CN112812349A - Method for preparing high-strength pure feather keratin gel by one-step method - Google Patents
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- 238000000034 method Methods 0.000 title claims abstract description 28
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- 108010076876 Keratins Proteins 0.000 claims abstract description 52
- 210000003746 feather Anatomy 0.000 claims abstract description 39
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 29
- 238000001035 drying Methods 0.000 claims abstract description 15
- 238000004108 freeze drying Methods 0.000 claims abstract description 6
- 238000005406 washing Methods 0.000 claims abstract description 6
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 21
- UMGDCJDMYOKAJW-UHFFFAOYSA-N thiourea Chemical compound NC(N)=S UMGDCJDMYOKAJW-UHFFFAOYSA-N 0.000 claims description 14
- 239000008367 deionised water Substances 0.000 claims description 11
- 229910021641 deionized water Inorganic materials 0.000 claims description 11
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- 238000003756 stirring Methods 0.000 claims description 8
- 239000004202 carbamide Substances 0.000 claims description 7
- 239000003960 organic solvent Substances 0.000 claims description 7
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 claims description 7
- 229940001584 sodium metabisulfite Drugs 0.000 claims description 7
- 235000010262 sodium metabisulphite Nutrition 0.000 claims description 7
- 238000001816 cooling Methods 0.000 claims description 6
- 238000001914 filtration Methods 0.000 claims description 6
- 239000004677 Nylon Substances 0.000 claims description 5
- 238000004140 cleaning Methods 0.000 claims description 5
- 229920001778 nylon Polymers 0.000 claims description 5
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 claims description 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 claims description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 4
- 150000001875 compounds Chemical class 0.000 claims description 4
- 108010025899 gelatin film Proteins 0.000 claims description 3
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- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 5
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- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 1
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- 238000011069 regeneration method Methods 0.000 description 1
- 235000010413 sodium alginate Nutrition 0.000 description 1
- 229940005550 sodium alginate Drugs 0.000 description 1
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- 230000017423 tissue regeneration Effects 0.000 description 1
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- 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
- C08J5/18—Manufacture of films or sheets
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- 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
- C08J9/00—Working-up of macromolecular substances to porous or cellular articles or materials; After-treatment thereof
- C08J9/28—Working-up of macromolecular substances to porous or cellular articles or materials; After-treatment thereof by elimination of a liquid phase from a macromolecular composition or article, e.g. drying of coagulum
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- 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
- C08J2389/00—Characterised by the use of proteins; Derivatives thereof
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- Health & Medical Sciences (AREA)
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Abstract
The invention provides a method for preparing high-strength pure feather keratin gel by a one-step method, which takes feathers as raw materials, and obtains pure keratin gel by high-temperature dissolution in a composite solution, low-temperature solidification, gel block washing with water, sponge is obtained by freeze drying, and membrane is obtained by room-temperature drying (thin gel). The preparation is prepared by a one-step method, and the process of dialysis (or isoelectric precipitation), drying and redissolution is not required to be performed consistently, so that the method is simple, environment-friendly, economical and efficient; secondly, the prepared gel, sponge and film have good mechanical strength; and has biocompatibility, cell adhesion and proliferation performance and no cytotoxicity. Therefore, the keratin fiber can be used as a natural keratin polymer material to be applied to the field of biological medicine.
Description
Technical Field
The invention relates to a method for preparing high-strength pure feather keratin gel by a one-step method, belonging to biomedical natural high polymer materials.
Background
Keratin-based biomaterials have been extensively studied in the biomedical field over the last decade. Numerous literature studies have shown that keratin has biodegradability, biocompatibility, promotes cell adhesion, supports cell proliferation, and has the function of synthesizing extracellular matrix (ECM). Furthermore, keratin has a structure of various functional groups, which can be fine-tuned and modified according to the desired function. For example, the modified keratin may be used to bind hydrophobic and hydrophilic drugs or to react with specific functional groups of the drug to immobilize the drug thereon or to modulate the degradation rate of the keratin matrix. Various forms of keratin-based biomedical materials have been developed, such as films, hydrogels, sponges, membranes, sponge scaffolds, dressings or fibers, and the like. The application in bone tissue engineering, ocular tissue regeneration, wound healing, nerve regeneration, skin replacement and controllable drug delivery. However, pure keratin materials have limited applications due to brittleness, poor mechanical and processing properties, and the like, and thus, the addition of plasticizers, other synthetic or natural polymers, and crosslinking agents is required to solve these disadvantages.
Keratin is the main component of feather, wool and horns, has a content of about 90 percent in the feather, and is insoluble protein with acid resistance, alkali resistance and enzyme resistance. The first step of keratin material preparation is to dissolve and extract keratin, and the reduction method is generally used at present to extract and prepare the keratin material through complicated steps such as dissolution, filtration, dialysis (or isoelectric point precipitation), drying, redissolution and the like, but there are only reports of high-strength keratin gel, sponge and membrane. For example, in the patent "a method for preparing feather keratin sponge using feather" (CN 102492166A), feather keratin sponge is prepared by dissolving feather in a solution prepared from detergent and redox agent, filtering the solution, dialyzing (or chromatographing) to obtain pure keratin solution, and directly freeze-drying. Patent "a method for preparing feather keratin sponge membrane with feather residue" (CN 102516580A), is an opaque feather keratin sponge membrane prepared by directly stacking insoluble feather residue after extracting keratin in feather by reduction method, although the membrane has certain flexibility, it is only the stacking of insoluble residue in feather. Other most keratin gel, sponge and membrane materials are compounded with other macromolecules (such as CN201510298838.8 and CN201510299512.7 are keratin composite sodium alginate, and CN201810587364.2 is the compound of keratin and PVA) or added with a cross-linking agent to improve the strength.
Disclosure of Invention
The invention aims to provide a method for preparing high-strength pure feather keratin gel by a one-step method.
Preparation of high-strength pure feather keratin gel
Dissolving defatted feathers in a dissolving solution to obtain a feather keratin dissolving solution, filtering to remove undissolved feather debris, cooling and solidifying filtrate, and washing off various chemical substances in the gel by using deionized water to obtain pure keratin gel; the dissolving solution contains urea, thiourea and sodium metabisulfite, and the molar concentrations of the urea, the thiourea and the sodium metabisulfite are respectively 2-8 mol/L, 2-5 mol/L, 0.2-1 mol/L and 0.5-2 mol/L.
Freeze-drying the pure keratin gel to obtain sponge; the freeze drying is carried out for 12-24 hours at the temperature of-80 to-40 ℃.
And drying the pure keratin gel at room temperature to obtain a gel film.
The degreased feather is obtained by slowly stirring and soaking cleaned feathers in an organic solvent for 2-4 hours, cleaning with deionized water for three times and drying; the organic solvent is petroleum ether, acetone or ethanol.
The mass ratio of the degreased feathers to the dissolving solution is 0.01: 1-0.01: 3.
The dissolving temperature of the degreased feather in the dissolving solution is 70-100 ℃, and the dissolving time is 1-3 h.
The nylon net for filtering is 300-500 meshes in specification.
The cooling temperature is 0-40 ℃, and the cooling time is 0.5-2 h.
The deionized water washing is to wash off all compounds remained in a dissolving solution in the gel by using deionized water, and the specific operation is to soak the gel in water, wherein the mass-volume ratio of the gel to the water is 0.001-0.01 g/mL, and the water is changed every 1-3 h for 4-8 times.
Second, characterization of the morphology and structure of keratin gel, sponge and membrane
1. Macroscopic topography
The appearance appearances of the freshly prepared keratin gel, the sponge and the film are respectively shown in figures 1 and 2, the keratin gel is semitransparent, and the content of keratin is 4-7%. The right side is the freeze-dried feather keratin sponge, slightly contracted and porous. The transparency of the keratin film is high.
2. Infrared spectroscopic analysis
The infrared absorption spectrum of the keratin sponge is shown in fig. 3. Wherein, the thickness is 3387cm-1、1648cm-1、1531cm-1、1237cm-1Is sucked byThe peak is a characteristic absorption peak of human keratin, and is respectively assigned to an amide A band (first double-frequency resonance absorption of NH stretching and amide II), an amide I band (C = O stretching), an amide II band (CN stretching and NH bending) and an amide III band (CN stretching and NH bending). Indicating successful extraction of keratin.
Performance test of keratin gel, sponge and film
1. Intensity of feather keratin gel, sponge and film
FIG. 4 feather keratin gel is slightly deformed, but still intact, under the pressure of a bottle filled with 2.5L of water. FIG. 5 is a graph of tensile mechanical properties of feather keratin film, showing that the keratin film has higher strength.
2. Cell proliferation potency and cytotoxicity
FIG. 6 is a fluorescent micrograph of L929 cells cultured in direct contact with feather keratin membrane and stained after 24h of culture, showing that the membrane has good cell proliferation ability and no cytotoxicity.
3. Drug Release Properties
The release performance of the keratin gel to the simulated drug (rhodamine B) in the PBS buffer solution with different pH values is shown in figure 7, and it can be seen from the figure that under different pH values, the cumulative release rate of the simulated drug (rhodamine B) is gradually increased along with the prolonging of time, the cumulative release rate in 19 days is about 80%, and the requirement of compound slow release indicates that the keratin gel has good slow release performance.
In conclusion, the feather is used as a raw material, and the pure keratin gel is obtained by dissolving the feather in the composite dissolving solution at a high temperature, solidifying the feather at a low temperature, washing off all chemical substances in the gel with water, freezing and drying the gel to obtain the sponge, and drying the sponge at room temperature to obtain the gel film. The method for preparing the high-strength pure feather keratin gel, sponge and membrane by the one-step method does not need complicated dialysis (or isoelectric point precipitation), drying and redissolution processes, is simple, environment-friendly, economical and efficient, and the prepared gel, sponge and membrane have good mechanical strength, biocompatibility, cell adhesion and proliferation performance, drug slow release performance and no cytotoxicity. Therefore, the keratin fiber can be used as a natural keratin polymer material to be applied to the field of biological medicine.
Drawings
FIG. 1 shows the macroscopic morphology of feather keratin gel and sponge;
FIG. 2 is a macroscopic view of a feather keratin membrane;
FIG. 3 is an infrared spectrum of feather keratin;
FIG. 4 pressure-bearing diagram of feather keratin gel;
FIG. 5 is a drawing of the tensile mechanical properties of feather keratin films;
FIG. 6 is a fluorescent microscope photograph of L929 cells cultured directly on feather keratin membrane;
FIG. 7 is a drug release profile obtained by feather keratin gel.
Detailed Description
The preparation of the high performance keratin gel, sponge and film and the drug release properties of the keratin gel of the present invention are further illustrated by the following specific examples.
Example 1
(1) And (3) slowly stirring and soaking the cleaned feather in an organic solvent for 2 hours, and cleaning the feather with deionized water, and drying the feather in an oven at 60 ℃.
(2) Preparing a dissolving solution, wherein the molar concentration of urea is 2mol/L, the molar concentration of thiourea is 2mol/L, the molar concentration of sodium metabisulfite is 0.5mol/L, and the molar concentration of SDS is 0.5 mol/L.
(3) Dispersing the degreased feather in a dissolving solution at a feed liquid mass ratio of 0.01:1, and stirring and dissolving for 1h at 70 ℃.
(4) After completion of the dissolution, the residue was filtered through a 300-mesh nylon net to remove undissolved feather debris.
(5) The filtrate is packed in a mould when the filtrate is hot and is cooled for 0.5h to solidify at 4 ℃.
(6) And taking out the solidified gel from the mold, soaking in water to remove various chemical substances, wherein the mass-volume ratio of the gel to the water is 0.001g/mL, replacing the water every 1h for 4 times to obtain the keratin gel.
(7) And drying the pure keratin gel at-80 ℃ for 12-24 h to obtain sponge, and drying at room temperature (thin gel) to obtain the membrane.
(8) Properties of the keratin gel: the gel has an accumulative release rate of 50% after 28 days for a simulated drug (rhodamine B) in a PBS buffer solution.
Example 2
(1) And (3) slowly stirring and soaking the cleaned feather in an organic solvent for 3 hours, and cleaning the feather with deionized water, and drying the feather in an oven at 60 ℃.
(2) Preparing a dissolving solution, wherein the molar concentration of the urea is 5mol/L, the molar concentration of the thiourea is 4mol/L, the molar concentration of the sodium metabisulfite is 1mol/L, and the molar concentration of SDS is 1 mol/L.
(3) Dispersing the degreased feather in a dissolving solution at a feed liquid mass ratio of 0.01:2, and stirring and dissolving for 2h at 80 ℃.
(4) After completion of the dissolution, the residue was filtered through a 300-mesh nylon net to remove undissolved feather debris.
(5) The filtrate is packed in a mould when the filtrate is hot and cooled for 1h at 20 ℃ to solidify.
(6) And taking out the solidified gel from the mold, soaking in water to remove various chemical substances, wherein the mass-volume ratio of the gel to the water is 0.005g/mL, and replacing the water every 2h for 6 times to obtain the keratin gel.
(7) Pure keratin gel is freeze-dried at-60 ℃ to obtain sponge, and dried (thin gel) at room temperature to obtain the membrane.
(8) Properties of the keratin gel: the gel has an accumulative release rate of 60 percent after 28 days for a simulated drug (rhodamine B) in a PBS buffer solution.
Example 3
(1) And (3) slowly stirring and soaking the cleaned feather in an organic solvent for 4 hours, and cleaning the feather with deionized water, and drying the feather in an oven at 60 ℃.
(2) Preparing a dissolving solution, wherein the molar concentration of the urea is 8mol/L, the molar concentration of the thiourea is 5mol/L, the molar concentration of the sodium metabisulfite is 2mol/L, and the molar concentration of SDS is 2 mol/L.
(3) Dispersing the degreased feather in a dissolving solution at a feed liquid mass ratio of 0.01:3, and stirring and dissolving for 3h at 100 ℃.
(4) After completion of the dissolution, the mixture was filtered through a 500-mesh nylon net to remove undissolved feather debris.
(5) The filtrate is subpackaged in a mould while the filtrate is hot and cooled for 2h at 30 ℃ for solidification.
(6) And taking out the solidified gel from the mold, soaking in water to remove various chemical substances, wherein the mass-volume ratio of the gel to the water is 0.01g/mL, replacing the water every 1h for 8 times, and thus obtaining the keratin gel.
(7) Pure keratin gel is freeze-dried at-40 deg.C to obtain sponge, and dried at room temperature (thin gel) to obtain membrane.
(8) Properties of the keratin gel: the gel has an accumulative release rate of 40% after 28 days for a simulated drug (rhodamine B) in a PBS buffer solution.
Claims (9)
1. Dissolving defatted feathers in a dissolving solution to obtain a feather keratin dissolving solution, filtering to remove undissolved feather debris, cooling and solidifying filtrate, and washing with deionized water to obtain pure keratin gel; the dissolving solution contains urea, thiourea and sodium metabisulfite, and the molar concentrations of the urea, the thiourea and the sodium metabisulfite are respectively 2-8 mol/L, 2-5 mol/L, 0.2-1 mol/L and 0.5-2 mol/L.
2. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: freeze-drying the pure keratin gel to obtain sponge; the freeze drying is carried out for 12-24 hours at the temperature of-80 to-40 ℃.
3. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: and drying the pure keratin gel at room temperature to obtain a gel film.
4. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the degreased feather is obtained by slowly stirring and soaking cleaned feathers in an organic solvent for 2-4 hours, cleaning with deionized water for three times and drying; the organic solvent is petroleum ether, acetone or ethanol.
5. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the mass ratio of the degreased feathers to the dissolving solution is 0.01: 1-0.01: 3.
6. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the dissolving temperature of the degreased feather in the dissolving solution is 70-100 ℃, and the dissolving time is 1-3 h.
7. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the nylon net for filtering is 300-500 meshes in specification.
8. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the cooling temperature is 0-40 ℃, and the cooling time is 0.5-2 h.
9. The method for preparing high-strength pure feather keratin gel in one step as claimed in claim 1, wherein: the deionized water washing is to wash each compound remained in a dissolving solution in the gel by using deionized water, and the specific operation is to soak the gel in water, wherein the mass-volume ratio of the gel to the water is 0.001-0.01 g/mL, and the water is changed every 1-3 h for 4-8 times.
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| CN113861357A (en) * | 2021-11-12 | 2021-12-31 | 天水师范学院 | High-strength feather keratin double-network hydrogel and preparation method thereof |
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| 庄媛: "羽毛残渣制备角蛋白海绵膜及其在环境治理中的应用", 《中国优秀硕士学位论文全文数据库 工程科技I辑》 * |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113861357A (en) * | 2021-11-12 | 2021-12-31 | 天水师范学院 | High-strength feather keratin double-network hydrogel and preparation method thereof |
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