WO2019151341A1 - Article moulé en résine renforcée par des fibres et procédé de fabrication d'un article moulé en résine renforcée par des fibres - Google Patents

Article moulé en résine renforcée par des fibres et procédé de fabrication d'un article moulé en résine renforcée par des fibres Download PDF

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WO2019151341A1
WO2019151341A1 PCT/JP2019/003218 JP2019003218W WO2019151341A1 WO 2019151341 A1 WO2019151341 A1 WO 2019151341A1 JP 2019003218 W JP2019003218 W JP 2019003218W WO 2019151341 A1 WO2019151341 A1 WO 2019151341A1
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Prior art keywords
fiber
woven fabric
amino acid
reinforced resin
resin molded
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PCT/JP2019/003218
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English (en)
Japanese (ja)
Inventor
昌己 竹本
竹市　親史
謙 今村
雄太 久野
上田　真也
内田　和広
正博 麻川
博幸 森
航 石田
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小島プレス工業株式会社
内浜化成株式会社
Ｓｐｉｂｅｒ株式会社
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Publication of WO2019151341A1 publication Critical patent/WO2019151341A1/fr

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    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B5/00—Layered products characterised by the non- homogeneity or physical structure, i.e. comprising a fibrous, filamentary, particulate or foam layer; Layered products characterised by having a layer differing constitutionally or physically in different parts
    • B32B5/22—Layered products characterised by the non- homogeneity or physical structure, i.e. comprising a fibrous, filamentary, particulate or foam layer; Layered products characterised by having a layer differing constitutionally or physically in different parts characterised by the presence of two or more layers which are next to each other and are fibrous, filamentary, formed of particles or foamed
    • B32B5/24—Layered products characterised by the non- homogeneity or physical structure, i.e. comprising a fibrous, filamentary, particulate or foam layer; Layered products characterised by having a layer differing constitutionally or physically in different parts characterised by the presence of two or more layers which are next to each other and are fibrous, filamentary, formed of particles or foamed one layer being a fibrous or filamentary layer
    • B32B5/28—Layered products characterised by the non- homogeneity or physical structure, i.e. comprising a fibrous, filamentary, particulate or foam layer; Layered products characterised by having a layer differing constitutionally or physically in different parts characterised by the presence of two or more layers which are next to each other and are fibrous, filamentary, formed of particles or foamed one layer being a fibrous or filamentary layer impregnated with or embedded in a plastic substance
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
    • C08J5/00—Manufacture of articles or shaped materials containing macromolecular substances
    • C08J5/04—Reinforcing macromolecular compounds with loose or coherent fibrous material

Definitions

  • the present invention relates to a fiber reinforced resin molded body and a method for producing a fiber reinforced resin molded body.
  • Patent Document 1 there is known a base material for a fiber-reinforced plastic molded body including a reinforcing fiber containing an aramid fiber and a carbon fiber, a matrix resin containing a thermoplastic resin, and a binder component.
  • the fiber-reinforced plastic molded body is molded by heating and pressing the substrate for fiber-reinforced plastic molded body at a temperature of 150 to 600 ° C. (above the glass transition temperature of the thermoplastic resin).
  • the molded body described in Patent Document 1 may have excellent bending strength, but has poor toughness and tends to be brittle fractured.
  • the present invention provides a fiber-reinforced resin molded body that can absorb a larger impact energy by breaking with a high load over a long stroke when an impact is applied, and a method for producing such a fiber-reinforced resin molded body. To do.
  • the present invention provides the following [1] to [8].
  • [1] Tensile strength of a base resin layer including carbon fiber and base resin and a woven fabric mainly composed of structural protein fibers is equal to or greater than the tensile elongation of the woven fabric.
  • a fiber-reinforced resin molded article obtained by laminating and adhering a woven fabric layer contained in a synthetic resin film / sheet having elongation.
  • [3] The fiber-reinforced resin molded article according to [1] or [2], wherein the synthetic resin film / sheet is made of thermoplastic polyurethane.
  • a base resin layer containing carbon fibers and a base resin, and a woven fabric mainly composed of structural protein fibers is equal to or higher than the tensile elongation of the woven fabric.
  • a method for producing a fiber-reinforced resin molded body comprising: a step of laminating a woven fabric layer incorporated in a synthetic resin film / sheet having elongation; and a step of heating and pressing the laminate. .
  • a method for producing a reinforced resin molding [7] The method for producing a fiber-reinforced resin molded article according to [5] or [6], wherein the base resin is a vinyl ester resin.
  • the fiber-reinforced resin molded body is broken with a high load over a long stroke when an impact is applied. Therefore, the fiber reinforced resin molded product can absorb a larger impact energy.
  • FIG. 1 is a cross-sectional view showing a fiber-reinforced resin molded body according to an embodiment of the present invention.
  • FIG. 2 is a diagram schematically showing an example of a spinning device for producing structural protein fibers.
  • FIG. 3 is a diagram schematically showing a hot press machine for producing a fiber-reinforced resin molded body according to an example.
  • FIG. 4 is a diagram showing the results of impact tests in Example 1 and Comparative Example 1.
  • FIG. 5 is a diagram showing the results of impact tests in Example 2 and Comparative Example 2.
  • FIG. 6 is a diagram showing the results of impact tests in Examples 3 and 4 and Comparative Example 3.
  • FIG. 7 is a diagram showing the results of impact tests in Examples 3 and 4 and Comparative Example 3.
  • the fiber-reinforced resin molded body according to the present embodiment is formed by laminating a base resin layer containing carbon fibers and a woven fabric layer, which is a synthetic resin film / sheet containing a woven fabric, in close contact with each other.
  • the fiber reinforced resin molded body 100 includes, for example, a base resin layer 60 including carbon fibers and a base resin, and a woven fabric 30 mainly composed of structural proteins formed on a synthetic resin film 50.
  • the inner woven fabric layers 40 are alternately laminated and have a structure in close contact.
  • the base resin layer 60 and the woven fabric layer 40 are in close contact with each other by being heated and pressurized.
  • the base resin layer 60 and the woven fabric layer 40 are not necessarily laminated alternately, and any one of the layers may be laminated continuously.
  • Examples of the base resin (matrix resin) of the base resin layer 60 include vinyl ester resin, unsaturated polyester, phenol resin, melamine resin, epoxy resin, urea resin, polyurethane, and the like.
  • the base resin is preferably a vinyl ester resin.
  • the fiber length of the carbon fiber is not particularly limited.
  • the carbon fiber may be a so-called long fiber (for example, a fiber having a fiber length exceeding 50 mm), a short fiber (for example, a fiber having a fiber length of 50 mm or less), or a continuous fiber.
  • the carbon fiber is preferably a short fiber.
  • the base resin layer 60 may be mixed with a filler, a curing agent, a low shrinkage agent, and an internal release agent.
  • Examples of the filler include calcium carbonate, aluminum hydride, barium sulfate, clay, mica and the like.
  • the base resin layer 60 is preferably CF-SMC (Carbon fiber Sheet Molding Compound).
  • the synthetic resin film 50 may be a synthetic resin sheet.
  • the thickness is different between the synthetic resin film and the synthetic resin sheet.
  • the synthetic resin film has a plate shape thinner than a predetermined thickness (for example, 0.2 to 0.25 mm), for example, and the synthetic resin sheet is a thin plate thicker than the predetermined thickness (for example, 0.2 to 0.25 mm), for example.
  • the synthetic resin film / sheet is preferably made of thermoplastic polyurethane (TPU).
  • Thermoplastic resin elastomers such as urethane rubber, silicone rubber, and fluoro rubber, and styrene, olefin, vinyl chloride, urethane, and amide thermoplastic elastomers are used for the synthetic resin film / sheet. Also good.
  • the tensile elongation of the synthetic resin film 50 is equal to the tensile elongation of the woven fabric 30 or larger than the tensile elongation of the woven fabric 30.
  • the tensile elongation is an elongation percentage (%) when one end of the film or sheet is fixed and the other end of the film or sheet is pulled and cut.
  • the load when the film or sheet is cut is called tensile strength.
  • the tensile elongation is the elongation (%) of the film or sheet when a load corresponding to the tensile strength is applied to the film or sheet.
  • the thicknesses of the base resin layer 60 and the woven fabric layer 40 can be set as appropriate.
  • the thickness of the base resin layer 60 may be equal to the thickness of the woven fabric layer 40, or the base resin layer 60 may be thicker than the woven fabric layer 40.
  • a fiber reinforced resin molded body 100 made of a laminate of the base resin layer 60 and the woven fabric layer 40 is formed into an appropriate shape as an impact absorbing member (structural member), for example, and applied to a moving body such as a vehicle.
  • the fiber reinforced resin molded body 100 can be molded by a known molding method. In the molded state, a cross section in which the base resin layer 60 and the woven fabric layer 40 are laminated may be exposed.
  • the use of the fiber reinforced resin molding 100 is not limited to moving bodies, such as a vehicle.
  • the presence of the woven fabric 30 in the synthetic resin film 50 means that the woven fabric 30 exists within the thickness range of the synthetic resin film 50.
  • the woven fabric 30 is impregnated with the synthetic resin that is the material of the synthetic resin film 50.
  • the woven fabric may be within the range of the thickness of the synthetic resin film / sheet, or the woven fabric may be exposed on the surface of the synthetic resin film / sheet.
  • the structural protein is a protein having a role of constructing a biological structure, and is different from functional proteins such as enzymes, hormones, and antibodies.
  • Examples of the structural protein include naturally occurring structural proteins such as fibroin, collagen, resilin, elastin and keratin. Fibroin produced by insects and spiders is known as a naturally occurring fibroin.
  • the structural protein according to this embodiment is preferably spider silk fibroin.
  • Spider silk fibroin includes natural spider silk fibroin and modified fibroin derived from natural spider silk fibroin.
  • natural spider silk fibroin include spider silk protein produced by spiders.
  • Modified fibroin means a fibroin having an amino acid sequence different from that of naturally occurring fibroin.
  • fibroin produced by insects include, for example, Bombyx mori, Kwako (Bombyx mandaraina), Tengea (Antheraea yamanai), ⁇ ⁇ (Antereaperanii), ⁇ ⁇ (Eriothyraminey) ), Silkworms (Samia cythia), chestnut worms (Caligula japonica), Chussa moth (Anthereaea mylitta), silkworms produced by silkworms such as Antheraea assamata, vespasam worms Examples include silk proteins.
  • fibroin produced by insects include silkworm fibroin L chain (GenBank accession number M76430 (base sequence), AAA27840.1 (amino acid sequence)).
  • Spider silk protein is a large toughened spider protein (MaSp) having a high toughness, a small toroidal spider protein (minor ampule spider protein, MiSp), and a whip according to the source organ.
  • MoSp toughened spider protein
  • MiSp small toroidal spider protein
  • Flagellform (Flag) tubular, aggregate, aggregate, aciform and piriform spider silk proteins are named.
  • Fibroin produced by spiders includes, for example, spiders belonging to the genus spider (Araneus spp.) Such as the spider spider, the spider spider, the red spider spider, and the bean spider, the genus spiders of the genus Araneus, the spider spider spider, the spider spider genus e Spiders, spiders such as spiders, spiders belonging to the genus Spider, spiders belonging to the genus Pronos, spiders belonging to the genus Trinofunda, such as Torinofundamas (genus Cyrtarachne) Spiders belonging to the genus (Gasteracantha), spiders belonging to the genus Spider (Ordgarius genus), such as the spiders, the spiders, and the spiders belonging to the genus Ordgarius Spiders belonging to the genus Argiope, such as the genus Argiope, spiders belonging to the genus Arachnura, such as the white-tailed spider, spiders belonging to the
  • Spiders belonging to the genus Azumigumi (Menosira), spiders belonging to the genus Dyschiriognatha (genus Dyschiriognatha) such as the common spider spider, the black spider spider, the genus Spider genus belonging to the genus Spider belonging to the genus (L) and the genus Spider belonging to the genus Usd Produced by spiders belonging to the family Tetragnathidae such as spiders belonging to the genus Prostenops
  • Examples include spider silk protein.
  • the spider silk protein include dragline proteins such as MaSp (MaSp1 and MaSp2) and ADF (ADF3 and ADF4), MiSp (MiSp1 and MiSp2), and the like.
  • fibroin produced by spiders include, for example, fibroin-3 (adf-3) [derived from Araneus diadematus] (GenBank accession numbers AAC47010 (amino acid sequence), U47855 (base sequence)), fibroin- 4 (adf-4) [derived from Araneus diadematus] (GenBank accession number AAC47011 (amino acid sequence), U47856 (base sequence)), dragline silk protein spidolin 1 [derived from Nephila clavipes (GenBank accession number AAC4, amino acid sequence A04) U37520 (base sequence)), major angul11ate spidroin 1 [La rodectus hesperus origin] (GenBank accession number ABR68856 (amino acid sequence), EF595246 (base sequence)), dragline silk protein spidroin 2 [Nephila clavata origin] (GenBank accession number AAL32447, amino acid sequence 45, amino acid sequence) major
  • Naturally derived fibroin include fibroin whose sequence information is registered in NCBI GenBank.
  • sequence information is registered in NCBI GenBank.
  • spidin, sample, fibroin, “silk and polypeptide”, or “silk and protein” is described as a keyword in DEFINITION from sequences including INV as DIVISION among the sequence information registered in NCBI GenBank. It can be confirmed by extracting a character string of a specific product from the sequence, CDS, and a sequence in which the specific character string is described from SOURCE to TISSUE TYPE.
  • the structural protein may be a polypeptide derived from the natural structural protein, that is, a recombinant polypeptide.
  • recombinant fibroin is produced in several heterologous protein production systems, and as a production method thereof, a transgenic goat, a transgenic silkworm, or a recombinant plant or mammalian cell is used.
  • Recombinant fibroin can be obtained, for example, by deleting one or more of the sequences encoding the (A) n motif from the cloned gene sequence of naturally occurring fibroin.
  • an amino acid sequence corresponding to the deletion of one or more (A) n motifs from the amino acid sequence of naturally derived fibroin is designed, and a nucleic acid encoding the designed amino acid sequence is chemically synthesized. You can also.
  • one or more amino acid residues are further substituted, deleted, inserted and / or added. The amino acid sequence corresponding to this may be modified.
  • substitution, deletion, insertion and / or addition of amino acid residues can be carried out by methods well known to those skilled in the art such as partial-directed mutagenesis. Specifically, Nucleic Acid Res. 10, 6487 (1982), Methods in Enzymology, 100, 448 (1983), and the like.
  • Recombinant polypeptide of a large sputum dragline protein is, for example, a protein comprising a domain sequence represented by Formula 1: [(A) n motif-REP] m (where, in Formula 1, (A) n The motif represents an amino acid sequence composed of 4 to 20 amino acid residues, and (A) the number of alanine residues relative to the total number of amino acid residues in the n motif is 80% or more, and REP is 10 to 200 amino acid residues. M represents an integer of 8 to 300.
  • a plurality of (A) n motifs may be the same amino acid sequence or different amino acid sequences. It may be the same amino acid sequence or a different amino acid sequence.
  • a protein containing the amino acid sequence represented by SEQ ID NO: 12 can be mentioned.
  • a protein comprising a domain sequence represented by Formula 2: [REP2] o (where, in Formula 2, o represents an integer of 5 to 300.
  • REP2 represents Gly 1X
  • An amino acid sequence composed of one Y, and X and Y represent any amino acid residue other than Gly, and a plurality of REP2s may be the same amino acid sequence or different amino acid sequences.
  • Specific examples include a protein containing the amino acid sequence represented by SEQ ID NO: 13.
  • amino acid sequence represented by SEQ ID NO: 13 corresponds to the repeat part and motif of the partial sequence of human collagen type 4 (NCBI Genbank accession number: CAA56335.1, GI: 3702452) obtained from the NCBI database.
  • An amino acid sequence represented by SEQ ID NO: 5 (tag sequence and hinge sequence) is added to the N-terminal of the amino acid sequence from the 301st residue to the 540th residue.
  • a protein comprising a domain sequence represented by Formula 3: [REP3] p (wherein, in Formula 3, p represents an integer of 4 to 300.
  • REP3 represents Ser 1 J 1 J represents an amino acid sequence composed of one Tyr, one Gly, one U-Pro, J represents an arbitrary amino acid residue, particularly preferably an amino acid residue selected from the group consisting of Asp, Ser, and Thr.
  • Plural REP3s may have the same or different amino acid sequences. Good). Specific examples include a protein containing the amino acid sequence represented by SEQ ID NO: 14.
  • the amino acid sequence shown in SEQ ID NO: 14 is the amino acid sequence of resilin (NCBI Genbank accession number NP 61157, Gl: 24654243), in which Thr at the 87th residue is replaced with Ser, and the Asn at the 95th residue.
  • the amino acid sequence shown by SEQ ID NO: 17 (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 is replaced with Asp.
  • Examples of recombinant polypeptides of elastin include proteins having amino acid sequences such as NCBI Genbank accession numbers AAC98395 (human), I47076 (sheep), and NP786966 (bovine). Specific examples include a protein containing the amino acid sequence represented by SEQ ID NO: 15.
  • the amino acid sequence represented by SEQ ID NO: 15 is the amino acid sequence represented by SEQ ID NO: 5 at the N-terminus of the amino acid sequence of residues 121 to 390 of the amino acid sequence of NCBI Genbank accession number AAC98395 (tag sequence). And a hinge arrangement).
  • Examples of the keratin recombinant polypeptide include Capra hircus type I keratin. Specific examples include a protein comprising the amino acid sequence represented by SEQ ID NO: 16 (amino acid sequence of NCBI Genbank accession number ACY30466).
  • the recombinant polypeptide is (i) an amino acid sequence represented by SEQ ID NO: 2, SEQ ID NO: 4 or SEQ ID NO: 10, or (ii) 90% or more of the amino acid sequence represented by SEQ ID NO: 2, SEQ ID NO: 4 or SEQ ID NO: 10. It may be a recombinant fibroin containing an amino acid sequence having the following sequence identity.
  • a recombinant fibroin comprising the amino acid sequence represented by SEQ ID NO: 2, SEQ ID NO: 4 or SEQ ID NO: 10 will be described.
  • the amino acid sequence represented by SEQ ID NO: 2 is separated from the amino acid sequence represented by SEQ ID NO: 1 corresponding to naturally-occurring fibroin (corresponding to naturally-occurring fibroin) every two from the N-terminal side to the C-terminal side ( A)
  • the n motif is deleted, and one [(A) n motif-REP] is inserted before the C-terminal sequence.
  • the amino acid sequence shown in SEQ ID NO: 4 is obtained by substituting all GGX in REP of the amino acid sequence shown in SEQ ID NO: 2 with GQX.
  • the amino acid sequence shown in SEQ ID NO: 10 has two alanine residues inserted in the C-terminal side of each (A) n motif of the amino acid sequence shown in SEQ ID NO: 4, and a part of glutamine (Q) residues. Substituted with a serine (S) residue and a part of the amino acid at the N-terminal side is deleted so as to be almost the same as the molecular weight of SEQ ID NO: 4.
  • the amino acid sequence shown in SEQ ID NO: 3 is obtained by substituting all GGX in REP of the amino acid sequence shown in SEQ ID NO: 1 with GQX.
  • a recombinant fibroin comprising an amino acid sequence having 90% or more sequence identity with the amino acid sequence shown in SEQ ID NO: 2, SEQ ID NO: 4 or SEQ ID NO: 10 will be described.
  • the recombinant fibroin includes an amino acid sequence having 90% or more sequence identity with the amino acid sequence represented by SEQ ID NO: 2, SEQ ID NO: 4 or SEQ ID NO: 10.
  • Recombinant fibroin is also a protein comprising a domain sequence represented by Formula 1: [(A) n motif-REP] m .
  • the sequence identity is preferably 95% or more.
  • the above-mentioned recombinant fibroin may contain a tag sequence at one or both of the N-terminal and C-terminal. This makes it possible to isolate, immobilize, detect and visualize recombinant fibroin.
  • tag sequences include affinity tags that use specific affinity (binding property, affinity) with other molecules.
  • affinity tag include a histidine tag (His tag).
  • His tag is a short peptide in which about 4 to 10 histidine residues are arranged, and has a property of specifically binding to a metal ion such as nickel. Therefore, a single tag of recombinant fibroin by metal chelating chromatography (chelating metal chromatography) is used. It can be used for separation.
  • Specific examples of the tag sequence include the amino acid sequence represented by SEQ ID NO: 5 (amino acid sequence containing a His tag).
  • GST glutathione-S-transferase
  • MBP maltose-binding protein
  • an “epitope tag” using an antigen-antibody reaction can also be used.
  • a peptide (epitope) exhibiting antigenicity as a tag sequence, an antibody against the epitope can be bound.
  • the epitope tag HA (peptide sequence of hemagglutinin of influenza virus) tag, myc tag, FLAG tag and the like can be mentioned.
  • recombinant fibroin can be easily purified with high specificity.
  • a tag sequence that can be separated with a specific protease can also be used.
  • Recombinant fibroin from which the tag sequence has been cleaved can also be recovered by treating the protein adsorbed via the tag sequence with a protease.
  • recombinant fibroin comprising a tag sequence, (iii) an amino acid sequence represented by SEQ ID NO: 7, SEQ ID NO: 9 or SEQ ID NO: 11, or (iv) SEQ ID NO: 7, SEQ ID NO: 9 or SEQ ID NO: 11 And recombinant fibroin comprising an amino acid sequence having 90% or more sequence identity with the amino acid sequence represented by
  • the recombinant polypeptide comprises (iii) an amino acid sequence represented by SEQ ID NO: 7, SEQ ID NO: 9 or SEQ ID NO: 11, or (iv) 90% or more of the amino acid sequence represented by SEQ ID NO: 7, SEQ ID NO: 9 or SEQ ID NO: 11. It may be a recombinant fibroin containing an amino acid sequence having the following sequence identity.
  • amino acid sequences represented by SEQ ID NOs: 6, 7, 8, 9 and 11 are the amino acid sequences represented by SEQ ID NO: 5 at the N-terminus of the amino acid sequences represented by SEQ ID NOs: 1, 2, 3, 4 and 10 (His tag). Is added).
  • Recombinant fibroin is also a protein comprising a domain sequence represented by Formula 1: [(A) n motif-REP] m .
  • the sequence identity is preferably 95% or more.
  • the structural protein preferably contains a recombinant polypeptide.
  • a recombinant polypeptide By including a recombinant polypeptide as a structural protein, it is possible to adjust the bending elastic modulus, bending strength, and hardness of the obtained molded product to desired numerical values.
  • the method for producing the recombinant polypeptide is described in detail below.
  • the target recombinant polypeptide can be obtained, for example, by a host transformed with an expression vector having a gene sequence encoding a structural protein and one or more regulatory sequences operably linked to the gene sequence. It can be produced by expressing a gene.
  • the method for producing the gene encoding the desired recombinant polypeptide is not particularly limited.
  • a gene encoding a natural structural protein can be used to produce the gene by a method of amplification and cloning by polymerase chain reaction (PCR) or the like, or chemical synthesis.
  • the method of chemical synthesis of the gene is not particularly limited.
  • AKTA oligopilot plus 10/100 GE Healthcare Japan Co., Ltd.
  • a gene can be chemically synthesized by a method of linking oligonucleotides automatically synthesized in step 1 by PCR or the like.
  • a gene encoding a polypeptide in which an amino acid sequence consisting of a start codon and a His10 tag is added to the N-terminus of the above amino acid sequence may be synthesized.
  • Regulatory sequences are sequences that control the expression of recombinant proteins in the host (for example, promoters, enhancers, ribosome binding sequences, transcription termination sequences, etc.), and can be appropriately selected depending on the type of host.
  • an inducible promoter that functions in a host cell and can induce expression of a target protein may be used.
  • An inducible promoter is a promoter that can control transcription by the presence of an inducer (expression inducer), absence of a repressor molecule, or physical factors such as an increase or decrease in temperature, osmotic pressure or pH value.
  • the type of expression vector can be appropriately selected according to the type of host, such as a plasmid vector, virus vector, cosmid vector, fosmid vector, artificial chromosome vector, and the like.
  • Suitable expression vectors are those that can replicate autonomously in the host cell or can be integrated into the host chromosome and contain a promoter at a position where the gene encoding the desired recombinant polypeptide can be transcribed. Used for.
  • any of prokaryotes and eukaryotes such as yeast, filamentous fungi, insect cells, animal cells and plant cells can be preferably used.
  • prokaryotes include bacteria belonging to the genus Escherichia, Brevibacillus, Serratia, Bacillus, Microbacterium, Brevibacterium, Corynebacterium, Pseudomonas and the like.
  • vectors for introducing a gene encoding a desired recombinant polypeptide include pBTrp2 (manufactured by Boehringer Mannheim), pGEX (manufactured by Pharmacia), pUC18, pBluescriptII, pSupex, pET22b, pCold, pUB110, pNCO2 (special No. 2002-238469).
  • Examples of eukaryotic hosts include yeast and filamentous fungi (molds, etc.).
  • yeast examples include yeasts belonging to the genus Saccharomyces, Pichia, Schizosaccharomyces and the like.
  • filamentous fungi examples include filamentous fungi belonging to the genus Aspergillus, the genus Penicillium, the genus Trichoderma and the like.
  • vectors examples include YEP13 (ATCC 37115) and YEp24 (ATCC 37051).
  • Any method can be used for introducing an expression vector into the host cell as long as it is a method for introducing DNA into the host cell.
  • a method using calcium ions [Proc. Natl. Acad. Sci. USA, 69, 2110 (1972)], electroporation method, spheroplast method, protoplast method, lithium acetate method, competent method, and the like.
  • the target recombinant polypeptide can be obtained, for example, by culturing a host transformed with the expression vector of the present invention in a culture medium, producing and accumulating the protein in the culture medium, and collecting the protein from the culture medium. Can be manufactured.
  • the method of culturing the host according to the present invention in a culture medium can be performed according to a method usually used for culturing a host.
  • the host culture medium according to the present invention contains a carbon source, a nitrogen source, inorganic salts, etc. that can be assimilated by the host. Any natural or synthetic medium may be used as long as the medium can efficiently culture the host.
  • Any carbon source may be used as long as it can be assimilated by the above-mentioned transformed microorganism.
  • Examples thereof include glucose, fructose, sucrose, and carbohydrates such as molasses, starch and starch hydrolyzate, acetic acid and propionic acid, etc.
  • Organic acids and alcohols such as ethanol and propanol can be used.
  • nitrogen source examples include ammonium salts of inorganic acids or organic acids such as ammonia, ammonium chloride, ammonium sulfate, ammonium acetate, and ammonium phosphate, other nitrogen-containing compounds, and peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal and soybean meal hydrolyzate, various fermented cells and digested products 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, and peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal and soybean meal hydrolyzate, various fermented cells and digested products thereof can be used.
  • inorganic salts examples include monopotassium phosphate, dipotassium phosphate, magnesium phosphate, magnesium sulfate, sodium chloride, ferrous sulfate, manganese sulfate, copper sulfate, and calcium carbonate.
  • Cultivation of prokaryotes such as E. coli or eukaryotes such as yeast can be performed under aerobic conditions such as shaking culture or deep aeration and agitation culture.
  • 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 the culture is preferably maintained at 3.0 to 9.0.
  • the pH of the culture medium can be adjusted using an inorganic acid, an organic acid, an alkaline solution, urea, calcium carbonate, ammonia, or the like.
  • antibiotics such as ampicillin and tetracycline may be added to the culture medium as needed during the culture.
  • an inducer may be added to the medium as necessary.
  • isopropyl- ⁇ -D-thiogalactopyranoside is used when cultivating a microorganism transformed with an expression vector using the lac promoter
  • indole acrylic is used when culturing a microorganism transformed with an expression vector using the trp promoter.
  • An acid or the like may be added to the medium.
  • the recombinant polypeptide according to the present invention can be isolated and purified by a method usually used for protein isolation and purification. For example, when the recombinant polypeptide is expressed in a dissolved state in the cell, the host cell is recovered by centrifugation after culturing and suspended in an aqueous buffer, followed by an ultrasonic crusher, a French press. Then, the host cells are disrupted with a Manton Gaurin homogenizer, dynomill, or the like to obtain a cell-free extract.
  • a method usually used for protein isolation and purification that is, a solvent extraction method, a salting-out method using ammonium sulfate, a desalting method, an organic solvent, etc.
  • Precipitation method anion exchange chromatography method using resin such as diethylaminoethyl (DEAE) -Sepharose, DIAION HPA-75 (manufactured by Mitsubishi Kasei), positive using resin such as S-Sepharose FF (manufactured by Pharmacia)
  • Electrophoresis methods such as ion exchange chromatography, hydrophobic chromatography using resins such as butyl sepharose and phenyl sepharose, gel filtration using molecular sieve, affinity chromatography, chromatofocusing, isoelectric focusing Etc. alone or in combination And use, it is possible to obtain a purified product.
  • the host cell when the recombinant polypeptide is expressed in the form of an insoluble substance in the cell, the host cell is similarly recovered, crushed, and centrifuged to obtain an insoluble recombinant polypeptide as a precipitate fraction. Recover.
  • the recovered recombinant polypeptide insoluble matter can be solubilized with a protein denaturant. After the operation, a purified product of the recombinant polypeptide can be obtained by the same isolation and purification method as described above.
  • the recombinant polypeptide When the recombinant polypeptide is secreted outside the cell, the recombinant polypeptide can be recovered from the culture supernatant. That is, a culture supernatant is obtained by treating the culture with a technique such as centrifugation, and a purified preparation can be obtained from the culture supernatant by using the same isolation and purification method as described above.
  • the structural protein fiber is obtained by spinning the above-described protein.
  • the structural protein fiber is preferably one obtained by spinning a polypeptide derived from a natural spider silk protein (modified spider silk protein).
  • the structural protein fiber can be produced by a known spinning method. That is, for example, when producing structural protein fibers, first, spider silk fibroin produced according to the above-described method is converted into dimethyl sulfoxide (DMSO), N, N-dimethylformamide (DMF), or hexafluoroisopronol ( A dope solution is prepared by adding to a solvent such as HFIP) together with an inorganic salt as a dissolution accelerator and dissolving. Next, using this dope solution, spinning can be performed by a known spinning method such as wet spinning, dry spinning, or dry wet spinning to obtain a target structural protein fiber.
  • DMSO dimethyl sulfoxide
  • DMF N-dimethylformamide
  • a dope solution is prepared by adding to a solvent such as HFIP
  • FIG. 2 is a schematic view showing an example of a spinning device for producing structural protein fibers.
  • a spinning device 10 shown in FIG. 2 is an example of a spinning device for dry and wet spinning, and has an extrusion device 1, a coagulation bath 20, a washing bath 21, and a drying device 4 in order from the upstream side. .
  • the extrusion apparatus 1 has a storage tank 7 in which a dope solution (spinning solution) 6 is stored.
  • the coagulation liquid 11 (for example, methanol) is stored in the coagulation bath 20.
  • the dope solution 6 is pushed out by a gear pump 8 attached to the lower end of the storage tank 7 from a nozzle 9 provided with an air gap 19 between the dope solution 6 and the coagulating solution 11.
  • the extruded dope liquid 6 is supplied into the coagulation 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 tub 21, washed with the washing liquid 12 in the washing tub 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 tub 21. It is done. At this time, for example, if the rotational speed of the second nip roller 14 is set to be faster than the rotational speed of the first nip roller 13, the structural protein fiber 36 drawn at a magnification according to the rotational speed ratio is obtained.
  • the structural protein fiber drawn in the cleaning liquid 12 leaves the cleaning bath 21 and is then dried when passing through the drying device 4, and then wound by a winder. In this way, the structural protein fiber is obtained as a wound product 5 that is finally wound around the winder by the spinning device 10.
  • Reference numerals 18a to 18g are thread guides.
  • the coagulation liquid 11 may be any solution that can be desolvated, and examples thereof include lower alcohols having 1 to 5 carbon atoms such as methanol, ethanol, and 2-propanol, and acetone.
  • the coagulation liquid 11 may appropriately contain water.
  • the temperature of the coagulation liquid 11 is preferably 0 to 30 ° C.
  • the distance through which the coagulated protein passes through the coagulation liquid 11 (substantially, the distance from the yarn guide 18a to the yarn guide 18b) has only to be a length that allows efficient desolvation, 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, and preferably 0.05 to 0.15 minutes. Further, stretching (pre-stretching) may be performed in the coagulating liquid 11.
  • stretching performed in the solution which added the organic solvent etc. to warm water may be sufficient as extending
  • the wet heat stretching temperature may be, for example, 50 to 90 ° C., and preferably 75 to 85 ° C.
  • an undrawn yarn (or predrawn yarn) can be drawn, for example, 1 to 10 times, and preferably 2 to 8 times.
  • the final draw ratio of the lower limit of the undrawn yarn (or predrawn yarn) is preferably more than 1 time, 2 times or more, 3 times or more, 4 times or more, 5 times or more, 6 times. Above, 7 times or more, 8 times or more, 9 times or more, and upper limit is preferably 40 times or less, 30 times or less, 20 times or less, 15 times or less, 14 times or less, 13 times or less 12 times or less, 11 times or less, and 10 times or less.
  • the structural protein fiber used for the production of the fabric containing the structural protein fiber may be a short fiber or a long fiber.
  • Structural protein fibers may be used alone or in combination with other fibers. That is, when manufacturing a cloth, a single yarn composed only of structural protein fibers and a composite yarn composed of a combination of structural protein fibers and other fibers may be used alone as material yarns. Alternatively, the single yarn and the composite yarn may be used in combination as the material yarn.
  • the single yarn includes twisted yarn, non-twisted yarn and the like.
  • the single yarn is preferably a twisted yarn.
  • the twisted yarn may be Z-twisted or S-twisted twisted yarn.
  • the composite yarn can include, for example, a blended yarn, a blended yarn, a covering yarn, and the like.
  • Other fibers are fibers that do not contain structural proteins.
  • other fibers include synthetic fibers such as nylon and polyester, recycled fibers such as cupra and rayon, and natural fibers such as cotton and hemp.
  • the content of the structural protein fiber is preferably 50% by mass or more, more preferably 80% by mass or more, based on the total amount of the woven fabric including the structural protein fiber. More preferably, it is 90% by mass or more.
  • the woven structure of the woven fabric may be, for example, a plain weave, a twill weave, a satin weave, or the like.
  • One type of yarn may be used, or a plurality of types may be used.
  • the basis weight of the woven fabric 30 is not particularly limited, but may be, for example, 10 to 500 g / m 2 .
  • a known method can be used as a method for producing a woven fabric from structural protein fibers.
  • the method for producing a woven fabric from structural protein fibers is not particularly limited.
  • the woven fabric can be produced by a known loom.
  • a base resin layer including short fibers of carbon fibers and a base resin such as vinyl ester resin is prepared.
  • the base resin layer is a CF-SMC base material.
  • a woven fabric made of structural protein fibers and a synthetic resin film / sheet having a tensile elongation equal to or greater than the tensile elongation of the woven fabric are prepared.
  • a silk textile having a twill weave structure or a spider silk textile having a twill weave structure is used as the woven fabric.
  • the synthetic resin film / sheet is made of a thermoplastic synthetic resin such as thermoplastic polyurethane
  • the woven fabric and the synthetic resin film / sheet are stacked (laminated), and heating and pressurization are performed in this state.
  • heating and pressurization for example, a hot press machine can be used.
  • the woven fabric is impregnated with the thermoplastic synthetic resin to obtain a woven fabric layer.
  • This synthetic resin film / sheet is a stress relaxation layer in a fiber reinforced resin molded product.
  • a CF-SMC base material which is a base resin layer, and a woven fabric layer are laminated to obtain a laminate.
  • the number of base resin layers and woven fabric layers in the laminate can be appropriately set.
  • One base resin layer and one woven fabric layer may be laminated, or two or more base resin layers and a woven fabric layer may be laminated.
  • a release paper may be interposed between the synthetic resin film / sheet and the heat press to easily peel the fiber reinforced resin molded product from the heat press.
  • the heating in the heating and pressing step is preferably performed at 80 to 200 ° C., more preferably 100 to 180 ° C., and further preferably 120 to 150 ° C.
  • the pressurization is preferably performed at 5 MPa or more, more preferably 10 MPa or more, and further preferably 15 MPa or more.
  • the time for which the treatment is continued under the condition is preferably 0 to 100 minutes, more preferably 1 to 50 minutes, and further preferably 3 to 10 minutes.
  • the manufacturing method is not limited to the above method, and an existing processing method according to the material may be used.
  • the synthetic resin film / sheet is not necessarily impregnated into the woven fabric in advance.
  • the laminated body laminated in the order of the base resin layer, the synthetic resin film / sheet, and the woven fabric is hot-pressed to produce a fiber-reinforced resin molded body. May be. That is, first, a base resin layer containing carbon fiber and base resin, a synthetic resin film / sheet, and a woven fabric mainly composed of structural protein fibers, which is equal to the tensile elongation of the synthetic resin film / sheet.
  • a woven fabric having a tensile elongation smaller than that of the synthetic resin film / sheet may be laminated in this order to obtain a laminated body, and then the laminated body may be heated and pressurized.
  • the conditions in the heating and pressing step in that case are the same as described above.
  • the amino acid sequence represented by SEQ ID NO: 12 is a region of 20 domain sequences present in the amino acid sequence represented by SEQ ID NO: 9 (however, several amino acid residues on the C-terminal side of the region are substituted).
  • the amino acid sequence represented by SEQ ID NO: 5 (including the His tag) is added to the N-terminus to the amino acid sequence in which a His tag is added to the C-terminus of the sequence of repeating 4 times.
  • a nucleic acid encoding the designed modified spider silk fibroin was synthesized.
  • the nucleic acid was added with an NdeI site at the 5 'end and an EcoRI site downstream of the stop codon.
  • This nucleic acid was cloned into a cloning vector (pUC118). Thereafter, the nucleic acid was cleaved by restriction enzyme treatment with NdeI and EcoRI, and then recombined with the protein expression vector pET-22b (+) to obtain an expression vector.
  • Escherichia coli BLR (DE3) was transformed with the obtained pET-22b (+) expression vector.
  • the transformed Escherichia coli was cultured in 2 mL of LB medium containing ampicillin for 15 hours.
  • the culture solution was added to 100 mL of a seed culture medium (Table 1) containing ampicillin so that the OD600 was 0.005.
  • the culture temperature was maintained at 30 ° C., and flask culture was performed until the OD600 reached 5 (about 15 hours) to obtain a seed culture.
  • the seed culture solution was added to a jar fermenter to which 500 ml of production medium (Table 2 below) was added so that the OD600 was 0.05.
  • the culture solution temperature was maintained at 37 ° C., and the culture was performed at a constant pH of 6.9.
  • the dissolved oxygen concentration in the culture solution was maintained at 20% of the dissolved oxygen saturation concentration.
  • a feed solution (glucose 455 g / 1 L, Yeast Extract 120 g / 1 L) was added at a rate of 1 mL / min.
  • the culture solution temperature was maintained at 37 ° C., and the culture was performed at a constant pH of 6.9.
  • the culture was performed for 20 hours while maintaining the dissolved oxygen concentration in the culture solution at 20% of the dissolved oxygen saturation concentration.
  • 1M isopropyl- ⁇ -thiogalactopyranoside (IPTG) was added to the culture solution to a final concentration of 1 mM to induce expression of the target modified fibroin.
  • the culture solution was centrifuged, and the cells were collected. SDS-PAGE is performed using cells prepared from the culture solution before and after the addition of IPTG, and the target modified spider silk is obtained by the appearance of a band of a size corresponding to the target modified fibroin depending on the addition of IPTG. Fibroin expression was confirmed.
  • the washed precipitate was suspended in 8M guanidine buffer (8M 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 60 ° C. And stirred for 30 minutes with a stirrer to dissolve. After dissolution, dialysis was performed with water using a dialysis tube (cellulose tube 36/32 manufactured by Sanko Junyaku Co., Ltd.). White aggregated protein obtained after dialysis was collected by centrifugation. Water was removed from the recovered aggregated protein with a freeze dryer to obtain the desired freeze-dried powder (structural protein powder) of modified fibroin.
  • 8M guanidine buffer 8M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0
  • the degree of purification of the target modified spider silk fibroin in the obtained lyophilized powder was confirmed by image analysis of the results of polyacrylamide gel electrophoresis of the powder using Totallab (nonlinear dynamics ltd.). As a result, the purity of any modified spider silk fibroin was about 85%.
  • Dry-wet spinning was performed using the dope solution obtained as described above and a known dry-wet spinning apparatus to obtain a monofilament made of spider fiber fibroin.
  • dry and wet spinning was performed under the following conditions.
  • Example 1 As Example 1, a woven fabric (spider yarn textile, woven structure: twill weave, basis weight: 230 g / m 2 , tensile elongation: 40.5%) produced using the structural protein fiber obtained above was used. As Example 2, a woven fabric (silk textile. Woven structure: twill weave, basis weight: 250 g / m) produced using silk (manufactured by Usui Yarn Co., Ltd., product name: Chun-Li Jonggetsu, yarn count: 16 pieces in 27). 2 and tensile elongation: 28.9%).
  • a CF-SMC base material (tensile elongation: 1.6%) in which carbon fiber short fibers (1 inch) were dispersed in a vinyl ester resin was used as the base resin layer.
  • the carbon fiber content in the CF-SMC substrate was 50% by mass.
  • hot melt manufactured by BASF, product name: Elastollan, product number: ET580, material: thermoplastic polyurethane
  • the synthetic resin film / sheet is referred to as a stress relaxation layer.
  • Example 1 the above-mentioned woven fabric of 200 mm ⁇ 200 mm was impregnated with a stress relaxation layer using a hot press machine.
  • Vf fiber volume content
  • the impregnation conditions were temperature: 130 ° C., pressure: 0.5 MPa, and time: 3 minutes.
  • the woven fabric impregnated with the stress relaxation layer was laminated on the CF-SMC base material, and this laminated body 80 was set in a hot press machine 200 (300 mm ⁇ 300 mm).
  • the release paper 70 was interposed between the experimental sample and the hot press machine 200.
  • the laminated body 80 was heated and pressurized using the hot press machine 200, and the fiber reinforced resin molding was shape
  • the input amount of the CF-SMC substrate was adjusted so that the experimental sample was 266 g. When the CF-SMC base material is molded alone, it becomes 266 g with a thickness of 2 mm. Experimental samples were controlled by total weight.
  • the molding conditions heat treating and pressing conditions) were set to temperature: 150 ° C., pressure: 18.7 MPa, and time: 3 minutes.
  • Comparative Examples 1 and 2 As Comparative Example 1, the same woven fabric as in Example 1 was used. As Comparative Example 2, the same woven fabric as in Example 2 was used. In any of the comparative examples, the CF-SMC base material and the 200 mm ⁇ 200 mm woven fabric were stacked and molded using the same 300 mm ⁇ 300 mm hot press machine as in the examples. The input amount of the CF-SMC substrate was adjusted so that the experimental sample was 266 g. As in the examples, the experimental samples were controlled by the total weight. The molding conditions (heating and pressing conditions) were set to temperature: 150 ° C., pressure: 18.7 MPa, and time: 3 minutes.
  • a drop weight impact test was performed for each of Examples 1 and 2 and Comparative Examples 1 and 2.
  • a falling weight type impact tester Instron
  • a sample fixed with a jig was given an impact by dropping the weight (falling weight), and the impact resistance was evaluated.
  • the test conditions were applied energy: 50 J and ambient temperature: 23 ° C.
  • the sample size was 100 mm ⁇ 100 mm
  • the impactor head diameter was 20 mm ⁇
  • the through-hole diameter of the jig was 75 mm ⁇ .
  • the sample was fixed by bolting at 8 points in total, 2 points in 4 directions.
  • the jig and the base were fixed with a vise.
  • Example 1 18.80J
  • Example 2 26.82J Comparative Example 1: 16.07J Comparative Example 2: 16.65J
  • Example 3 and 4 and Comparative Example 3 In Examples 1 and 2 and Comparative Examples 1 and 2, the weights of the experimental samples were combined, but the thickness of the base resin layer (CF-SMC) was 1.1 mm. The same woven fabric used in 1 was sandwiched between two synthetic resin films / sheets used in Example 1 (plate thickness 0.6 mm), and the same heat and pressure molding as in Example 1 was performed. Example 3 and 4 were used. Although Examples 3 and 4 are the same, the impact input direction in the drop weight impact test is different. An example in which an impact was inputted to the woven fabric layer side was designated as Example 3, and an example in which an impact was inputted to the base resin side was designated as Example 4 (see FIG. 6). The base resin layer itself having a plate thickness of 1.1 mm was used as Comparative Example 3. For these Examples 3 and 4 and Comparative Example 3, a drop weight impact test was conducted in the same manner as in Examples 1 and 2 and Comparative Examples 1 and 2.
  • Example 3 6.89J
  • Example 4 7.45J Comparative Example 3: 5.60J
  • the fiber-reinforced resin molded body is broken with a high load over a long stroke when an impact is applied. Therefore, the fiber reinforced resin molded product can absorb a larger impact energy.

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Abstract

La présente invention concerne un article moulé en résine renforcée par des fibres qui est obtenu par stratification et collage d'une couche de résine de matériau de base qui comprend des fibres de carbone et une résine de matériau de base, et une couche de tissu tissé dans laquelle un tissu tissé ayant des fibres de protéine structurale en tant que matériau principal est incorporé dans un(e) film/feuille de résine synthétique ayant un allongement à la traction qui est supérieur ou égal à l'allongement à la traction du tissu tissé.
PCT/JP2019/003218 2018-01-30 2019-01-30 Article moulé en résine renforcée par des fibres et procédé de fabrication d'un article moulé en résine renforcée par des fibres WO2019151341A1 (fr)

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CN113717411A (zh) * 2021-09-13 2021-11-30 浙江理工大学 一种抗冲击碳纤维复合材料的制备方法
CN113773572A (zh) * 2021-08-22 2021-12-10 茂泰(福建)鞋材有限公司 一种改性生物碳酸钙eva环保鞋底的制备方法

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JP2022173689A (ja) 2021-05-10 2022-11-22 株式会社小松製作所 電動シリンダ及び作業機械

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