CN101805776A - Method for preparing antler collagen - Google Patents
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- CN101805776A CN101805776A CN201010143575A CN201010143575A CN101805776A CN 101805776 A CN101805776 A CN 101805776A CN 201010143575 A CN201010143575 A CN 201010143575A CN 201010143575 A CN201010143575 A CN 201010143575A CN 101805776 A CN101805776 A CN 101805776A
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Abstract
The invention belongs to the technical field of collagen extraction and purification and particularly relates to a method comprising the following steps: firstly, extracting collagen from antlers on the basis of the water extraction method and further subjecting the collagen to enzymolysis by trypsin to obtain the collagen with good water-solubility. The method comprises the following steps: brushing and cleaning the surface of the antler; soaking the antler in running water until the water is clear; taking out the antler and draining water from the antler; grinding the antler into fine powder; adding distilled water by the solid-liquid ratio of 1:5 to 1:15 (g/ml); then, stirring and heating on a heating plate until the antler solution is boiled; starting to time for 2 to 4 hours after boiling; centrifuging; repeating the operations for 2 to 4 times; merging the supernatant obtained during the repeated operations; adding trypsin (wherein the mass ratio between the trypsin and the zymolyte is 1:8,000 to 1:15,000) for conducting the enzymolysis process for 15min to 90min; heating to inactivate the trypsin; centrifuging; concentrating the supernatant; filtering with a 0.2mum-0.45mum filter membrane; and freezing-drying the filtrate in a vacuum to obtain the collagen powder. The method of the invention has the advantages of simple and easy-to-operate process and stable experimental result. Therefore, the method is suitable for large-scale industrialized production.
Description
Technical field
The invention belongs to collagen protein and extract the purification technique field, be specifically related to a kind of water extraction that adopted before this and extract antler collagen, use trypsin digestion again, thereby obtain the method for water-soluble good collagen protein.
Background technology
Deer horn dish another name " Cornu Cervi ", " deer horn disk stripping ", " ossificational antler ", after being male spotted deer (CervusnipponTemminok) or red deer (Cervuse laphusk) jagsaw young pilose antler, the ossified disbud that comes off in next year, the plate-like material that to be the boundary between pilose antler is ossified and unossified very hard (profound scholar is virtuous. Chinese animal drugs will [M]. and Changchun: Jilin science tech publishing house, 1996:69326941).Among the peoplely be usually used in treating mazoitis, dislike sore, carbuncle is swollen etc.
Collagen has complete triple-helix structure, and molecular weight is approximately 300,000, is insoluble to cold water and hot water, can not be utilized by proteolytic enzyme; Gelatin is the denatured products of collagen under acid, alkali, enzyme or high temperature action, and it is not the protein of homogeneous, but a kind of mixture of hot solubility, temperature drops to below 30 ℃ and forms gel, and heating is liquefaction then; Collagen protein is the hydrolysate of collagen or gelatin, has less molecular mass, dissolves in cold water, and easier degraded, is easily absorbed by human consumption.(Jiang Tingda, collagen and collagen protein [M], Beijing, Chemical Industry Press, 2006,2).
The growth of collagen protein and body, aging and disease have extremely close getting in touch.Collagen protein not only has beauty treatment, preventing osteoporosis, improves articulation health, improves blood circulation, is good for the stomach, improves effects such as body immunity, and have excellent biological compatibility, trophicity, reparation, moisture retention, compatibleness and affinity, so be widely used in functional products such as biomedical material, makeup, food and healthcare products.Proline content seldom in the overwhelming majority's protein, and the content of proline(Pro) and oxyproline is the highest in the range protein in the collagen protein, this two seed amino acid is a cyclic amino acid, can pin whole tropocollagen molecule, make it to be difficult to draw back, so collagen has micro-elasticity and very strong tensile strength.
Collagen protein is one of main functional component of deer horn dish.Deerhorn Glue can warm invigorating the liver and kidney, beneficial intensive culture blood, is used for that impotence involuntary emission, the acid of waist knee are cold, consumptive disease is won thin, metrostaxis, the hematuria of having blood in stool, cloudy subcutaneous ulcer swell and ache; Refuse of deerhorn Glue has the effect of warming the kidney to activate YANG, astringing to arrest bleeding, be used for deficiency of spleen-YANG and kidneyYANG, the few vomiting and diarrhoea of food, leukorrhea, the enuresis, frequent micturition, metrostaxis, ulcer productive cough (Zhang Baoxiang, Jin Chunai, Zhao Yanping. the chemical ingredients of deer horn dish and development and use [J]. extraordinary economic animals and plants, 2005, (12): 7.).Wu waits the people quietly by the experimental observation of big white mouse gastric mucosa damage is found; Deerhorn Glue solution can also reduce the gastric mucosa damage index; strengthen gastric mucosal barrier; has significant provide protection (Wu Jing; Yu Shilong, Wang Feng, etc. Deerhorn Glue is to the experimental study [J] of rat stomach mucous membrane provide protection. practical medical journal; 2007,23 (17): 2636).Experiment showed, that Deerhorn Glue can also obviously increase small white mouse content of hemoglobin and thymic weight, have the effect of significant antifatigue effect and increase immunizing power.Therefore Deerhorn Glue be can consider to develop and the qi-restoratives labor that is suitable for the elderly, the protective foods (Bao Haiying that improves body resistance against diseases are developed into, open clever, Deng Minglu. the research situation of homemade deer horn and DEVELOPMENT PROSPECT [J]. Jilin Agriculture University's journal, 1995,17 (4): 96).
Adopt modern zymolysis technique, production has active small molecules antler collagen, it is the high-tech project of a low risk, high production, have very high economic benefit and social benefit, can improve that the deer horn dish technological element of a product is low, the single situation of product forms, increase the added value of product and the market competitiveness, for deer horn dish Products Development has been opened up new road.
Summary of the invention
The preparation method who the purpose of this invention is to provide a kind of antler collagen, it is to extract deer horn dish collagen with water extraction earlier, press the collagen that optimised process extracts with trypsin digestion again, determine enzymatic hydrolysis condition with the efficient gel chromatography, concentrate, centrifugal, the supernatant liquor freeze-drying is obtained antler collagen.
The preparation method of antler collagen of the present invention comprises the steps:
1) get the deer horn dish, the outwash surface puts that to be dipped to water in the flowing water clear, and taking-up drains, and wears into fine powder, crosses 200 mesh sieves, and is standby;
2) get the above-mentioned deer horn dish of handling well, 1: 5～1: 15 (g/ml) adding distil water of pressing solid-liquid ratio, place on the hot-plate heated and boiled while stirring then, heating 2～4 hours is continued in the boiling back, then well-done deer horn dish is put to room temperature, centrifugal (4500～5000rpm/min, 25～45min), the gained precipitation adopts aforesaid method to extract altogether 2～4 times, discard precipitation, merging multiple extraction supernatant liquor is settled in the 200ml volumetric flask, be gelatin solution, get 1ml and measure protein content with the Folin-phenol reagent process, collagen content is 60.30～66.50% (mass percents).
3) get step 2) gelatin solution 200ul, 0.2um～0.45um membrane filtration gets 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the gelatin solution retention time is 10～12min;
4) to step 2) gelatin solution in add the tryptic ratio of 1g in 8000g～15000g deer horn dish, add trypsinase, place 37 ℃ of thermostat water baths then, be warming up to 80～100 ℃ behind enzymolysis 15～90min immediately, insulation 10～15min makes the trypsinase inactivation; Taking-up is placed to room temperature, and centrifugal (4500～5000rpm, 25～45min) discards precipitation, and supernatant liquor is collagen solution.
5) get collagen solution 200ul in the step 4),, get 20ul filtrate sample introduction with 0.2um～0.45um membrane filtration, record efficient gel color atlas, the collagen protein retention time is about 19～22min after the hydrolysis;
6) heating of the collagen solution in the step 4) is concentrated, be concentrated into concentration and be about 1～2g/ml (by deer horn dish powder), be placed to room temperature,, promptly get collagen protein powder the filtrate freeze-drying; The collagen protein powder yield is 20.34～30.65% (with the over dry restatements).
Adopt the HPLC-C18 post to measure amino acid whose quality percentage composition in the antler collagen powder, the results are shown in Table 1.
The advantage that the collagen protein of the present invention's preparation has
1, experimental technique is simple to operation, and experimental result is stable, produces greatly applicable to industry.
What 2, the present invention adopted is the distilled water lixiviate, prevents that amino acid structure from destroying.
3, the present invention adopts trypsin digestion, the contrast stomach en-, and enzymolysis time is short, the enzymatic hydrolysis condition gentleness, enzymolysis degree height, gained collagen protein state is relatively good.
4, the present invention adopts the method for enzymolysis after the hydrolysis, can guarantee that the peptide chain structure of collagen protein keeps comparatively complete.
5, the tropocollagen molecule amount is approximately 300000Da, is insoluble to cold water and hot water, can not be utilized by proteolytic enzyme, and the gelatin relative molecular mass is higher, only be dissolved in hot water, be insoluble to cold water, and the collagen molecules amount is mainly about 10000Da, dissolve in cold water, and easily degraded, utilization promptly easily is absorbed by the body.
6, the inventive method is easy, and the collagen protein that obtains not only can be used for food, and makeup etc. aspect its pharmacological action, also are widely used.
Description of drawings
Fig. 1: the high performance liquid phase gel chromatography figure of gelatin solution and collagen solution.
Wherein, curve A is gelatin solution high performance liquid phase gel chromatography figure; Curve B is collagen solution high performance liquid phase gel chromatography figure behind 1: 8000 enzymolysis 1.5h; Curve C is collagen solution high performance liquid phase gel chromatography figure behind 1: 10000 enzymolysis 1.5h; Curve D is high performance liquid phase gel chromatography figure behind 1: 15000 enzymolysis 1.5h.Adopt U.S. Agilent1100 high performance liquid phase, TSKgelG2000SW (XL) gel column is measured.Chromatographic condition: moving phase is 0.1M Na
2HPO
4, 0.1M NaH
2PO
4, 0.1M Na
2SO
4, pH6.6, flow velocity are 0.5ml/min.Standard molecular weight: 15.48min, molecular weight 75000Da; 17.04min, molecular weight 43000Da; 18.93min, molecular weight 29000Da; 19.85min, molecular weight 13700Da; 21.23min, molecular weight 6500Da.
This figure shows: deer pallet collagen retention time is about 12min, and molecular weight ratio is bigger, through the most of collagen retention time behind the trypsin digestion behind 19min, molecular weight obviously diminishes, when enzymolysis time was 1.5h, along with the increase of enzyme amount, hydrolysis result was become better and better.
Adopt U.S. Agilent1100 high efficiency liquid phase, (4.6 * 150mm) measure Wondasil C18 post. Chromatographic condition: mobile phase A: 0.1mol/L sodium acetate buffer solution (pH6.4)-acetonitrile (97: 3); Mobile phase B: acetonitrile-water (4: 1). Flow velocity: 1.0ml/min; Column temperature: 35 ℃; Detect wavelength: 254nm; Sample size: 20 μ l.
Table 1: the quality percentage composition of 18 seed amino acids in the antler collagen
| Amino acid | Content % | Amino acid | Content % |
| Glycine | 31.512 | Aspartic acid | 1.957 |
| Alanine | 14.175 | Serine | 2.673 |
| Proline | 15.657 | Valine | 2.111 |
| Hydroxyproline | 6.710 | Threonine | 1.962 |
| Arginine | 7.249 | Isoleucine | 0.806 |
| Lysine | 6.666 | Tyrosine | 0.411 |
| Glutamic acid | 2.600 | Methionine | 0.299 |
| Leucine | 3.046 | Histidine | 0.245 |
| Phenylalanine | 1.928 | Cystine | - |
Embodiment
Embodiment 1:
1) get the deer horn dish, the outwash surface puts that to be dipped to water in the flowing water clear, and taking-up drains, and wears into fine powder, crosses 200 mesh sieves, and is standby.
2) get the above-mentioned deer horn dish 10g that handles well, 1: 15 (g/ml) adding distil water of pressing solid-liquid ratio places on the hot-plate heated and boiled while stirring, the boiling back opening entry time then, after 4 hours filtrate is placed to room temperature, centrifugal (4500rpm/min, 30min), precipitation is extracted 3 times altogether with above-mentioned method, discards precipitation, merging 3 supernatant liquors is settled in the 200ml volumetric flask, be gelatin solution, get 1ml and measure protein content, protein content 62.58% (mass percent) with Folin-phenol method.
3) get 2) middle gelatin solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the gelatin solution retention time is about 12min, the results are shown in A in the accompanying drawing.
4) to 2) added trypsinase 0.00125g than 1: 8000 by enzyme-to-substrate in the supernatant liquor, place 37 ℃ of thermostat water bath enzymolysis 1.5h, be warming up to immediately behind the 1.5h more than 80 ℃, keep 10min, make the trypsinase inactivation.Taking-up is placed to room temperature, and centrifugal (4500rpm/min, 30min) discards precipitation, and supernatant liquor is collagen solution.
5) get 4) middle collagen solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the collagen protein retention time is about 19min after the hydrolysis, the results are shown in D in the accompanying drawing.
6) with 4) collagen solution is concentrated into 10ml, is placed to room temperature, and freeze-drying promptly gets collagen protein powder, weighs, calculated yield, yield is 22.26% (with the over dry restatement).
Embodiment 2:
1) get the deer horn dish, the outwash surface puts that to be dipped to water in the flowing water clear, and taking-up drains, and wears into fine powder, crosses 200 mesh sieves, and is standby.
2) get the above-mentioned deer horn dish 10g that handles well, 1: 10 (g/ml) adding distil water of pressing solid-liquid ratio places on the hot-plate heated and boiled while stirring, the boiling back opening entry time then, after 4 hours filtrate is placed to room temperature, centrifugal (4500rpm/min, 30min), precipitation is extracted 2 times altogether with above-mentioned method, discards precipitation, merging twice supernatant liquor is settled in the 200ml volumetric flask, be gelatin solution, get 1ml and measure protein content with Folin-phenol method, protein content is 63.31% (mass percent).
3) get 2) middle gelatin solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the gelatin solution retention time is about 12min, the results are shown in A in the accompanying drawing.
4) to 2) added trypsinase 0.0010g than 1: 10000 by enzyme-to-substrate in the supernatant liquor, place 37 ℃ of thermostat water bath enzymolysis 1.5h, be warming up to immediately behind the 1.5h more than 80 ℃, keep 10min, make the trypsinase inactivation.Taking-up is placed to room temperature, and centrifugal (4500rpm/min, 30min) discards precipitation, and supernatant liquor is collagen solution.
5) get 4) middle collagen solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the collagen protein retention time is about 21min after the hydrolysis, the results are shown in C in the accompanying drawing.
6) with 4) collagen solution is concentrated into 10ml, is placed to room temperature, and freeze-drying promptly gets collagen protein powder, weighs, calculated yield, yield is 22.17% (with the over dry restatement).
Embodiment 3:
1) get the deer horn dish, the outwash surface puts that to be dipped to water in the flowing water clear, and taking-up drains, and wears into fine powder, crosses 200 mesh sieves, and is standby.
2) get the above-mentioned deer horn dish 10g that handles well, 1: 5 (g/ml) adding distil water of pressing solid-liquid ratio stirs the back as for heated and boiled on the hot-plate, the boiling back opening entry time, after 3 hours filtrate is placed to room temperature, centrifugal (4500rpm/min, 30min) takes out supernatant, and precipitation is extracted 3 times altogether with above-mentioned method, 3 supernatant liquors merging are settled in the 200ml volumetric flask, be gelatin solution, get 1ml and measure protein content with Folin-phenol method, protein content is 62.67% (mass percent).
3) get 2) middle gelatin solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the gelatin solution retention time is about 12min, the results are shown in A in the accompanying drawing.
4) to 2) added trypsinase 0.00067g than 1: 15000 by enzyme-to-substrate in the supernatant liquor, place 37 ℃ of thermostat water bath enzymolysis 1.5h, be warming up to immediately behind the 1.5h more than 80 ℃, keep 10min, make the trypsinase inactivation.Taking-up is placed to room temperature, and centrifugal (4500rpm/min, 30min) discards precipitation, and supernatant liquor is collagen solution.
5) get 4) middle collagen solution 200ul, the 0.45um membrane filtration is got 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the collagen protein retention time is about 19min after the hydrolysis, the results are shown in B in the accompanying drawing.
6) with 4) collagen solution is concentrated into 10ml, is placed to room temperature, and freeze-drying promptly gets collagen protein powder, weighs, calculated yield, yield is 22.33% (with the over dry restatement).
Claims (5)
1. the preparation method of an antler collagen comprises the steps:
1) get the deer horn dish, the outwash surface puts that to be dipped to water in the flowing water clear, and taking-up drains, and wears into fine powder, crosses 200 mesh sieves, and is standby;
2) get the above-mentioned deer horn dish of handling well and add distilled water, place on the hot-plate heated and boiled while stirring then, heating 2～4 hours is continued in the boiling back, then well-done deer horn dish is put to the room temperature centrifugal, the gained precipitation adopts aforesaid method to extract altogether 2～4 times, discard precipitation, merge multiple extraction supernatant liquor and be settled in the 200ml volumetric flask, be gelatin solution;
3) to step 2) gelatin solution add trypsinase, place 37 ℃ of thermostat water baths then, be warming up to 80～100 ℃ behind enzymolysis 15～90min immediately, insulation 10～15min makes the trypsinase inactivation; Taking-up is placed to room temperature, discards precipitation after centrifugal, and supernatant liquor is collagen solution;
4) heating of the collagen solution in the step 3) is concentrated, be concentrated into concentration and be about 1～2g/ml, be placed to room temperature,, promptly get collagen protein powder the filtrate freeze-drying.
2. the preparation method of a kind of antler collagen as claimed in claim 1 is characterized in that: step 2) in be ratio adding distil water in the deer horn dish of handling well in solid-liquid ratio 1g: 5ml～1g: 15ml.
3. the preparation method of a kind of antler collagen as claimed in claim 1 is characterized in that: be to add the tryptic ratio of 1g in 8000g～15000g deer horn dish to add trypsinase in gelatin solution in the step 3).
4. the preparation method of a kind of antler collagen as claimed in claim 1, it is characterized in that: in step 2) finish after, get step 2) gelatin solution 200ul, 0.2um～0.45um membrane filtration, get 20ul filtrate sample introduction, record high performance liquid phase gel filtration chromatography figure, the gelatin solution retention time is 10～12min.
5. the preparation method of a kind of antler collagen as claimed in claim 1, it is characterized in that: after step 3) finishes, get the collagen solution 200ul in the step 3), with 0.2um～0.45um membrane filtration, get 20ul filtrate sample introduction, record efficient gel color atlas, the collagen protein retention time is 19～22min after the hydrolysis.
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Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102702307A (en) * | 2012-06-01 | 2012-10-03 | 吉林农业大学 | Method for producing antler base concentrated protein |
| CN102698852A (en) * | 2012-06-01 | 2012-10-03 | 吉林农业大学 | Method for preparing sika antler base superfine powder with smashing method |
| CN106399441A (en) * | 2016-11-17 | 2017-02-15 | 吉林农业大学 | Preparation method of sika deer coronet collagen hydrolysate peptide |
| CN106749498A (en) * | 2016-11-17 | 2017-05-31 | 吉林农业大学 | A kind of CORNU CERVI disk antibacterial peptide/albumen and its application with antibacterial effect |
| CN106990192A (en) * | 2017-04-17 | 2017-07-28 | 大连工业大学 | A kind of method for determining collagen molecules quality |
| CN107519203A (en) * | 2017-09-11 | 2017-12-29 | 中国农业科学院特产研究所 | A kind of preparation method of Cornu Cervi cowl zymolyte, Cornu Cervi cowl zymolyte piece |
| CN109170120A (en) * | 2018-06-08 | 2019-01-11 | 赵雅洲 | The method and Cornu Cervi bulking machine of extruding enzymatic isolation method extraction Cornu Cervi collagen |
| CN116898879A (en) * | 2023-08-25 | 2023-10-20 | 吉林农业大学 | Cornu Cervi Degelatinatum, its preparation method and application in preparing medicine for treating nonspecific inflammation |
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2010
- 2010-04-12 CN CN201010143575A patent/CN101805776A/en active Pending
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Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102702307A (en) * | 2012-06-01 | 2012-10-03 | 吉林农业大学 | Method for producing antler base concentrated protein |
| CN102698852A (en) * | 2012-06-01 | 2012-10-03 | 吉林农业大学 | Method for preparing sika antler base superfine powder with smashing method |
| CN106399441A (en) * | 2016-11-17 | 2017-02-15 | 吉林农业大学 | Preparation method of sika deer coronet collagen hydrolysate peptide |
| CN106749498A (en) * | 2016-11-17 | 2017-05-31 | 吉林农业大学 | A kind of CORNU CERVI disk antibacterial peptide/albumen and its application with antibacterial effect |
| CN106399441B (en) * | 2016-11-17 | 2020-08-21 | 吉林农业大学 | Preparation method of sika antler collagen hydrolysis peptide |
| CN106990192A (en) * | 2017-04-17 | 2017-07-28 | 大连工业大学 | A kind of method for determining collagen molecules quality |
| CN106990192B (en) * | 2017-04-17 | 2019-05-21 | 大连工业大学 | A method of measurement collagen molecules quality |
| CN107519203A (en) * | 2017-09-11 | 2017-12-29 | 中国农业科学院特产研究所 | A kind of preparation method of Cornu Cervi cowl zymolyte, Cornu Cervi cowl zymolyte piece |
| CN109170120A (en) * | 2018-06-08 | 2019-01-11 | 赵雅洲 | The method and Cornu Cervi bulking machine of extruding enzymatic isolation method extraction Cornu Cervi collagen |
| CN116898879A (en) * | 2023-08-25 | 2023-10-20 | 吉林农业大学 | Cornu Cervi Degelatinatum, its preparation method and application in preparing medicine for treating nonspecific inflammation |
| CN116898879B (en) * | 2023-08-25 | 2024-02-23 | 吉林农业大学 | Cornu Cervi Degelatinatum, its preparation method and application in preparing medicine for treating nonspecific inflammation |
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Application publication date: 20100818 |