WO2019065764A1 - Procédé de production de fibre et procédé de production de tissu - Google Patents

Procédé de production de fibre et procédé de production de tissu Download PDF

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Publication number
WO2019065764A1
WO2019065764A1 PCT/JP2018/035752 JP2018035752W WO2019065764A1 WO 2019065764 A1 WO2019065764 A1 WO 2019065764A1 JP 2018035752 W JP2018035752 W JP 2018035752W WO 2019065764 A1 WO2019065764 A1 WO 2019065764A1
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Prior art keywords
protein
fiber
fabric
raw material
producing
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PCT/JP2018/035752
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English (en)
Japanese (ja)
Inventor
紘介 田山
成樹 荻野
内田　和広
正博 麻川
博幸 森
航 石田
上田　真也
Original Assignee
スーパーレジン工業株式会社
内浜化成株式会社
Ｓｐｉｂｅｒ株式会社
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Application filed by スーパーレジン工業株式会社, 内浜化成株式会社, Ｓｐｉｂｅｒ株式会社 filed Critical スーパーレジン工業株式会社
Priority to JP2019545577A priority Critical patent/JP7242539B2/ja
Publication of WO2019065764A1 publication Critical patent/WO2019065764A1/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
    • D02—YARNS; MECHANICAL FINISHING OF YARNS OR ROPES; WARPING OR BEAMING
    • D02J—FINISHING OR DRESSING OF FILAMENTS, YARNS, THREADS, CORDS, ROPES OR THE LIKE
    • D02J1/00—Modifying the structure or properties resulting from a particular structure; Modifying, retaining, or restoring the physical form or cross-sectional shape, e.g. by use of dies or squeeze rollers
    • D02J1/22—Stretching or tensioning, shrinking or relaxing, e.g. by use of overfeed and underfeed apparatus, or preventing stretch
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06C—FINISHING, DRESSING, TENTERING OR STRETCHING TEXTILE FABRICS
    • D06C7/00—Heating or cooling textile fabrics

Definitions

  • the present invention relates to a method of producing fibers and a method of producing fabrics.
  • Some protein fibers have the property of shrinking due to contact with moisture, heat (eg, immersion in water or hot water, exposure to a high humidity environment, etc.). This characteristic is a factor that causes various problems in the manufacturing process and productization.
  • Patent Document 1 immerses, in a tensioned state, a silk fabric of high twist yarn use after completion of refining in water, another solvent, or a mixed system thereof.
  • a shrink-proof processing method of silk fabric characterized by heating for a predetermined time.
  • Patent Document 2 describes a method of processing silk fibers which imparts washability and antifouling properties to silk fibers which are woven and formed into a dough-like shape, wherein water soluble cyanuric chloride derivatives or water soluble vinyl is added to the silk fibers.
  • a process for preventing deterioration using a sulfone derivative as a cross-linking agent, a shrink-proofing using any of a steaming method, a vacuum steaming method, or a sunfoliating method, and a water repelling process using a fluorine-based water repellent A method of processing silk fibers is disclosed.
  • protein fibers are expected as substitute fibers for fibers such as glass fibers and carbon fibers used for composite materials such as fiber reinforced plastic (FRP) from the increase of environmental awareness.
  • FRP fiber reinforced plastic
  • it is required to maintain a predetermined size and shape even when exposed to a high temperature environment (for example, 130 ° C. or higher) in the process of producing the composite material.
  • an object of the present invention is to provide a fiber containing protein and a method for producing the same, in which contraction due to heat is sufficiently suppressed.
  • Another object of the present invention is to provide a fabric having a protein-containing fiber and a method for producing the same, wherein contraction due to heat is sufficiently suppressed.
  • a method for producing a fiber comprising: preparing a raw material fiber containing a protein fiber, fixing the end of the raw material fiber, and heating the raw material fiber with the end fixed in a gas. .
  • the structural protein fiber comprises fibroin-like protein fiber.
  • a method for producing a fabric comprising: preparing a raw material fabric containing protein fibers; and fixing the outer peripheral portion of the raw material fabric, and heating the raw material fabric with the outer peripheral portion fixed in a gas. .
  • the heating step is a step of heating the raw material fabric to 100 ° C. or higher.
  • the present invention it is possible to provide a protein-containing fiber and a method for producing the same, in which thermal contraction is sufficiently suppressed. According to the present invention, it is possible to provide a fabric having a protein-containing fiber in which thermal contraction is sufficiently suppressed, and a method for producing the same.
  • FIG. 1 is a schematic view showing an example of a spinning apparatus for producing protein fibers.
  • the method for producing a fiber according to the present embodiment comprises preparing a raw material fiber containing protein fiber, fixing the end of the raw material fiber, and heating the raw material fiber having the fixed end fixed in a gas. And.
  • the protein is preferably a structural protein.
  • 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
  • the raw material fiber which concerns on this embodiment contains protein fiber.
  • the raw fiber preferably comprises protein fiber.
  • the protein fiber according to this embodiment is a fiber obtained by spinning the above-mentioned protein, preferably a fiber obtained by spinning a structural protein (structural protein fiber), more preferably a fiber obtained by spinning a fibroin-like protein (fibroin-like protein fiber ), Particularly preferably fibers obtained by spinning spider silk fibroin-like proteins (a spider silk fibroin-like protein fibers).
  • 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.
  • 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 protein fiber, a single yarn consisting only of protein fiber, and a composite yarn consisting of protein fiber and other fibers in combination are used alone or in combination. May be
  • 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.
  • a filament yarn is suitably used as the single yarn and the composite yarn.
  • the single yarn is preferably a twisted yarn, in which case 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 end portion of the raw material fiber including the protein fiber prepared as described above is fixed (fixing step).
  • Fixation of the raw material fiber may be any one as long as the shrinkage of the raw material fiber can be reduced (for example, less than 5% contraction rate based on the initial length of the raw material fiber) in the heating step described later. Fixation of the raw material fiber may be performed, for example, by stretching the raw material fiber of a predetermined length without loosening in a state where no external force is applied (natural state) and fixing the both ends of the fiber in this state.
  • the end of the raw fiber may be fixed as long as at least the end of the raw fiber is fixed, and the whole may be fixed by sandwiching the whole raw fiber between two metal plates.
  • the fixing means of the raw material fiber is not particularly limited, and any fixing means may be used.
  • the fixing means is preferably removable, and examples thereof include an adhesive tape, an adhesive, and a clamp.
  • the atmosphere is not limited,
  • the atmosphere, inert gas atmosphere, etc. may be sufficient.
  • the inert gas may, for example, be nitrogen or argon.
  • the heating step may be performed under pressurized conditions or reduced pressure conditions, as necessary.
  • the heating step may be performed in a near vacuum condition.
  • the heating temperature in the heating step may be appropriately selected according to the intended use environment of the fiber, and may be, for example, 100 ° C. or more, 110 ° C. or more, or 130 ° C. or more.
  • the heating temperature in the heating step is preferably 240 ° C. or less, more preferably 180 ° C. or less, still more preferably 150 ° C. or less, from the viewpoint of suppressing protein decomposition and the like.
  • 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 method for producing a fabric according to the present embodiment prepares a raw material cloth containing protein fibers, fixes the outer peripheral portion of the raw material cloth, and heats the raw material cloth with the outer peripheral portion fixed in a gas And.
  • the protein fiber As the protein fiber, the above-mentioned protein fiber can be used.
  • 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.
  • Known methods can be used as a method of producing a fabric containing protein fibers.
  • the fabric is manufactured by a weaving machine or a knitting machine.
  • the fabric is a non-woven fabric, it is produced by a known method such as a needle punch method.
  • the thickness of the fabric may be, for example, 1 mm or less, or 0.2 mm or less.
  • the fabric weight of the 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 outer peripheral part of the raw material fabric containing the protein fiber prepared as mentioned above is fixed (fixing process).
  • Fixation of the raw material fabric may be any one that can reduce the shrinkage of the raw material fabric (for example, less than 5% of the shrinkage rate based on the initial area of the raw material fabric) in the heating step.
  • Fixation of the raw material cloth may be performed, for example, by spreading the raw material cloth of a predetermined area in a state where no external force is applied (natural state) so as not to cause wrinkles and the like and fixing the outer peripheral portion of the raw material cloth in this state.
  • the fixing of the outer peripheral portion of the raw material fabric may be performed as long as a part or all of the outer peripheral portion of the raw material fabric is fixed, and the entire raw material fabric may be fixed by being sandwiched between two metal plates. Good.
  • the fixing means of the raw material fabric is not particularly limited, and any fixing means may be used.
  • the fixing means is preferably removable, and examples thereof include an adhesive tape, an adhesive, and a clamp.
  • the raw material fabric in a state in which the outer peripheral portion is fixed is heated in a gas (heating step).
  • the heating conditions may be performed under the same conditions as the heating process for the raw material fibers.
  • the fiber containing protein fiber or the fabric containing the protein fiber obtained by the manufacturing method according to the present embodiment is one in which the occurrence of shrinkage due to heat is sufficiently suppressed, and for example, high temperature treatment is included in the manufacturing process Can also be suitably used in composite materials such as fiber reinforced plastic (FRP).
  • FRP fiber reinforced plastic
  • the fiber or the fabric obtained by the method for producing a fiber according to the present embodiment and the method for producing a fabric has reduced shrinkage when exposed to heat.
  • shrinkage is considered to occur when the secondary structure or tertiary structure of the protein in the protein fiber is changed due to heating.
  • the raw material fiber or raw material fabric is heated. Since the end portion of the fiber or the outer peripheral portion of the raw material fabric is fixed, it is possible to suppress the dimensional change of the raw material fiber and the raw material fabric even if the above-mentioned change of the higher order structure occurs.
  • the fiber or fabric obtained by the method of manufacturing a fiber according to the present embodiment and the method of manufacturing a fabric becomes one in which the shrinkage due to heat is sufficiently suppressed. .
  • 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 woven fabric with spider silk fibroin-like protein fiber (preparation of ply yarn and woven fabric) 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). And the 0.2-mm-thick plain weave woven fabric (raw material cloth 1) was produced using this plied yarn. The fabric weight of the raw material fabric 1 was 114 g / m ⁇ 2 >. The raw material cloth 1 obtained above was cut into a length of 100 mm and a width of 100 mm to obtain a test piece 1.
  • test piece 1 obtained above was placed on a base plate (aluminum plate), and four sides (outer periphery) of the test piece 1 were fixed to the base plate with an adhesive tape.
  • the test piece 1 is placed in the same atmosphere as the atmosphere and in an oven adjusted to 130 ° C., heated for 1 hour, and then cooled at room temperature to obtain the target woven fabric 1. Obtained.
  • the obtained woven fabric 1 was placed on a base plate and, without being fixed, was allowed to stand in an oven adjusted to 130 ° C. and exposed to a high temperature environment for 1 hour.
  • the woven fabric 1 was checked visually with a ruler, and it was found that shrinkage was not seen even after exposure to an environment of 130 ° C. for 1 hour, and a shrink-proofing effect was obtained.
  • Example 1 The test piece 1 obtained above was evaluated in the same manner as Example 1. That is, the test piece 1 was placed on a base plate and, without being fixed, was allowed to stand in an oven adjusted to 130 ° C. and exposed to a high temperature environment for 1 hour. Similar to Example 1, when checked with a ruler and visually confirmed, the test piece 1 showed shrinkage. The shrinkage rate of the test piece 1 was a reduction of about 36% based on the area of the test piece 1 before exposure to the high temperature environment.
  • Example 2 In Example 1 described above, the adjusted test piece 1 was attached using a frame made of aluminum and the four sides were fixed using a clamp. The test piece 1 was immersed in the water of normal temperature (25 degreeC) for 30 minutes in this state. Then, it was naturally dried in the state which fixed the test piece 1 exposed to water. The test piece which cut the woven fabric after drying in length 100 mm x width 100 mm was made into the woven fabric C1.
  • the woven fabric C1 obtained above was evaluated in the same manner as in Example 1.
  • the shrinkage factor of the woven fabric C1 was a 36% reduction based on the area of the woven fabric C1 before exposure to the high temperature environment.
  • Example 2 The same test piece 1 was used as the test piece 1 described above.
  • test piece 2 obtained above was allowed to stand still in a flat plate-shaped mold press, and the test piece 2 was fixed by the flat metal plate by pressing the test piece 2 at 0.125 MPa to fix the entire surface of the test piece 2 .
  • the test piece 2 was heated by raising the set temperature of the mold press to 150 ° C. in the air over 30 minutes and holding it at 150 ° C. for 3 hours. Then, the target woven fabric 2 was obtained by cooling a metal mold at room temperature.
  • the obtained woven fabric 2 was evaluated as follows. That is, the obtained woven fabric 2 was placed on a base plate and, without being fixed, was allowed to stand in an oven adjusted to 150 ° C. and exposed to a high temperature environment for 1 hour. The woven fabric 2 was visually checked with a ruler, and it was found that shrinkage was not seen even after exposure to an environment of 150 ° C. for 1 hour, and a shrink-proofing effect was obtained.
  • Example 3 A woven fabric 3 was obtained in the same manner as in Example 2 except that the set temperature of the die press was changed to 130 ° C. The obtained woven fabric 3 was evaluated in the same manner as in Example 2. As a result, the shrinkage rate of the woven fabric 3 is 2% or less based on the area of the woven fabric 3 before exposure to a high temperature environment. It was confirmed that it was obtained.
  • Example 4 A woven fabric 4 was obtained in the same manner as in Example 2 except that the set temperature of the die press was changed to 110 ° C. The obtained woven fabric 4 was evaluated in the same manner as in Example 2. As a result, the shrinkage ratio of the woven fabric 4 is 3% or less based on the area of the woven fabric 3 before exposure to a high temperature environment. It was confirmed that it was obtained.

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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)
  • Yarns And Mechanical Finishing Of Yarns Or Ropes (AREA)

Abstract

La présente invention concerne, selon un aspect, un procédé de production de fibre qui comprend : une étape de fixation dans laquelle des fibres de matière de départ comprenant des fibres de protéine sont préparées et les extrémités des fibres de matière de départ sont fixées ; et une étape de chauffage dans laquelle les fibres de matière de départ dont les extrémités sont fixées sont chauffées dans un gaz.
PCT/JP2018/035752 2017-09-29 2018-09-26 Procédé de production de fibre et procédé de production de tissu WO2019065764A1 (fr)

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Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH03213565A (ja) * 1990-01-18 1991-09-18 Taikei Sangyo Kk 防縮性絹織物の製造法
JPH06294068A (ja) * 1993-04-02 1994-10-21 Nohashi Kk 動物繊維製品の形状固定化方法
JP2002371460A (ja) * 2001-04-10 2002-12-26 Five Foxes Co Ltd 絹織物に水洗い可能なプリーツをつける加工方法並びに水洗い可能なプリーツをつけた絹織物
JP2014029054A (ja) * 2012-06-28 2014-02-13 Spiber Inc 原着タンパク質繊維及びその製造方法

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH03213565A (ja) * 1990-01-18 1991-09-18 Taikei Sangyo Kk 防縮性絹織物の製造法
JPH06294068A (ja) * 1993-04-02 1994-10-21 Nohashi Kk 動物繊維製品の形状固定化方法
JP2002371460A (ja) * 2001-04-10 2002-12-26 Five Foxes Co Ltd 絹織物に水洗い可能なプリーツをつける加工方法並びに水洗い可能なプリーツをつけた絹織物
JP2014029054A (ja) * 2012-06-28 2014-02-13 Spiber Inc 原着タンパク質繊維及びその製造方法

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