WO2020067518A1 - Corps moulé par injection, composition pour moulage par injection et procédé de production de corps moulé par injection - Google Patents

Corps moulé par injection, composition pour moulage par injection et procédé de production de corps moulé par injection Download PDF

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Publication number
WO2020067518A1
WO2020067518A1 PCT/JP2019/038383 JP2019038383W WO2020067518A1 WO 2020067518 A1 WO2020067518 A1 WO 2020067518A1 JP 2019038383 W JP2019038383 W JP 2019038383W WO 2020067518 A1 WO2020067518 A1 WO 2020067518A1
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Prior art keywords
protein
injection molded
injection
amino acid
molded article
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Ceased
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PCT/JP2019/038383
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English (en)
Japanese (ja)
Inventor
昌己 竹本
秀雄 平田
晋 清末
内田　和広
正博 麻川
英任 安間
望月　大介
洸樹 松井
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Koito Manufacturing Co Ltd
Kojima Industries Corp
Spiber Inc
Uchihama Kasei Co Ltd
Original Assignee
Koito Manufacturing Co Ltd
Kojima Industries Corp
Spiber Inc
Uchihama Kasei Co Ltd
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Publication of WO2020067518A1 publication Critical patent/WO2020067518A1/fr
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    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B29—WORKING OF PLASTICS; WORKING OF SUBSTANCES IN A PLASTIC STATE IN GENERAL
    • B29C—SHAPING OR JOINING OF PLASTICS; SHAPING OF MATERIAL IN A PLASTIC STATE, NOT OTHERWISE PROVIDED FOR; AFTER-TREATMENT OF THE SHAPED PRODUCTS, e.g. REPAIRING
    • B29C45/00—Injection moulding, i.e. forcing the required volume of moulding material through a nozzle into a closed mould; Apparatus therefor
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
    • C08L101/00—Compositions of unspecified macromolecular compounds
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
    • C08L23/00—Compositions of homopolymers or copolymers of unsaturated aliphatic hydrocarbons having only one carbon-to-carbon double bond; Compositions of derivatives of such polymers
    • C08L23/02—Compositions of homopolymers or copolymers of unsaturated aliphatic hydrocarbons having only one carbon-to-carbon double bond; Compositions of derivatives of such polymers not modified by chemical after-treatment
    • C08L23/10—Homopolymers or copolymers of propene
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
    • C08L89/00—Compositions of proteins; Compositions of derivatives thereof

Definitions

  • the present invention relates to an injection molded article.
  • the present invention also relates to a composition for injection molding and a method for producing an injection molded article.
  • the injection molded article is a molded article of a resin composition molded by an injection molding method.
  • the injection molding method is applicable to various shapes and is a method with good production efficiency. Therefore, the injection molding is used in a wide range of fields.
  • Patent Document 1 discloses a method of obtaining a molded product by using a resin composition containing a polyamide / polypropylene resin and wollastonite for injection molding.
  • thermoplastic resin and protein short fibers having a fiber length of 24 mm or less dispersed in the thermoplastic resin.
  • thermoplastic resin can function as the matrix resin and the protein short fibers can function as the reinforcing fibers.
  • the protein short fibers may include spider silk fibroin-like protein fibers.
  • thermoplastic resin may contain polypropylene.
  • thermoplastic resin and protein short fibers having a fiber length of 24 mm or less.
  • the protein short fibers may include spider silk fibroin-like protein fibers.
  • thermoplastic resin may contain polypropylene.
  • Still another aspect of the present invention is a heating step of heating the composition for injection molding to obtain a fluid material, an injecting step of injecting the fluid material into a mold, and injecting the mold into the mold. And a cooling step of cooling the flow material obtained to obtain an injection molded body.
  • an injection-molded article that can exhibit excellent bending characteristics regardless of the content of the inorganic filler. Further, according to the present invention, there are provided an injection molding composition for forming the injection molded article, and a production method for producing the injection molded article.
  • the injection molded article according to the present embodiment includes a thermoplastic resin and protein short fibers having a fiber length of 24 mm or less dispersed in the thermoplastic resin.
  • the thermoplastic resin can function as a matrix resin and the protein short fibers can function as reinforcing fibers, and thus have excellent bending characteristics. Therefore, the injection molded article according to the present embodiment can exhibit excellent bending characteristics regardless of the content of the inorganic filler.
  • the thermoplastic resin is not particularly limited, and may be any thermoplastic resin capable of dispersing short protein fibers as the matrix resin.
  • the thermoplastic resin include polyamide resin (eg, nylon), polypropylene, polyethylene, polystyrene, polyacetal, polycarbonate, ABS, AES, PET, PBT, PPS, LCP, PEEK, and the like.
  • the content of the thermoplastic resin may be, for example, 40% by volume or more, and is preferably 50% by volume or more, more preferably 60% by volume or more, from the viewpoint of the dispersibility of the protein short fibers.
  • the protein short fibers can be referred to as fibers (protein fibers) having a fiber length of 24 mm or less and composed of proteins.
  • the length of the protein short fiber is not particularly limited as long as it is 24 mm or less, and may be, for example, 12 mm or less, or 7 mm or less.
  • the fiber length of the protein short fiber is preferably 1 mm or more, more preferably 4 mm or more, from the viewpoint of further improving the mechanical strength of the injection molded article.
  • the injection molded article may include protein short fibers having a fiber length shorter than the above value due to breakage during molding or the like. For example, 90% by mass or more of the protein short fibers is 1 mm or more (more (Preferably 4 mm or more).
  • the content of the protein short fibers may be, for example, 60% by volume or less, preferably 50% by volume or less, and more preferably 40% by volume or less.
  • the protein constituting the protein short fiber 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 a modified protein obtained by modifying a part of the amino acid sequence (for example, 10% or less of the amino acid sequence) based on the amino acid sequence of the naturally occurring structural protein It may be.
  • structural proteins include fibroin (for example, spider silk, silkworm silk, etc.), collagen, resilin, elastin, keratin, and proteins derived therefrom.
  • Examples of the fibroin-like protein include a protein containing a domain sequence represented by 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, and an integer of 10 to 20. It may be an integer, an integer from 4 to 16, an integer from 8 to 16, or an integer from 10 to 16.
  • the number of alanine residues relative to the total number of amino acids in the (A) n motif may be 40% or more, and is 60% or more, 70% or more, 80% or more, 90% or more, or 100%.
  • 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 have the same amino acid sequence or different amino acid sequences.
  • a plurality of REP1s may have the same amino acid sequence or different amino acid sequences.
  • Examples of the fibroin-like protein include a protein containing the amino acid sequence represented by SEQ ID NO: 1.
  • Examples of the collagen-like protein include a protein 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 residue other than Gly.
  • a plurality of REP2s may have the same amino acid sequence or different amino acid sequences.
  • Examples of the collagen-like protein include a protein containing the amino acid sequence represented by SEQ ID NO: 2.
  • amino acid sequence represented by SEQ ID NO: 2 is a repeat portion and a motif of a partial sequence of human collagen type 4 obtained from the NCBI database (Accession number of GenBank of NCBI: CAA56335.1, GI: 3702452).
  • the amino acid sequence of SEQ ID NO: 6 (tag sequence and hinge sequence) is added to the N-terminal of the amino acid sequence from the 301st residue to the 540th residue.
  • resilin-like protein examples include a protein 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-JJ-Tyr-Gly-U-Pro.
  • J represents an arbitrary amino acid residue, and is preferably an amino acid residue selected from the group consisting of Asp, Ser and Thr.
  • U represents an arbitrary amino acid residue, preferably an amino acid residue selected from the group consisting of Pro, Ala, Thr and Ser.
  • a plurality of REP3s may have the same amino acid sequence or different amino acid sequences.
  • Examples of the resilin-like protein include a protein containing the amino acid sequence represented by SEQ ID NO: 3.
  • SEQ ID NO: 3 in the amino acid sequence of resilin (NCBI GenBank Accession No. NP 611157, Gl: 246654243), the Th at the 87th residue is replaced with Ser, and the 95th residue is replaced with Ser.
  • the amino acid sequence represented by SEQ ID NO: 7 (tag sequence) is added to the N-terminal of the amino acid sequence from the 19th residue to the 321st residue of the sequence in which Asn of the eye is substituted with Asp.
  • elastin-like protein examples include proteins having an amino acid sequence such as NCBI GenBank accession numbers AAC98395 (human), I47076 (sheep), and NP786966 (bovine).
  • examples of the elastin-like protein include a protein containing the amino acid sequence represented by SEQ ID NO: 4.
  • the amino acid sequence represented by SEQ ID NO: 4 is the amino acid sequence represented by SEQ ID NO: 6 at the N-terminus of the amino acid sequence from residue 121 to residue 390 of the amino acid sequence of GenBank Accession No. AAC98395 of NCBI. (Tag sequence and hinge sequence).
  • Keratin-like protein includes, for example, type I keratin of Capra hircus.
  • Examples of the keratin-like protein include a protein containing the amino acid sequence represented by SEQ ID NO: 5 (the amino acid sequence of NCBI GenBank accession number ACY30466).
  • the structural protein is preferably a fibroin-like protein, more preferably a spider silk fibroin-like protein.
  • the protein according to this 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, Those produced by expressing the nucleic acid can be used.
  • the method for producing the nucleic acid encoding the target protein is not particularly limited.
  • the nucleic acid can be produced by a method of amplifying and cloning by the polymerase chain reaction (PCR) using a gene encoding a natural structural protein, or by chemical synthesis.
  • the method for chemically synthesizing nucleic acids is not particularly limited. For example, based on amino acid sequence information of structural proteins obtained from the NCBI web database or the like, AKTA oligopilot plus 10/100 (manufactured by GE Healthcare Japan)
  • a nucleic acid can be chemically synthesized by a method of linking oligonucleotides automatically synthesized by PCR or the like by PCR or the like.
  • nucleic acid encoding a protein consisting of an amino acid sequence obtained by adding an amino acid sequence consisting of an initiation codon and a His10 tag to the N-terminus of the above amino acid sequence may be synthesized. Good.
  • the regulatory sequence is a sequence that controls the expression of the recombinant protein in the host (for example, a promoter, an enhancer, a ribosome binding sequence, a transcription termination sequence, and the like), and can be appropriately selected depending on the type of the host.
  • An inducible promoter that functions in a host cell and can induce the expression of a target protein may be used as the promoter.
  • An inducible promoter is a promoter that can control transcription by the presence of an inducer (expression inducer), the absence of a repressor molecule, or a physical factor such as an increase or decrease in temperature, osmotic pressure, or pH value.
  • the type of the expression vector may be a plasmid vector, a virus vector, a cosmid vector, a fosmid vector, an artificial chromosome vector or the like, and can be appropriately selected according to the type of the host.
  • the expression vector those capable of autonomous replication in a host cell or integration into a host chromosome and containing a promoter at a position where a nucleic acid encoding a protein of interest can be transcribed are suitably used. .
  • any of prokaryotes and eukaryotes such as yeast, filamentous fungi, insect cells, animal cells, and plant cells can be suitably used.
  • prokaryotes include bacteria belonging to the genus Escherichia, Brevibacillus, Serratia, Bacillus, Microbacterium, Brevibacterium, Corynebacterium, Pseudomonas, and the like.
  • examples of a vector for introducing a nucleic acid encoding a protein of interest include pBTrp2 (manufactured by Boehringer Mannheim), pGEX (manufactured by Pharmacia), pUC18, pBluescriptII, pSuex, pET22b, pCold, and the like.
  • pUB110, pNCO2 JP-A-2002-238569) and the like.
  • Examples of eukaryotic hosts include yeast and filamentous fungi (such as mold).
  • yeast include yeast belonging to the genus Saccharomyces, the genus Pichia, the genus Schizosaccharomyces, and the like.
  • filamentous fungi include filamentous fungi belonging to the genus Aspergillus, Penicillium, Trichoderma, and the like.
  • examples of a vector into which a nucleic acid encoding a target protein is introduced include YEp13 (ATCC37115), YEp24 (ATCC37051) and the like.
  • any method for introducing the expression vector into the host cell any method can be used 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, spheroplast, protoplast, lithium acetate, competent, 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, and the like can be performed according to the method described in Molecular Cloning, 2nd edition, and the like. .
  • the target protein can be produced, for example, by culturing a host transformed with an expression vector in a culture medium, producing and accumulating the protein in the culture medium, and collecting the protein from the culture medium.
  • the method of culturing the host in the culture medium can be performed according to a method usually used for culturing the host.
  • the culture medium of the host contains a carbon source, a nitrogen source, inorganic salts, and the like which can be utilized by the host, so that the culture of the host can be efficiently performed.
  • a natural medium and a synthetic medium may be used as long as the medium can be used.
  • the carbon source may be any as long as the transformed host can assimilate, for example, glucose, fructose, sucrose, and molasses containing these, carbohydrates such as starch and starch hydrolyzate, acetic acid and propionic acid. And alcohols such as ethanol and propanol.
  • the nitrogen source for example, ammonia, ammonium chloride, ammonium sulfate, ammonium salts of inorganic or organic acids such as ammonium acetate and ammonium phosphate, other nitrogen-containing compounds, and peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal, soybean meal hydrolyzate, various fermented cells and digests thereof can be used.
  • ammonia, ammonium chloride, ammonium sulfate, ammonium salts of inorganic or organic acids such as ammonium acetate and ammonium phosphate, other nitrogen-containing compounds, and peptone, meat extract, yeast extract, corn steep liquor, Casein hydrolyzate, soybean meal, soybean meal hydrolyzate, various fermented cells and digests thereof can be used.
  • potassium (I) phosphate potassium (II) phosphate, magnesium phosphate, magnesium sulfate, sodium chloride, ferrous sulfate, manganese sulfate, copper sulfate, calcium carbonate, and the like can be used.
  • ⁇ Cultivation of prokaryotes such as Escherichia coli or eukaryotes such as yeast can be performed under aerobic conditions such as shaking culture or deep aeration stirring culture.
  • the culture temperature is, for example, 15 to 40 ° C.
  • the culturing 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 during the culture.
  • an inducer may be added to the medium as necessary.
  • isopropyl- ⁇ -D-thiogalactopyranoside or the like is used.
  • 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 the cells, after culturing, the host cells are collected by centrifugation, suspended in an aqueous buffer, and then sonicated with a sonicator, French press, and Manton Gaulin. The host cells are crushed with a homogenizer and a dynomill to obtain a cell-free extract. From the supernatant obtained by centrifuging the cell-free extract, a purified sample can be obtained by a method usually used for protein isolation and purification.
  • the host cell When the protein is expressed by forming an insoluble form in the cell, the host cell is similarly recovered, crushed, and centrifuged to collect the protein insoluble form as a precipitate fraction.
  • the insoluble form of the recovered protein can be solubilized with a protein denaturant. After this operation, a purified sample of the protein can be obtained by the same isolation and purification method as described above.
  • the protein can be recovered from the culture supernatant. That is, a culture supernatant is obtained by treating the culture by a technique such as centrifugation, and a purified sample can be obtained from the culture supernatant by using the same isolation and purification method as described above.
  • Methods commonly used for the isolation and purification of proteins include solvent extraction, salting out with ammonium sulfate, desalting, precipitation with organic solvents, diethylaminoethyl (DEAE) -Sepharose, DIAION @ HPA-75 (Mitsubishi).
  • Anion exchange chromatography using a resin such as Kasei Co., Ltd .
  • cation exchange chromatography using a resin such as S-Sepharose @ FF (manufactured by Pharmacia); and resins such as butyl sepharose and phenyl sepharose.
  • Examples include hydrophobic chromatography, gel filtration using a molecular sieve, affinity chromatography, chromatofocusing, and electrophoresis such as isoelectric focusing. These methods may be used alone or in combination.
  • the protein short fiber may be a protein fiber obtained by spinning the above-mentioned protein and cut into a predetermined fiber length.
  • the protein fiber is preferably a fiber spun structural protein (structural protein fiber), more preferably a fiber spun fibroin-like protein (fibroin-like protein fiber), particularly preferably a fiber spun spider silk fibroin-like protein ( Spider silk fibroin-like protein fiber).
  • the protein fiber can be produced by spinning a protein by a known spinning method. That is, when producing a protein fiber, first, a protein produced according to the above-mentioned method is converted into dimethyl sulfoxide (DMSO), N, N-dimethylformamide (DMF), hexafluoroisopronol (HFIP), or the like.
  • a dope solution is prepared by adding to a solvent together with an inorganic salt as a dissolution promoter and dissolving the same. Then, using this dope solution (spinning stock solution), spinning is performed by a known spinning method such as wet spinning, dry spinning, or dry-wet spinning to obtain a target protein fiber.
  • FIG. 1 is a schematic diagram showing an example of a spinning device for producing protein fibers.
  • the spinning device 10 shown in FIG. 1 is an example of a spinning device for dry-wet spinning, and includes 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 extruder 1 has a storage tank 7 in which the dope solution (spinning stock 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 from a nozzle 9 provided with an air gap 19 between the dope solution 6 and the coagulation solution 11 by a gear pump 8 attached to the lower end of the storage tank 7.
  • 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 bath 21 and washed by 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.
  • Can be At this time for example, if the rotation speed of the second nip roller 14 is set higher than the rotation speed of the first nip roller 13, the protein fibers 36 drawn at a magnification corresponding to the rotation speed ratio are obtained.
  • the protein fiber 36 drawn in the washing liquid 12 is separated from the inside of the washing tub 21, dried when passing through the drying device 4, and then wound up by a winder. In this way, the protein fibers 36 are finally obtained by the spinning device 10 as the wound material 5 wound on a winder.
  • 18a to 18g are yarn guides.
  • the coagulating liquid 11 may be any organic solvent capable of extracting (desolvating) the solvent from the dope liquid 6 extruded from the nozzle 9.
  • organic solvent include lower alcohols having 1 to 5 carbon atoms such as methanol, ethanol and 2-propanol, and acetone.
  • the coagulating liquid 11 may appropriately contain water.
  • the temperature of the coagulating liquid 11 is preferably 0 to 30 ° C.
  • the distance that the coagulated protein passes through the coagulating liquid 11 (substantially, the distance from the yarn guide 18a to the yarn guide 18b) may be long enough to efficiently remove the solvent, 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 is preferably 0.05 to 0.15 minutes.
  • the fiber containing the coagulated protein may be drawn (pre-drawn) in the coagulating liquid 11.
  • the cleaning liquid 12 water can be mainly used.
  • the cleaning liquid 12 may include those listed as agents so that they can be used in the coagulation liquid 11.
  • the drawing performed in the washing bath 21 when obtaining the protein fiber may be so-called wet heat drawing performed in hot water, a solution obtained by adding an organic solvent or the like to hot water, or the like.
  • the temperature for the wet heat stretching 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, from 1 to 10 times, and preferably from 2 to 8 times.
  • the protein fiber may be further drawn (so-called dry heat drawing).
  • the lower limit of the final draw ratio of the 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 undrawn 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 or more. Hereinafter, it is 12 times or less, 11 times or less, or 10 times or less.
  • the injection molded article according to the present embodiment may further include components other than those described above.
  • the injection molded article may further contain a filler.
  • the shape of the filler is not particularly limited, and may be, for example, a fibrous shape, a granular shape including a spherical shape or an ellipsoidal shape, or a plate shape.
  • the material constituting the filler is not particularly limited.
  • carbon carbon fiber or the like
  • glass glass fiber, glass beads, glass balloon, etc.
  • talc mica
  • calcium carbonate aluminum hydroxide
  • barium sulfate whisker
  • Examples include metal powders such as wollastonite, montmorillonite, copper, and aluminum, and chemical fibers such as cellulose, PA, PET, aramid, PP, and PC.
  • the content of the filler is not particularly limited, but is, for example, 60% by volume or less, preferably 50% by volume or less, and may be 0% by volume (that is, the injection molded body does not contain the filler).
  • the content of the filler may be, for example, 1% by volume or more, or may be 40% by volume or more, from the viewpoint of sufficiently obtaining the reinforcing effect of the filler.
  • the injection molded body according to the present embodiment may further include other components included in a known injection molded body.
  • Other components include, for example, a weather resistance deterioration inhibitor, an antistatic agent, an antioxidant, an internal mold release agent, a surface modifier, and the like.
  • composition for injection molding includes a thermoplastic resin and protein short fibers having a fiber length of 24 mm or less.
  • the thermoplastic resin may be the above-described thermoplastic resin.
  • the protein short fiber may be the above-described protein short fiber.
  • composition for injection molding according to the present embodiment may further include the above-described filler, and may further include the other components described above.
  • the content of each component in the composition for injection molding may be the same as the content in the above-mentioned injection molded article.
  • the injection molded article according to the present embodiment may be a molded article formed by an injection molding method. That is, the method of manufacturing the injection molded body may be any method as long as the injection molded body is molded by the injection molding method. Examples of the method for producing the injection molded body include the following method.
  • the method for producing an injection-molded article includes a heating step of heating the above-described composition for injection molding to obtain a fluid material, an injecting step of injecting the fluid material into a mold, And a cooling step of cooling the flowable material injected into the mold to obtain an injection-molded body.
  • the heating temperature in the heating step is not particularly limited as long as it is a temperature at which the composition for injection molding can exhibit sufficient fluidity (that is, a temperature at which a fluid material having sufficient fluidity is obtained).
  • the heating temperature may be, for example, 120 ° C. or higher, and preferably 130 ° C. or higher.
  • the heating temperature may be, for example, 150 ° C. or lower, and preferably 140 ° C. or lower.
  • heating may be performed under pressure.
  • the pressure conditions are not particularly limited as long as the composition for injection molding can exhibit sufficient fluidity.
  • the pressing condition may be, for example, 20 MPa or more, and preferably 25 MPa or more. Further, the pressing condition may be, for example, 45 MPa or less, and more preferably 30 MPa or less.
  • the fluid material is injected into the mold. At this time, it is preferable to apply pressure to the fluid material so that the fluid material is injected into the details in the mold. In the pouring step, it is preferable that the mold is heated in order to prevent the fluidized material from solidifying before the inside of the mold is sufficiently filled. These pressure and heating conditions can be appropriately adjusted according to the fluidity of the fluid material, the shape in the mold, and the like.
  • the fluid material injected into the mold is cooled and solidified, and a molded body having a shape corresponding to the shape in the mold is obtained.
  • the cooling method is not particularly limited, and can be appropriately selected from known methods.
  • nucleic acid encoding PRT799 was synthesized.
  • An NdeI site at the 5 'end and an 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 nucleic acid was digested with NdeI and EcoRI and cut out, followed by recombination into a protein expression vector pET-22b (+) to obtain an expression vector.
  • the seed culture solution was added to a jar fermenter to which 500 mL of a production medium (Table 2) had been added so that the OD 600 was 0.05.
  • the temperature of the culture was maintained at 37 ° C., and the culture was performed at a constant pH of 6.9. Further, the concentration of dissolved oxygen in the culture solution was maintained at 20% of the saturated concentration of dissolved oxygen.
  • a feed solution (455 g / 1 L of glucose, Yeast Extract 120 g / 1 L) was added at a rate of 1 mL / min.
  • the temperature of the culture was maintained at 37 ° C., and the culture was performed at a constant pH of 6.9. Further, 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. Thereafter, 1 M isopropyl- ⁇ -thiogalactopyranoside (IPTG) was added to the culture solution to a final concentration of 1 mM to induce the expression of the target protein. Twenty hours after the addition of IPTG, the culture was centrifuged to collect the cells. SDS-PAGE was performed using cells prepared from the culture solution before and after the addition of IPTG, and the expression of the target protein was confirmed by the appearance of a band of the target protein size dependent on the addition of IPTG.
  • IPTG isopropyl- ⁇ -thiogalactopyranoside
  • the precipitate after washing is suspended in 8M guanidine buffer (8M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0) so as to have a concentration of 100 mg / mL. Stirred for minutes to dissolve. After dissolution, dialysis was performed with water using a dialysis tube (cellulose tube 36/32 manufactured by Sanko Junyaku Co., Ltd.). The white aggregated protein obtained after the dialysis was collected by centrifugation, water was removed with a lyophilizer, and the lyophilized powder was recovered to obtain a spider silk fibroin-like protein "PRT799".
  • 8M guanidine buffer 8M guanidine hydrochloride, 10 mM sodium dihydrogen phosphate, 20 mM NaCl, 1 mM Tris-HCl, pH 7.0
  • DMSO dimethylsulfoxide
  • Spider silk fibroin-like protein fibers (PRT799) were cut to an average length of 5 mm using a desktop fiber cutting machine (NP-300, manufactured by INTEC) to obtain protein short fibers.
  • Example 1 The obtained short protein fiber and polypropylene (AZ864E4, manufactured by Sumitomo Chemical Co., Ltd.) are kneaded at a ratio of 1.25: 98.75 (mass ratio) and pelletized to obtain a pellet-like kneaded material.
  • the kneading was performed with a mixer.
  • injection molding was performed using an injection molding machine (EC40N, manufactured by Toshiba Machine Co., Ltd.) using the pelletized kneaded material as a molding raw material to obtain an injection molded body of 150 mm ⁇ 150 mm ⁇ 3 mm.
  • ⁇ Bending test 1> The obtained injection-molded body was cut into 80 mm ⁇ 25 mm in two directions, one direction (hereinafter, vertical direction) and a direction perpendicular to it (hereinafter, horizontal direction), to obtain a test piece for a bending test.
  • a tester AG-50kNX, manufactured by Shimadzu Corporation
  • the maximum bending stress of the test piece and the yield strain when the maximum bending stress was developed were measured.
  • the distance between the fulcrums was 40 mm
  • the test speed was 5 mm / min
  • the indenter radius was 5 mm
  • the fulcrum radius was 2 mm.
  • Table 3 shows the results.
  • the yield strain indicates the yield strain when the maximum bending stress occurs.
  • Example 1 Injection molding was performed in the same manner as in Example 1 except that polypropylene was used as a molding raw material without using protein short fibers to obtain an injection molded article. About the obtained injection molded body, the maximum bending stress and the yield strain when the maximum bending stress was developed were measured in the same manner as in Example 1. Table 3 shows the results.
  • Example 2 The protein short fibers and polypropylene (MA3N, manufactured by Nippon Polypropylene Co., Ltd.) were kneaded at a ratio of 1: 9 (mass ratio) and pelletized to obtain a pellet-like kneaded product. The kneading was performed with a mixer. Next, the kneaded material in the form of a pellet was injection-molded using an injection molding machine (EC40N, manufactured by Toshiba Machine Co., Ltd.) to obtain a type A1 multipurpose test piece specified by ISO20753.
  • MA3N manufactured by Nippon Polypropylene Co., Ltd.
  • ⁇ Bending test 2> A bending test was performed on the obtained injection molded body according to ISO178, and the bending elastic modulus and the bending strength were measured. The test speed was 5 mm / min. Table 4 shows the results.
  • Example 2 Injection molding was performed in the same manner as in Example 2 using polypropylene as a molding raw material without using protein short fibers to obtain an injection molded article. With respect to the obtained injection molded article, the flexural modulus, flexural strength, tensile strength, impact strength, and deflection temperature under load (HDT) were measured in the same manner as in Example 2. Table 4 shows the results.
  • the injection molded article of the present invention can exhibit excellent bending characteristics regardless of the content of the inorganic filler, and thus can be suitably used for applications where the use of the inorganic filler is restricted.

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  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Medicinal Chemistry (AREA)
  • Polymers & Plastics (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Manufacturing & Machinery (AREA)
  • Mechanical Engineering (AREA)
  • Compositions Of Macromolecular Compounds (AREA)
  • Injection Moulding Of Plastics Or The Like (AREA)

Abstract

L'invention concerne un corps moulé par injection contenant une résine thermoplastique et des fibres protéiniques courtes qui ont une longueur de fibre inférieure ou égale à 24 mm et qui sont dispersées dans la résine thermoplastique.
PCT/JP2019/038383 2018-09-28 2019-09-27 Corps moulé par injection, composition pour moulage par injection et procédé de production de corps moulé par injection Ceased WO2020067518A1 (fr)

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPWO2022014525A1 (fr) * 2020-07-15 2022-01-20

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2025187819A1 (fr) * 2024-03-07 2025-09-12 Ｓｐｉｂｅｒ株式会社 Matériau composite renforcé par des fibres et son procédé de production

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH07310019A (ja) * 1994-05-17 1995-11-28 Idemitsu Petrochem Co Ltd 絹フィブロイン超微粉末含有熱可塑性樹脂組成物の成形品及び複合成形品
JP2010018683A (ja) * 2008-07-09 2010-01-28 Univ Of Ryukyus 射出成形用バガス繊維強化ポリプロピレン樹脂材とその製造方法および成形品
JP2017056594A (ja) * 2015-09-15 2017-03-23 日立化成株式会社 フィブロイン複合体、及びその製造方法
WO2018034111A1 (fr) * 2016-08-19 2018-02-22 国立研究開発法人理化学研究所 Composition de moulage composite comprenant une protéine de type fibroïne, et procédé de production de la composition de moulage composite
WO2019066028A1 (fr) * 2017-09-29 2019-04-04 内浜化成株式会社 Matériau composite renforcé par des fibres, additif pour matériau composite renforcé par des fibres et procédé de production d'un matériau composite renforcé par des fibres

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2742347B2 (ja) * 1991-11-07 1998-04-22 工業技術院長 生分解性不織布成型容器
EP3766686A1 (fr) * 2015-09-17 2021-01-20 Roberto Velozzi Jerez Panneaux composites porteurs, matériaux, produits et procédés de fabrication et d'utilisation associés

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH07310019A (ja) * 1994-05-17 1995-11-28 Idemitsu Petrochem Co Ltd 絹フィブロイン超微粉末含有熱可塑性樹脂組成物の成形品及び複合成形品
JP2010018683A (ja) * 2008-07-09 2010-01-28 Univ Of Ryukyus 射出成形用バガス繊維強化ポリプロピレン樹脂材とその製造方法および成形品
JP2017056594A (ja) * 2015-09-15 2017-03-23 日立化成株式会社 フィブロイン複合体、及びその製造方法
WO2018034111A1 (fr) * 2016-08-19 2018-02-22 国立研究開発法人理化学研究所 Composition de moulage composite comprenant une protéine de type fibroïne, et procédé de production de la composition de moulage composite
WO2019066028A1 (fr) * 2017-09-29 2019-04-04 内浜化成株式会社 Matériau composite renforcé par des fibres, additif pour matériau composite renforcé par des fibres et procédé de production d'un matériau composite renforcé par des fibres

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPWO2022014525A1 (fr) * 2020-07-15 2022-01-20
WO2022014525A1 (fr) * 2020-07-15 2022-01-20 Ｓｐｉｂｅｒ株式会社 Agent d'ouverture de fibres
JP7804285B2 (ja) 2020-07-15 2026-01-22 Ｓｐｉｂｅｒ株式会社 開繊剤

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