CN111424426A - Silk fabric maintenance agent and preparation method thereof - Google Patents
Silk fabric maintenance agent and preparation method thereof Download PDFInfo
- Publication number
- CN111424426A CN111424426A CN202010435324.3A CN202010435324A CN111424426A CN 111424426 A CN111424426 A CN 111424426A CN 202010435324 A CN202010435324 A CN 202010435324A CN 111424426 A CN111424426 A CN 111424426A
- Authority
- CN
- China
- Prior art keywords
- silk fabric
- macroglobulin
- agent
- solution
- silk
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 239000004744 fabric Substances 0.000 title claims abstract description 54
- 238000012423 maintenance Methods 0.000 title claims abstract description 24
- 238000002360 preparation method Methods 0.000 title claims abstract description 15
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 44
- 108010063045 Lactoferrin Proteins 0.000 claims abstract description 18
- 102000010445 Lactoferrin Human genes 0.000 claims abstract description 18
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 claims abstract description 18
- 229940078795 lactoferrin Drugs 0.000 claims abstract description 18
- 235000021242 lactoferrin Nutrition 0.000 claims abstract description 18
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 claims abstract description 13
- 239000001768 carboxy methyl cellulose Substances 0.000 claims abstract description 13
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 claims abstract description 13
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 claims abstract description 13
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 claims abstract description 12
- 108010052968 leupeptin Proteins 0.000 claims abstract description 12
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 claims abstract description 12
- 235000018102 proteins Nutrition 0.000 claims abstract description 11
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 11
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 9
- 238000003756 stirring Methods 0.000 claims abstract description 8
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 claims abstract 3
- 239000000243 solution Substances 0.000 claims description 24
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims description 20
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 12
- 229910052742 iron Inorganic materials 0.000 claims description 10
- 238000000108 ultra-filtration Methods 0.000 claims description 9
- 239000007853 buffer solution Substances 0.000 claims description 8
- 239000000287 crude extract Substances 0.000 claims description 8
- 238000000034 method Methods 0.000 claims description 8
- 239000012506 Sephacryl® Substances 0.000 claims description 6
- 238000010521 absorption reaction Methods 0.000 claims description 6
- 238000011033 desalting Methods 0.000 claims description 6
- 238000005227 gel permeation chromatography Methods 0.000 claims description 6
- 239000012528 membrane Substances 0.000 claims description 6
- 239000011780 sodium chloride Substances 0.000 claims description 6
- 239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 claims description 3
- 235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 claims description 3
- 239000000730 antalgic agent Substances 0.000 claims 1
- 239000004365 Protease Substances 0.000 abstract description 24
- 108091005804 Peptidases Proteins 0.000 abstract description 21
- -1 antinocidin Chemical compound 0.000 abstract description 6
- 244000005700 microbiome Species 0.000 abstract description 5
- 239000004753 textile Substances 0.000 abstract description 4
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 1
- 230000009965 odorless effect Effects 0.000 abstract 1
- 102000035195 Peptidases Human genes 0.000 description 20
- 235000019419 proteases Nutrition 0.000 description 17
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 11
- 230000000694 effects Effects 0.000 description 11
- 230000005764 inhibitory process Effects 0.000 description 9
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 229960001322 trypsin Drugs 0.000 description 5
- 241000894006 Bacteria Species 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 108010022355 Fibroins Proteins 0.000 description 4
- 108090000526 Papain Proteins 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 229940055729 papain Drugs 0.000 description 4
- 235000019834 papain Nutrition 0.000 description 4
- 108090000317 Chymotrypsin Proteins 0.000 description 3
- 230000000844 anti-bacterial effect Effects 0.000 description 3
- 229960002376 chymotrypsin Drugs 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 108090000712 Cathepsin B Proteins 0.000 description 2
- 102000004225 Cathepsin B Human genes 0.000 description 2
- 108010067770 Endopeptidase K Proteins 0.000 description 2
- CWYNVVGOOAEACU-UHFFFAOYSA-N Fe2+ Chemical compound [Fe+2] CWYNVVGOOAEACU-UHFFFAOYSA-N 0.000 description 2
- 108010088842 Fibrinolysin Proteins 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 108010067372 Pancreatic elastase Proteins 0.000 description 2
- 102000016387 Pancreatic elastase Human genes 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 239000013522 chelant Substances 0.000 description 2
- 238000005034 decoration Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000010612 desalination reaction Methods 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 229960001484 edetic acid Drugs 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000010985 leather Substances 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 239000011259 mixed solution Substances 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 229940012957 plasmin Drugs 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- BDOYKFSQFYNPKF-UHFFFAOYSA-N 2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;sodium Chemical compound [Na].[Na].OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O BDOYKFSQFYNPKF-UHFFFAOYSA-N 0.000 description 1
- 108010087765 Antipain Proteins 0.000 description 1
- 102000005572 Cathepsin A Human genes 0.000 description 1
- 108010059081 Cathepsin A Proteins 0.000 description 1
- 102000003908 Cathepsin D Human genes 0.000 description 1
- 108090000258 Cathepsin D Proteins 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 102000008133 Iron-Binding Proteins Human genes 0.000 description 1
- 108010035210 Iron-Binding Proteins Proteins 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 108010027597 alpha-chymotrypsin Proteins 0.000 description 1
- SDNYTAYICBFYFH-TUFLPTIASA-N antipain Chemical compound NC(N)=NCCC[C@@H](C=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 SDNYTAYICBFYFH-TUFLPTIASA-N 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000003796 beauty Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 150000003278 haem Chemical class 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 238000010422 painting Methods 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 229940093429 polyethylene glycol 6000 Drugs 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
- D06M15/01—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with natural macromolecular compounds or derivatives thereof
- D06M15/15—Proteins or derivatives thereof
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M13/00—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment
- D06M13/322—Treating fibres, threads, yarns, fabrics or fibrous goods made from such materials, with non-macromolecular organic compounds; Such treatment combined with mechanical treatment with compounds containing nitrogen
- D06M13/325—Amines
- D06M13/342—Amino-carboxylic acids; Betaines; Aminosulfonic acids; Sulfo-betaines
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
- D06M15/01—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with natural macromolecular compounds or derivatives thereof
- D06M15/03—Polysaccharides or derivatives thereof
- D06M15/05—Cellulose or derivatives thereof
- D06M15/09—Cellulose ethers
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M2101/00—Chemical constitution of the fibres, threads, yarns, fabrics or fibrous goods made from such materials, to be treated
- D06M2101/02—Natural fibres, other than mineral fibres
- D06M2101/10—Animal fibres
Landscapes
- Engineering & Computer Science (AREA)
- Textile Engineering (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
- Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)
- Detergent Compositions (AREA)
Abstract
The invention relates to the field of textile maintenance, and discloses a silk fabric maintenance agent and a preparation method thereof, wherein the preparation method comprises the following steps of (1) α2Purifying macroglobulin, (2) purifying lactoferrin, leupeptin, antinocidin, disodium edetate α2Adding macroglobulin solution and sodium carboxymethylcellulose into water, stirring, and making into silk fabric caring agent. The silk fabric maintenance agent mainly comprises protein, is colorless and odorless, has similar properties with silk fabric, can inhibit the growth of microorganisms for a long time after being sprayed on the surface of the silk fabric, and simultaneously inhibits the action of protease released by the microorganismsThe durability of the silk fabric is greatly enhanced.
Description
Technical Field
The invention relates to the field of textile maintenance, in particular to a silk fabric maintenance agent and a preparation method thereof.
Background
With the continuous development of the textile industry in China, silk becomes one of the most important fabrics in export textiles in China. However, high-grade silk fabrics such as silk paintings are susceptible to environmental influences during long-term storage, and microorganisms such as bacteria and fungi present in the environment are liable to adhere to the silk fabrics and propagate, thereby contaminating the silk fabrics and affecting the beauty of the silk fabrics. And the protease produced by the microorganism can also disintegrate the silk fabrics, thereby destroying the taking and collecting values of the silk fabrics. Therefore, there is a need to develop a maintenance agent which can stay on the surface of silk fabrics for a long time and has long-term protection effect on the silk fabrics.
Disclosure of Invention
In view of the above, the present invention provides a silk fabric care agent and a preparation method thereof, wherein the silk fabric care agent is sprayed on the surface of silk fabric to inhibit the growth of microorganisms for a long time, and simultaneously inhibit the action of protease released by the microorganisms, thereby greatly enhancing the durability of the silk fabric.
In order to solve the technical problem, the invention provides a preparation method of a silk fabric maintenance agent, which comprises the following steps:
s1, taking α2Concentrating M crude extract, passing through Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L Tris-HClpH8.0 buffer solution containing 0.5 mol/L NaCl, detecting eluate at absorption peak of 280nm, collecting eluate of first peak, ultrafiltering, desalting, and concentrating to obtain α2A macroglobulin solution;
s2, preparing the components of the lactoferrin, the leupeptin, the antinocidin, the disodium ethylene diamine tetraacetate α2Adding macroglobulin solution and sodium carboxymethylcellulose into water, stirring, and making into silk fabric caring agent.
Preferably, in step S1, the ultrafiltration membrane has a molecular weight cut-off of 300-500 kDa.
Preferably, in step S1, the α2The macroglobulin solution has a protein concentration of 80-100. mu.g/L.
Preferably, in step S2, the lactoferrin, leupeptin, antinocidin, disodium edetate, α2The dosage ratio of macroglobulin solution and sodium carboxymethylcellulose to water is (8-10), (3.5-4), (0.5-2), (8.4-16.8), (3-5), (10-30), (1000) m L.
Preferably, in step S2, the iron saturation of the lactoferrin is 5% to 9%.
Preferably, in step S2, the molecular weight of the sodium carboxymethyl cellulose is 10-20 kDa.
The invention also provides a silk fabric maintenance agent prepared by the preparation method.
Compared with the prior art, the invention has the following beneficial effects:
the silk fabric maintenance agent contains lactoferrin, leupeptin, antinocidin, disodium edetate and α2The macroglobulin, wherein the disodium ethylene diamine tetraacetate not only can effectively inhibit the protease activity, but also can chelate ferrous iron, thereby effectively playing the antibacterial action of the lactoferrin. The invention effectively inhibits the degradation of the silk fabrics by the protease by utilizing the mutual synergistic action of a plurality of protease inhibitors, and finally realizes the long-acting protection of the silk fabrics.
Detailed Description
The invention will be better understood from the following examples. However, those skilled in the art will readily appreciate that the description of the embodiments is only for illustrating the present invention and should not be taken as limiting the invention as detailed in the claims.
All of the starting materials of the present invention, without particular limitation as to their source, may be purchased commercially or prepared according to conventional methods well known to those skilled in the art.
The invention provides a preparation method of a silk fabric maintenance agent, which comprises the following steps of firstly taking α2Concentrating M crude extract, separating with Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L pH8.0Tris-HCl buffer solution containing 0.5 mol/L NaCl, detecting eluate at absorption peak of 280nm, collecting first peak eluate, ultrafiltering, desalting, and concentrating to obtain α2Macroglobulin solution, and lactoferrin, leupeptin, antinocidin, disodium edetate, α2Adding macroglobulin solution and sodium carboxymethylcellulose into water, stirring, and making into silk fabric caring agent.
In the invention, the cut-off molecular weight of the ultrafiltration membrane adopted in the ultrafiltration desalination process is preferably 300-500kDa, and α obtained after ultrafiltration desalination and concentration2The protein concentration of macroglobulin solution is preferably 80-100 mug/L. in the preparation process of the silk fabric care agent, lactoferrin, leupeptin, antinocidin, disodium edetate, α2Of macroglobulin solution and sodium carboxymethylcellulose with waterThe dosage proportion is preferably (8-10) g, (3.5-4) g, (0.5-2) g, (8.4-16.8) g, (3-5) m L, (10-30) g:1000m L, wherein the iron saturation of lactoferrin is preferably 5-9%, and the molecular weight of sodium carboxymethylcellulose is preferably 10-20 kDa.
The invention also provides a silk fabric maintenance agent prepared by the preparation method.
The lactoferrin (L F) adopted in the silk fabric maintenance agent is an important non-heme iron binding glycoprotein in milk, and is a monomer glycoprotein with bactericidal activity in neutrophil granules, the bacteriostasis of L F is that the lactoferrin can be highly bound with iron, so that bacteria (except lactobacillus) can lose essential elemental iron required by growth and can not grow, the bacteriostasis effect of L F is influenced by various factors, particularly, the iron content of L F plays a role in determining the bacteriostasis of the bacteria, and after L F is saturated by iron, the bacteriostasis property of the bacteria can disappear.
α used in the silk fabric caring agent2Macroglobulins bind to a number of proteolytic enzymes, such as many endopeptidases (including serine, sulfhydryl, carboxyproteolytic and some metalloproteolytic enzymes) that inhibit the activity of these enzymes, in particular plasmin, pepsin, chymotrypsin, trypsin and cathepsin D.
The leupeptin used in the silk fabric care agent of the present invention can inhibit serine and cysteine proteases, trypsin, papain, cathepsin B, plasmin, kallikrein, and the like, but does not inhibit chymotrypsin.
The anti-pain element adopted in the silk fabric maintenance agent can inhibit trypsin, papain, cathepsin A, cathepsin B and the like.
The ethylene diamine tetraacetic acid disodium adopted in the silk fabric maintenance agent can complex ions in a system, has the effect of inhibiting protease, and can chelate ferrous iron to effectively play the antibacterial effect of lactoferrin.
By utilizing the mutual synergistic action of a plurality of protease inhibitors, the silk fabric maintenance agent effectively inhibits the degradation of various proteases to silk fabrics, and finally realizes the long-acting protection of the silk fabrics.
In order to further illustrate the present invention, the following will describe in detail a silk fabric caring agent and a preparation method thereof provided by the present invention with reference to examples.
α2The preparation method of the M crude extract comprises the following steps:
adding 0.1% (w/v) soybean trypsin inhibitor into fresh pig plasma at-5 deg.C, adding EDTA (ethylene diamine tetraacetic acid) solution to make its final concentration 10 mmol/L, performing fractional precipitation with 5% -18% polyethylene glycol 6000, stirring for 60min, centrifuging at 10000r/min at 4 deg.C for 30min, dissolving and precipitating with 5 times of 50 mmol/L pH7.4 Tris-HCl solution, and dialyzing with 50 mmol/L pH7.4 Tris-HCl solution to obtain α2M crude extract.
Example 1
1、α2Purification of macroglobulin by taking α2Concentrating M crude extract, passing through Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L pH8.0Tris-HCl buffer solution containing 0.5 mol/L NaCl, detecting eluate under absorption peak of 280nm, collecting eluate of first peak, ultrafiltering with ultrafiltration membrane with molecular weight cutoff of 400kDa, desalting, and concentrating to obtain α2Macroglobulin solution, the protein concentration of which is determined by BCA protein quantitative kit to be 90 mu g/L;
2. 9g of lactoferrin with iron saturation of 7 percent, 3.8g of leupeptin, 1.5g of antinocidin, 12.8g of disodium edetate, 4m of α prepared in step 1 of L2Adding macroglobulin solution and 20g sodium carboxymethylcellulose with molecular weight of 15kDa into 1000m L water, stirring thoroughly, and mixing to obtain silk fabric caring agent A.
Example 2
1、α2Purification of macroglobulin by taking α2Concentrating M crude extract, passing through Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L pH8.0Tris-HCl buffer solution containing 0.5 mol/L NaCl, detecting eluate at absorption peak of 280nm, collecting eluate of first peak, ultrafiltering with ultrafiltration membrane with molecular weight cutoff of 300kDa, desalting, and concentrating to obtain α2Macroglobulin solution, the protein concentration of which is determined by BCA protein quantitative kit to be 80 mug/L;
2.8g of lactoferrin with iron saturation of 5%, 3.5g of leupeptin, 0.5g of antinocidin, 8.4g of disodium edetate, 3m of α prepared in step 1 of L2Adding macroglobulin solution and 10g sodium carboxymethylcellulose with molecular weight of 20kDa into 1000m L water, stirring thoroughly, and mixing to obtain silk fabric caring agent B.
Example 3
1、α2Purification of macroglobulin by taking α2Concentrating M crude extract, passing through Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L pH8.0Tris-HCl buffer solution containing 0.5 mol/L NaCl, detecting eluate at absorption peak of 280nm, collecting eluate of first peak, ultrafiltering with ultrafiltration membrane with molecular weight cutoff of 500kDa, desalting, and concentrating to obtain α2Macroglobulin solution, the protein concentration of which is determined by BCA protein quantitative kit to be 100 mu g/L;
2. 10g of lactoferrin with iron saturation of 9 percent, 4g of leupeptin, 2g of antinocidin, 16.8g of disodium edetate, 5m of α prepared in step 1 of L2Adding macroglobulin solution and 30g of sodium carboxymethylcellulose with molecular weight of 10kDa into 1000m L water, and stirring to obtain silk fabric caring agent C.
Protease inhibitory Activity assay
In order to measure the inhibitory activity of the silk fabric care agent against protease, various commercially available proteases were used as the target enzymes for the measurement, including trypsin (trypsin, SIGMA t1426), α -chymotrypsin (chymotrypsin, SIGMA c4129), elastase (elastase, SIGMA 45124), proteinase K (protease K, rock 11060325) and papain (papain, SANGON P16J12), and these enzymes were mixed in equal mass ratios to prepare a complex protease.
The activity test comprises the following steps of diluting a certain amount of compound protease with 100mM pH7.4Tris-HCl buffer solution to 100 mg/L of compound protease solution, mixing 800 mu L of compound protease solution with 200 mu L of silk fabric maintenance agent (silk fabric maintenance agent A, silk fabric maintenance agent B, silk fabric maintenance agent C, commercial Jiebao MT-18 silk handfeel agent and leather Laimei silk handfeel agent) to obtain 5 mixed solutions, standing at 37 ℃ for 5min, adding 9.0m L5 wt% of silk fibroin solution (molecular weight 10 kDa-400 kDa) into the mixed solutions, reacting for 24h, collecting the permeate by an ultrafiltration centrifugal tube, measuring 280nm absorbance by a spectrophotometer as the O.D value of a treatment tube, replacing the silk maintenance agent with 100mM pH7.4Tris-HCl buffer solution as a control tube, measuring the O.D value of the control tube according to the method, repeating the experiment for 5 times, wherein the result is represented by the average value of +/-and the protein inhibition ratio is calculated according to the following formula:
the inhibition ratio (%) - (the o.d value of the control tube-the o.d value of the treated tube)/the o.d value of the control tube × 100%. the greater the inhibition ratio, the stronger the inhibition effect of the silk maintaining agent on its protease, and the smaller the inhibition ratio, the smaller the inhibition effect, the results of the test of the activity of the protease by the silk maintaining agent are shown in table 1.
TABLE 1 results of inhibition of protease activity by silk conditioner
| Sample (I) | O.D value of control tube | O.D value of treated tube | Inhibition ratio (%) |
| Example 1 | 0.344±0.023 | 0.036±0.004 | 89.33±1.59 |
| Example 2 | 0.368±0.032 | 0.051±0.002 | 86.03±1.43 |
| Example 3 | 0.334±0.022 | 0.043±0.004 | 87.10±1.85 |
| Jiebao MT-18 silk feeling agent | 0.350±0.024 | 0.318±0.016 | 8.919±4.849 |
| Leather Laimei silk feeling agent | 0.354±0.025 | 0.327±0.031 | 7.849±3.548 |
The silk fibroin can be degraded by adding the compound protease liquid, and the results in table 1 show that the silk fabric maintenance agent prepared by the invention can effectively inhibit the activity of the compound protease, obviously slow down the hydrolysis of the silk fibroin and show higher inhibition rate. The commercially available silk feeling agent does not have a remarkable protease-inhibiting property, and thus cannot efficiently slow down the hydrolysis of silk fibroin.
The present invention provides a silk fabric caring agent and a method for preparing the same, and a plurality of methods and ways for implementing the technical scheme, the above description is only a preferred embodiment of the present invention, it should be noted that, for those skilled in the art, a plurality of modifications and decorations can be made without departing from the principle of the present invention, and these modifications and decorations should also be regarded as the protection scope of the present invention. All the components not specified in the present embodiment can be realized by the prior art.
Claims (7)
1. The preparation method of the silk fabric maintenance agent is characterized by comprising the following steps:
s1, taking α2Concentrating M crude extract, passing through Sephacryl S-300 gel chromatography column, eluting with 100 mmol/L Tris-HClpH8.0 buffer solution containing 0.5 mol/L NaCl, detecting eluate at absorption peak of 280nm, collecting eluate of first peak, ultrafiltering, desalting, and concentrating to obtain α2A macroglobulin solution;
s2, preparing the components of the lactoferrin, the leupeptin, the antinocidin, the disodium ethylene diamine tetraacetate α2Adding macroglobulin solution and sodium carboxymethylcellulose into water, stirring, and making into silk fabric caring agent.
2. The method as claimed in claim 1, wherein the ultrafiltration membrane has a molecular weight cut-off of 300-500kDa in step S1.
3. The method of claim 1, wherein in step S1, the step α is performed2The macroglobulin solution has a protein concentration of 80-100. mu.g/L.
4. The method of claim 1, wherein in step S2, the lactoferrin, leupeptin, antalgic agent, disodium edetate, α2The dosage ratio of macroglobulin solution and sodium carboxymethylcellulose to water is (8-10), (3.5-4), (0.5-2), (8.4-16.8), (3-5), (10-30), (1000) m L.
5. The method of claim 1, wherein the iron saturation of the lactoferrin is 5% to 9% in step S2.
6. The method of claim 1, wherein the molecular weight of the sodium carboxymethyl cellulose is 10-20kDa in step S2.
7. The silk fabric care agent prepared by the preparation method according to any one of claims 1 to 6.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010435324.3A CN111424426B (en) | 2020-05-21 | 2020-05-21 | Silk fabric maintenance agent and preparation method thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010435324.3A CN111424426B (en) | 2020-05-21 | 2020-05-21 | Silk fabric maintenance agent and preparation method thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN111424426A true CN111424426A (en) | 2020-07-17 |
| CN111424426B CN111424426B (en) | 2022-03-11 |
Family
ID=71553300
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202010435324.3A Active CN111424426B (en) | 2020-05-21 | 2020-05-21 | Silk fabric maintenance agent and preparation method thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN111424426B (en) |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106769297A (en) * | 2016-12-12 | 2017-05-31 | 浙江理工大学 | A kind of method that Ancient Silk Textile is determined based on proteomics |
-
2020
- 2020-05-21 CN CN202010435324.3A patent/CN111424426B/en active Active
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106769297A (en) * | 2016-12-12 | 2017-05-31 | 浙江理工大学 | A kind of method that Ancient Silk Textile is determined based on proteomics |
Also Published As
| Publication number | Publication date |
|---|---|
| CN111424426B (en) | 2022-03-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Pandya et al. | Anticoagulant proteases from western diamondback rattlesnake (Crotalus atrox) venom | |
| McMullen et al. | Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule | |
| Bjarnason et al. | Proteolytic specificity and cobalt exchange of hemorrhagic toxin e, a zinc protease isolated from the venom of the western diamondback rattlesnake (Crotalus atrox) | |
| Cheng et al. | Identification and inhibitory activity against α-thrombin of a novel anticoagulant peptide derived from oyster (Crassostrea gigas) protein | |
| Kopitar et al. | Intracellular distribution of neutral proteinases and inhibitors in pig leucocytes: isolation of two inhibitors of neutral proteinases | |
| Sumi et al. | Studies on human urinary trypsin inhibitor 1. Its modification on treatment of urine with acid | |
| Amarant et al. | Isolation and complete amino acid sequence of two fibrinolytic proteinases from the toxic Saturnid caterpillar Lonomia achelous | |
| CN103073638A (en) | Method for purifying ulinastatin via affinity chromatography | |
| Potempa et al. | An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center. | |
| Tanaka et al. | Purification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds | |
| DE2734427C3 (en) | Process for the recovery of thrombin-like enzymes from snake venom | |
| TRAVIS et al. | Kinetic studies on the interaction of α 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases | |
| CA2174231C (en) | Process for preparing an inter-alpha-trypsine inhibitor concentrate for therapeutical use, and concentrate thus obtained | |
| Sundd et al. | Purification and characterization of a highly stable cysteine protease from the latex of Ervatamia coronaria | |
| CN111424426B (en) | Silk fabric maintenance agent and preparation method thereof | |
| CN103724428A (en) | Method for improving column efficiency purified ulinastatin through resin regeneration | |
| Schmidt et al. | Chymotrypsin-like neutral protease from lysosomes of human polymorphonuclear leukocytes | |
| Pejaudier et al. | Appraisal of the protein composition of prothrombin complex concentrates of different origins | |
| Kamboj et al. | Purification and characterization of cathepsin B from goat brain | |
| Potempa et al. | Comparative properties of three functionally different but structurally related serpin variants from horse plasma | |
| Choi et al. | Purification and partial characterization of TFase, a fibrinolytic enzyme from the fruiting bodies of the medicinal and edible mushroom, Tremella fuciformis | |
| HOCHSTRAfşER et al. | New proteinase inhibitors in the secretion of some mucous membranes of the human body | |
| JPS5928394B2 (en) | Endoproteinase-Lys-C from bacteria, method for obtaining it, and method for determining sequence order of proteins and peptides | |
| Matsuoka et al. | Inhibitory effects of ONO-3307 on various proteases and tissue thromboplastin in vitro and on experimental thrombosis in vivo | |
| CN108059670A (en) | A kind of ulinastatin purification process based on affinity column |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20240715 Address after: 230000 B-1015, wo Yuan Garden, 81 Ganquan Road, Shushan District, Hefei, Anhui. Patentee after: HEFEI MINGLONG ELECTRONIC TECHNOLOGY Co.,Ltd. Country or region after: China Address before: 226019 Jiangsu city of Nantong province sik Road No. 9 Patentee before: NANTONG University Country or region before: China |
|
| TR01 | Transfer of patent right |