CN102391374A - Preparation method of active collagen with triple-helix structure - Google Patents
Preparation method of active collagen with triple-helix structure Download PDFInfo
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Abstract
The invention relates to a preparation method of collagen; fresh pigskin is used as a raw material; the raw material is treated by pretreatment, fat removal, and acid-enzyme treatment; ultrasonic treatment is employed to further improve extraction efficiency; and finally purification is performed to prepare a collagen product with high purity. The preparation method of collagen has high extraction efficiency, and the product purity is up to above 98%. The product is active collagen with a maintained triple-helix structure, has low immunogenicity and high biocompatibility, is biodegradable, and is applicable to medical purposes.
Description
Technical field
The present invention relates to a kind of preparation method with active collagen of triple-helix structure, belong to the protein engineering field, this product has reduced immunogenicity, high-biocompatibility for keeping the active collagen of triple-helix structure, and is biodegradable, is applicable to medical use.
Background technology
Collagen is that the vertebrates in-vivo content is the abundantest, one group of scleroprotein of most widespread; Molecular weight is about 300000; All can form the supramolecule aggregation in the extracellular, be present in a large number in bone, cartilage, tendon and the skin, account for the 25%-33% of human body or other animal body total protein contents.The collagen that often contains several types in the same tissue is main with certain often.Type i collagen is dispersed throughout the each several part of human body, is mainly in skin, tendon and the ligament, has very strong anti-Zhang Nengli.The II Collagen Type VI mainly is present in hyaline cartilage, the vitreum, has stronger anti-pressure ability.The III Collagen Type VI is distributed widely in the big tissue of extensibility, like loose connective tissue etc., has extensibility and complaisance.Wherein, type i collagen accounts for 90% of the total collagen quantity of organism, and therefore, the use of type i collagen in biomaterial is also the most extensive.
Collagen is identical in the molecular level structure, is made up of 3 a chain polypeptide, and each bar collagen chain all is the left hand helix configuration.Article 3, the left hand helix chain is wound in the right-handed helix structure again each other, and promptly superhelix is the unique triple helices structure of collagen protein, makes its molecular structure highly stable.Article 3, chain is rich in glycocoll, proline(Pro) and L-Ala, lacks halfcystine and tryptophane, and tyrosine content is also very low, but contains unique hydroxylation amino acid (oxyproline and L-Hydroxylysine).Because fibriilar directivity and the difference that becomes beam diameter and density, there is textural difference in the collagen of different tissues, and has separately function and constitutional features.In reticular tissue, collagen is except mechanical support, or cell adhesion and the important substance basis of moving, and therefore, collagen is considered to form occurrence factor important in fetal development and the tissue regeneration, in organizational project, is used widely.
Can be called as collagen, must be that proteinoid that its triple-helix structure does not change, and also remains with complete biological activity.And collagen protein is the hydrolysate of collagen, and the triple-helix structure of collagen thoroughly unclamps, and becomes 3 peptide chains freely, and is degraded into polydisperse peptide section, comprising little peptide.Therefore collagen protein is a polypeptide mixture, relative molecular weight from several thousand to several ten thousand, and MWD is very wide, does not have biological activity, can be dissolved in cold water, and can be by the proteolytic enzyme utilization.
A kind of preparation method of collagen is disclosed among the CN1110284, with acid extraction, the salt deposition, membrane filtration, last freeze-drying, its extraction efficiency and purity are all lower.It is the method for feedstock production collagen protein with the cod skin that CN101250218 discloses a kind of, and its preparation method can destroy the triple-helix structure of collagen.The prior art disclosed method is often destroyed the triple-helix structure of collagen in the extraction preparation process of collagen, perhaps extraction efficiency is lower, can't realize can either retentive activity collagen triple-helix structure, improve extraction efficiency and purity again simultaneously.
Summary of the invention
To above-mentioned situation, the purpose of this invention is to provide a kind of preparation method with active collagen of triple-helix structure.The present invention uses sour enzyme to combine to handle the preparation method who adds gradual ultrasonication, not only can keep the triple-helix structure of collagen, has improved the extraction efficiency of collagen simultaneously significantly.The present invention uses H
2O
2Solution-treated add sour dissolved salt analyse purifying add the dialysis purifying effectively raise the collagen product gas purity.
A kind of preparation method with active collagen of triple-helix structure comprises the steps: that raw materials pretreatment, grease removal, sour enzyme combine processing, ultrasonication, H
2O
2Solution-treated, sour dissolved salt are analysed purifying, dialysis purifying, drying.
Described raw material is to be selected from a kind of in fresh porcine skin, ox-hide, the ox heel string.
Described sour enzyme combines to be treated to: immerse in 0.6～0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600～700mg/L through pretreated raw material, continue to stir about 25～30 hours.
Described ultrasonication preferably adopts gradual ultrasonication, uses 100～200W supersound process 30 minutes earlier, re-uses 200～300W supersound process 30 minutes, uses 300～400W supersound process at last 1 hour.
Described a kind of preparation method with active collagen of triple-helix structure, concrete steps are following:
(1) get fresh porcine skin, oil layer and trichocutis are removed in cutting, remove impurity, clean; Pigskin is broken into fine granularity,, adds the aqueous sodium hydroxide solution of 0.01～0.03mol/L according to 1: 30～1: 40 ratio of solid-to-liquid ratio; In 6～8 ℃ of immersions 1～2 hour, filter, subsequent use;
(2) in above-mentioned pretreated pigskin, adding quality is the anhydrous diethyl ether or the acetone of 6～8 times of pigskin quality, in 35～40 ℃ of backflow 5-8 hours, afterwards with distilled water flushing to free from extraneous odour, subsequent use;
(3) above-mentioned pigskin is immersed in 0.6～0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600～700mg/L, continue to stir about 25～30 hours;
(4) said mixture is adopted gradual ultrasonication, used 100～200W supersound process 30 minutes earlier, re-used 200～300W supersound process 30 minutes, used 300～400W supersound process at last 1 hour;
(5) the H2O2 solution of adding 2～3% mixes and left standstill 2～4 hours, regulates pH to 5.0, and is centrifugal;
(6) get supernatant, add NaCl, stirred 20-30 hour, centrifugal, throw out adds the dissolving of 0.6-0.7moL/L Glacial acetic acid min. 99.5, and is centrifugal, gets supernatant, regulates pH to 7.5, adds NaCl, stirs 20-30 hour, centrifugal;
(7) throw out that step (6) is obtained is dissolved in 0.6～0.7moL/L Glacial acetic acid min. 99.5, and the Glacial acetic acid min. 99.5 with 0.6～0.7moL/L is extracellular fluid dialysis dialysis 2 times earlier, each 4 hours; Be extracellular fluid dialysis dialysis 5～7 times again with zero(ppm) water; Each 4 hours, extremely outer liquid detected less than cl ions, obtains collagen liquid;
(8), obtain having the active collagen of triple-helix structure with the aforesaid liquid lyophilize.
Described size with triple-helix structure active collagen is generally 20000～30000 dalton.
The acid enzyme combines to handle: sour enzyme combination processing of the present invention is meant through pretreated raw material immerses in 0.6～0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600～700mg/L, continues stirring about 25～30 hours.This method has combined acid system and Enzymatic Extraction to prepare the characteristics of collagen, has prevented the destruction of active collagen triple-helix structure is effectively raised extraction efficiency.
Ultrasonication: sour enzyme of the present invention combines processing to be meant the gradual ultrasonication of employing, uses 100～200W supersound process 30 minutes earlier, re-uses 200～300W supersound process 30 minutes, uses 300～400W supersound process at last 1 hour.The present invention adopts ultrasonication combined acid Enzymatic Extraction to prepare collagen protein, finds through experimental study, adopts ultrasonication can effectively improve extraction efficiency.Adopt gradual ultrasonication to compare, can better prevent the destruction of the triple-helix structure of collagen, and effectively reduce the production energy consumption in ultrasonication stage with adopting the constant power supersound process.
Beneficial effect of the present invention: the present invention uses sour enzyme to combine to handle the preparation method who adds gradual ultrasonication; Reduced destruction to the full extent to collagen structure; The triple-helix structure that keeps active collagen, the extraction efficiency that the while has been improved collagen has significantly reduced production cost.Simultaneously, gradual ultrasonication has also reduced energy consumption in the ultrasonication link to a certain extent.The present invention uses H
2O
2Solution-treated add sour dissolved salt analyse purifying add the dialysis purifying effectively raise the collagen product gas purity.The collagen product that method of the present invention directly makes has reduced immunogenicity and high-biocompatibility, through suitability for industrialized production, and is widely used in medical product, as: skin substitute products, bone surrogate, collagen protein dressing, biotechnology film etc.
Embodiment
Below in conjunction with embodiment, further set forth the present invention:
Embodiment 1
(1) get fresh ox-hide, cut and remove oil layer and trichocutis, remove impurity, clean, ox-hide is broken into fine granularity,, add the aqueous sodium hydroxide solution of 0.03mol/L,, filter in 6～8 ℃ of immersions 2 hours according to 1: 30 ratio of solid-to-liquid ratio, subsequent use;
(2) in above-mentioned pretreated ox-hide, adding quality is the anhydrous diethyl ether or the acetone of 8 times of ox-hide quality, refluxed 8 hours in 35 ℃, afterwards with distilled water flushing to free from extraneous odour, subsequent use;
(3) above-mentioned ox-hide is immersed in 0.6mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 700mg/L, continue to stir about 25 hours;
(4) said mixture is adopted gradual ultrasonication, used the 100W supersound process 30 minutes earlier, re-used the 300W supersound process 30 minutes, used the 400W supersound process at last 1 hour;
(5) H of adding 2%
2O
2Solution mixes and left standstill 4 hours, regulates pH to 5.0, and is centrifugal;
(6) get supernatant, add NaCl, stirred 20 hours, centrifugal, throw out adds the dissolving of 0.7moL/L Glacial acetic acid min. 99.5, and is centrifugal, gets supernatant, regulates pH to 7.5, adds NaCl, stirs 20 hours, centrifugal;
(7) throw out that step (6) is obtained is dissolved in the 0.7moL/L Glacial acetic acid min. 99.5, and the Glacial acetic acid min. 99.5 with 0.7moL/L is extracellular fluid dialysis dialysis 2 times earlier, each 4 hours; Be extracellular fluid dialysis dialysis 5 times again with zero(ppm) water; Each 4 hours, extremely outer liquid detected less than cl ions, obtains collagen liquid;
(8), obtain having the active collagen of triple-helix structure with the aforesaid liquid lyophilize.
Embodiment 2
(1) get the fresh bovine heel string, cut and remove oil layer and trichocutis, remove impurity, clean, the ox heel string is broken into fine granularity,, add the aqueous sodium hydroxide solution of 0.01mol/L,, filter in 6～8 ℃ of immersions 1 hour according to 1: 40 ratio of solid-to-liquid ratio, subsequent use;
(2) in above-mentioned pretreated ox heel string, adding quality is the anhydrous diethyl ether or the acetone of 6 times of ox heel string quality, refluxed 5 hours in 40 ℃, afterwards with distilled water flushing to free from extraneous odour, subsequent use;
(3) above-mentioned ox heel string is immersed in 0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600mg/L, continue to stir about 30 hours;
(4) said mixture is adopted gradual ultrasonication, used the 100W supersound process 30 minutes earlier, re-used the 200W supersound process 30 minutes, used the 300W supersound process at last 1 hour;
(5) H of adding 3%
2O
2Solution mixes and left standstill 2 hours, regulates pH to 5.0, and is centrifugal;
(6) get supernatant, add NaCl, stirred 30 hours, centrifugal, throw out adds the dissolving of 0.6moL/L Glacial acetic acid min. 99.5, and is centrifugal, gets supernatant, regulates pH to 7.5, adds NaCl, stirs 30 hours, centrifugal;
(7) throw out that step (6) is obtained is dissolved in the 0.6moL/L Glacial acetic acid min. 99.5, and the Glacial acetic acid min. 99.5 with 0.6moL/L is extracellular fluid dialysis dialysis 2 times earlier, each 4 hours; Be extracellular fluid dialysis dialysis 7 times again with zero(ppm) water; Each 4 hours, extremely outer liquid detected less than cl ions, obtains collagen liquid;
(8), obtain having the active collagen of triple-helix structure with the aforesaid liquid lyophilize.
Embodiment 3
(1) get fresh porcine skin, cut and remove oil layer and trichocutis, remove impurity, clean, pigskin is broken into fine granularity,, add the aqueous sodium hydroxide solution of 0.02mol/L,, filter in 6～8 ℃ of immersions 1.5 hours according to 1: 35 ratio of solid-to-liquid ratio, subsequent use;
(2) in above-mentioned pretreated pigskin, adding quality is the anhydrous diethyl ether or the acetone of 7 times of pigskin quality, refluxed 6 hours in 37 ℃, afterwards with distilled water flushing to free from extraneous odour, subsequent use;
(3) above-mentioned pigskin is immersed in 0.65mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 650mg/L, continue to stir about 28 hours;
(4) said mixture is adopted gradual ultrasonication, used the 150W supersound process 30 minutes earlier, re-used the 250W supersound process 30 minutes, used the 350W supersound process at last 1 hour;
(5) H of adding 2.5%
2O
2Solution mixes and left standstill 3 hours, regulates pH to 5.0, and is centrifugal;
(6) get supernatant, add NaCl, stirred 25 hours, centrifugal, throw out adds the dissolving of 0.65moL/L Glacial acetic acid min. 99.5, and is centrifugal, gets supernatant, regulates pH to 7.5, adds NaCl, stirs 25 hours, centrifugal;
(7) throw out that step (6) is obtained is dissolved in the 0.65moL/L Glacial acetic acid min. 99.5, and the Glacial acetic acid min. 99.5 with 0.65moL/L is extracellular fluid dialysis dialysis 2 times earlier, each 4 hours; Be extracellular fluid dialysis dialysis 6 times again with zero(ppm) water; Each 4 hours, extremely outer liquid detected less than cl ions, obtains collagen liquid;
(8), obtain having the active collagen of triple-helix structure with the aforesaid liquid lyophilize.
Claims (5)
1. the preparation method with active collagen of triple-helix structure is characterized in that, comprises the steps: that raw materials pretreatment, grease removal, sour enzyme combine processing, ultrasonication, H
2O
2Solution-treated, sour dissolved salt are analysed purifying, dialysis purifying, drying.
2. preparation method according to claim 1 is characterized in that, described raw material is to be selected from a kind of in fresh porcine skin, ox-hide, the ox heel string.
3. preparation method according to claim 1 is characterized in that, described sour enzyme combines to be treated to: immerse in 0.6～0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600～700mg/L through pretreated raw material, continue to stir about 25～30 hours.
4. preparation method according to claim 1; It is characterized in that described ultrasonication preferably adopts gradual ultrasonication, used 100～200W supersound process 30 minutes earlier; Re-use 200～300W supersound process 30 minutes, used 300～400W supersound process at last 1 hour.
5. preparation method according to claim 1 is characterized in that concrete steps are following:
(1) get fresh porcine skin, oil layer and trichocutis are removed in cutting, remove impurity, clean; Pigskin is broken into fine granularity,, adds the aqueous sodium hydroxide solution of 0.01～0.03mol/L according to 1: 30～1: 40 ratio of solid-to-liquid ratio; In 6～8 ℃ of immersions 1～2 hour, filter, subsequent use.
(2) in above-mentioned pretreated pigskin, adding quality is the anhydrous diethyl ether or the acetone of 6～8 times of pigskin quality, in 35～40 ℃ of backflow 5-8 hours, afterwards with distilled water flushing to free from extraneous odour, subsequent use.
(3) above-mentioned pigskin is immersed in 0.6～0.7mol/L Glacial acetic acid min. 99.5 and the pepsic mixed solution of 600～700mg/L, continue to stir about 25～30 hours.
(4) said mixture is adopted gradual ultrasonication, used 100～200W supersound process 30 minutes earlier, re-used 200～300W supersound process 30 minutes, used 300～400W supersound process at last 1 hour.
(5) H of adding 2～3%
2O
2Solution mixes and left standstill 2～4 hours, regulates pH to 5.0, and is centrifugal.
(6) get supernatant, add NaCl, stirred 20-30 hour, centrifugal, throw out adds the dissolving of 0.6-0.7moL/L Glacial acetic acid min. 99.5, and is centrifugal, gets supernatant, regulates pH to 7.5, adds NaCl, stirs 20-30 hour, centrifugal.
(7) throw out that step (6) is obtained is dissolved in 0.6～0.7moL/L Glacial acetic acid min. 99.5, and the Glacial acetic acid min. 99.5 with 0.6～0.7moL/L is extracellular fluid dialysis dialysis 2 times earlier, each 4 hours; Be extracellular fluid dialysis dialysis 5～7 times again with zero(ppm) water; Each 4 hours, extremely outer liquid detected less than cl ions, obtains collagen liquid.
(8), obtain having the active collagen of triple-helix structure with the aforesaid liquid lyophilize.
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Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN103966294A (en) * | 2013-02-02 | 2014-08-06 | 深圳兰度生物材料有限公司 | Extraction method for bioactive collagen |
| CN106317909A (en) * | 2016-08-25 | 2017-01-11 | 董晓 | Preparing method of antibacterial medical grade thin film material |
| CN106591406A (en) * | 2016-11-23 | 2017-04-26 | 江南大学 | Method for preparing bone gelatin by ultrasonic assisted enzyme method |
| CN106589113A (en) * | 2016-11-17 | 2017-04-26 | 北京华信佳音医疗科技发展有限责任公司 | Method for extracting collagen from bovine achilles tendons |
| CN106866816A (en) * | 2017-04-14 | 2017-06-20 | 桂林融通科技有限公司 | The acid-enzyme binding-method of collagen is extracted from pigskin |
| CN107441549A (en) * | 2017-06-16 | 2017-12-08 | 无锡贝迪生物工程股份有限公司 | A kind of preparation method of collagen Heparan sulfate combine dressing |
| CN108192941A (en) * | 2018-03-07 | 2018-06-22 | 广州创尔生物技术股份有限公司 | A kind of method of quality control of biologically active collagen |
| CN110563834A (en) * | 2019-09-25 | 2019-12-13 | 成都奇璞生物科技有限公司 | Collagen extraction method |
| CN111388742A (en) * | 2020-04-26 | 2020-07-10 | 无锡贝迪生物工程股份有限公司 | Collagen dressing capable of releasing antibiotics in sustained and controlled manner and preparation method thereof |
| CN113667009A (en) * | 2021-07-13 | 2021-11-19 | 尚诚怡美(成都)生物科技有限公司 | Collagen with triple-helical structure and preparation method thereof |
| CN114634563A (en) * | 2022-02-16 | 2022-06-17 | 惠州华阳医疗器械有限公司 | Active collagen extracting solution, preparation method and system thereof, skin care product and preparation method thereof |
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| CN103966294A (en) * | 2013-02-02 | 2014-08-06 | 深圳兰度生物材料有限公司 | Extraction method for bioactive collagen |
| CN106317909A (en) * | 2016-08-25 | 2017-01-11 | 董晓 | Preparing method of antibacterial medical grade thin film material |
| CN106589113A (en) * | 2016-11-17 | 2017-04-26 | 北京华信佳音医疗科技发展有限责任公司 | Method for extracting collagen from bovine achilles tendons |
| CN106591406B (en) * | 2016-11-23 | 2020-03-24 | 江南大学 | Method for preparing bone gelatin by using ultrasonic-assisted enzyme method |
| CN106591406A (en) * | 2016-11-23 | 2017-04-26 | 江南大学 | Method for preparing bone gelatin by ultrasonic assisted enzyme method |
| CN106866816A (en) * | 2017-04-14 | 2017-06-20 | 桂林融通科技有限公司 | The acid-enzyme binding-method of collagen is extracted from pigskin |
| CN107441549A (en) * | 2017-06-16 | 2017-12-08 | 无锡贝迪生物工程股份有限公司 | A kind of preparation method of collagen Heparan sulfate combine dressing |
| CN108192941A (en) * | 2018-03-07 | 2018-06-22 | 广州创尔生物技术股份有限公司 | A kind of method of quality control of biologically active collagen |
| CN110563834A (en) * | 2019-09-25 | 2019-12-13 | 成都奇璞生物科技有限公司 | Collagen extraction method |
| CN111388742A (en) * | 2020-04-26 | 2020-07-10 | 无锡贝迪生物工程股份有限公司 | Collagen dressing capable of releasing antibiotics in sustained and controlled manner and preparation method thereof |
| CN113667009A (en) * | 2021-07-13 | 2021-11-19 | 尚诚怡美(成都)生物科技有限公司 | Collagen with triple-helical structure and preparation method thereof |
| CN113667009B (en) * | 2021-07-13 | 2023-04-28 | 尚诚怡美(成都)生物科技有限公司 | Three-helix structure collagen and preparation method thereof |
| CN114634563A (en) * | 2022-02-16 | 2022-06-17 | 惠州华阳医疗器械有限公司 | Active collagen extracting solution, preparation method and system thereof, skin care product and preparation method thereof |
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Address after: 214000, Jiangsu, Wuxi province Mashan biological medicine industry park (business place, Wuxi, Binhu District, Mashan, Mei Liang Road, No. 132) Patentee after: Wuxi Betty biological engineering Limited by Share Ltd Address before: 214063, Mashan biological pharmaceutical industry park (Ziyun Road), Binhu District, Jiangsu, Wuxi Province Patentee before: Wuxi Biot Bio-technology Co., Ltd. |