asp, Ser and Thr.
  • U is any amino acid residue, preferably an amino acid residue selected from the group consisting of Pro, Ala, Thr and Ser.
  • the plurality of REP3 may be identical to each other or different from each other.
  • resilin-like protein for example, a protein comprising the amino acid sequence shown by SEQ ID NO: 3 can be mentioned.
  • Th in position 87 is substituted with Ser in the amino acid sequence of resilin (Genci Accession Nos. NP 611 157, Gl: 24654243 of NCBI), and 95
  • the amino acid sequence shown by SEQ ID NO: 7 (His tag sequence) is added to the N-terminus of the amino acid sequence from the 19th residue to the 321st residue of the sequence in which Asn is substituted with Asp.
  • elastin-like proteins examples include proteins having amino acid sequences such as NCBI Accession Nos. AAC98395 (human), I47076 (sheep) and NP786966 (bovine) from GenBank.
  • elastin-like protein for example, a protein comprising the amino acid sequence shown by SEQ ID NO: 4 can be mentioned.
  • the amino acid sequence shown by SEQ ID NO: 4 is the amino acid sequence shown by SEQ ID NO: 6 at the N-terminal of the amino acid sequence from the 121st residue to the 390rd residue of the amino acid sequence of Accession No. AAC98395 of NCBI GenBank. (Tag sequence and hinge sequence) are added.
  • keratin-like proteins examples include, for example, type I keratin of Capra hircus and the like.
  • a keratin-like protein for example, a protein comprising the amino acid sequence shown in SEQ ID NO: 5 (the amino acid sequence of NCBI GenBank accession number ACY30466) can be mentioned.
  • the structural protein is preferably a fibroin-like protein, more preferably a spider silk fibroin-like protein.
  • the protein according to the present embodiment is, for example, a host transformed with an expression vector having a nucleic acid sequence encoding a protein of interest and one or more regulatory sequences operably linked to the nucleic acid sequence. What was produced by expressing the said nucleic acid can be used.
  • the nucleic acid can be produced by a method of amplification and cloning by polymerase chain reaction (PCR) or the like, or chemical synthesis, using a gene encoding a natural structural protein.
  • the chemical synthesis method of the nucleic acid is not particularly limited, and, for example, AKTA oligopilot plus 10/100 (manufactured by GE Healthcare Japan Co., Ltd.) based on the amino acid sequence information of the structural protein obtained from the NCBI web database etc.
  • Nucleic acids can be chemically synthesized by a method of linking oligonucleotides that have been automatically synthesized by PCR etc. by PCR etc.
  • the regulatory sequence is a sequence that controls the expression of a recombinant protein in a host (for example, a promoter, an enhancer, a ribosome binding sequence, a transcription termination sequence, etc.), and can be appropriately selected depending on the type of host.
  • a promoter an inducible promoter which functions in a host cell and is capable of inducible expression of a target protein may be used.
  • An inducible promoter is a promoter that can control transcription by physical factors such as the presence of an inducer (expression inducer), the absence of a repressor molecule, or the increase or decrease of temperature, osmotic pressure or pH value.
  • the type of expression vector may be a plasmid vector, a viral vector, a cosmid vector, a fosmid vector, an artificial chromosome vector or the like, and can be appropriately selected according to the type of host.
  • a vector capable of autonomous replication in a host cell or capable of integration into the host chromosome and containing a promoter at a position capable of transcribing a nucleic acid encoding a target protein is suitably used. .
  • any of prokaryotes and eukaryotes such as yeast, filamentous fungi, insect cells, animal cells and plant cells can be suitably used.
  • prokaryote examples include bacteria belonging to the genus Escherichia, Brevibacillus, Serratia, Bacillus, Microbacterium, Microbacterium, Brevibacterium, Corynebacterium and Pseudomonas.
  • examples of vectors for introducing a nucleic acid encoding a target protein include pBTrp2 (manufactured by Boehringer Mannheim), pGEX (manufactured by Pharmacia), pUC18, pBluescriptII, pSupex, pET22b, pCold, Examples thereof include pUB110 and pNCO2 (Japanese Patent Application Laid-Open No. 2002-238569).
  • Eukaryotic hosts can include, for example, yeast and filamentous fungi (molds and the like).
  • yeast the yeast which belongs to Saccharomyces genus, Pichia genus, Schizosaccharomyces genus etc. can be mentioned, for example.
  • filamentous fungi include filamentous fungi belonging to the genus Aspergillus, Penicillium, and Trichoderma.
  • examples of vectors into which a nucleic acid encoding a target protein is introduced include YEp13 (ATCC 37115) and YEp24 (ATCC 37051).
  • any method of introducing DNA into the host cell can be used.
  • a method for introducing the expression vector into the host cell for example, a method using calcium ion [Proc. Natl. Acad. Sci. USA, 69, 2110 (1972)], electroporation method, spheroplast method, protoplast method, lithium acetate method, competent method and the like.
  • a method for expressing a nucleic acid by a host transformed with an expression vector in addition to direct expression, secretory production, fusion protein expression, etc. may be performed according to the method described in Molecular Cloning 2nd Edition, etc. it can.
  • the target protein can be produced, for example, by culturing a host transformed with an expression vector in a culture medium, causing the protein to be produced and accumulated in the culture medium, and collecting the protein from the culture medium.
  • the method of culturing the host in a culture medium can be carried out according to a method usually used for culturing the host.
  • the culture medium for the host contains a carbon source, nitrogen source, inorganic salts and the like that can be used by the host, and the host can be cultured efficiently.
  • a natural medium or a synthetic medium may be used as long as the medium can be used.
  • the carbon source may be any source as long as the transformed host can assimilate, for example, glucose, fructose, sucrose, and molasses containing them, carbohydrates such as starch and starch hydrolysate, acetic acid and propionic acid And the like, and alcohols such as ethanol and propanol can be used.
  • Nitrogen sources include, for example, ammonium, ammonium salts of inorganic acids or organic acids such as ammonia, ammonium chloride, ammonium sulfate, ammonium acetate and ammonium phosphate, other nitrogen-containing compounds, peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal and soybean meal hydrolyzate, various fermented cells and digests thereof can be used.
  • inorganic acids or organic acids such as ammonia, ammonium chloride, ammonium sulfate, ammonium acetate and ammonium phosphate
  • other nitrogen-containing compounds such as peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal and soybean meal hydrolyzate, various fermented cells and digests thereof can be used.
  • potassium monophosphate potassium monobasic, magnesium phosphate, magnesium sulfate, sodium chloride, ferrous sulfate, manganese sulfate, copper sulfate, calcium carbonate and the like can be used.
  • the culture of a prokaryote such as E. coli or a eukaryote such as yeast can be performed under aerobic conditions such as shake culture or submerged aeration culture, for example.
  • the culture temperature is, for example, 15 to 40 ° C.
  • the culture time is usually 16 hours to 7 days.
  • the pH of the culture medium during culture is preferably maintained at 3.0 to 9.0. Adjustment of the pH of the culture medium can be carried out using an inorganic acid, an organic acid, an alkaline solution, urea, calcium carbonate, ammonia and the like.
  • Antibiotics such as ampicillin and tetracycline may be added to the culture medium as needed during culture.
  • an inducer may be added to the medium as needed.
  • indole acrylic An acid or the like may be added to the medium.
  • Isolation and purification of the target protein produced and accumulated by the host can be performed by a commonly used method. For example, when the protein is expressed in a dissolved state in cells, after completion of culture, host cells are recovered by centrifugation and suspended in an aqueous buffer, and then sonicator, French press, Manton Gaulin The host cells are disrupted by a homogenizer, dynomill or the like to obtain a cell-free extract. From the supernatant obtained by centrifuging the cell-free extract, a purified preparation can be obtained by a method usually used for protein isolation and purification.
  • the host cell when the protein forms an insoluble form in cells and is expressed, the host cell is similarly recovered and then disrupted and centrifuged to recover the insoluble form of the protein as a precipitate fraction.
  • the recovered insoluble form of protein can be solubilized with a protein denaturant. After the operation, a purified preparation of protein can be obtained by the same isolation and purification method as described above.
  • the protein When the protein is secreted extracellularly, the protein can be recovered from the culture supernatant. That is, the culture supernatant is treated by a method such as centrifugation to obtain a culture supernatant, and a purified preparation can be obtained from the culture supernatant by using the same isolation and purification method as described above.
  • Methods commonly used for isolation and purification of proteins include solvent extraction, salting out with ammonium sulfate, desalting, precipitation with organic solvents, diethylaminoethyl (DEAE) -sepharose, DIAION HPA-75
  • Protein fibers can be produced by spinning proteins by known spinning methods. That is, when producing a protein fiber, first, the protein produced according to the above-mentioned method may be dimethylsulfoxide (DMSO), N, N-dimethylformamide (DMF), or hexafluoroisopronol (HFIP), etc. It is added to a solvent together with an inorganic salt as a dissolution promoter and dissolved to prepare a dope solution. Then, using this dope solution (spinning stock solution), it can be spun by a known spinning method such as wet spinning, dry spinning or dry-wet spinning to obtain the target protein fiber.
  • DMSO dimethylsulfoxide
  • DMF N, N-dimethylformamide
  • HFIP hexafluoroisopronol
  • FIG. 1 is a schematic view showing an example of a spinning apparatus for producing protein fibers.
  • the spinning device 10 shown in FIG. 1 is an example of a spinning device for dry-wet spinning, and comprises an extrusion device 1, a coagulation bath 20, a washing bath 21, and a drying device 4 in this order from the upstream side. .
  • the extrusion device 1 has a storage tank 7, in which a dope solution (spinning stock solution) 6 is stored.
  • Coagulation liquid 11 eg, methanol
  • the dope solution 6 is pushed out from a nozzle 9 provided by opening a air gap 19 between the dope solution 6 and the coagulating solution 11 by a gear pump 8 attached to the lower end of the storage tank 7.
  • the extruded dope 6 is supplied into the coagulating liquid 11 through the air gap 19.
  • the solvent is removed from the dope solution 6 in the coagulation solution 11 to coagulate the protein.
  • the coagulated protein is guided to the washing bath 21 and washed with the washing liquid 12 in the washing bath 21, and then sent to the drying device 4 by the first nip roller 13 and the second nip roller 14 installed in the washing bath 21.
  • a protein fiber 36 drawn at a magnification corresponding to the rotational speed ratio is obtained.
  • the protein fibers 36 drawn in the washing solution 12 are released when passing through the washing bath 21 and then dried when passing through the drying device 4 and then taken up by a winder.
  • the protein fiber 36 is obtained by the spinning device 10 as a roll 5 which is finally wound on a winder.
  • Reference numerals 18a to 18g denote yarn guides.
  • the coagulating solution 11 may be an organic solvent capable of extracting (desolving) the solvent from the dope 6 extruded from the nozzle 9.
  • organic solvents include lower alcohols having 1 to 5 carbon atoms such as methanol, ethanol and 2-propanol, and acetone.
  • the coagulation liquid 11 may contain water as appropriate.
  • the temperature of the coagulating solution 11 is preferably 0 to 30 ° C.
  • the distance the coagulated protein passes in the coagulation liquid 11 (substantially, the distance from the yarn guide 18a to the yarn guide 18b) may be any length that enables efficient solvent removal, for example, 200 to 500 mm It is.
  • the residence time in the coagulating liquid 11 may be, for example, 0.01 to 3 minutes, preferably 0.05 to 0.15 minutes.
  • the fiber containing the coagulated protein may be drawn (pre-stretched) in the coagulating liquid 11.
  • Mainly water can be used as the cleaning liquid 12.
  • the cleaning solution 12 may include those listed as agents for use in the coagulation solution 11.
  • the stretching performed in the washing bath 21 when obtaining the protein fiber may be so-called wet heat stretching performed in warm water, in a solution in which an organic solvent or the like is added to warm water, or the like.
  • the temperature of the wet heat drawing may be, for example, 50 to 90 ° C., preferably 75 to 85 ° C.
  • the undrawn yarn (or pre-drawn yarn) can be drawn, for example, 1 to 10 times, preferably 2 to 8 times.
  • the protein fiber When passing through the drying device 4 in the present embodiment, the protein fiber may be further drawn (so-called dry heat drawing).
  • the lower limit of the draw ratio of the final protein fiber is preferably more than 1 time, 2 times or more, 3 times or more, 4 times or more, 5 times or more of the lower limit of the unstretched yarn (or pre-drawn yarn). , 6 times or more, 7 times or more, 8 times or more, or 9 times or more, and the upper limit thereof is preferably 40 times or less, 30 times or less, 20 times or less, 15 times or less, 14 times or less, 13 times Hereinafter, it is 12 times or less, 11 times or less, or 10 times or less.
  • a known method can be used as a method of producing a raw material fabric containing protein fibers.
  • the raw material fabric is produced by a weaving machine or a knitting machine.
  • a raw material fabric is a nonwoven fabric, it is produced by well-known methods, such as a needle punch method.
  • the thickness of the raw material fabric may be, for example, 1 mm or less, or 0.2 mm or less.
  • the fabric weight of the raw material fabric may be, for example, 1 g / m 2 or more, 50 g / m 2 or more, 80 g / m 2 or more, or 100 g / m 2 or more.
  • the raw material fiber or raw material fabric containing the protein fiber prepared as described above is accommodated in a deformable container, and the pressure in the container is reduced (second step).
  • the deformable container can be deformed to closely adhere to the raw material fiber stored in the container when the pressure in the container is reduced to increase the degree of vacuum, and the degree of vacuum can be maintained. I say a container.
  • the raw material fiber or raw material fabric is accommodated in the container, and the pressure in the container is reduced, whereby the container itself shields the raw material fiber or raw material fabric from the external atmosphere.
  • the raw material fiber or raw material fabric stored in the container is shielded from the external gas and the like by the container.
  • the degree of vacuum in the container is increased, the deformable fiber is fixed so as to be in close contact with the raw material fiber or raw material fabric accommodated inside, thereby fixing the raw material fiber or raw material fabric.
  • the raw material fiber or raw material fabric present inside the container is pressurized by the pressure difference between the pressure inside the container and the pressure outside the container.
  • the deformable container is preferably a bag having a bag made of film material.
  • a bag film etc. are mentioned, for example.
  • the deformable container may be any airtight film-like one, for example, a fluorine-based material such as polyethylene terephthalate (PET), polypropylene (PP), polytetrafluoroethylene (PTFE) and polyvinylidene fluoride (PVDF). It is formed of film, nylon 6, nylon 6, 6, polyethylene, rubber, polyimide, and polyetheretherketone (PEEK).
  • the degree of vacuum in the container is preferably 30 kPa or less, more preferably 20 kPa or less, and still more preferably 10 kPa or less.
  • the degree of vacuum in the container can be confirmed by a manometer.
  • the second step may be a step including replacing the inside of the container with, for example, dry air, an inert gas atmosphere, or the like before reducing the pressure in the container after storing the raw material fiber in the container.
  • Nitrogen, argon, etc. can be mentioned as an inert gas.
  • the raw material fiber or the raw material fabric is heated and pressurized from the outside of the container decompressed as described above (third step).
  • the heating and pressurizing in the third step may be performed simultaneously, or may be performed after heating the material fiber or the material fabric. Heating and pressurization are preferably performed simultaneously.
  • the third step can be performed, for example, using an autoclave or the like.
  • the heating temperature is preferably 50 ° C. or more, more preferably 70 ° C. or more, and still more preferably 100 ° C. or more. It is excellent by the improvement effect of the tensile strength of a fiber and a fabric as heating temperature is 100 degreeC or more.
  • the heating temperature is preferably 240 ° C. or less, more preferably 180 ° C. or less, and still more preferably 150 ° C. or less, from the viewpoint of further suppressing the decomposition and the like of the protein.
  • the heating temperature means the ambient temperature at which the raw material fiber or the container containing the raw material fabric is placed, and usually means the set temperature of an autoclave or the like.
  • the heating temperature may be constant or may be adjusted to gradually increase the temperature.
  • the heating time is not particularly limited, and may be, for example, 30 minutes or more, or 50 minutes or more.
  • the heating time may also be, for example, 5 hours or less, or 3 hours or less.
  • the pressure at the time of pressurization is preferably 0.05 MPa or more, more preferably 0.08 MPa or more, and still more preferably 0.1 MPa or more.
  • the pressure is 0.05 MPa or more, the effect of improving the tensile strength of fibers and fabrics is excellent.
  • the pressure is 0.05 MPa or more, not only the tensile strength improvement effect but also the elongation improvement effect and the heat shrinkage prevention effect can be obtained.
  • the pressure means the pressure of the environment in which the raw material fiber or the container containing the raw material fabric is placed, and usually means the set pressure of an autoclave or the like.
  • the fiber or fabric containing protein fiber obtained by the manufacturing method according to the present embodiment is excellent in tensile strength.
  • the tensile strength of a fiber or fabric containing protein fibers obtained by the manufacturing method according to this embodiment can be, for example, 5 N or more, and can be improved by 50% or more from the initial tensile strength.
  • the tensile strength is a value measured by a tensile tester (load measuring device LTS manufactured by Minebea Mitsumi Co., Ltd.), and indicates the maximum load value observed until breakage.
  • amino acid sequence shown by SEQ ID NO: 1 has an amino acid sequence obtained by substituting, inserting and deleting amino acid residues for the purpose of improving the productivity with respect to the amino acid sequence of fibroin derived from Nephila clavipes
  • amino acid sequence (tag sequence and hinge sequence) shown in SEQ ID NO: 6 is added to the N-terminus.
  • nucleic acid encoding PRT799 was synthesized.
  • the NdeI site at the 5 'end and the EcoRI site downstream of the stop codon were added to the nucleic acid.
  • the nucleic acid was cloned into a cloning vector (pUC118). Thereafter, the same nucleic acid was digested with NdeI and EcoRI, cut out, and then recombined into a protein expression vector pET-22b (+) to obtain an expression vector.
  • Protein expression E. coli BLR (DE3) was transformed with pET22b (+) expression vector containing a nucleic acid encoding a protein having the amino acid sequence shown by SEQ ID NO: 1.
  • the transformed E. coli was cultured in 2 mL of LB medium containing ampicillin for 15 hours.
  • the culture solution was added to 100 mL of seed culture medium (Table 1) containing ampicillin so that the OD 600 was 0.005.
  • the culture solution temperature was maintained at 30 ° C., and flask culture was performed until the OD 600 reached 5 (about 15 hours) to obtain a seed culture solution.
  • the seed culture solution was added to a jar fermenter to which 500 mL of production medium (Table 2) was added so that the OD 600 was 0.05.
  • the temperature of the culture solution was maintained at 37 ° C., and the culture was controlled at a constant pH of 6.9. Also, the dissolved oxygen concentration in the culture solution was maintained at 20% of the dissolved oxygen saturation concentration.
  • the feed solution (glucose 455 g / 1 L, Yeast Extract 120 g / 1 L) was added at a rate of 1 mL / min.
  • the temperature of the culture solution was maintained at 37 ° C., and the culture was controlled at a constant pH of 6.9. Further, the culture was carried out for 20 hours while maintaining the dissolved oxygen concentration in the culture solution at 20% of the dissolved oxygen saturation concentration. Thereafter, 1 M isopropyl- ⁇ -thiogalactopyranoside (IPTG) was added to the culture solution to a final concentration of 1 mM to induce expression of the target protein. Twenty hours after the addition of IPTG, the culture solution was centrifuged to recover the cells. SDS-PAGE was performed using cells prepared from the culture solution before IPTG addition and after IPTG addition, and the expression of the target protein was confirmed by the appearance of a band of the target protein size depending on IPTG addition.
  • IPTG isopropyl- ⁇ -thiogalactopyranoside
  • the washed precipitate is suspended in 8 M guanidine buffer (8 M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0) to a concentration of 100 mg / mL, and 30 at 60 ° C. Stir with a stirrer for a minute to dissolve. After dissolution, dialysis was performed with water using a dialysis tube (cellulose tube 36/32 manufactured by Sanko Pure Chemical Industries, Ltd.). The white aggregated protein obtained after dialysis was recovered by centrifugation, the water was removed by a lyophilizer, and the lyophilized powder was recovered to obtain a spider silk fibroin-like protein "PRT 799".
  • 8 M guanidine buffer 8 M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0
  • DMSO dimethylsulfoxide
  • Example 1 Preparation of ply yarn using spider silk fibroin-like protein fiber> A plurality of monofilaments obtained as described above are bundled into 180 denier to obtain a Z-twisted twisted yarn. Two such twisted yarns were used to obtain a 360 denier ply yarn (raw material fiber 1). The obtained raw material fiber 1 was obtained.
  • the raw material fiber 1 was accommodated in a bag material, and the degree of vacuum was adjusted until the internal pressure became 400 Pa by a vacuum pump inside the bag material.
  • the raw material fiber 1 contained in a vacuum bag and placed under reduced pressure was placed in an autoclave apparatus while being contained in a bag material, and then heated and pressurized under the following conditions.
  • the set temperature of the autoclave was raised to 40 ° C.
  • the temperature was gradually raised to 130 ° C. at a temperature rising rate of 2 ° C./min, and after reaching 130 ° C., the temperature was maintained at this temperature for 2 hours. During this time, the pressure was maintained at 0.3 MPa.
  • the target fiber 1 was obtained by removing the fibers from the vacuum bag after heating and pressing.
  • FIG. 2 is a view showing the results of the tensile test in Example 1, and is a view showing the stress-strain characteristics obtained in Example 1.
  • FIG. 3 is a diagram showing the results of the tensile test in Comparative Example 1, and is a diagram showing the stress-strain characteristics obtained in Comparative Example 1.
  • Example 2 The raw material fiber 1 prepared in Example 1 is put into the bag material, and the raw material fiber 1 is placed on a base plate (aluminum plate) instead of the operation of reducing the pressure inside the bag material, Fixed.
  • the raw material fiber 1 was placed in an autoclave together with a fixed base plate, and heated and pressed under the same conditions as in Example 1 with the raw material fiber exposed in the space in the autoclave.
  • a tensile test was conducted in the same manner as in Example 1 using the fiber thus obtained as a sample.
  • FIG. 4 is a diagram showing the results of the tensile test in Comparative Example 2, and is a diagram showing the stress-strain characteristics obtained in Comparative Example 2.
  • the fiber obtained by the method according to the present invention has an improved tensile strength as compared with the raw material fiber.

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  • Engineering & Computer Science (AREA)
  • Textile Engineering (AREA)
  • Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Peptides Or Proteins (AREA)
  • Treatment Of Fiber Materials (AREA)
  • Artificial Filaments (AREA)

Abstract

La présente invention concerne, selon un aspect, un procédé de production d'une fibre ou d'un tissu, le procédé comprenant : une première étape consistant à préparer un tissu brut, ou un tissu brut contenant respectivement une fibre de protéine ; une deuxième étape consistant à placer la fibre brute ou le tissu brut dans un récipient déformable et à décomprimer l'intérieur du récipient ; et une troisième étape consistant à chauffer et à mettre sous pression la fibre brute ou le tissu brut depuis l'extérieur du récipient décomprimé.
PCT/JP2018/035698 2017-09-29 2018-09-26 Procédé de production de fibre ou de tissu WO2019065735A1 (fr)

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Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US11001679B2 (en) 2016-02-15 2021-05-11 Modern Meadow, Inc. Biofabricated material containing collagen fibrils
US11214844B2 (en) 2017-11-13 2022-01-04 Modern Meadow, Inc. Biofabricated leather articles having zonal properties
US11352497B2 (en) 2019-01-17 2022-06-07 Modern Meadow, Inc. Layered collagen materials and methods of making the same

Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS5126385A (en) * 1974-08-28 1976-03-04 Tore Textile Entojohisenbutsu no senshokuhoho
JPS61244524A (ja) * 1985-04-23 1986-10-30 Takeshi Honda 成形用フエルト材の化粧成形方法
JPS63159572A (ja) * 1986-12-22 1988-07-02 山本　和夫 かさ高不織布の圧縮復元方法とその装置
JPH06123053A (ja) * 1992-10-08 1994-05-06 Ashida Seisakusho:Kk 巻糸の蒸熱セット方法
JP2001262461A (ja) * 2000-03-16 2001-09-26 Ishikawa Pref Gov 編織物の仕上げ加工方法
JP2009280947A (ja) * 2008-04-25 2009-12-03 Mitsubishi Rayon Co Ltd 蓄熱性布帛および中綿用不織布

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20210388557A1 (en) * 2017-03-10 2021-12-16 Spiber Inc. Method for Producing Protein Fiber, and Method for Shrinking Protein Fiber

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS5126385A (en) * 1974-08-28 1976-03-04 Tore Textile Entojohisenbutsu no senshokuhoho
JPS61244524A (ja) * 1985-04-23 1986-10-30 Takeshi Honda 成形用フエルト材の化粧成形方法
JPS63159572A (ja) * 1986-12-22 1988-07-02 山本　和夫 かさ高不織布の圧縮復元方法とその装置
JPH06123053A (ja) * 1992-10-08 1994-05-06 Ashida Seisakusho:Kk 巻糸の蒸熱セット方法
JP2001262461A (ja) * 2000-03-16 2001-09-26 Ishikawa Pref Gov 編織物の仕上げ加工方法
JP2009280947A (ja) * 2008-04-25 2009-12-03 Mitsubishi Rayon Co Ltd 蓄熱性布帛および中綿用不織布

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US11001679B2 (en) 2016-02-15 2021-05-11 Modern Meadow, Inc. Biofabricated material containing collagen fibrils
US11214844B2 (en) 2017-11-13 2022-01-04 Modern Meadow, Inc. Biofabricated leather articles having zonal properties
US11352497B2 (en) 2019-01-17 2022-06-07 Modern Meadow, Inc. Layered collagen materials and methods of making the same

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