CN105213295A - A kind of recombination human source collagen protein face and preparation method thereof - Google Patents
A kind of recombination human source collagen protein face and preparation method thereof Download PDFInfo
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Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/96—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution
- A61K8/97—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution from algae, fungi, lichens or plants; from derivatives thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- 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]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/02—Preparations for care of the skin for chemically bleaching or whitening the skin
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Dermatology (AREA)
- Biochemistry (AREA)
- Botany (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Cosmetics (AREA)
Abstract
The invention discloses a kind of recombination human source collagen protein face and preparation method thereof, the preparation method of this recombination human source collagen protein face comprises the following steps: recombination human source collagen protein face is by carrier and mask matrix solution composition, by acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring completely after, abundant swelling 12h, methyl hydroxybenzoate is added in system, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM, dispersed with stirring is complete, be heated to 50 DEG C, 30 minutes are incubated under vacuum.The effective defying age of the present invention, wrinkle reduction, increase skin elasticity, keep the young state of skin.
Description
Technical field
The present invention relates to a kind of recombination human source collagen protein face and preparation method thereof.
Background technology
Urban woman is often in the face of the immense pressure worked and live, and add the severe contamination of environment, skin is subjected to very large injury, show as that skin of face is intensely dark, corse sweat pore, easily raw comedo, microgroove increases, and accelerates old and feeble, brings very large puzzlement to the vast personage of liking to be beautiful.Facial film is the one in daily cosmetics, and it is by being attached to face blink, temporarily isolated extraneous air and pollutant, for skin provides a large amount of nutrition and moisture, makes skin become soft beautiful, high resilience.
In order to make facial film have more function, usually needing to add various active substance and making facial film reach the effects such as better whitening, moisturizing, defying age, anti-acne.Due to, collagen protein contains the hydrophilic groups such as more amino and hydroxyl, effectively can realize the effect of locking water, moisturizing.Meanwhile, collagen protein can be synthesized endogenous collagen by percutaneous absorption, wrinkle reduction, makes skin high resilience.In addition, collagen protein has certain reparation and the effect for the treatment of to ultraviolet injury and comedo, and adds in cosmetics features such as showing good compatibility, stability and antibiotic property to.But absorbability and the safety of existing animal sources collagen protein class facial film are poor, can not very effectively play a role, and consumer can not relievedly use.
Recombination human source collagen protein is the tripeptides repetitive sequence feature based on human III type collagen protein α 1 chain collagen domain Gly-X-Y, successfully pichia yeast genetic engineering bacteria is constructed by the method for MOLECULE DESIGN and gene chemical synthesis, carry out high density fermentation, obtain cell exocrine type destination protein, there is following characteristic:
(1) reduced immunogenicity: because recombination human source collagen protein builds according to the gene sequence characteristic of human collagen albumen, and in experimentation, specific screening and modification are also carried out to sequence, amino residue such as easily causing the tryptophan of organism immune response has been foreclosed.
(2) virus-free hidden danger: animal sources collagen protein also exists a fatal shortcoming and there is viral hidden danger exactly, as bird flu virus, crazy heifer disease virus, foot and mouth disease, mycoplasma and chlamydia etc.The recombination human source collagen protein obtained by gene engineering research then overcomes this weakness, and its expression system is yeast, and whole experimentation is sterile working, and the collagen protein therefore obtained can not carry exogenous virus.
(3) good water solubility: maxima solubility can reach 20%, is easy to be absorbed by body.
(4) extraction process is simple, purity of protein is high: recombination human source collagen protein is cell exocrine type albumen, without the need to carrying out break process to thalline, only needs to carry out isolation and purification to fermented supernatant fluid, and the kind of cell exocrine type albumen is few, be convenient to obtain the higher destination protein of purity.
(5) molecular structure determined: can carry out pointed decoration and enzyme action, plays the most accurate repair to skin.
By carrying out the effect of specificity enzyme action to RHC, generating micromolecular collagen bioactive peptide, being conducive to the absorption of skin and the generation of endogenous collagen protein, reduce microgroove.Therefore, developing a kind of recombination human source collagen protein face is task place of the present invention, aims to provide a kind of effect cosmetics with stronger wrinkle removal, anti-acne, moisturizing and nourishing.
Summary of the invention
In order to overcome the defect that traditional collagen protein class facial film exists, the invention provides one to have multiple moistening effect, effectively wrinkle reduction, keep elasticity of skin, removing acne, safety is high, absorbability good, cause organism immune response hardly, recombination human source collagen protein face of efficient lock water and preparation method thereof.
The present invention solves above-mentioned technical problem by following technical proposals: a kind of recombination human source collagen protein face, is characterized in that, it is made up of the aminoacid sequence shown in SEQIDNO:1, and containing 599 aminoacid, molecular weight is 55.0kDa.
The present invention also provides a kind of preparation method of recombination human source collagen protein face, it is characterized in that, it comprises the following steps: recombination human source collagen protein face is by carrier and mask matrix solution composition, mask matrix solution is made up of the raw material of following weight percentage ratio: micromolecule recombination human source collagen peptide 0.02 ~ 2 part, hamamelis extract 1 ~ 3 part, hyaluronic acid 0.01 ~ 0.5 part, ceramide 0.01 ~ 1 part, betanin 0.5 ~ 2 part, pantothenylol 1 ~ 2 part, Tremella extract 0.05 ~ 0.2 part, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer 0.1 ~ 1 part, xanthan gum 0.1 ~ 1 part, glycerol 3 ~ 5 parts, butanediol 1 ~ 3 part, methyl hydroxybenzoate 0.1 ~ 0.2 part, EDETATE SODIUM 0.03 ~ 0.05 part, sodium hydroxide 0.04 ~ 0.4 part, Cremophor RH40 0.5 ~ 1 part, deionized water 75 ~ 80 parts, under GMP production environment condition, described facial film preparation method is carried out according to following processing step: after acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring is complete, abundant swelling 12h, methyl hydroxybenzoate, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM is added in system, dispersed with stirring is complete, be heated to 50 DEG C, under vacuum, be incubated 30 minutes, in above-mentioned solution, add sodium hydroxide, adjust ph, add Cremophor RH40 afterwards, dispersed with stirring is complete, when solution temperature is down to 20 DEG C, add pantothenylol, vacuum stirring is uniformly dispersed, by the material censorship of gained, after qualified by QB/T2872 standard test, 300 orders pack out sample after filtering.
Preferably, the preparation method of described micromolecule recombination human source collagen peptide is as follows: with the RHC shown in SEQIDNO:1 for raw material, be mixed with the protein solution of 10 ~ 20g/L, add pH to 8 ~ 9 that 1MNaOH solution regulates solution while stirring, 50 DEG C of heating in water bath, add the compound protease effect 2 ~ 5h of 0.1 ~ 2%, after enzyme action completes, temperature is increased to 90 DEG C, maintain 15min, be separated under high speed centrifugation condition, collect supernatant, be the micromolecule RHC protein peptide solution that molecular weight is 204 ~ 2729Da, vacuum lyophilization obtains finished product.
Preferably, described compound protease is that E.C. 3.4.21.64 and trypsin are in mass ratio for the ratio of 1:5 ~ 15 carries out compound.
Preferably, the material of described carrier is the one in non-woven fabrics, silkworm silk or biological fiber.
Positive progressive effect of the present invention is: the effective defying age of the present invention, and wrinkle reduction, increase skin elasticity, keep the young state of skin.The effective anti-acne of the present invention, replenishing collagen, repairs damage skin, eliminates slight cicatrix.The potent moisturizing of the present invention, compact skin.Safety of the present invention is high, seldom causes allergic reaction.Carrier medium of the present invention is in non-woven fabrics, silkworm silk or biological fiber, and production environment is GMP10 ten thousand grades, ten thousand grades, local, the working condition of pharmaceutical grade, and safety is high, pollute less, can relievedly use.
Detailed description of the invention
By following examples, more specific description is carried out to the present invention, but the present invention is not by the restriction of these embodiments.
Described recombination human source collagen protein (RecombinantHuman-sourceCollagen, RHC) is made up of the aminoacid sequence shown in SEQIDNO:1, and containing 599 aminoacid, molecular weight is 55.0kDa.First the present invention carries out fixed point enzyme action to RHC, forms micromolecule recombination human source collagen peptide.Facial film of the present invention is by carrier and mask matrix solution composition, and described mask matrix solution contains following component: deionized water, glycerol, butanediol, hyaluronic acid, micromolecule recombination human source collagen peptide, ceramide, pantothenylol, Hamamelis virginiana extract, Tremella extract, betanin, xanthan gum, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, methyl hydroxybenzoate, EDETATE SODIUM, sodium hydroxide, Cremophor RH40.This kind of facial film can supplement endogenous collagen protein, long-acting performance lock water moisture-keeping efficacy, makes that skin is clear thoroughly, water profit, delicate, simultaneously effective removing acne.
Embodiment 1: E.C. 3.4.21.64 associating trypsin carries out enzyme action to recombined human derived collagen albumen
Implementation method: solution recombination human source collagen protein being mixed with 10g/L, after regulating pH to 9.0, temperature 50 C, adding E.C. 3.4.21.64 amount is 0.1%, and Trypsin enzyme amount is 1%, hydrolysis 3h.In course of reaction, maintain pH value by dripping 1MNaOH solution.After having reacted, temperature is increased to 90 DEG C, maintains the enzyme denaturing reaction of 15min, be separated under high speed centrifugation condition after cooling, collect supernatant and carry out vacuum lyophilization.By carrying out HPLC detection to sample, the molecular weight ranges of the collagen peptide obtained after determining enzyme action is 204-2729Da.
Embodiment 2: the preparation method of recombination human source collagen protein face
Recombination human source collagen protein face is by carrier and mask matrix solution composition, mask matrix solution is made up of the raw material of following weight percentage ratio: micromolecule recombination human source collagen peptide 2 parts, hamamelis extract 3 parts, hyaluronic acid 0.5 part, Cer EOS part, betanin 2 parts, pantothenylol 1 part, Tremella extract 0.2 part, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer 1 part, xanthan gum 1 part, glycerol 5 parts, butanediol 1 part, methyl hydroxybenzoate 0.1 ~ 0.2 part, EDETATE SODIUM 0.05 part, sodium hydroxide 0.04 part, Cremophor RH40 0.5 part, deionized water 75 parts.Adopt above-mentioned Formulation Implementation production technology: after acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring is complete, abundant swelling 12h, methyl hydroxybenzoate, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM is added in system, dispersed with stirring is complete, be heated to 50 DEG C, under vacuum, be incubated 30 minutes.In above-mentioned solution, add sodium hydroxide, adjust ph, add Cremophor RH40 afterwards, dispersed with stirring is complete.When solution temperature is down to 20 DEG C, add pantothenylol, vacuum stirring is uniformly dispersed; By the material censorship of gained, after qualified by QB/T2872 standard test, 300 orders pack out sample after filtering.
Embodiment 3: the preparation method of recombination human source collagen protein face
Recombination human source collagen protein face is by carrier and mask matrix solution composition, mask matrix solution takes each component according to following mass percent formula: micromolecule recombination human source collagen peptide 0.02 part, hamamelis extract 1 part, hyaluronic acid 0.02 part, ceramide 0.02 part, betanin 0.5 part, pantothenylol 2 parts, Tremella extract 0.1 part, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer 0.15 part, xanthan gum 0.1 part, glycerol 4 parts, butanediol 3 parts, methyl hydroxybenzoate 0.1 part, EDETATE SODIUM 0.03 part, sodium hydroxide 0.06 part, Cremophor RH40 0.9 part, deionized water 80 parts.Adopt above-mentioned Formulation Implementation production technology: after acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring is complete, abundant swelling 12h, methyl hydroxybenzoate, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM is added in system, dispersed with stirring is complete, be heated to 50 DEG C, under vacuum, be incubated 30 minutes.In above-mentioned solution, add sodium hydroxide, adjust ph, add Cremophor RH40 afterwards, dispersed with stirring is complete.When solution temperature is down to 20 DEG C, add pantothenylol, vacuum stirring is uniformly dispersed; By the material censorship of gained, after qualified by QB/T2872 standard test, 300 orders pack out sample after filtering.
Embodiment 4: the preparation method of recombination human source collagen protein face
Recombination human source collagen protein face is by carrier and mask matrix solution composition, mask matrix solution is made up of the raw material of following weight percentage ratio: micromolecule recombination human source collagen peptide 1 part, hamamelis extract 2 parts, hyaluronic acid 0.3 part, ceramide 0.3 part, betanin 1 part, pantothenylol 1.5 parts, Tremella extract 0.1 part, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer 0.5 part, xanthan gum 0.5 part, glycerol 4 parts, butanediol 2 parts, methyl hydroxybenzoate 0.15 part, EDETATE SODIUM 0.04 part, sodium hydroxide 0.2 part, Cremophor RH40 0.8 part, deionized water 78 parts, under GMP production environment condition, described facial film preparation method is carried out according to following processing step: after acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring is complete, abundant swelling 12h, methyl hydroxybenzoate, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM is added in system, dispersed with stirring is complete, be heated to 50 DEG C, under vacuum, be incubated 30 minutes, in above-mentioned solution, add sodium hydroxide, adjust ph, add Cremophor RH40 afterwards, dispersed with stirring is complete, when solution temperature is down to 20 DEG C, add pantothenylol, vacuum stirring is uniformly dispersed, by the material censorship of gained, after qualified by QB/T2872 standard test, 300 orders pack out sample after filtering.
The present invention can reduce the zest of facial film to skin, safe and reliable, minimizing skin allergy.Multiple wetting agent collocation is used, potent performance moisturizing lock water effect simultaneously.And, recombination human source collagen egg add potent performance anti-aging effects.
One aspect of the present invention relates to a kind of recombination human source collagen protein (being called for short recombination human source collagen protein of the present invention), and it is made up of the aminoacid sequence shown in SEQIDNO:1.
SEQIDNO:1
GPPGEPGNPGSPGNQGQPGNKGSPGNPGQPGNEGQPGQPGQNGQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPGQPGNPGQPGEQGKPGNQGPAGEPGNPGSPGNQGQPGNK
GSPGNPGQPGNEGQPGQPGQNGQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPGQPGNPGQPGEQGKPGNQGPAGEPGNPGSPGNQGQPGNKGSPGNPGQPGNEGQPGQPGQN
GQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPG
QPGNPGQPGEQGKPGNQGPAGEPGNPGSPGNQGQPGNKGS
PGNPGQPGNEGQPGQPGQNGQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPGQPGNPGQPGEQGKPGNQGPAGEPGNPGSPGNQGQPGNKGSPGNPGQPGNEGQPGQPGQNGQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPGQPGNPGQPGEQGKPGNQGPAGEPGNPGSPGNQGQPGNKGSPGNPGQPGNEGQPGQPGQNGQPGEPGSNGPQGSQGNPGKNGQPGSPGSQGSPGNQGSPGQPGNPGQPGEQGKPGNQGPAGG
The recombination human source collagen protein according to claim 1 of recombination human source collagen protein of the present invention to be Chinese patent application publication number be CN102443057A, it can adopt gene engineering expression method disclosed in the open CN102443057A of such as this Chinese patent application to prepare.
Table 1 represents that recombination human source collagen protein is through E.C. 3.4.21.64 (ProteinaseK) and trypsin Trypsin) length of theoretical peptide section after common enzyme action and molecular weight.
Clipped position | Enzyme | Sequence after shearing | Peptide chain length | Molecular weight |
5 | Proteinase K | GPPGE | 5 | 455.468 |
21 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
33 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
47 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
62 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
92 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
102 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
104 | Proteinase K | GE | 2 | 204.183 |
120 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
132 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
146 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
161 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
191 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
201 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
203 | Proteinase K | GE | 2 | 204.183 |
219 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
231 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
245 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
260 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
290 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
300 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
302 | Proteinase K | GE | 2 | 204.183 |
318 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
330 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
344 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
359 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
389 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
399 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
401 | Proteinase K | GE | 2 | 204.183 |
417 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
429 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
443 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
458 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
488 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
498 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
500 | Proteinase K | GE | 2 | 204.183 |
516 | Trypsin | PGNPGSPGNQGQPGNK | 16 | 1505.567 |
528 | Proteinase K | GSPGNPGQPGNE | 12 | 1110.105 |
542 | Proteinase K | GQPGQPGQNGQPGE | 14 | 1350.367 |
557 | Trypsin | PGSNGPQGSQGNPGK | 15 | 1381.424 |
587 | Proteinase K | NGQPGSPGSQGSPGNQGSPGQPGNPGQPGE | 30 | 2728.744 |
597 | Proteinase K | QGKPGNQGPA | 10 | 953.022 |
599 | End of sequence | GG | 2 | 132.119 |
Above-described embodiment is to explanation of the present invention, is not limitation of the invention, anyly all belongs to protection scope of the present invention to the scheme after the present invention carries out simple transformation.
Claims (5)
1. a recombination human source collagen protein face, is characterized in that, it is made up of the aminoacid sequence shown in SEQIDNO:1, and containing 599 aminoacid, molecular weight is 55.0kDa.
2. the preparation method of a recombination human source collagen protein face, it is characterized in that, it comprises the following steps: recombination human source collagen protein face is by carrier and mask matrix solution composition, mask matrix solution is made up of the raw material of following weight percentage ratio: micromolecule recombination human source collagen peptide 0.02 ~ 2 part, hamamelis extract 1 ~ 3 part, hyaluronic acid 0.01 ~ 0.5 part, ceramide 0.01 ~ 1 part, betanin 0.5 ~ 2 part, pantothenylol 1 ~ 2 part, Tremella extract 0.05 ~ 0.2 part, acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer 0.1 ~ 1 part, xanthan gum 0.1 ~ 1 part, glycerol 3 ~ 5 parts, butanediol 1 ~ 3 part, methyl hydroxybenzoate 0.1 ~ 0.2 part, EDETATE SODIUM 0.03 ~ 0.05 part, sodium hydroxide 0.04 ~ 0.4 part, Cremophor RH40 0.5 ~ 1 part, deionized water 75 ~ 80 parts, under GMP production environment condition, described facial film preparation method is carried out according to following processing step: after acrylic acid (ester) class/C10-30 alkylol acrylamide acid esters cross linked polymer, Tremella extract, hamamelis extract, ceramide, xanthan gum, hyaluronic acid, deionized water, glycerol and butanediol dispersed with stirring is complete, abundant swelling 12h, methyl hydroxybenzoate, betanin, micromolecule recombination human source collagen peptide, EDETATE SODIUM is added in system, dispersed with stirring is complete, be heated to 50 DEG C, under vacuum, be incubated 30 minutes, in above-mentioned solution, add sodium hydroxide, adjust ph, add Cremophor RH40 afterwards, dispersed with stirring is complete, when solution temperature is down to 20 DEG C, add pantothenylol, vacuum stirring is uniformly dispersed, by the material censorship of gained, after qualified by QB/T2872 standard test, 300 orders pack out sample after filtering.
3. the preparation method of recombination human source collagen protein face as claimed in claim 2, it is characterized in that, the preparation method of described micromolecule recombination human source collagen peptide is as follows: with the RHC shown in SEQIDNO:1 for raw material, be mixed with the protein solution of 10 ~ 20g/L, add pH to 8 ~ 9 that 1MNaOH solution regulates solution while stirring, 50 DEG C of heating in water bath, add the compound protease effect 2 ~ 5h of 0.1 ~ 2%, after enzyme action completes, temperature is increased to 90 DEG C, maintain 15min, be separated under high speed centrifugation condition, collect supernatant, be the micromolecule RHC protein peptide solution that molecular weight is 204 ~ 2729Da, vacuum lyophilization obtains finished product.
4. the preparation method of recombination human source collagen protein face as claimed in claim 3, is characterized in that, described compound protease is that E.C. 3.4.21.64 carries out compound with the ratio that trypsin is 1:5 ~ 15 in mass ratio.
5. the preparation method of recombination human source collagen protein face as claimed in claim 4, it is characterized in that, the material of described carrier is the one in non-woven fabrics, silkworm silk or biological fiber.
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Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101721343A (en) * | 2009-11-06 | 2010-06-09 | 烟台海岸带可持续发展研究所 | Deep-sea fish skin collagen peptide firming and anti-ageing face mask and preparing method |
CN102443057A (en) * | 2011-10-26 | 2012-05-09 | 南京理工大学 | Recombinant humanized collagen and its preparation method |
CN104173251A (en) * | 2014-09-15 | 2014-12-03 | 王书敏 | Whitening mask containing yak ossein peptide and preparation method of whitening mask |
CN104622765A (en) * | 2015-03-06 | 2015-05-20 | 广东雅丽洁精细化工有限公司 | Beauty mask containing compound type collagen and high-low molecular hyaluronic acid |
CN104840375A (en) * | 2015-04-11 | 2015-08-19 | 广东医学院 | A group of coenzyme Q10 masks with effects of spot removing, wrinkle preventing and whitening |
-
2015
- 2015-11-06 CN CN201510746718.XA patent/CN105213295B/en active Active
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101721343A (en) * | 2009-11-06 | 2010-06-09 | 烟台海岸带可持续发展研究所 | Deep-sea fish skin collagen peptide firming and anti-ageing face mask and preparing method |
CN102443057A (en) * | 2011-10-26 | 2012-05-09 | 南京理工大学 | Recombinant humanized collagen and its preparation method |
CN104173251A (en) * | 2014-09-15 | 2014-12-03 | 王书敏 | Whitening mask containing yak ossein peptide and preparation method of whitening mask |
CN104622765A (en) * | 2015-03-06 | 2015-05-20 | 广东雅丽洁精细化工有限公司 | Beauty mask containing compound type collagen and high-low molecular hyaluronic acid |
CN104840375A (en) * | 2015-04-11 | 2015-08-19 | 广东医学院 | A group of coenzyme Q10 masks with effects of spot removing, wrinkle preventing and whitening |
Non-Patent Citations (1)
Title |
---|
任俊凤等: "河豚鱼皮胶原蛋白肽的提取及其抗氧化活性的研究", 《河豚鱼皮胶原蛋白肽的提取及其抗氧化活性的研究》》 * |
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