CN101381411B - Sipunculid collagen protein and preparation method thereof - Google Patents
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Abstract
The present invention discloses sipunculan collagen and a preparation method thereof. A sipunculan body wall is taken as a raw material to obtain white or light yellow powder through the extraction by enzyme or acid, the thermal contraction temperature of the powder is between 53.30 and 54.50 DEG C, the average value of isoelectric points is between 4.65 and 4.90, the molecular weight is between 116KD and 200KD, the sugar content is between 0.50 and 0.90mg/100mg, the content of amino acid is between 90 and 95mg/100mg, the content of hydroxyproline in the amino acid is between 9.5 and 11.5 percent (weight), and the sipunculan collagen has a triple helical structure consisting of three peptide chains, absorbs within the range of between 1235cm<-1> and 1450cm<-1> of an infrared spectrum, and has stronger absorption at 1651.42cm<-1> of the infrared spectrum. The sipunculan collagen has universal characteristics of animal collagen such as biocompatibility, low immunogenicity, gelation property, water absorption, water retention property, emulsifying property and so on, also has high dispersion and low adhesive property, is used in fields such as medicine, cosmetics and food and particularly has apparent promotion action to the healing of wounds.
Description
Technical field
The present invention relates to biological collagen, be specifically related to Sipunculid collagen protein and preparation method thereof.
Background technology
Collagen protein is the structural protein of animal, because the structure of its structure or its hydrolyzate is similar to the collagen structure of human skin, the amino of its molecule and carboxylic group have very high surfactivity and excellent biological compatibility, when therefore being used for makeup skin are had no stimulation.Therefore tool water-absorbent and retentiveness are used for the water retention capacity that makeup can strengthen skin because collagen protein has been rich in hydrophilic radical such as hydroxyl, prevent that moisture from evaporating from skin surface, and then improve pachylosis, lacklustre situation.In addition collagen protein also have reduced immunogenicity and and host cell and the tissue between excellent biological compatibility is arranged, can promote platelet aggregation and promote the anastalsis that blood plasma lumps, therefore collagen protein is the biomedical material that a class has multiple good characteristic, is used widely in medical field.
Collagen protein and water bonded are very capable, not only have gelation but also emulsifying property is arranged, and this character makes collagen can be used as weighting agent and gel in food, also can emulsification expand in acid and alkaline medium, so can be applicable to prepare industrial chemicals.Present collagen product mainly is to extract from the skin of livestock product such as pig, ox and bone, and in recent years owing to the outburst of mad cow disease and foot and mouth disease, there is hidden danger in the product in livestock products source; Therefore begin to seek from fishery products, to extract collagen protein.As Granted publication number is CN100345867C, the day for announcing is on October 31st, 2007, name is called the patent of invention of " a kind of acid soluble fish skin collagen and preparation method thereof ", disclose with the fish-skin is raw material, by chopping, remove noncollagen protein and impurity, degreasing, extract, saltout, purifying, obtain the pure white spongiform collagen of fish skin that is after the drying, its molecular weight is greater than 60000, contain three xenogenesis α chains, dissolve in neutral salt solution or acidic solution at low temperatures, be of similar shape with derived collagen, size and amino acid are formed, contain abundant glycine in the collagen of fish skin, proline(Pro) and oxyproline, its hydrolysate also contains physiologically active peptide.Its disclosed preparation method is for obtaining vat liquor by 0.1mol/L citric acid and 0.5mol/L acetic acid with the preparation of 1:0.1～10, vat liquor lixiviate fish-skin with 5～25 times of fish-skin weight, under 4～10 ℃ of temperature condition, lixiviate 10～24 hours, through centrifugal, saltout, centrifugal, purifying obtains collagen of fish skin after dry again.Granted publication number is CN100369929C, the day for announcing is on February 20th, 2008, name is called the patent of invention of " jellyfish collagen and preparation method thereof ", also disclose from the mesogloea of jellyfish and extracted the jellyfish collagen that obtains white or light yellow solid powder, its bulk density is 0.11～0.645g/ml, the single chain molecule amount is 10～300,000 dalton, sugar content is 2.5～5%, aminoacids content is 80～95%mg/100mg, wherein aspartic acid accounts for 7.9～8.3%, and L-glutamic acid accounts for 10.0～12.9%.Its preparation method be the jellyfish mesogloea with proteolysis from, the proteolytic enzyme consumption is 0.2～1%, dissociation temperature is 10～30 ℃, the time of dissociating is 10～48 hours.
The collagen protein of various natural extract has been widely used in the fields such as makeup, medicine, food, but differences such as the composition group of the collagen protein that extraction obtains from different animal bodies, spirane structure, its physicochemical property is also different, therefore just difference to some extent of physiological function, Application Areas and effect just emphasize particularly on different fields a little.
Sipunculida (Sipunculoidea) is divided into two guiding principles, 4 orders, 6 sections and 17 genus, about 300 kinds; Kind surplus China has 60, existing only find 40 surplus kind.The coastal distribution of China is mainly leather bag siphon-worm, body Sipunculus, Sipunculus nudus.The body wall of siphon-worm is made up of epithelium, stratum corneum, dermal appendage, collagen fiber layer, basilar membrane, circular layer, longitudinal muscle layer and coelarium, collagen fiber layer all has distribution at the whole body body surface of siphon-worm, and it is neat and orderly, therefore collagen protein is flourishing, the content of the collagen protein of content height, especially tentacle is very high.
Summary of the invention
Problem to be solved by this invention provides a kind of Sipunculid collagen protein, this collagen protein has the universal feature of animal collagen: biocompatibility, reduced immunogenicity, gelation, water-absorbent, retentiveness and emulsifying property, also have high dispersion and low tackiness, can be used for fields such as medicine, makeup, food, wound healing is had obvious facilitation.
The present invention also provides the preparation method of this collagen protein.
The present invention solves the problems of the technologies described above the technical scheme that is adopted: with the siphon-worm body wall of removing noncollagen protein is raw material, by aspartic protease or volumetric molar concentration is the acid extraction of 0.2～2.0mol/L, through centrifugal, saltout, centrifugal again, dialysis, step of freeze drying obtains, this Sipunculid collagen protein is white or faint yellow powder, its heat shrink temperature is 53.00～55.00 ℃, iso-electric point mean value is 4.60～4.90, the molecular weight of this Sipunculid collagen protein is 116KD～200KD (kilodalton), sugar content is 0.50～0.90mg/100mg, aminoacids content is 90～95mg/100mg, hydroxyproline content is 9.5%～11.5% (weight) in the described amino acid, this Sipunculid collagen protein is the triple-helix structure that three kinds of peptide chains are formed, at the 1235cm of infrared spectra
-1～1450cm
-1Scope in exist to absorb, at the 1651.42cm of infrared spectra
-1Stronger absorption appears in the place.
The wherein a kind of of described peptide chain is the dimer of two α peptide chains.
One of preparation method of described Sipunculid collagen protein comprises the steps:
The siphon-worm body wall that a will remove noncollagen protein evenly grinds, and joins in the acetate buffer solution that final concentration is 0.5mol and is mixed with homogenizing fluid, the volume ratio 100:1 of acetate buffer solution and siphon-worm body wall;
B adds aspartic protease in homogenizing fluid, the weight ratio of aspartic protease and siphon-worm body wall is 1:50～400, and enzymolysis is 10～60 hours under 0～100 ℃ of temperature condition;
The enzyme that goes out after the c enzymolysis is finished, the homogenizing fluid of the enzyme that will go out are under 4 ℃ of temperature condition, with the centrifugal 10min of 8000rpm, the supernatant liquor of winning, throw out be the method enzymolysis once more of b set by step, and be centrifugal equally then, get second supernatant liquor, merging first supernatant liquor and second supernatant liquor is total supernatant liquor;
D adds NaCl solution at total supernatant liquor, makes its final concentration reach 2mol/L, leaves standstill to collagen protein to precipitate fully;
E under 4 ℃ of temperature condition, with the centrifugal 20min of 8000rpm, obtains the collagen protein precipitation again;
F is dissolved in the collagen protein precipitation in the dialyzate of 0.1～0.5mol/L repeatedly, places the dialysis of dialysis tubing flowing water, to AgNO
3Solution can not detect extracellular fluid dialysis and has Cl
-Till, obtain dialyzed solution;
H obtains the solubility in acid Sipunculid collagen protein with the dialyzed solution lyophilize.
Described aspartic protease is a stomach en-, and the weight ratio of stomach en-and siphon-worm body wall is 1:50～350, and enzymolysis is 20～40 hours under 35～40 ℃ of temperature condition; Pepsic optimal pH is between 1.5-2.2; Also can use papoid, trypsinase, bromeline or compound protease to replace stomach en-.
The preparation method's of described Sipunculid collagen protein two comprises the steps:
1) the siphon-worm body wall that will remove noncollagen protein evenly grinds, and joins in the acetate buffer solution that final concentration is 0.5mol and is mixed with homogenizing fluid, the volume ratio 100:1 of acetate buffer solution and siphon-worm body wall;
2) adding volumetric molar concentration in homogenizing fluid is the acid of 0.2～2.0mol/L, and acid is 1:50～400 with the weight ratio of siphon-worm body wall, and acidolysis is 10～60 hours under 0～100 ℃ of temperature condition;
3) after acidolysis is finished, with homogenizing fluid 4 ℃ with the centrifugal 10min of 8000rpm, the supernatant liquor of winning, throw out be the method acidolysis once more of b set by step, and be centrifugal equally then, second supernatant liquor, merging first supernatant liquor and second supernatant liquor is total supernatant liquor;
4) add NaCl solution at total supernatant liquor, make final concentration reach 2mol/L, leave standstill to collagen protein and precipitate fully;
5) again 4 ℃ with the centrifugal 20min of 8000rpm, obtain the collagen protein precipitation;
6) the collagen protein precipitation is dissolved in the dialyzate of 0.1～0.5mol/L repeatedly, places the dialysis of dialysis tubing flowing water, to AgNO
3Solution can not detect extracellular fluid dialysis and has Cl
-Till, obtain dialyzed solution;
7), obtain the solubility in acid Sipunculid collagen protein with the dialyzed solution lyophilize.
In step 2) in, described acid is acetic acid, the volumetric molar concentration of described acetic acid is 0.8～1.4mol/L.
In step 2) in, described acid is citric acid, the volumetric molar concentration of described citric acid is 0.8～2.0mol/L.
In step 2) in, described acid is hydrochloric acid, the volumetric molar concentration of described hydrochloric acid is 0.2～0.8mol/L
Compared with prior art, the invention has the advantages that with the siphon-worm body wall be raw material, by aspartic protease or volumetric molar concentration is the acid extraction of 0.2～2.0mol/L, through centrifugal, saltout, centrifugal again, dialysis, step of freeze drying obtains, it is white or faint yellow powder, heat shrink temperature is 53.00～55.00 ℃, iso-electric point mean value is 4.60～4.90, its molecular weight is 116KD～200KD, sugar content is 0.50～0.90mg/100mg, and aminoacids content is 90～95mg/100mg, and hydroxyproline content is 9.5%～11.5% (weight) in the described amino acid, this Sipunculid collagen protein is the triple-helix structure that three kinds of peptide chains are formed, at the 1235cm of infrared spectra
-1～1450cm
-1Scope in exist to absorb, at the 1651.42cm of infrared spectra
-1Stronger absorption appears in the place.This Sipunculid collagen protein has the universal feature of animal collagen, as biocompatibility, reduced immunogenicity, gelation, water-absorbent, retentiveness and emulsifying property etc., also have high dispersion and low tackiness, the tackiness of this Sipunculid collagen protein gel is-6.00～-6.16 under 20 ℃ of temperature.Sipunculid collagen protein of the present invention can be used for fields such as medicine, makeup, food, especially wound healing is had obvious facilitation.With this Sipunculid collagen protein of acidic protein enzyme extraction, extraction yield can reach more than 50%, can reach more than 70% with stomach en-, and with this Sipunculid collagen protein of acid extraction, extraction yield is lower, is generally about 20%.
Description of drawings
Fig. 1 is the Sipunculid collagen protein infrared spectrogram of embodiment 1;
Fig. 2 is the Sipunculid collagen protein electrophorogram of embodiment 1;
Fig. 3 is the Sipunculid collagen protein electrophorogram of embodiment 2;
Fig. 4 is the Sipunculid collagen protein infrared spectrogram of embodiment 2.
Embodiment
Embodiment describes in further detail the present invention below in conjunction with accompanying drawing.
Embodiment 1
Remove noncollagen protein after the siphon-worm body wall cleaned, evenly grind then, join in the acetate buffer solution that final concentration is 0.5mol and be mixed with homogenizing fluid, the volume ratio 100:1 of acetate buffer solution and siphon-worm body wall; Add stomach en-in homogenizing fluid, the weight ratio of stomach en-and siphon-worm body wall is 1:150, and enzymolysis is about 30 hours under 35～40 ℃ of temperature condition; The enzyme that goes out after enzymolysis is finished, the homogenizing fluid of the enzyme that will go out are under 4 ℃ of temperature condition, with the centrifugal 10min of 8000rpm, the same once more enzymolysis of the supernatant liquor of winning, throw out, centrifugal equally then, get second supernatant liquor, merging first supernatant liquor and second supernatant liquor is total supernatant liquor; Add NaCl solution at total supernatant liquor, make its final concentration reach 2mol/L, leave standstill to collagen protein and precipitate fully; Under 4 ℃ of temperature condition,, obtain the collagen protein precipitation again with the centrifugal 20min of 8000rpm; The collagen protein precipitation is dissolved in the dialyzate of 0.1～0.5mol/L repeatedly, places the dialysis of dialysis tubing flowing water, to AgNO
3Solution can not detect extracellular fluid dialysis and has Cl
-Till, obtain dialyzed solution; With the dialyzed solution lyophilize, the pulverulent solubility in acid Sipunculid collagen protein that obtains being white in color, more than the extraction rate reached to 75%, extraction yield is collagen protein total amount * 100% in the amount/siphon-worm body wall that extracts the collagen protein that obtains.Measure this Sipunculid collagen protein infrared spectra, as can be seen from Figure 1 at 1235cm
-1～1450cm
-1Has absorption band (N-H and C-H distortion, stretching vibration) in the scope, at the 1651.42cm of infrared spectra
-1Stronger absorption peak (C=O stretching vibration) appears in the place; Infrared spectra determination of infrared spectroscopy, sweep limit are 4000cm
-1～400cm
-1This Sipunculid collagen protein of electrophoresis, as can be seen from Figure 2 near 116KD～200KD, exist three clearly band be respectively α, β, γ component, the molecular weight of representing this collagen protein is at 116KD～200KD, has complete triple-helix structure, and the β component is more, measures to such an extent that the β component is the dimer of two α peptide chains; Electrophoresis method is the SDS-PAGE vertical slab electrophoresis, uses coomassie brilliant blue staining.
The heat shrink temperature that records this Sipunculid collagen protein with the routine biochemistry method is 53.30 ℃, and iso-electric point mean value is 4.70, and sugared content is 0.58mg/100mg, and aminoacids content is 92.33mg/100mg, and hydroxyproline content is 10.99% (weight) in the amino acid.With viscosity measuring instrument and to calculate the tackiness of gel under 20 ℃ of temperature that this Sipunculid collagen protein makes be-6.04.
Embodiment 2
Substantially the same manner as Example 1, different just replace stomach en-to the acidolysis of siphon-worm body wall with citric acid, the volumetric molar concentration of citric acid is 1.6mol/L, the weight ratio of citric acid and siphon-worm body wall is 1:200, obtain being faint yellow pulverulent solubility in acid Sipunculid collagen protein, more than the extraction rate reached to 22%.Measure this Sipunculid collagen protein infrared spectra, as can be seen from Figure 4 Sipunculid collagen protein is at 1235cm
-1～1450cm
-1Has absorption band in the scope, at the 1651.42cm of infrared spectra
-1Stronger absorption peak appears in the place.This Sipunculid collagen protein of electrophoresis, as can be seen from Figure 3 near 116KD～200KD, exist three clearly band be respectively α, β, γ component, the molecular weight of also representing this collagen protein is at 116KD～200KD, has complete triple-helix structure, and the β component is more, measures to such an extent that the β component is the dimer of two α peptide chains.
The heat shrink temperature that records this Sipunculid collagen protein with the routine biochemistry method is 54.50 ℃, and iso-electric point mean value is 4.85, and sugared content is 0.75mg/100mg, and aminoacids content is 91.45mg/100mg, and hydroxyproline content is 10.35% (weight) in the amino acid.With viscosity measuring instrument and to calculate the tackiness of this Sipunculid collagen protein gel under 20 ℃ of temperature be-6.15.
Glycine accounts for 31.0%～35.0% (weight) in the amino acid of Sipunculid collagen protein; L-Ala accounts for 11.0%～15.0%; 5%, the four kind of sum that respectively accounts for of L-glutamic acid, aspartic acid, arginine and Serine accounts for 27%; All the other are the lower Histidine of content, tyrosine, methionine(Met), Methionin etc.
The test example
With Sipunculid collagen protein of the present invention the callus ability of laboratory animal is tested
1 modelling, laboratory animal is formed the surface of a wound with operation, make the hemorrhage and surrounding tissue oedema of the surface of a wound, treat surface of a wound blood coagulation, be divided into blank group and medication group at random, blank group is to allow its surface of a wound nature callus, the medication group be with the even scumbling of Sipunculid collagen protein of the present invention on the surface of the surface of a wound, once a day until decrustation, observe two groups of surface of a wound scars after surface of a wound callus situation and the callus separately;
2 surface of a wound callus, postoperative 2d, it almost all is that blood clot covers that blank is formed face, the particulate state granulation seldom, surface of a wound surrounding tissue oedema is still comparatively obvious; Medication is formed face surrounding tissue oedema and is alleviated to some extent, and the granulation tissue growth is obvious, and the part has grown thin layer or some columnar epithelium, and the edge of wound contraction of skin is obvious; Postoperative 4d, blank group has 1/3 wound moistening, still has exudate, and contraction of wounds is not obvious, and rarely seen thin layer granulation is not seen significantly new epithelize, and the whole wounds of medication group do not have infection, and epidermis is down and all have a large amount of granulation tissue hyperplasias to repair wounds in the flesh layer; Postoperative 6d, blank is formed face only 80% by the granulation tissue filling, and epithelial growth is less, and hair grows less, and medication is formed face all fully by the granulation tissue filling, and major part has epithelial growth, as seen has more hair to grow; Postoperative 8d, the crust that face is formed in medication begins nature and comes off, and blank group wanted 3-5 day, just begins to come off.
3 scars, treat that two groups of wound crusts all come off after, medication forms that the scar that face forms is not obvious, skin surface is more smooth, it is obvious that blank is formed the scar that face forms, scar is rough and uneven in surface, most of recessed skin surface.
Claims (1)
1. the preparation method of Sipunculid collagen protein is characterized in that comprising the steps:
The siphon-worm body wall that a will remove noncollagen protein evenly grinds, and joins in the acetate buffer solution that final concentration is 0.5mol and is mixed with homogenizing fluid, the volume ratio of acetate buffer solution and siphon-worm body wall 100: 1;
B adds stomach en-in homogenizing fluid, the weight ratio of stomach en-and siphon-worm body wall is 1: 50～350, and enzymolysis is 20～40 hours under 35～40 ℃ of temperature condition;
The enzyme that goes out after the c enzymolysis is finished, the homogenizing fluid of the enzyme that will go out are under 4 ℃ of temperature condition, with the centrifugal 10min of 8000rpm, the supernatant liquor of winning, throw out be the method enzymolysis once more of b set by step, and be centrifugal equally then, get second supernatant liquor, merging first supernatant liquor and second supernatant liquor is total supernatant liquor;
D adds NaCl solution at total supernatant liquor, makes its final concentration reach 2mol/L, leaves standstill to collagen protein to precipitate fully;
E under 4 ℃ of temperature condition, with the centrifugal 20min of 8000rpm, obtains the collagen protein precipitation again;
F is dissolved in the collagen protein precipitation in the dialyzate of 0.1～0.5mol/L repeatedly, places the dialysis of dialysis tubing flowing water, to AgNO
3Solution can not detect extracellular fluid dialysis and has Cl
-Till, obtain dialyzed solution;
H is with the dialyzed solution lyophilize, obtain the solubility in acid Sipunculid collagen protein, this Sipunculid collagen protein is white or faint yellow powder, its heat shrink temperature is 53.00～55.00 ℃, iso-electric point mean value is 4.60～4.90, the molecular weight of this Sipunculid collagen protein is 116KD～200KD, sugar content is 0.50～0.90mg/100mg, aminoacids content is 90～95mg/100mg, the oxyproline weight content is 9.5%～11.5% in the described amino acid, this Sipunculid collagen protein is the triple-helix structure that three kinds of peptide chains are formed, at the 1235cm of infrared spectra
-1～1450cm
-1Scope in exist to absorb, at the 1651.42cm of infrared spectra
-1Stronger absorption appears in the place.
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| WO2012015055A1 (en) * | 2010-07-30 | 2012-02-02 | 株式会社ニッピ | Collagen powder and/or collagen-derived powder, and production method for same |
| CN102336806A (en) * | 2011-09-23 | 2012-02-01 | 华东理工大学 | Angiotensin converting enzyme (ACE) inhibitor |
| CN104146233B (en) * | 2014-04-30 | 2015-09-09 | 浙江省海洋水产养殖研究所 | Natural flavouring utilizing siphon-worm to prepare and preparation method thereof |
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| CN109884153B (en) * | 2019-03-11 | 2021-07-20 | 淮海工学院 | Novel method for judging integrity of triple-helix structure of type I collagen |
| CN110201000A (en) * | 2019-07-11 | 2019-09-06 | 广东海洋大学 | A kind of preparation method and applications with the Sipunculus nudus enzymolysis protein Gly-His-Lys for promoting Wound Healing |
| CN110538312A (en) * | 2019-08-30 | 2019-12-06 | 广东海洋大学 | skin wound repair ointment and preparation method thereof |
| CN110538198A (en) * | 2019-08-30 | 2019-12-06 | 广东海洋大学 | application of Sipunculus nudus water extract in wound repair |
| CN110638999A (en) * | 2019-08-30 | 2020-01-03 | 广东海洋大学 | Application of Sipunculus nudus collagen peptide in wound repair |
| CN110642940A (en) * | 2019-10-21 | 2020-01-03 | 华侨大学 | Preparation method of sipunculus nudus non-denatured collagen |
| CN112679580B (en) * | 2021-01-14 | 2022-12-16 | 南方海洋科学与工程广东省实验室(湛江) | Sipunculus nudus oligopeptide capable of promoting bone development and preparation method and application thereof |
| CN117143693A (en) * | 2023-09-11 | 2023-12-01 | 鲟力泰悦(武汉)生物科技有限公司 | Liver-protecting sturgeon protein peptide wine and preparation process thereof |
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