CN110467668A - A kind of extracting method of type III collagen - Google Patents
A kind of extracting method of type III collagen Download PDFInfo
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- CN110467668A CN110467668A CN201910851074.9A CN201910851074A CN110467668A CN 110467668 A CN110467668 A CN 110467668A CN 201910851074 A CN201910851074 A CN 201910851074A CN 110467668 A CN110467668 A CN 110467668A
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- 102000001187 Collagen Type III Human genes 0.000 title claims abstract description 31
- 108010069502 Collagen Type III Proteins 0.000 title claims abstract description 31
- 238000000034 method Methods 0.000 title claims abstract description 30
- 210000003491 skin Anatomy 0.000 claims abstract description 44
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 22
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 17
- 230000007071 enzymatic hydrolysis Effects 0.000 claims abstract description 16
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims abstract description 16
- 241001465754 Metazoa Species 0.000 claims abstract description 15
- 239000012530 fluid Substances 0.000 claims abstract description 14
- 239000004365 Protease Substances 0.000 claims abstract description 11
- 239000002253 acid Substances 0.000 claims abstract description 11
- 230000008569 process Effects 0.000 claims abstract description 11
- 238000001035 drying Methods 0.000 claims abstract description 10
- 108091005804 Peptidases Proteins 0.000 claims abstract description 9
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 9
- 210000002615 epidermis Anatomy 0.000 claims abstract description 7
- 239000000284 extract Substances 0.000 claims abstract description 7
- 239000000843 powder Substances 0.000 claims abstract description 3
- 239000000243 solution Substances 0.000 claims description 26
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 9
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 claims description 9
- 238000002360 preparation method Methods 0.000 claims description 8
- 235000019419 proteases Nutrition 0.000 claims description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 6
- 102000004190 Enzymes Human genes 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 3
- 229940088598 enzyme Drugs 0.000 claims description 3
- 239000000203 mixture Substances 0.000 claims description 3
- 235000006408 oxalic acid Nutrition 0.000 claims description 3
- 108090000526 Papain Proteins 0.000 claims description 2
- 102000057297 Pepsin A Human genes 0.000 claims description 2
- 108090000284 Pepsin A Proteins 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims description 2
- 239000012528 membrane Substances 0.000 claims description 2
- 229940055729 papain Drugs 0.000 claims description 2
- 235000019834 papain Nutrition 0.000 claims description 2
- 229940111202 pepsin Drugs 0.000 claims description 2
- 239000008267 milk Substances 0.000 claims 1
- 210000004080 milk Anatomy 0.000 claims 1
- 235000013336 milk Nutrition 0.000 claims 1
- 102000008186 Collagen Human genes 0.000 description 24
- 108010035532 Collagen Proteins 0.000 description 24
- 229920001436 collagen Polymers 0.000 description 24
- 238000004140 cleaning Methods 0.000 description 5
- 210000001772 blood platelet Anatomy 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 241000283690 Bos taurus Species 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 239000003292 glue Substances 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 235000005979 Citrus limon Nutrition 0.000 description 2
- 244000248349 Citrus limon Species 0.000 description 2
- 239000012620 biological material Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000002980 postoperative effect Effects 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 108010034596 procollagen Type III-N-terminal peptide Proteins 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 208000010110 spontaneous platelet aggregation Diseases 0.000 description 2
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 102000002734 Collagen Type VI Human genes 0.000 description 1
- 108010043741 Collagen Type VI Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 241000219000 Populus Species 0.000 description 1
- 108010077465 Tropocollagen Proteins 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 235000011054 acetic acid Nutrition 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 235000011167 hydrochloric acid Nutrition 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000036555 skin type Effects 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- 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]
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
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Abstract
The present invention provides a kind of extracting method of type III collagen, it is the following steps are included: (1) pre-processes: taking the fresh skin of animal, it is added to after being cleaned using clear water in the acid solution of 5-20 times of skin weight, 12-72h is impregnated at 4-40 DEG C, it is washed again with clear water, up to eluate to neutrality；(2) it removes the peel: the epidermis of animal is cut respectively with fat deposit, retain skin corium；(3) it is beaten: skin being cut into bulk, the clear water of 2-8 times of weight is added, block-like skin treatment pulp will be cut into using refiner；(4) it extracts: adding the protease of the 0.05-5% of skin weight into homogenate, digest 12-48h under the conditions of 20-40 DEG C；(5) it digests: the clostridiopetidase A of skin weight 0.01-0.5% being added into the solution after enzymatic hydrolysis, digests 12-48h under the conditions of 30-40 DEG C.(6) ultrafiltration: ultrafiltration membrance filter digests solution, collects trapped fluid；(7) dry: the trapped fluid of collection to be placed in drying in freeze drier, the powder after drying is type III collagen.
Description
Technical field
The invention belongs to biochemical industry separation fields, in particular it relates to a kind of preparation method of type III collagen.
Background technique
Collagen is the native biopolymer with triple-helix structure, is the most abundant protein of animal in-vivo content, is fed
It in all proteins about 30% is collagen with newborn animal.Collagen is distributed widely in each histoorgan of human body, with
Content highest in connective tissue.Since it is the main constituents of Various Tissues in body, cell and institutional framework are played
Bracket effect, has important influence to the morphosis of cell and tissue, metabolism, growth and differentiation etc..Collagen is by 3
Chain composition, about 1000 amino acid residues of every peptide chain form difference according to the amino acid of its every chain, collagen can there are many
Type, at present in the mammalian body it has been found that 27 kinds of different types of collagens, the property of different collagen exist certain poor
It is different.
Type III collagen is a kind of important fiber formation collagen, accounts for about the 5-20% of whole collagen content in human body.III
Collagen Type VI is hollow organ's such as blood vessel of elastoresistance, a kind of important constituent in uterus and enteron aisle, also in its hetero-organization
Occur in conjunction with type i collagen, such as newborn skin.There is no processing completely for the most of III tropocollagen molecules found in cartilage, and contain
In conjunction with the disulfide bond of N-terminal propetide.
Type III collagen provides elasticity and integrality for many tissues, it is reported that it there are also other functions.1975,
It is earliest about type III collagen researches show that it to influence Human Platelet Aggregation, the calf skin type III glue of cyanogen bromide processing
Originating in a kind of raw peptide can promote the platelet adhesion reaction in human blood.Balleisen in 1979 confirms that platelet aggregation can lead to
Cross the I that antibody is applied to and is directly acted on, II on type III collagenous fibres and is suppressed, to prevent collagen and blood platelet
Direct physical contact.1993, Chiang etc. isolated a 47kDa memebrane protein from blood platelet and proves it and type III glue
Original interaction.Currently known blood platelet is interacted by specific glycoprotein and nonconformity element receptor and type III collagen
(Monnet and Fauvel-Lafeve, 2000).Type III collagen also passes through the interaction with cell surface receptor integrin, In
It plays a role in cell adherence, migration, proliferation and differentiation.In addition, passing through wound, peritonaeum and serum to postoperative patient
The detection of the liquid of middle collection, 2-3 days after surgery increase (Haukipuro of peptide level before the N-terminal of type III precollagen (PIIINP)
Et al., 1987).Postoperative 5th day, the PIIINP level of patient with operation was 1000 times of non-patient with operation.These discovery explanations
Type III collagen is necessary to wound healing.In terms of regeneration material, I type and type III collagen are for the bladder wall
The transplanting of acellular matrix and regeneration effect influence it is very significant (European Urology Supplements, 2003,2-1:
121)。
Due to collagen under native state solution not soluble in water, be directly separated different types of collagen there are certain difficulty,
It is also the hot spot of collagen research in technical field of biological material in recent years.Poplar forest etc. is prepared for people using the method for genetic recombination
Type III collagen has sequence (a kind of recombination human source collagen and preparation method thereof application number 102443057.A).Based on base
The collagen technology of preparing of cause is different from the method for preparing collagen as raw material using animal skin or bone, and cost is relatively low, the glue of preparation
Former purity is higher, but gene recombination technology can only prepare a chain local sequence living of collagen, and has three spirals in preparation
There are difficulty in terms of the collagen of structure.Jiang Bo etc. uses fresh regeneration ox-hide for raw material, using digesting, saltout, be denaturalized and renaturation
Technology be prepared for ox type III collagen (Jiang Bo, Li Xia, Chen Lu etc., the preparation method of medical grade type III collagen, application number
200910216686.7), but process is relatively complicated.
There is some difference for the thermal denaturation temperature of different collagen, and the collagen after thermal denaturation can pass through the enzyme of non-collagen class
It degrades.Therefore, the denaturation that different collagen can be achieved is controlled by temperature, and different collagen can be achieved after enzyme is added
Selective enzymolysis, be realize separation different collagen a kind of good method.
Summary of the invention
For the high situation of type III collagen preparation difficulty, it is an object of that present invention to provide a kind of extraction sides of type III collagen
Method, method includes the following steps:
(1) it pre-processes: taking the fresh skin of animal, the acid solution of 5-20 times of skin weight is added to after cleaning using clear water
In, 12-72h is impregnated at 4-40 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) it is beaten: skin being cut into bulk, the clear water of 2-8 times of weight is added, block-like skin will be cut into using refiner
Handle pulp.
(4) it extracts: adding the protease of the 0.05-5% of skin weight into homogenate, digest 12- under the conditions of 20-40 DEG C
48h。
(5) it digests: the clostridiopetidase A of skin weight 0.01-0.5% being added into the solution after enzymatic hydrolysis, in 30-40 DEG C of condition
Lower enzymatic hydrolysis 12-48h.
(6) ultrafiltration: ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection to be placed in drying in freeze drier, the powder after drying is type III collagen.
Preferably, in the step (1) acid solution soaking process, the acid solution used is acetic acid, hydrochloric acid, oxalic acid, lemon
The aqueous solution of lemon acid or the mixture of these acid solutions.
Preferably, in the step (1) acid solution soaking process, the total concentration of the acid solution used is 0.1-3mol/
L。
Preferably, protease used in the step (4) is pepsin, papain, in trypsase
It is one or more of.
Preferably, in the step (6) ultra-filtration process, the molecular cut off range of the ultrafiltration membrane used is 50k-
150kD。
Preferably, the fresh skin is fresh sucking pig skin or cow skin.
A kind of extracting method of type III collagen of the invention has easy to operate, dependence of the process conditions to instrument and equipment
Property it is lower, it is easy to accomplish the advantages of, and the type III collagen purity is high that this method is prepared, molecular weight is big, can be used as a kind of reason
The biomaterial thought, for fields such as organizational project, medical instrument, tissue repair, medicine controlled releasing and animal cell cultures.
Specific embodiment
The present invention is specifically described below by specific embodiment, it is worth mentioning that, the present embodiment is only used
In to a kind of implementation method of the present invention, the whole of the invention patent can not be represented, can not be interpreted as protecting model to the present invention
The limitation enclosed can also make several adjustment or improvement, these are all in the case where not departing from the precondition of design of essence of the invention
It belongs to the scope of protection of the present invention.
Embodiment 1:
(1) it pre-processes: taking fresh sucking pig skin 1kg, the 0.1mol/L hydrochloric acid solution of 5kg is added to after cleaning using clear water
In, 72h is impregnated at 4 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) it is beaten: skin being cut into bulk, 2kg clear water is added, block-like skin treatment will be cut into using refiner and be slurried
Shape.
(4) it extracts: 50g protease, 20 DEG C of enzymatic hydrolysis 48h being added into homogenate.
(5) it digests: the clostridiopetidase A of 1.5g, 30 DEG C of enzymatic hydrolysis 48h being added into the solution after enzymatic hydrolysis.
(6) ultrafiltration: the use of molecular weight is that 50kDa ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection is placed in freeze drier to dry, acquisition type III collagen 0.1kg after drying.
Embodiment 2:
(1) it pre-processes: taking fresh sucking pig skin 2kg, the 1mol/L acetic acid solution of 20kg is added to after cleaning using clear water
In, 48h is impregnated at 15 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) it is beaten: skin being cut into bulk, 8kg clear water is added, block-like skin treatment will be cut into using refiner and be slurried
Shape.
(4) it extracts: 60g protease, 30 DEG C of enzymatic hydrolysis 36h being added into homogenate.
(5) it digests: 0.2g clostridiopetidase A, 40 DEG C of enzymatic hydrolysis 36h being added into the solution after enzymatic hydrolysis.
(6) ultrafiltration: the use of molecular weight is that 80kDa ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection is placed in freeze drier to dry, acquisition type III collagen 0.23kg after drying.
Embodiment 3:
(1) it pre-processes: taking the cow skin 2kg of animal, the 2mol/L oxalic acid solution of 30kg is added to after cleaning using clear water
In, 36h is impregnated at 25 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) be beaten: skin being cut into bulk, 12kg clear water is added, using refiner will be cut into block-like skin treatment at
Pulpous state.
(4) it extracts: 30g protease being added into homogenate, 35 DEG C of enzymatic hydrolysis are for 24 hours.
(5) it digests: 6g clostridiopetidase A being added into the solution after enzymatic hydrolysis, 37 DEG C of enzymatic hydrolysis are for 24 hours.
(6) ultrafiltration: the use of molecular weight is that 120kDa ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection is placed in freeze drier to dry, acquisition type III collagen 0.19kg after drying.
Embodiment 4:
(1) it pre-processes: taking the cow skin 3kg of animal, the 3mol/L citric acid that 60kg is added to after cleaning using clear water is molten
In liquid, 12h is impregnated at 40 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) be beaten: skin being cut into bulk, 24kg clear water is added, using refiner will be cut into block-like skin treatment at
Pulpous state.
(4) it extracts: 0.5g protease being added into homogenate, 35 DEG C of enzymatic hydrolysis are for 24 hours.
(5) it digests: 15g clostridiopetidase A, 40 DEG C of enzymatic hydrolysis 12h being added into the solution after enzymatic hydrolysis.
(6) ultrafiltration: the use of molecular weight is that 120kDa ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection is placed in freeze drier to dry, acquisition type III collagen 0.45kg after drying.
Claims (6)
1. a kind of extracting method of type III collagen, which is characterized in that method includes the following steps:
(1) it pre-processes: taking the fresh skin of animal, be added to after being cleaned using clear water in the acid solution of 5-20 times of skin weight,
12-72h is impregnated at 4-40 DEG C, is washed again with clear water, up to eluate to neutrality.
(2) it removes the peel: in the horizontal direction being cut the epidermis of animal respectively with fat deposit using cutter, retain skin corium.
(3) it is beaten: skin being cut into bulk, the clear water of 2-8 times of weight is added, block-like skin treatment will be cut into using refiner
Pulp.
(4) it extracts: adding the protease of the 0.05-5% of skin weight into homogenate, digest 12-48h under the conditions of 20-40 DEG C.
(5) it digests: the clostridiopetidase A of skin weight 0.01-0.5%, enzyme under the conditions of 30-40 DEG C being added into the solution after enzymatic hydrolysis
Solve 12-48h.
(6) ultrafiltration: ultrafiltration membrance filter digests solution, collects trapped fluid；
(7) dry: the trapped fluid of collection to be placed in drying in freeze drier, the powder after drying is type III collagen.
2. a kind of extracting method of type III collagen according to claim 1, which is characterized in that used in preparation step (1)
Acid solution be acetic acid, hydrochloric acid, oxalic acid, the mixture of the aqueous solution of citric acid or these solution.
3. a kind of extracting method of type III collagen according to claim 2, which is characterized in that sour total dense in acid solution
Degree control is in 0.1-3mol/L.
4. a kind of extracting method of type III collagen according to claim 1, which is characterized in that make in the step (4)
Protease is pepsin, papain, one or more of trypsase.
5. a kind of extracting method of type III collagen according to claim 1, which is characterized in that in preparation step (6),
The molecular cut off range of the ultrafiltration membrane used is 50k-150kD.
6. a kind of extracting method of type III collagen according to claim 1, which is characterized in that the fresh skin is new
Fresh milk pigskin or cow skin.
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