WO2009153923A1 - 可溶性羽毛ケラチン蛋白質の製造方法 - Google Patents

可溶性羽毛ケラチン蛋白質の製造方法 Download PDF

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Publication number
WO2009153923A1
WO2009153923A1 PCT/JP2009/002451 JP2009002451W WO2009153923A1 WO 2009153923 A1 WO2009153923 A1 WO 2009153923A1 JP 2009002451 W JP2009002451 W JP 2009002451W WO 2009153923 A1 WO2009153923 A1 WO 2009153923A1
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Prior art keywords
solution
keratin protein
feather keratin
soluble
producing
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Ceased
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PCT/JP2009/002451
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English (en)
French (fr)
Japanese (ja)
Inventor
新井幸三
篠塚雅子
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ECOLOGYSUPPORT Co Ltd
Ibaraki Prefecture
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ECOLOGYSUPPORT Co Ltd
Ibaraki Prefecture
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08H—DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS
    • C08H1/00—Macromolecular products derived from proteins
    • 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
    • C08L89/04—Products derived from waste materials, e.g. horn, hoof or hair

Definitions

  • the present invention relates to a method for producing a soluble feather keratin protein that treats feathers produced by waste chicken, broiler treatment, etc., and converts them into soluble feather keratin protein.
  • feathers produced by waste chicken and broiler processing are finely cut and used as fertilizer, but most are incinerated. In recent years, a large amount of duvets have been discarded, but most of these have been incinerated.
  • feathers are natural resources, and attempts have been made to solubilize feather fibers from the standpoint of effectively using discarded feathers. Examples of these attempts include, for example, Patent Documents 1, 2, and 3.
  • Patent Document 1 discloses that after a keratin protein fiber having a crosslinked structure is reduced in a liquid, insoluble matters are removed, and a reducing agent is further removed to obtain soluble keratin. It is the manufacturing method of soluble keratin by adding after removing a thing.
  • Patent Document 2 is a method for producing a feather keratin hydrolyzate or a salt thereof comprising at least the following steps (A) to (C): (A) A step of softening the feathers by immersing the feathers in a non-alkaline aqueous solution with or without a reducing agent and increasing the temperature to 121 to 136 ° C. while applying pressure to 0.2 to 0.32 MPa. (B) After adjusting the pH of the feather-containing non-alkaline aqueous solution obtained by the step (A) to alkali by adding a base, a protease is added to cause a hydrolysis reaction, thereby partially softening the feathers. The process of digesting.
  • the partially digested feather obtained in step (B) is selected from (I) a step of chemically modifying with a hydrophilic substituent, and / or (II) urea, alcohol, polyhydric alcohol A dissolution step of solubilizing the polymer in an aqueous solution containing one or more types.
  • Patent Document 3 describes (1) oligo ⁇ -keratin derivatives obtained by shape conversion and transformation by alkali treatment, and / or (2) shape conversion by ultraviolet irradiation treatment subsequent to the treatment of (1) above. And a method for solubilizing or microemulsifying and dispersing a water-insoluble substance in the presence of an aqueous solution of an oligo ⁇ -keratin derivative obtained by transformation.
  • the present invention provides a low-cost, high-yield production method for converting feathers that are produced during waste chicken or broiler treatment or duvet disposal and difficult to effectively use as they are into soluble feather keratin protein. It is a problem to be solved.
  • a thioglycolic acid (TGA) solution adjusted to be alkaline is added to water in which bird's feathers are immersed, and the mixture is shaken with stirring, and the solution obtained in the first step is brought near neutrality.
  • TGA thioglycolic acid
  • the thioglycolic acid solution in the first step is adjusted to be alkaline with a hydroxide of lithium, sodium, ammonium or potassium.
  • these solutions are adjusted to pH 8.0-13.
  • the adjustment of the solution in the second step to near neutrality is performed by adding acetic acid to the solution.
  • the solution was adjusted to pH 5 to 8.0.
  • the stirring and shaking in the first step is carried out while maintaining the solution at 20 to 50 ° C. This was done for 120 hours.
  • 5 of the present invention is the method for producing soluble feather keratin protein of 1, 2, 3 or 4 of the present invention, wherein hydrogen peroxide, sodium bromate or air is used as the oxidizing agent in the second step. It is.
  • soluble feather keratin protein of 1, 2, 3 or 4 of the present invention is the method for producing a soluble feather keratin protein of 1, 2, 3 or 4 of the present invention, wherein hydrogen peroxide or sodium bromate is used as an oxidizing agent in the second step, and the hydrogen peroxide Alternatively, sodium bromate is gradually added continuously for a certain period of time in the first half of the standing time.
  • the present invention is the method for producing the soluble feather keratin protein of 1, 2, 3 or 4 of the present invention, wherein air is used as an oxidizing agent in the second step, and the air is allowed to stand for the entire period of time. It is to be added by continuous bubbling.
  • the method for producing the soluble feather keratin protein of 1, 2, 3, 4, 5, 6 or 7 of the present invention wherein insoluble matter is removed from the solution obtained in the second step, The solution is adjusted to around pH 2 to 4 to precipitate dissolved feather keratin protein, and the precipitated feather keratin protein is recovered by centrifugation.
  • 9 of the present invention is a method for producing the soluble feather keratin protein of 1, 2, 3, 4, 5, 6 or 7 of the present invention, wherein the solution obtained in the second step is adjusted to pH 7-8, Before and after this adjustment, the solution was filtered to remove insoluble matters, and then the solution was desalted through a column with a molecular weight cut off of 1000 to 5000 to separate dissolved feather keratin protein. The feather keratin protein was recovered by collecting the fractions and freeze-drying them.
  • feathers produced by waste chicken or broiler treatment can be easily and inexpensively converted into soluble feather keratin protein, which can be used effectively.
  • Feather keratin fibers have a large network structure with a high crosslink density due to the presence of a large amount of disulfide (-SS-) bonds between or within the protein molecules, and solubilization is difficult.
  • a disulfide bond is cleaved by reduction and converted into a sulfhydryl group to eliminate keratin chain crosslinking. Even if it appears that the polymer dissolution conditions are satisfied, it does not actually dissolve easily.
  • the high molecular weight keratin peptide chain does not dissolve in water only by ionization of the sulfhydryl group.
  • a protein containing a sulfhydryl group has high reactivity and is rapidly oxidized in air and insolubilized. According to the method for producing a soluble feather keratin protein of 1 of the present invention, it is possible to solve such a problem by a simple method and to obtain a soluble feather keratin protein having a high yield and stability.
  • the pH of the thioglycolic acid solution can be adjusted appropriately.
  • the pH of the solution can be easily adjusted prior to the introduction of the oxidizing agent.
  • the reaction can proceed well.
  • the generated cysteine residue is oxidized to form a disulfide bond.
  • Two kinds of reactions among the three kinds of reactions can be easily and satisfactorily caused, but among the three kinds, other kinds of reactions that inhibit the dissolution of keratin can be suppressed.
  • each of the oxidizing agents is gradually added during the first half of the standing time as described above, or the total time thereof. In this way, two of the three reactions that oxidize the generated cysteine residue and generate a disulfide bond are efficiently generated and dissolved. Another kind of reaction which inhibits can be suppressed effectively.
  • the soluble feather keratin protein can be favorably recovered from the solution.
  • the method for producing the soluble feather keratin protein of the present invention comprises adding a thioglycolic acid solution adjusted to alkalinity to water dipped in bird feathers, and stirring and shaking the solution obtained in the first process. And a second step of producing a soluble feather keratin protein by adding the oxidizing agent to this solution and leaving it for a predetermined time while adding an oxidizing agent.
  • the target feathers are those of birds, and feathers generated by waste chickens or broiler treatment are particularly planned, but are not limited thereto.
  • Such bird feathers which are the raw materials, are pre-washed with a neutral detergent to remove dirt, then washed with water to remove the neutral detergent, then air-dried and chopped to 1-5 mm. .
  • the first step is started.
  • the feather is immersed in water.
  • This water is suitably 20 to 200 times the weight of the feather.
  • the thioglycolic acid solution is adjusted to be alkaline and added to the water. It is appropriate to determine the amount of thioglycolic acid dissolved so that the thioglycolic acid solution concentration is about 0.05 to 5 mol / l.
  • the thioglycolic acid solution is preferably adjusted to pH 9.0 to 13, but various bases can be freely employed for this purpose. For example, lithium, sodium, ammonium, or potassium hydroxide can be employed.
  • the thioglycolic acid adjusted to alkalinity is added to the water which immersed the feather, and this is stirred and shaken. The stirring and shaking are suitably performed for 1/3 to 120 hours while maintaining the solution at 20 to 50 ° C.
  • the cystine residue of the keratin protein molecule constituting the feather is reduced by thioglycolic acid as follows.
  • the disulfide group of the cystine residue is reduced by thioglycolic acid under the above alkaline and temperature conditions, and a part of the disulfide group is converted into a sulfhydryl group to form a cysteine residue.
  • CMAD carboxymethylalanyl sulfide residue
  • carboxymethylalanyl sulfide residue thus produced is further reduced by thioglycolic acid as shown in Chemical Formula 2, and a part of the disulfide group is similarly converted to a sulfhydryl group to convert the cysteine residue. And simultaneously produces dithiodiglycolic acid (DTDG).
  • thioglycolic acid as shown in Chemical Formula 2
  • a part of the disulfide group is similarly converted to a sulfhydryl group to convert the cysteine residue.
  • DTDG dithiodiglycolic acid
  • the dissolution condition of the high molecular keratin protein molecular chain is satisfied, but the pK value of the sulfhydryl group is about 9 (pK value as amino acid cysteine is 8.35), In a normal pH range where no hydrolysis of the peptide chain occurs, the high molecular weight keratin peptide chain cannot be dissolved in water only by ionization of the sulfhydryl group.
  • the solution obtained in the first step is adjusted to near neutral, and left for a predetermined time while adding an oxidizing agent to this solution to produce soluble feather keratin protein.
  • the adjustment of the solution to pH 5 to 8.0 can be freely performed using various acids.
  • acetic acid is used and adjusted to the pH by adding it.
  • this solution is allowed to stand for a predetermined time while adding an oxidizing agent and maintaining it at around 20 ° C.
  • the oxidizing agent hydrogen peroxide, sodium bromate or air can be used.
  • hydrogen peroxide or sodium bromate it is appropriate to gradually add the oxidant continuously during a certain period of the first half of the total time of leaving. .
  • the solution concentration of the oxidizing agent is suitably 1/10 2 to 1/10 mol / l.
  • air it is appropriate to add the air by continuously bubbling during the entire standing time.
  • the solution should be kept at around 20 ° C.
  • the predetermined time of standing while maintaining the temperature around 20 ° C. and adding the oxidizing agent is about 3 to 10 hours. This can produce soluble feather keratin.
  • chemical formula 3 is a disulfide bond formation reaction caused by the oxidation of sulfhydryl groups bound to the keratin protein molecular chain, which is a high molecular chain.
  • the reaction rate of the generated disulfide bond is compared with the reaction rate of the keratin polymer chain of formula 4-the low molecule (thioglycolic acid) and the reaction rate of the low molecules producing the dithiodiglycolic acid (DTDG) of formula 5. And small enough.
  • Chemical formula 5 is a reaction between low molecular weight thioglycolic acids, which is unrelated to the reaction of feather keratin protein. Chemical formula 5 has the fastest reaction rate among the above three oxidation reactions, and is rapid. To produce dithiodiglycolic acid.
  • the soluble feather keratin protein produced as described above is recovered from the above solution as follows.
  • the solution is adjusted to pH 3-4 with acetic acid or hydrochloric acid to precipitate feather keratin protein.
  • the precipitated feather keratin protein can be separated from the solution by centrifugation.
  • the insoluble matter can be removed from the solution by filtration or the like.
  • the protein can be stored in an acetic acid acid paste in a cool and dark place.
  • feather keratin protein can be obtained in a solid state by passing through a column packed with a gel having a molecular weight cut off of 1000 to 5000, desalting and fractionating, and lyophilizing all fractions.
  • the protein can be stored in a cool and dark place.
  • the feather keratin protein in order to make the feather keratin protein soluble in water, as shown in Chemical Formula 2, the feather keratin protein is reduced with an excess of thioglycolic acid, and then Chemical Formula 4, As shown in Chemical Formula 5 and Chemical Formula 6, the system is oxidized to convert the remaining sulfhydryl group in the solution into a mixed disulfide group (carboxymethylalanyl disulfide group).
  • a sufficient amount of mixed disulfide groups can be introduced into the high molecular weight feather keratin protein molecular chain.
  • feathers produced by waste chickens or broiler treatments can be easily and inexpensively converted into soluble feather keratin proteins, which are effectively used. can do.
  • Futon batting feathers (white goose 100%) were washed with a neutral detergent, then washed with water and dried. 1 g of each feather was put into four 300 ml flasks, and 50 ml of 0.2 mol / l thioglycolic acid solution adjusted to pH 11.0 with sodium hydroxide was added to three of them. 50 ml of 0.5 mol / l thioglycolic acid solution adjusted to pH 11.0 with sodium hydroxide was added to the book, and the Na-TGA concentration of 0.5 mol / l was added.
  • Precipitate weight and insoluble residue weight Wres were measured after vacuum drying.
  • the residue yield Yres (%) was calculated from the insoluble residue weight by the following equation (1).
  • Example 1 the yield of soluble feather keratin protein obtained at a TGA concentration of 0.2 mol / l or more, a temperature of 30 ° C. or more, and a reaction time of 48 hours or more is Reach over 95%. 84% was also obtained by reduction reaction at 50 ° C. for 1/3 hour.
  • Futon batting feathers (white goose 100%) were washed with a neutral detergent, then washed with water, dried and chopped to about 5 mm.
  • the feathers were put into 10 flasks of 50 ml each in an amount of 0.2 g and pH 9.0, 10.0, 10.5, 10.75, 11.0, 11.25, 11.5, 12. 10 ml of a 0.2 mol / l thioglycolic acid solution adjusted to 0, 12.5, and 13.0 was added to the flask, and these were stirred and shaken at 30 ° C. for 48 hours. Then, the pH was adjusted to 7 with acetic acid.
  • Table 2 shows the relationship between the pH change of the sodium thioglycolate (Na-TGA) reduction system and the lyophilized yield Ysol.
  • Futon batting feathers (white goose 100%) were washed with a neutral detergent, then washed with water, dried and chopped to about 5 mm. 0.2g each of these feathers was put into six 50ml flasks and 10ml of 0.025, 0.05, 0.10, 0.15, 0.20, 0.50mol / l thioglycolic acid solution adjusted to pH 11.0 with sodium hydroxide was added to each flask. These were stirred and shaken at 30 ° C. for 48 hours, and then these solutions were brought to 30 ° C. and adjusted to pH 7 with acetic acid.
  • Table 3 shows the relationship between changes in thioglycolic acid (Na-TGA) concentration, freeze-dried yield, and residue yield.
  • Example 3 as can be understood from the data in Table 3, the freeze-dried yield and the residue dry yield greatly change depending on the thioglycolic acid concentration, and the thioglycolic acid concentration is the yield of soluble feather keratin protein. It was found to have a decisive influence on the rate. From the data in Table 3, it was found that the best results were obtained when the thioglycolic acid concentration was 0.20 mol / l, and that both the lyophilization yield and the residue yield agreed within experimental error.
  • Futon batting feathers (white goose 100%) were washed with a neutral detergent, then washed with water, dried and chopped to about 5 mm. This feather is put into 5 ml flasks of 0.2 g each, and 0.20 mol / l thioglycolic acid solution adjusted to pH 11.0 with sodium hydroxide is 5, 6, 8, 10 and 20 ml (as bath ratio). , 25, 30, 40, 50 and 100 times each) were added to the above flasks, and after stirring and shaking at 30 ° C. for 48 hours, the solutions were brought to 30 ° C. and adjusted to pH 7 with acetic acid. .
  • Example 4 As can be seen from the data in Table 4, when the bath ratio is 50 times, the yield shows the maximum value.
  • TGA thioglycolic acid
  • -SS- disulfide
  • the soluble feather keratin protein obtained by changing the pH of the reducing system was characterized by molecular weight using SDS-PAGE electrophoresis.
  • SDS-PAGE electrophoresis As a sample, conditions of pH 10.0 and 10.5 in Table 2 in Example 2 (reduction: 0.2 mol / l Na-TGA 10 mL (50 times bath ratio), 30 ° C., 48 h; oxidation: 0.2 mol / l NaBrO 3 , FIG. 1 shows SDS electrophoresis patterns obtained at 30 ° C. and 24 h. With lyophilized yields of 71.5 and 88.0%, respectively, along with that of untreated feathers. The molecular weight of any sample was about 12600, which was a monodispersed protein similar to the untreated feather (original) protein, and it was found that the molecular weight did not decrease due to the solubilization treatment.
  • feathers produced by waste chickens, broiler treatments, etc. it is possible to treat feathers produced by waste chickens, broiler treatments, etc., and easily convert them into soluble keratin proteins, such as repairing damaged hair or nails, etc. It can be effectively used in the field of cosmetics, foods such as functional protein films and protein molded products, industrial fields, and fertilizers to be introduced into paddy fields.

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PCT/JP2009/002451 2008-06-16 2009-06-02 可溶性羽毛ケラチン蛋白質の製造方法 Ceased WO2009153923A1 (ja)

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2010155823A (ja) * 2008-12-03 2010-07-15 Milbon Co Ltd 毛髪処理方法及び毛髪処理剤
WO2010143484A1 (ja) * 2009-06-12 2010-12-16 株式会社ミルボン 毛髪処理剤及び毛髪処理剤用原料
JP2011144127A (ja) * 2010-01-13 2011-07-28 Milbon Co Ltd 毛髪処理剤及び毛髪処理剤用原料
CN119662303A (zh) * 2025-02-17 2025-03-21 淄博凯美可工贸有限公司 一种原油预处理破乳剂的制备方法

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8575313B2 (en) 2010-11-19 2013-11-05 Universiti Malaysia Pahang Process for extracting keratin

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH07126296A (ja) * 1993-05-24 1995-05-16 Kao Corp 可溶化蛋白質
JPH092919A (ja) * 1995-06-19 1997-01-07 Kao Corp 新規ゲル化剤及びゲル組成物

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2007176863A (ja) * 2005-12-28 2007-07-12 Gunei Shoji Kk 可溶化蛋白質の製造方法

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH07126296A (ja) * 1993-05-24 1995-05-16 Kao Corp 可溶化蛋白質
JPH092919A (ja) * 1995-06-19 1997-01-07 Kao Corp 新規ゲル化剤及びゲル組成物

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2010155823A (ja) * 2008-12-03 2010-07-15 Milbon Co Ltd 毛髪処理方法及び毛髪処理剤
WO2010143484A1 (ja) * 2009-06-12 2010-12-16 株式会社ミルボン 毛髪処理剤及び毛髪処理剤用原料
KR20120046108A (ko) * 2009-06-12 2012-05-09 가부시키가이샤 미르본 모발처리제 및 모발처리제용 원료
KR101951923B1 (ko) 2009-06-12 2019-02-25 가부시키가이샤 미르본 모발처리제 및 모발처리제용 원료
JP2011144127A (ja) * 2010-01-13 2011-07-28 Milbon Co Ltd 毛髪処理剤及び毛髪処理剤用原料
CN119662303A (zh) * 2025-02-17 2025-03-21 淄博凯美可工贸有限公司 一种原油预处理破乳剂的制备方法

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