CN113512104A - Preparation method of pig hoof nail keratin - Google Patents
Preparation method of pig hoof nail keratin Download PDFInfo
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- CN113512104A CN113512104A CN202110461494.3A CN202110461494A CN113512104A CN 113512104 A CN113512104 A CN 113512104A CN 202110461494 A CN202110461494 A CN 202110461494A CN 113512104 A CN113512104 A CN 113512104A
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- keratin
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- 102000011782 Keratins Human genes 0.000 title claims abstract description 64
- 108010076876 Keratins Proteins 0.000 title claims abstract description 64
- 210000000003 hoof Anatomy 0.000 title claims abstract description 16
- 238000002360 preparation method Methods 0.000 title claims abstract description 10
- 239000011259 mixed solution Substances 0.000 claims abstract description 37
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims abstract description 29
- 239000004202 carbamide Substances 0.000 claims abstract description 29
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 29
- 239000000843 powder Substances 0.000 claims abstract description 25
- 239000000243 solution Substances 0.000 claims abstract description 25
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims abstract description 24
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims abstract description 16
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 14
- 239000008367 deionised water Substances 0.000 claims abstract description 13
- 229910021641 deionized water Inorganic materials 0.000 claims abstract description 13
- 238000000605 extraction Methods 0.000 claims abstract description 12
- 238000010438 heat treatment Methods 0.000 claims abstract description 12
- 239000006228 supernatant Substances 0.000 claims abstract description 12
- 239000004201 L-cysteine Substances 0.000 claims abstract description 8
- 235000013878 L-cysteine Nutrition 0.000 claims abstract description 8
- 238000005303 weighing Methods 0.000 claims abstract description 7
- 239000002244 precipitate Substances 0.000 claims abstract description 6
- 238000004108 freeze drying Methods 0.000 claims abstract description 5
- 238000000227 grinding Methods 0.000 claims abstract description 5
- 238000005406 washing Methods 0.000 claims abstract description 5
- 238000000034 method Methods 0.000 claims description 10
- 238000007710 freezing Methods 0.000 claims description 4
- 230000008014 freezing Effects 0.000 claims description 4
- 241000282898 Sus scrofa Species 0.000 description 20
- 239000000463 material Substances 0.000 description 5
- 210000003746 feather Anatomy 0.000 description 3
- 101710200191 Feather keratin Proteins 0.000 description 2
- 241000282894 Sus scrofa domesticus Species 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 210000004209 hair Anatomy 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 238000001878 scanning electron micrograph Methods 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 210000002268 wool Anatomy 0.000 description 2
- 241000233866 Fungi Species 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 150000001371 alpha-amino acids Chemical class 0.000 description 1
- 235000008206 alpha-amino acids Nutrition 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 239000003337 fertilizer Substances 0.000 description 1
- 210000003284 horn Anatomy 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000000413 hydrolysate Substances 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 108010059345 keratinase Proteins 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 210000001724 microfibril Anatomy 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Images
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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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4741—Keratin; Cytokeratin
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Cosmetics (AREA)
Abstract
The invention discloses a preparation method of pig hoof nail keratin, which comprises the following steps: a, weighing a certain amount of urea reagent, and adding the urea reagent into deionized water to prepare a urea solution with a certain concentration; b, adding pig nail powder into the obtained urea solution in a proportion to obtain a first mixed solution; c, adding L-cysteine into the obtained mixed solution according to a proportion to obtain a second mixed solution; d, dropwise adding a NaOH solution into the obtained second mixed solution, adjusting the pH value, and then placing the mixed solution in a digital display constant-temperature water bath kettle for water bath heating for a period of time; e, taking out the second mixed solution after a period of time, and centrifuging the mixed solution by using a high-speed refrigerated centrifuge to obtain a supernatant for later use; and F, dropwise adding Hcl into the supernatant, adjusting the pH until dissolved keratin is precipitated, washing the precipitate with deionized water, freeze-drying in a vacuum freeze dryer, and grinding to obtain fresh keratin powder, wherein the extracted keratin has high extraction rate and high purity.
Description
Technical Field
The invention relates to the technical field of biosolid powder, in particular to a preparation method of pig hoof nail keratin.
Background
Many natural high molecular materials with good properties exist in nature, the reasonable utilization of the materials can reduce the problem of environmental pollution caused by artificial synthesis and high molecular materials, and the development concept of green chemistry is met. Among them, keratin is a fibrous connective protein widely present in living bodies, and is classified into soft keratin and hard keratin, mainly present in hooves, feathers, hair, skin and horns of vertebrates. The keratin resources in China are very rich, but are not fully developed and utilized at present. Keratin is utilized in various fields at present, wherein feather keratin can be used as high-quality feed protein, feather coarse powder obtained by primary processing can be used for producing amino acid fertilizer, and hydrolysate of feather can also be utilized in tanning industry. Some skin diseases occur because keratinase produced by fungi permeates the skin, and keratin can be used in the pharmaceutical industry and the like by utilizing this property. Therefore, the application development of the keratin material is very rapid, and the keratin material has very good development prospect in a plurality of fields.
The keratin has a three-stage molecular structure, the primary structure of the keratin is formed by connecting 19 kinds of alpha-amino acids (-NHCO-) through peptide bonds, and the amino acid sequences and the contents of the keratin in different organisms are greatly different. Its secondary structure comprises two structures of alpha-helix and beta-sheet, and the keratin contained in ordinary human hair and wool belongs to alpha-helix structure, while the keratin contained in ordinary hoof and scales belongs to beta-sheet structure. Wherein the alpha-helical structure has good expansion and contraction performance, and the beta-folded structure has good tensile strength, so that part of keratin has strong toughness and mechanical strength. Its tertiary molecular structure is a lightly coiled alpha-helix of keratin, called supercoiled structure. The supercoils form dimers, which are the true physical structural subunits of the microfibrils, and are referred to as "molecular pairs". The main acting forces among the keratin macromolecule main chains are hydrogen bonds, disulfide bonds and salt bonds, so that common solvents or acid-base solutions cannot dissolve keratin, stronger acid-base solutions can dissolve keratin, and peptide chains are broken while intermolecular action and secondary and tertiary structures of keratin are damaged.
At present, the application of keratin is very wide in China, the extraction and application of wool keratin and the extraction and application of feather keratin have higher extraction rate, but the extraction and application of pig nail keratin cannot be better developed due to the hardness of pig nail, so that the invention mainly solves the problem of low extraction rate of pig nail keratin.
Disclosure of Invention
The invention aims to provide a preparation method of pig nail keratin, which aims to solve the problems that the hardness of the existing pig nail is hard and the existing technology is inconvenient to extract in the background technology.
In order to achieve the purpose, the invention provides the following technical scheme: a preparation method of pig hoof nail keratin comprises the following steps:
(A) weighing a certain amount of urea reagent, and adding the urea reagent into deionized water to prepare a urea solution with a certain concentration;
(B) adding pig nail powder into the obtained urea solution in a proportion to obtain a first mixed solution;
(C) and adding L-cysteine into the obtained mixed solution in a ratio to obtain a second mixed solution.
(D) And dropwise adding a NaOH solution into the obtained second mixed solution, adjusting the pH value, and then placing the mixed solution in a digital display constant-temperature water bath kettle for water bath heating for a period of time.
(E) And taking out the second mixed solution after a period of time, and centrifuging the mixed solution by using a high-speed refrigerated centrifuge to obtain a supernatant for later use.
(F) And (3) dropwise adding Hcl into the supernatant, adjusting the pH until dissolved keratin is precipitated, washing the precipitate with deionized water, freeze-drying in a vacuum freeze dryer, and grinding to obtain fresh keratin powder.
Preferably, the keratin extraction rate is up to 81%.
Preferably, in the step (a), the urea reagent is dissolved in sterile deionized water, heated and stirred in a water bath at 70 ℃, and cooled to room temperature after being dissolved.
Preferably, in the step (B), pig nail powder is added to the urea solution, and the weight ratio of the pig nail powder to the urea solution is 1: 15.
Preferably, in the step (C), the amount of L-cysteine is 15% of the total amount of the pig nail powder.
Preferably, in the step (D), the concentration of NaOH is 50%, the pH of the mixed solution is adjusted to 11.5, the water bath heating temperature is 70 ℃, and the heating time is 16 h.
Preferably, in the step (E), the rotation speed of the high-speed freezing centrifuge is 10000r/m, and the time is 20 min.
Preferably, in the step (F), when the concentration of Hcl is 0.2mol/L and the pH is adjusted to 4, the dissolved keratin is completely precipitated.
Compared with the prior art, the invention has the beneficial effects that: the preparation method of the pig nail keratin comprises the following steps:
1. compared with other modes, the keratin extracted by the method has higher extraction rate, has the extraction rate as high as 81 percent, and does not consume and waste other consumables;
2. the keratin extracted by the method has high purity, does not contain inferior partial impurities, and has high extraction purity.
Drawings
FIG. 1 is a scanning electron micrograph of ungula Sus Domestica keratin;
FIG. 2 is a scanning electron micrograph of ungula Sus Domestica powder.
Detailed Description
The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the embodiments of the present invention, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
The invention provides a technical scheme that: a preparation method of pig hoof nail keratin comprises the following steps:
a, weighing a certain amount of urea reagent, and adding the urea reagent into deionized water to prepare a urea solution with a certain concentration;
b, adding pig nail powder into the obtained urea solution in a proportion to obtain a first mixed solution;
and C, adding L-cysteine into the obtained mixed solution in a ratio to obtain a second mixed solution.
And D, dropwise adding a NaOH solution into the obtained second mixed solution, adjusting the pH value, and then placing the mixed solution in a digital display constant-temperature water bath kettle for water bath heating for a period of time.
And E, taking out the second mixed solution after a period of time, and centrifuging the mixed solution by using a high-speed refrigerated centrifuge to obtain a supernatant for later use.
And F, dropwise adding Hcl into the supernatant, adjusting the pH until dissolved keratin is precipitated, washing the precipitate with deionized water, freeze-drying in a vacuum freeze dryer, and grinding to obtain fresh keratin powder.
The extraction rate of the keratin is as high as 81 percent.
In the step A, dissolving a urea reagent in sterile deionized water, heating and stirring in a water bath at 70 ℃, and cooling to room temperature after dissolving.
And in the step B, pig nail powder is added into the urea solution, and the weight ratio of the pig nail powder to the urea solution is 1: 15.
In the step C, the amount of the L-cysteine accounts for 15% of the total amount of the pig nail powder.
In the step D, the concentration of NaOH is 50%, the pH value of the mixed solution is adjusted to 11.5, the water bath heating temperature is 70 ℃, and the heating time is 16 h.
In the step E, the rotating speed of the high-speed freezing centrifugal machine is 10000r/m, and the time is 20 min.
In step F, when the Hcl concentration is 0.2mol/L and the pH is adjusted to 4, the dissolved keratin is completely precipitated.
Example (b): extracting the pig nail keratin:
weighing 24g of urea reagent, adding the urea reagent into a proper amount of deionized water, stirring and dissolving, and then carrying out constant volume preparation by using a 100ml volumetric flask to prepare a 4mol/L urea solution for later use; respectively weighing 30g of urea solution and 3g of pig nail powder to prepare mixed solution, then weighing 0.45g of L-cysteine reagent, adding the mixed solution into the mixed solution, shaking uniformly, adjusting the PH of the mixed solution to 11.5 by using NaOH solution with the mass fraction of 50%, placing the mixed solution in a digital display constant temperature water shaking table, and heating the mixed solution in a water bath for 16 hours, wherein the temperature is set at 70 ℃, and the vibration amplitude is 150 r/min. Taking out the keratin powder after 16h, centrifuging the keratin powder by using a high-speed refrigerated centrifuge to obtain supernatant, freezing the supernatant by using the refrigerated centrifuge for 20min, taking the supernatant by 10000r for later use, adjusting the pH of the supernatant to 4 by using HcL solution of 0.2mol/L until dissolved keratin is precipitated, washing the precipitate by using deionized water, and then freeze-drying the precipitate by using a vacuum freeze dryer to obtain fresh keratin, and grinding the fresh keratin into powder to obtain the keratin powder.
The above description is only of the preferred embodiments of the present invention, and it should be noted that: it will be apparent to those skilled in the art that various modifications and adaptations can be made without departing from the principles of the invention and these are intended to be within the scope of the invention.
Although embodiments of the present invention have been shown and described, it will be appreciated by those skilled in the art that changes, modifications, substitutions and alterations can be made in these embodiments without departing from the principles and spirit of the invention, the scope of which is defined in the appended claims and their equivalents.
Claims (8)
1. A preparation method of pig hoof nail keratin is characterized in that: the method comprises the following steps:
(A) weighing a certain amount of urea reagent, and adding the urea reagent into deionized water to prepare a urea solution with a certain concentration;
(B) adding pig nail powder into the obtained urea solution in a proportion to obtain a first mixed solution;
(C) adding L-cysteine into the obtained mixed solution in a proportion to obtain a second mixed solution;
(D) dropwise adding a NaOH solution into the obtained second mixed solution, adjusting the pH value, and then placing the mixed solution in a digital display constant-temperature water bath kettle for water bath heating for a period of time;
(E) taking out the second mixed solution after a period of time, centrifuging the mixed solution by using a high-speed refrigerated centrifuge, and taking supernatant for later use;
(F) and (3) dropwise adding Hcl into the supernatant, adjusting the pH until dissolved keratin is precipitated, washing the precipitate with deionized water, freeze-drying in a vacuum freeze dryer, and grinding to obtain fresh keratin powder.
2. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: the keratin extraction rate is as high as 81%.
3. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (A), the urea reagent is dissolved in sterile deionized water, heated and stirred in a water bath at 70 ℃, and cooled to room temperature after being dissolved.
4. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (B), pig nail powder is added into the urea solution, and the weight ratio of the pig nail powder to the urea solution is 1: 15.
5. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (C), the amount of the L-cysteine accounts for 15% of the total amount of the pig nail powder.
6. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (D), the concentration of NaOH is 50%, the pH value of the mixed solution is adjusted to 11.5, the heating temperature of the water bath is 70 ℃, and the heating time is 16 h.
7. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (E), the rotating speed of the high-speed freezing centrifugal machine is 10000r/m, and the time is 20 min.
8. The method of claim 1, wherein the porcine hoof nail keratin is prepared by: in the step (F), when the concentration of Hcl is 0.2mol/L and the pH is adjusted to 4, the dissolved keratin is completely precipitated.
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| Application Number | Priority Date | Filing Date | Title |
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| CN202110461494.3A CN113512104A (en) | 2021-04-27 | 2021-04-27 | Preparation method of pig hoof nail keratin |
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| CN202110461494.3A CN113512104A (en) | 2021-04-27 | 2021-04-27 | Preparation method of pig hoof nail keratin |
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Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5696164A (en) * | 1994-12-22 | 1997-12-09 | Johnson & Johnson Consumer Products, Inc. | Antifungal treatment of nails |
| US20100196302A1 (en) * | 2007-06-28 | 2010-08-05 | Alane Beatriz Vermelho | Keratin Hydrolysates, Process for Their Production and Cosmetic Composition Containing the Same |
| CN103981247A (en) * | 2014-06-03 | 2014-08-13 | 中国农业科学院农产品加工研究所 | Preparation method of keratin |
| US20150080552A1 (en) * | 2011-08-17 | 2015-03-19 | Keranetics Llc | Methods for extracting keratin proteins |
| CN108716122A (en) * | 2018-06-06 | 2018-10-30 | 叶建民 | A kind of preparation method of modified fish oil keratin stiffening agent |
| CN110511405A (en) * | 2019-10-11 | 2019-11-29 | 四川大学 | A kind of antimicrobial form keratin based aquagel and preparation method thereof |
-
2021
- 2021-04-27 CN CN202110461494.3A patent/CN113512104A/en active Pending
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5696164A (en) * | 1994-12-22 | 1997-12-09 | Johnson & Johnson Consumer Products, Inc. | Antifungal treatment of nails |
| US20100196302A1 (en) * | 2007-06-28 | 2010-08-05 | Alane Beatriz Vermelho | Keratin Hydrolysates, Process for Their Production and Cosmetic Composition Containing the Same |
| US20150080552A1 (en) * | 2011-08-17 | 2015-03-19 | Keranetics Llc | Methods for extracting keratin proteins |
| CN103981247A (en) * | 2014-06-03 | 2014-08-13 | 中国农业科学院农产品加工研究所 | Preparation method of keratin |
| CN108716122A (en) * | 2018-06-06 | 2018-10-30 | 叶建民 | A kind of preparation method of modified fish oil keratin stiffening agent |
| CN110511405A (en) * | 2019-10-11 | 2019-11-29 | 四川大学 | A kind of antimicrobial form keratin based aquagel and preparation method thereof |
Non-Patent Citations (3)
| Title |
|---|
| MING HE等: "Blend modification of feather keratin-based films using sodium alginate", 《J.APPL.POLYM.SCI.》 * |
| 袁艳红等: "一种角蛋白发泡液的制备", 《精细化工》 * |
| 袁艳红等: "还原剂对猪蹄甲发泡蛋白泡沫性能及结构的影响", 《2011智能信息技术应用学会会议论文集》 * |
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Application publication date: 20211019 |
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