CN110387397B - Preparation method of sheep skin collagen oligopeptide - Google Patents
Preparation method of sheep skin collagen oligopeptide Download PDFInfo
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- CN110387397B CN110387397B CN201910805071.1A CN201910805071A CN110387397B CN 110387397 B CN110387397 B CN 110387397B CN 201910805071 A CN201910805071 A CN 201910805071A CN 110387397 B CN110387397 B CN 110387397B
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- 241001494479 Pecora Species 0.000 title claims abstract description 55
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 54
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 54
- 238000002360 preparation method Methods 0.000 title claims abstract description 15
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 28
- 238000001914 filtration Methods 0.000 claims abstract description 20
- 238000000034 method Methods 0.000 claims abstract description 15
- 239000003729 cation exchange resin Substances 0.000 claims abstract description 14
- 238000001179 sorption measurement Methods 0.000 claims abstract description 13
- 238000002791 soaking Methods 0.000 claims abstract description 9
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 claims abstract description 8
- 239000003957 anion exchange resin Substances 0.000 claims abstract description 8
- 238000001035 drying Methods 0.000 claims abstract description 6
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 50
- 235000013372 meat Nutrition 0.000 claims description 12
- 108091005658 Basic proteases Proteins 0.000 claims description 10
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- 102000004190 Enzymes Human genes 0.000 claims description 8
- 108090000790 Enzymes Proteins 0.000 claims description 8
- 108010019160 Pancreatin Proteins 0.000 claims description 8
- 229940088598 enzyme Drugs 0.000 claims description 8
- 238000010438 heat treatment Methods 0.000 claims description 8
- 229940055695 pancreatin Drugs 0.000 claims description 8
- 239000012528 membrane Substances 0.000 claims description 7
- 239000000843 powder Substances 0.000 claims description 7
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- 230000000694 effects Effects 0.000 claims description 3
- 238000001816 cooling Methods 0.000 claims description 2
- 230000002779 inactivation Effects 0.000 claims description 2
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- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
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- 241000124008 Mammalia Species 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
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- 238000011033 desalting Methods 0.000 description 1
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- 229940079593 drug Drugs 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
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- 238000009776 industrial production Methods 0.000 description 1
- 229910017053 inorganic salt Inorganic materials 0.000 description 1
- 238000002356 laser light scattering Methods 0.000 description 1
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- 235000016709 nutrition Nutrition 0.000 description 1
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- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 239000011087 paperboard Substances 0.000 description 1
- BWHMMNNQKKPAPP-UHFFFAOYSA-L potassium carbonate Substances [K+].[K+].[O-]C([O-])=O BWHMMNNQKKPAPP-UHFFFAOYSA-L 0.000 description 1
- 229910000027 potassium carbonate Inorganic materials 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
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- 238000000108 ultra-filtration Methods 0.000 description 1
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- 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]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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Abstract
The invention provides a preparation method of sheep skin collagen oligopeptide, which takes fresh sheep skin as a raw material, and obtains the sheep skin collagen oligopeptide with the molecular weight of less than 1000Da through the steps of alkaline electrolyzed water soaking, enzymolysis treatment, anion and cation exchange resin adsorption, filtration, concentration, drying and the like. The preparation method does not use acid or alkali, and adjusts the pH of oligopeptide by adsorption of anion and cation exchange resin, so that the oligopeptide is more beneficial to skin absorption. In addition, the method has the advantages of low cost, environmental protection, small oligopeptide molecular weight and industrial application prospect.
Description
Technical Field
The invention relates to a preparation method of oligopeptide. More particularly, relates to a preparation method of sheep skin collagen oligopeptide.
Background
Collagen is a biological macromolecule, is a main component in animal connective tissues, is also a functional protein with the largest content and the widest distribution in mammals, and accounts for one third of the total amount of proteins in mammals. The collagen is used as a natural degradable polymer and has the advantages of high biological activity, good biocompatibility, proper degradation speed and the like.
Collagen peptides are hydrolysates of collagen. Generally, collagen peptides consisting of 2 to 10 amino acids are called oligopeptides, which are absorbed and utilized by the human body without being decomposed. With the increasing age of people and the influence of factors such as nutrition, sunlight, environment and the like, the capability of synthesizing collagen peptide of a human body is gradually reduced, and the content of the collagen peptide in the skin is gradually reduced. It follows that collagen peptides play an important role in the health and beauty of human skin.
Patent CN101297673B discloses a method for preparing fish collagen oligopeptide, which selects deashed and degreased dried fish scales as raw materials to produce fish collagen oligopeptide powder with average molecular weight of 700 Dalton. Patent CN103205480B discloses a method for producing collagen oligopeptide from fish skin or fish bone, which is characterized in that small molecular components are intercepted through two times of enzymolysis and ultrafiltration, so that the proportion of oligopeptide with the molecular weight of less than 580Da in the product is increased from 40-50% to 65-75%. The oligopeptide products described in both patents do not have a molecular weight of 100% below 1000Da, but have an average molecular weight below 1000Da or a majority of the components have a molecular weight below 1000Da, and are therefore not pure oligopeptide products. Patent CN104479995B discloses a method for extracting collagen from sheepskin, which uses acid and alkali reagents in the process of sheepskin treatment, and the production of a large amount of acid and alkali waste water in industrial production is liable to cause environmental pollution. Although the average molecular weights of the obtained collagens were 1012Da and 937Da, respectively, the viscosities were as high as 2.8 mPaS and 3.1 mPaS. This shows that the collagen of sheepskin in patent CN104479995B contains a certain proportion of macromolecular components in addition to small molecular polypeptides.
Therefore, there is a need to provide a process for the preparation of oligopeptides which can obtain molecular weights of less than 1000Da and which does not generate waste acids and waste alkalis.
Disclosure of Invention
The invention aims to provide a preparation method of sheep skin collagen oligopeptide, which uses environment-friendly alkaline electrolyzed water to obtain oligopeptide with the molecular weight of less than 1000 Da.
The invention also aims to provide the sheep skin collagen oligopeptide prepared by the method.
In order to achieve the purpose, the invention adopts the following technical scheme:
a preparation method of sheep skin collagen oligopeptide comprises the following steps:
(1) soaking sheepskin with fat, meat and wool removed in 50-60 deg.C water for 20-40min, and pulverizing into pieces with diameter of 1-1.5 cm;
(2) mixing the sheepskin fragments with alkaline electrolyzed water with the pH of 10-12.5, keeping the pH constant, stirring for 30min, heating to 75-80 ℃, and keeping the temperature constant for 3-5 h;
(3) cooling to 45-55 deg.C, adding alkaline protease or/and pancreatin, and performing enzymolysis for 3-5 hr; then heating to 90-95 ℃ for inactivation for 20-40 min;
(4) settling, centrifuging and filtering to obtain a sheepskin collagen peptide solution;
(5) sequentially carrying out exchange adsorption on the sheep skin collagen peptide solution through cation exchange resin and anion exchange resin, wherein the pH value of the sheep skin collagen peptide solution after exchange adsorption is 5.5-6.0;
(6) filtering, concentrating and drying the sheep skin collagen peptide solution with the pH value of 5.5-6.0 to obtain the sheep skin collagen oligopeptide powder.
In the present invention, the alkaline electrolyzed water used includes, but is not limited to, electrolyzed K2CO3Solution, which contains mainly cations, hydroxide ions and oxygen ions. The alkaline electrolyzed water can change the collagen of the sheep skin from a compact and ordered structure to a loose and disordered structure, and is beneficial to the enzymolysis of the collagen of the sheep skin into small molecular peptides under the action of heating and protease. Through a preparation mode of combining alkaline electrolyzed water and protease, the content of oligopeptide in the sheep skin collagen peptide solution obtained in the invention is up to 98% or more, and the utilization rate of sheep skin collagen is greatly improved. Meanwhile, the alkaline electrolyzed water also has reducibility and oxidation resistance, can effectively kill and inhibit microorganisms existing in the sheep skin protein, ensures the stability of the sheep skin protein amount in the preparation process, and improves the oxidation resistance activation activity of the sheep skin peptide protein.
In addition, the invention adopts anion-cation exchange resin to carry out exchange adsorption treatment on the sheep skin collagen peptide solution so as to remove color, peculiar smell and salts in the sheep skin collagen peptide solution, and controls the temperature and the dosage of the resin to ensure that the pH value of the sheep skin collagen peptide solution after the exchange adsorption treatment is 5.5-6.0, thereby being suitable for human skin absorption and avoiding using acid and alkali liquor to adjust the pH value.
Preferably, the specific process of step (1) is: shearing the wool on the sheepskin to about 1cm by using a sheepskin shearing machine; removing fat and meat on the sheepskin by a meat remover; soaking in 50-60 deg.C hot water for 20-40min, and removing residual short hair from sheepskin with hair removing machine; crushing sheepskin into pieces with diameter of 1-1.5cm by a crusher.
Preferably, for example, the pH of the alkaline electrolyzed water in step (2) includes, but is not limited to, 10.25 to 12.25, 10.5 to 12.00, 10.75 to 11.75, 11.00 to 11.50.
Preferably, the weight ratio of the sheepskin fragments to the alkaline electrolyzed water in the step (2) is 1: 2-4. The amount of alkaline electrolyzed water is such that the sheepskin fragments are evenly distributed therein and that all parts of the sheepskin fragments are completely immersed therein.
Preferably, in the step (3), when the alkaline protease and the pancreatin are added simultaneously, the weight ratio of the alkaline protease to the pancreatin is 1: 1.
Preferably, the amount of enzyme added in step (3) is 0.8% -2.0% of the weight of the sheepskin fragments. Further, for example, the enzyme is added in an amount that is a percentage of the weight of the sheepskin fragments including, but not limited to, 1.0%, 1.2%, 1.4%, 1.6%, and 1.8%. The enzyme added is sufficient to allow the enzymatic hydrolysis of the sheep skin proteins into polypeptides, which are further broken down into oligopeptides.
Preferably, the filtration in step (4) is performed by fine filtration with cardboard at an operating pressure of 0.1-0.2 MPa. And (3) obtaining a clear sheepskin collagen peptide solution after sedimentation and centrifugation, and further filtering the clear sheepskin collagen peptide solution by a paperboard fine filter to obtain a clear light yellow sheepskin collagen peptide solution.
Preferably, the exchange adsorption in step (5) is carried out at 42-45 ℃.
Preferably, the volume ratio of the sheep skin collagen peptide solution to the cation exchange resin and the anion exchange resin in the step (5) is 100:4:6
The appropriate exchange adsorption temperature and the dosage of the cation exchange resin and the anion exchange resin can adjust the pH of the obtained sheepskin collagen peptide solution of 5.5-6.0 to be close to the pH of human skin, thereby being beneficial to the absorption of the skin and increasing the moisture content of the skin.
Microporous membrane filters known in the art can be used in the present invention, preferably, the filtration process in step (6) is a nanofiltration membrane, and the operation pressure is 1.0-1.5 MPa. The filter membrane is mainly used for protein hydrolysate with the molecular weight cutoff of less than 1000Da, and the nanofiltration membrane body has charge property and higher desalting performance, so that inorganic salt can be removed, and the purity of the obtained oligopeptide is ensured.
Preferably, the concentration process in the step (6) is to concentrate to a concentration of 30% in a triple effect evaporation device; the drying mode is spray drying.
The second purpose of the invention is to provide the sheep skin collagen oligopeptide prepared by the method, wherein the molecular weight of the sheep skin collagen oligopeptide is less than 1000Da, and the sheep skin collagen oligopeptide has wide application value in the industries of medicines, health care products, cosmetics and the like.
The invention has the following beneficial effects:
the invention provides a preparation method of sheep skin collagen oligopeptide, which takes fresh sheep skin as a raw material, and obtains the sheep skin collagen oligopeptide with the molecular weight of less than 1000Da through the steps of alkaline electrolyzed water soaking, enzymolysis treatment, anion and cation exchange resin adsorption, filtration, concentration, drying and the like. The alkaline electrolyzed water treatment not only changes the collagen of the sheepskin from compact order to loose disorder, provides conditions for the enzymolysis of the protein into oligopeptide, but also inhibits microorganisms in the sheepskin protein. Meanwhile, the treatment method combining alkaline electrolyzed water and protease ensures that the content of oligopeptide in the obtained sheep skin collagen peptide solution exceeds 98 percent, thereby greatly improving the utilization rate of collagen. In addition, the preparation method does not use acid or alkali, and adjusts the pH value of the oligopeptide by the adsorption of anion-cation exchange resin, so that the oligopeptide is more beneficial to skin absorption.
In addition, the method has the advantages of low cost, environmental protection, small oligopeptide molecular weight and industrial application prospect.
Detailed Description
In order to more clearly illustrate the invention, the invention is further described below in connection with preferred embodiments. It is to be understood by persons skilled in the art that the following detailed description is illustrative and not restrictive, and is not to be taken as limiting the scope of the invention.
Example 1
1. Fresh sheepskin, shearing the wool on the sheepskin to about 1cm by a sheepskin shearing machine.
2. The meat remover removes fat and meat on the sheepskin.
3. Soaking in 50 deg.C hot water for 40min, and removing short hair from sheepskin with hair remover.
4. The sheepskin was crushed with a crusher to a diameter of about 1 cm.
5. And (3) putting the crushed sheep skin into a reaction tank, adding alkaline electrolyzed water with the weight 2 times that of the sheep skin, wherein the pH value of the electrolyzed water is 12.5, stirring for 30 minutes to stabilize the pH value of the feed liquid, heating to 80 ℃, and keeping for 3 hours at 80 ℃.
6. Reducing the temperature in the tank to 45 ℃, adding alkaline protease, wherein the adding amount of the alkaline protease is 1.3 percent of the weight of the sheep skin, and performing enzymolysis for 4 hours.
7. The temperature was raised to 95 ℃ and maintained for 20 minutes.
8. And centrifuging by using a sedimentation centrifuge to obtain a clarified sheep skin collagen peptide solution.
9. Filtering with a cardboard fine filter under 0.1-0.2Mpa to obtain clear yellowish collagen peptide solution.
10. And (2) passing through anion-cation exchange resin, passing through cation resin, then passing through anion resin, wherein the temperature is 42-45 ℃, the volume ratio of the cation resin to the sheepskin collagen peptide solution is 4:100, the volume ratio of the anion resin to the sheepskin collagen peptide solution is 6:100, the pH value of the solution obtained after exchange is 5.5-6.0, and the molecular weight of more than 98% of components in the obtained sheepskin collagen peptide solution is less than 1000Da through laser light scattering and chromatographic column combined system detection.
11. Pure oligopeptide components with the molecular weight of below 1000Da are intercepted by using a nanofiltration membrane under the filtering pressure of 1.0-1.5 MPa; concentrating the pure oligopeptide solution to 30% concentration by using a triple-effect evaporation device; and (3) carrying out spray drying by using spray drying equipment to obtain the pure oligopeptide powder of the sheepskin collagen.
The molecular weight of the collagen oligopeptide of sheepskin obtained in example 1 is completely less than 1000Da, and the average molecular weight is 730 Da.
Example 2
1. Fresh sheepskin, shearing the wool on the sheepskin to about 1cm by a sheepskin shearing machine.
2. The meat remover removes fat and meat on the sheepskin.
3. Soaking in 60 deg.C hot water for 20 min, and removing short hair from sheepskin with hair remover.
4. The sheepskin was crushed with a crusher to a diameter of about 1 cm.
5. And (3) putting the crushed sheep skin into a reaction tank, adding alkaline electrolyzed water with the weight 3 times that of the sheep skin, wherein the pH value of the electrolyzed water is 10.0, stirring for 30 minutes to stabilize the pH value of the feed liquid, heating to 75 ℃, and keeping for 5 hours at 75 ℃.
6. Reducing the temperature in the tank to 55 ℃, adding pancreatin, wherein the adding amount of the pancreatin is 0.8 percent of the weight of the sheep skin, and performing enzymolysis for 5 hours.
7. The temperature was raised to 90 ℃ and maintained for 30 minutes.
8. And centrifuging by using a sedimentation centrifuge to obtain a clarified sheep skin collagen peptide solution.
9. Filtering with a cardboard fine filter under 0.1-0.2MPa to obtain clear yellowish collagen peptide solution.
10. And (2) passing through anion-cation exchange resin, namely passing through cation resin and then anion resin at the temperature of 42-45 ℃, wherein the volume ratio of the cation resin to the sheepskin collagen peptide solution is 4:100, the volume ratio of the anion resin to the sheepskin collagen peptide solution is 6:100, the pH of the solution obtained after exchange is 5.5-6.0, and the molecular weight of more than 98 percent of components in the obtained sheepskin collagen peptide solution is less than 1000 Da.
11. Pure oligopeptide components with the molecular weight of below 1000Da are intercepted by using a nanofiltration membrane under the filtering pressure of 1.0-1.5 MPa; (ii) a Concentrating the pure oligopeptide solution to 30% concentration by using a triple-effect evaporation device; and (3) carrying out spray drying by using spray drying equipment to obtain the pure oligopeptide powder of the sheepskin collagen.
The molecular weight of the sheep skin collagen oligopeptide obtained in example 2 is completely less than 1000Da, and the average molecular weight is 790 Da.
Example 3
1. Fresh sheepskin, shearing the wool on the sheepskin to about 1cm by a sheepskin shearing machine.
2. The meat remover removes fat and meat on the sheepskin.
3. Soaking in 55 deg.C hot water for 30min, and removing short hair from sheepskin with hair remover.
4. The sheepskin was crushed with a crusher to a diameter of about 1 cm.
5. And (3) putting the crushed sheep skin into a reaction tank, adding alkaline electrolyzed water with the weight 4 times that of the sheep skin, wherein the pH value of the electrolyzed water is 11.0, stirring for 30 minutes to stabilize the pH value of the feed liquid, heating to 80 ℃, and keeping at 80 ℃ for 4 hours.
6. Reducing the temperature in the tank to 50 ℃, adding a mixture of pancreatin and alkaline protease (mass ratio is 1:1), wherein the total addition of the enzymes is 1.8% of the weight of the sheep skin, and performing enzymolysis for 3 hours.
7. The temperature was raised to 95 ℃ and maintained for 40 minutes.
8. And centrifuging by using a sedimentation centrifuge to obtain a clarified sheep skin collagen peptide solution.
9. Filtering with a cardboard fine filter under 0.1-0.2Mpa to obtain clear yellowish collagen peptide solution.
10. And (2) passing through anion-cation exchange resin, passing through cation resin, then passing through anion resin, wherein the temperature is 42-45 ℃, the volume ratio of the cation resin to the sheepskin collagen peptide solution is 4:100, the volume ratio of the anion resin to the sheepskin collagen peptide solution is 6:100, the pH of the solution obtained after exchange is 5.5-6.0, and the molecular weight of more than 98% of components in the obtained sheepskin collagen peptide solution is less than 1000 Da.
11. Pure oligopeptide components with the molecular weight of below 1000Da are intercepted by using a nanofiltration membrane under the filtering pressure of 1.0-1.5 MPa; (ii) a Concentrating the pure oligopeptide solution to 30% concentration by using a triple-effect evaporation device; and (3) carrying out spray drying by using spray drying equipment to obtain the pure oligopeptide powder of the sheepskin collagen.
The molecular weight of the collagen oligopeptide of sheepskin obtained in example 3 is completely less than 1000Da, and the average molecular weight is 680 Da.
The physicochemical indexes of the collagen oligopeptides obtained in examples 1, 2 and 3 were measured according to "collagen peptide of national standard for food safety" GB31645-2018, and the results are shown in table 1.
TABLE 1 test data
Through the data in table 1, it can be found that the purity of the sheepskin collagen oligopeptide obtained by the preparation process provided by the invention is high.
Comparative example
1. Fresh sheepskin, shearing the wool on the sheepskin to about 1cm by a sheepskin shearing machine.
2. The meat remover removes fat and meat on the sheepskin.
3. Soaking in 55 deg.C hot water for 30min, and removing short hair from sheepskin with hair remover.
4. The sheepskin was crushed with a crusher to a diameter of about 1 cm.
5. Putting the crushed sheep skin into a reaction tank, adding a mixture of pancreatin and alkaline protease (mass ratio is 1:1), wherein the total addition amount of the enzymes is 1.8% of the weight of the sheep skin, and performing enzymolysis for 3 hours.
6. The temperature was raised to 95 ℃ and maintained for 40 minutes.
7. And centrifuging by using a sedimentation centrifuge to obtain a clarified sheep skin collagen peptide solution.
8. Filtering with a cardboard fine filter under 0.1-0.2MPa to obtain clear yellowish collagen peptide solution.
9. Passing through anion-cation exchange resin, passing through cation resin, then passing through anion resin, at 42-45 deg.C, the volume ratio of cation resin to collagen peptide solution is 4:100, the volume ratio of anion resin to collagen peptide solution is 6:100, and the pH of the solution obtained after exchange is 5.5-6.0.
10. Concentrating the pure oligopeptide solution to 30% concentration by using a triple-effect evaporation device; and (3) carrying out spray drying by using spray drying equipment to obtain the sheepskin collagen polypeptide powder.
The molecular weight component of the sheep skin collagen polypeptide obtained in the comparative example is 46.9 percent which is far less than the oligopeptide content of 98 percent in the examples 1-3, and the molecular weight component is less than 1000 Da; furthermore, the average molecular weight of 1860Da was approximately 1000Da higher than that of the oligopeptide obtained in examples 1-3.
It should be understood that the above-mentioned embodiments of the present invention are only examples for clearly illustrating the present invention, and are not intended to limit the embodiments of the present invention, and it will be obvious to those skilled in the art that other variations or modifications may be made on the basis of the above description, and all embodiments may not be exhaustive, and all obvious variations or modifications may be included within the scope of the present invention.
Claims (5)
1. A preparation method of sheep skin collagen oligopeptide with the molecular weight of less than 1000Da is characterized by comprising the following steps:
(1) soaking sheepskin with fat, meat and wool removed in 50-60 deg.C water for 20-40min, and pulverizing into pieces with diameter of 1-1.5 cm;
(2) mixing the sheepskin fragments with alkaline electrolyzed water with the pH of 10-12.5, keeping the pH constant, stirring for 30min, heating to 75-80 ℃, and keeping the temperature constant for 3-5 h;
(3) cooling to 45-55 deg.C, adding alkaline protease or/and pancreatin, and performing enzymolysis for 3-5 hr; then heating to 90-95 ℃ for inactivation for 20-40 min;
(4) settling, centrifuging and filtering to obtain a sheepskin collagen peptide solution;
(5) sequentially carrying out exchange adsorption on the sheep skin collagen peptide solution through cation exchange resin and anion exchange resin, wherein the pH value of the sheep skin collagen peptide solution after exchange adsorption is 5.5-6.0;
(6) filtering, concentrating and drying the sheep skin collagen peptide solution with the pH value of 5.5-6.0 to obtain sheep skin collagen oligopeptide powder;
the weight ratio of the sheepskin fragments to the alkaline electrolyzed water in the step (2) is 1: 2-4;
the amount of the enzyme added in the step (3) is 0.8-2.0% of the weight of the sheepskin fragments;
the exchange adsorption in the step (5) is carried out at 42-45 ℃;
in the step (5), the volume ratio of the sheep skin collagen peptide solution to the cation exchange resin and the anion exchange resin is 100:4: 6.
2. The process according to claim 1, wherein in the step (3), when the alkaline protease and the pancreatic enzyme are added simultaneously, the weight ratio of the alkaline protease to the pancreatic enzyme is 1: 1.
3. The method according to claim 1, wherein the filtration in step (4) is a fine filtration of cardboard at an operating pressure of 0.1 to 0.2 MPa.
4. The method according to claim 1, wherein the nanofiltration membrane is used in the filtration process in the step (6), and the operating pressure is 1.0 to 1.5 Mpa.
5. The method according to claim 1, wherein the concentration in step (6) is carried out in a triple effect evaporation apparatus to a concentration of 30%; the drying mode is spray drying.
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