CN112724244A - Bovine bone collagen peptide and production method thereof - Google Patents
Bovine bone collagen peptide and production method thereof Download PDFInfo
- Publication number
- CN112724244A CN112724244A CN202110142515.5A CN202110142515A CN112724244A CN 112724244 A CN112724244 A CN 112724244A CN 202110142515 A CN202110142515 A CN 202110142515A CN 112724244 A CN112724244 A CN 112724244A
- Authority
- CN
- China
- Prior art keywords
- bone
- enzymolysis
- bovine bone
- temperature
- enzyme
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 210000000988 bone and bone Anatomy 0.000 title claims abstract description 137
- 241000283690 Bos taurus Species 0.000 title claims abstract description 78
- 102000008186 Collagen Human genes 0.000 title claims abstract description 77
- 108010035532 Collagen Proteins 0.000 title claims abstract description 77
- 229920001436 collagen Polymers 0.000 title claims abstract description 77
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 54
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 14
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims abstract description 40
- 238000001914 filtration Methods 0.000 claims abstract description 30
- 239000012528 membrane Substances 0.000 claims abstract description 26
- 238000001728 nano-filtration Methods 0.000 claims abstract description 24
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims abstract description 21
- 239000000919 ceramic Substances 0.000 claims abstract description 21
- 239000000843 powder Substances 0.000 claims abstract description 21
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims abstract description 18
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 claims abstract description 13
- 239000002994 raw material Substances 0.000 claims abstract description 13
- 239000000126 substance Substances 0.000 claims abstract description 11
- 239000012535 impurity Substances 0.000 claims abstract description 8
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims abstract description 7
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 claims abstract description 7
- 239000011575 calcium Substances 0.000 claims abstract description 7
- 229910052791 calcium Inorganic materials 0.000 claims abstract description 7
- 238000001694 spray drying Methods 0.000 claims abstract description 7
- 238000000746 purification Methods 0.000 claims abstract description 6
- 239000007788 liquid Substances 0.000 claims description 46
- 239000000463 material Substances 0.000 claims description 40
- 102000004190 Enzymes Human genes 0.000 claims description 30
- 108090000790 Enzymes Proteins 0.000 claims description 30
- 229940088598 enzyme Drugs 0.000 claims description 30
- 230000002255 enzymatic effect Effects 0.000 claims description 20
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 19
- 239000000413 hydrolysate Substances 0.000 claims description 15
- 238000000034 method Methods 0.000 claims description 13
- 229940036811 bone meal Drugs 0.000 claims description 11
- 239000002374 bone meal Substances 0.000 claims description 11
- 102000029816 Collagenase Human genes 0.000 claims description 10
- 108060005980 Collagenase Proteins 0.000 claims description 10
- 229960002424 collagenase Drugs 0.000 claims description 10
- 230000009849 deactivation Effects 0.000 claims description 10
- 239000012153 distilled water Substances 0.000 claims description 10
- 238000010438 heat treatment Methods 0.000 claims description 10
- 230000007935 neutral effect Effects 0.000 claims description 10
- 229930000044 secondary metabolite Natural products 0.000 claims description 10
- 238000005406 washing Methods 0.000 claims description 10
- 238000003860 storage Methods 0.000 claims description 8
- 238000004140 cleaning Methods 0.000 claims description 7
- 238000005507 spraying Methods 0.000 claims description 6
- 108090000526 Papain Proteins 0.000 claims description 5
- 102000057297 Pepsin A Human genes 0.000 claims description 5
- 108090000284 Pepsin A Proteins 0.000 claims description 5
- 239000004365 Protease Substances 0.000 claims description 5
- 108010009736 Protein Hydrolysates Proteins 0.000 claims description 5
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 5
- 102000004142 Trypsin Human genes 0.000 claims description 5
- 108090000631 Trypsin Proteins 0.000 claims description 5
- 238000006243 chemical reaction Methods 0.000 claims description 5
- 238000001816 cooling Methods 0.000 claims description 5
- 238000005238 degreasing Methods 0.000 claims description 5
- 108010007119 flavourzyme Proteins 0.000 claims description 5
- 238000004108 freeze drying Methods 0.000 claims description 5
- 229940055729 papain Drugs 0.000 claims description 5
- 235000019834 papain Nutrition 0.000 claims description 5
- 229940111202 pepsin Drugs 0.000 claims description 5
- 239000012466 permeate Substances 0.000 claims description 5
- 239000006228 supernatant Substances 0.000 claims description 5
- 239000012588 trypsin Substances 0.000 claims description 5
- 229960001322 trypsin Drugs 0.000 claims description 5
- 239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 claims description 4
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 claims description 4
- MKPXGEVFQSIKGE-UHFFFAOYSA-N [Mg].[Si] Chemical compound [Mg].[Si] MKPXGEVFQSIKGE-UHFFFAOYSA-N 0.000 claims description 4
- CSDREXVUYHZDNP-UHFFFAOYSA-N alumanylidynesilicon Chemical compound [Al].[Si] CSDREXVUYHZDNP-UHFFFAOYSA-N 0.000 claims description 4
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 claims description 4
- 229910052782 aluminium Inorganic materials 0.000 claims description 4
- 235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 claims description 4
- 239000011777 magnesium Substances 0.000 claims description 4
- 229910052749 magnesium Inorganic materials 0.000 claims description 4
- 230000000415 inactivating effect Effects 0.000 claims description 3
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 claims 1
- 229910052710 silicon Inorganic materials 0.000 claims 1
- 239000010703 silicon Substances 0.000 claims 1
- 239000000047 product Substances 0.000 abstract description 17
- 238000000605 extraction Methods 0.000 abstract description 5
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 abstract description 4
- 239000006227 byproduct Substances 0.000 abstract description 3
- 239000003925 fat Substances 0.000 abstract description 3
- 238000012545 processing Methods 0.000 abstract description 3
- 102000015636 Oligopeptides Human genes 0.000 abstract description 2
- 108010038807 Oligopeptides Proteins 0.000 abstract description 2
- 239000002639 bone cement Substances 0.000 abstract description 2
- 235000012000 cholesterol Nutrition 0.000 abstract description 2
- 238000002386 leaching Methods 0.000 abstract description 2
- 102000004169 proteins and genes Human genes 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 10
- 230000000694 effects Effects 0.000 description 8
- 210000003491 skin Anatomy 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 229910052799 carbon Inorganic materials 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 238000002834 transmittance Methods 0.000 description 4
- 238000010411 cooking Methods 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 229960002591 hydroxyproline Drugs 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000005374 membrane filtration Methods 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 2
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 230000010718 Oxidation Activity Effects 0.000 description 1
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 1
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 230000037182 bone density Effects 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 210000004207 dermis Anatomy 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 238000007599 discharging Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000005265 energy consumption Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 230000004907 flux Effects 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000003786 sclera Anatomy 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 235000014347 soups Nutrition 0.000 description 1
- 208000010110 spontaneous platelet aggregation Diseases 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000009278 visceral effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention belongs to the field of collagen peptide, and relates to bovine bone collagen peptide and a production method thereof, wherein the production method comprises the following steps: (1) pretreating raw materials; (2) purifying raw materials; (3) shaking and leaching the acetic acid solution; (4) carrying out primary enzymolysis; (5) carrying out secondary enzymolysis; (6) filtering with activated carbon; (7) filtering with inorganic nanofiltration ceramic membrane; (8) concentrating; (9) and (5) spray drying. The invention fully utilizes the byproducts of the processing of cattle, namely the ox bone, to prepare the collagen peptide, has low cost, and the extraction rate of the collagen is more than 85 percent; the prepared yak bone collagen oligopeptide is white or faint yellow powder, the purity is more than 90%, the molecular weight is less than 1000Da, and no peculiar smell exists; according to the invention, after the ox bone is prepared into bone powder, the non-collagen substance, fat and calcium in the ox bone paste can be basically separated and removed by using NaOH solution, n-hexane solution and ethylenediaminetetraacetic acid disodium salt concentrated solution for purification, and the prepared active peptide product is not sticky and basically does not contain impurities such as fat, cholesterol and the like.
Description
Technical Field
The invention belongs to the field of collagen peptides, and particularly relates to bovine bone collagen peptide and a production method thereof.
Background
The collagen is rich in amino acids such as glycine, proline, hydroxyproline and the like required by human bodies. Collagen is a high molecular functional protein, which is the main component of skin and accounts for 80% of the proportion of the dermis layer of the skin, and forms a fine elastic net in the skin, firmly locks water and supports the skin. The collagen is a spiral fibrous protein formed by twisting three peptide chains, is also the most abundant protein in human body, is widely distributed in connective tissues, skin, bones, visceral intercellular substances, muscle cavities, ligaments, sclera and other parts, approximately accounts for more than 30 percent of the total protein of the human body, is rich in collagen characteristic amino acids such as proline, hydroxyproline and the like required by the human body, and is an important component in human body cells, particularly skin extracellular matrix. Collagen is a macromolecular protein, the molecular weight of which is above 300,000Da, and cannot be directly absorbed by human bodies.
Collagen peptide is a product of collagen hydrolysis, and is a substance between amino acids and macromolecular protein, two or more amino acids are dehydrated and condensed to form a plurality of peptide bonds to form a peptide, and a plurality of peptides are folded in multiple stages to form a protein molecule. Peptides are precise fragments of proteins whose molecules are only nanometer in size. Modern researches show that compared with protein, the peptide is easier to digest and absorb, can rapidly provide energy for organisms, has the characteristics of no protein denaturation, low allergy, good water solubility and the like, and has multiple bioactive functions. The bovine bone collagen peptide obtained by enzymolysis of collagen peptide extracted from bovine bone has special functional effects in increasing bone density, preventing and treating osteoarthritis and osteoporosis, inhibiting activity of angiotensin converting enzyme, inhibiting activity of platelet aggregation, resisting oxidation activity and resisting tumor activity.
Chinese invention patent application (CN201510556199.0) discloses a preparation method of bovine bone collagen peptide, which relates to a preparation method of protein peptide. The invention mainly aims to solve the problems of low extraction rate, easy browning, high energy consumption and long production period of the existing production process for preparing the bovine bone collagen peptide by adopting two crushing, two re-cooking, high-temperature cooking and ultrafiltration membrane concentration technologies in sequence on bovine bones and combining a specific complex enzyme preparation. The method comprises the following steps: firstly, screening; secondly, crushing for the first time; thirdly, secondary crushing; fourthly, cleaning; fifthly, high-temperature extraction; sixthly, re-boiling for the second time; seventhly, filtering and separating; eighthly, liquid-liquid separation; ninth, enzymolysis; tenth, sterilizing and inactivating enzyme; eleven, solid-liquid separation; twelfth, concentrating by using an ultrafiltration membrane, thirteen, and spray drying; fourteen, packaging to obtain the bovine bone collagen peptide.
Chinese patent application (CN201710823158.2) discloses a method for extracting bovine bone collagen peptide. Comprises the following steps of firstly, breaking bone; secondly, feeding and cleaning; thirdly, feeding, cooking and discharging soup; fourthly, hydrolysis and filtration; fifthly, concentration; sixthly, drying and spraying powder. The extraction rate of the bovine bone collagen peptide obtained by the method is not enough, and the small molecular active polypeptide is not enough.
Disclosure of Invention
The invention aims to provide the bovine bone collagen peptide which is simple and safe, easy to operate, low in cost and high in purity of the produced product and the production method thereof, so that byproducts of bovine processing are fully utilized, waste is turned into wealth, and the bovine bone collagen peptide with wide application prospect is developed.
The technical scheme for solving the technical problems is as follows:
a method for producing bovine bone collagen peptide comprises the following steps:
(1) pretreatment of raw materials: removing impurities on bones of the ox bones, crushing the ox bones into bone blocks of 2-3 cm by using a bone crusher, cleaning the crushed ox bones, and crushing the ox bones into 50 meshes;
(2) raw material purification: placing the crushed bovine bone meal into 0.1mol/L NaOH solution with the mass being 18-20 times of that of the crushed bovine bone meal, shaking for 1-3 hours at the temperature of 3-5 ℃ to remove non-collagen substances, filtering, repeatedly washing a bone sample with distilled water to be neutral, draining, placing the bone sample into n-hexane solution with the concentration of 10% according to the material-to-liquid ratio of 1: 6-8, shaking for degreasing for 1-3 hours at the temperature of 3-5 ℃ to remove fat, filtering, repeatedly washing the bone sample with distilled water to be neutral, draining, adding the bone sample into 0.25mol/L disodium ethylenediamine tetraacetate concentrated solution according to the material-to-liquid ratio of 1: 8-10, shaking for decalcification for 1-3 hours at the temperature of 3-5 ℃ to remove calcium, and freeze-drying to obtain purified bovine bone meal;
(3) placing the purified bovine bone meal into 0.5mol/L acetic acid solution according to the material-to-liquid ratio of 1: 8-10, extracting for 10-20h under shaking at the temperature of 3-5 ℃, centrifuging and collecting supernatant to obtain bovine bone collagen solution;
(4) primary enzymolysis: adjusting the pH value of the bovine bone collagen solution to 7-9, and adding bone collagenase to carry out ultrasonic-assisted enzymolysis, wherein the primary enzymolysis temperature is 50-55 ℃, the primary enzymolysis time is 1-3 h, and the addition amount of the bone collagenase is 0.1-0.3% of the mass of the bovine bone collagen; after enzymolysis, heating to 80-85 ℃, keeping the temperature for 10-20 min, and inactivating enzyme to obtain primary enzymolysis liquid;
(5) secondary enzymolysis: adjusting the pH value of the primary enzymolysis liquid to 5-7, adding a secondary compound enzyme for ultrasonic-assisted enzymolysis, wherein the secondary compound enzyme adopts pepsin, trypsin, papain and flavourzyme, and obtaining a secondary enzymolysis liquid after the secondary enzymolysis reaction is finished; carrying out microwave enzyme deactivation treatment on the secondary enzymatic hydrolysate, and obtaining enzyme-deactivated enzymatic hydrolysate after the microwave enzyme deactivation is finished;
(6) filtering with activated carbon: adding activated carbon into the enzyme-deactivated enzymolysis liquid, wherein the adding amount of the activated carbon is 2-4% of the mass of the enzyme-deactivated enzymolysis liquid, heating the enzyme-deactivated enzymolysis liquid to 80-100 ℃, and preserving the heat for 5-10 min; then cooling to 70-80 ℃, separating by diatomite, decoloring and removing fishy smell to obtain enzymatic hydrolysate;
(7) filtering with an inorganic nanofiltration ceramic membrane: filtering the enzymatic hydrolysate filtered by the activated carbon by using an inorganic nanofiltration ceramic membrane with the molecular weight cutoff of 800Da to obtain a permeate which is a high-purity bovine bone collagen peptide solution;
(8) concentration: controlling the material temperature to be 55-65 ℃, concentrating the material fed into the concentrator in each batch for no more than 30 minutes under the vacuum degree of 0.06-0.08 Mpa until the Baume degree is 20-22 Be, and temporarily storing the concentrated solution in a concentrated solution storage tank;
(9) spray drying: the material temperature is 45-50 ℃, the Baume degree is 20-22 Bee, the air inlet temperature of the spraying tower is adjusted to be 180-190 ℃, the air outlet temperature is 85-95 ℃, and the materials are dried into powder.
Further, the filter element of the inorganic nanofiltration ceramic membrane in the step (7) is made of any one of siliceous material, aluminous material, magnesian material, silicoaluminophosphate material and silicomagnesian material. After enzymolysis, a technical means of filtering by using an inorganic nanofiltration ceramic membrane is adopted to remove substances which are not easy to dissolve and sugar components which are easy to absorb moisture, so that the water re-solubility of the finally obtained collagen peptide finished product is improved, and the finished product is not easy to absorb moisture and agglomerate in the storage process. Compared with an organic nanofiltration membrane, the inorganic nanofiltration ceramic membrane has the advantages of organic solvent resistance, high temperature resistance, acid and alkali resistance, high mechanical strength, large flux and long service life. The method only needs to adopt a nanofiltration membrane for treatment once, obviously simplifies the process steps compared with the prior art which needs to adopt an ultrafiltration membrane to intercept macromolecular substances and adopt a nanofiltration membrane for desalination and concentration, and has different membrane treatment effects.
Further, the method produces the obtained bovine bone collagen peptide.
Compared with the prior art, the invention has the beneficial effects that: (1) the invention fully utilizes the byproducts of the processing of cattle, namely the ox bone, to prepare the collagen peptide, has low cost, and the extraction rate of the collagen is more than 85 percent; the prepared yak bone collagen oligopeptide is white or faint yellow powder, the purity is more than 90%, the molecular weight is less than 1000Da, and no peculiar smell exists;
(2) after the bovine bone is prepared into bone powder, the non-collagen substances, fat and calcium in the bovine bone paste can be basically separated and removed by purifying NaOH solution, normal hexane solution and ethylene diamine tetraacetic acid disodium salt concentrated solution, and the prepared active peptide product is not sticky and basically does not contain impurities such as fat, cholesterol and the like;
(3) the bovine bone collagen peptide is filtered and purified by adopting secondary enzymolysis in cooperation with activated carbon and an inorganic nanofiltration ceramic membrane, so that the impurity removal and concentration effects are good, and the method is suitable for large-scale industrial production.
Detailed Description
In order to make the technical means, the creation characteristics, the achievement purposes and the effects of the invention easy to understand, the invention is further described with the specific embodiments.
Example 1
A method for producing bovine bone collagen peptide comprises the following steps:
(1) pretreatment of raw materials: removing impurities on bones of the ox bones, crushing the ox bones into bone blocks of 2cm by using a bone crusher, cleaning the crushed ox bones, and crushing the ox bones into 50 meshes;
(2) raw material purification: placing the crushed bovine bone powder into 0.1mol/L NaOH solution with the mass being 18 times of that of the crushed bovine bone powder, shaking for 3 hours at the temperature of 3 ℃ to remove non-collagen substances, filtering, repeatedly washing a bone sample to be neutral by using distilled water, draining, placing the bone sample into n-hexane solution with the concentration of 10% according to the material-liquid ratio of 1:6, shaking for degreasing for 3 hours at the temperature of 3 ℃, filtering, repeatedly washing the bone sample to be neutral by using distilled water, draining, adding the bone sample into 0.25mol/L disodium ethylenediamine tetraacetate concentrated solution according to the material-liquid ratio of 1:8, shaking for decalcification for 3 hours at the temperature of 3 ℃, removing calcium, and freeze-drying to obtain purified bovine bone powder;
(3) placing the purified bovine bone meal into 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:8, shaking and leaching for 20h under the condition of the temperature of 3, centrifuging and collecting supernatant to obtain bovine bone collagen solution;
(4) primary enzymolysis: adjusting the pH value of the bovine bone collagen solution to 7, and adding bone collagenase to carry out ultrasonic-assisted enzymolysis, wherein the primary enzymolysis temperature is 50 ℃, the primary enzymolysis time is 3 hours, and the adding amount of the bone collagenase is 0.1 percent of the mass of the bovine bone collagen; heating to 80 deg.C after enzymolysis, maintaining the temperature for 10min to inactivate enzyme to obtain primary enzymolysis liquid;
(5) secondary enzymolysis: adjusting the pH value of the primary enzymolysis liquid to 5, adding a secondary compound enzyme for ultrasonic-assisted enzymolysis, wherein the secondary compound enzyme adopts pepsin, trypsin, papain and flavourzyme, and obtaining a secondary enzymolysis liquid after the secondary enzymolysis reaction is finished; carrying out microwave enzyme deactivation treatment on the secondary enzymatic hydrolysate, and obtaining enzyme-deactivated enzymatic hydrolysate after the microwave enzyme deactivation is finished;
(6) filtering with activated carbon: adding active carbon into the enzyme-deactivated enzymolysis liquid, wherein the adding amount of the active carbon is 2% of the mass of the enzyme-deactivated enzymolysis liquid, heating the enzyme-deactivated enzymolysis liquid to 80 ℃, and preserving the heat for 5 min; then cooling to 70 ℃, separating by diatomite, decoloring and removing fishy smell to obtain enzymatic hydrolysate;
(7) filtering with an inorganic nanofiltration ceramic membrane: filtering the enzymatic hydrolysate filtered by the activated carbon by using an inorganic nanofiltration ceramic membrane with the molecular weight cutoff of 800Da to obtain a permeate which is a high-purity bovine bone collagen peptide solution;
(8) concentration: controlling the material temperature at 55 ℃, concentrating the material fed into the concentrator in each batch for no more than 30 minutes under the vacuum degree of 0.06MPa until the Baume degree is 20 Be, and temporarily storing the concentrated solution in a concentrated solution storage tank;
(9) spray drying: the material temperature is 45 ℃, the baume degree is 20 Be, the air inlet temperature of the spraying tower is adjusted to be 180 ℃, the air outlet temperature is 85 ℃, and the materials are dried into powder.
The filter element of the inorganic nanofiltration ceramic membrane in the step (7) is made of any one of siliceous material, aluminum material, magnesium material, silicon-aluminum material and silicon-magnesium material.
Example 2
A method for producing bovine bone collagen peptide comprises the following steps:
(1) pretreatment of raw materials: removing impurities on bones of the ox bones, crushing the ox bones into bone blocks of 2cm by using a bone crusher, cleaning the crushed ox bones, and crushing the ox bones into 50 meshes;
(2) raw material purification: placing the crushed bovine bone powder into 0.1mol/L NaOH solution with the mass 20 times of the crushed bovine bone powder, shaking for 3 hours at the temperature of 4 ℃ to remove non-collagen substances, filtering, repeatedly washing a bone sample to be neutral by using distilled water, draining, placing the bone sample into n-hexane solution with the concentration of 10% according to the material-liquid ratio of 1:7, shaking for degreasing for 3 hours at the temperature of 4 ℃, filtering, repeatedly washing the bone sample to be neutral by using distilled water, draining, adding the bone sample into 0.25mol/L disodium ethylenediamine tetraacetic acid concentrated solution according to the material-liquid ratio of 1:8, shaking for decalcification for 3 hours at the temperature of 4 ℃, removing calcium, and freeze-drying to obtain purified bovine bone powder;
(3) placing the purified bovine bone meal into 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:8, extracting for 20 hours at the temperature of 4 ℃ by shaking, centrifuging and collecting supernatant to obtain bovine bone collagen solution;
(4) primary enzymolysis: adjusting the pH value of the bovine bone collagen solution to 8, and adding bone collagenase to carry out ultrasonic-assisted enzymolysis, wherein the primary enzymolysis temperature is 53 ℃, the primary enzymolysis time is 3 hours, and the adding amount of the bone collagenase is 0.1 percent of the mass of the bovine bone collagen; heating to 83 deg.C after enzymolysis, maintaining the temperature for 20min to inactivate enzyme to obtain primary enzymolysis liquid;
(5) secondary enzymolysis: adjusting the pH value of the primary enzymolysis liquid to 6, adding a secondary compound enzyme for ultrasonic-assisted enzymolysis, wherein the secondary compound enzyme adopts pepsin, trypsin, papain and flavourzyme, and obtaining a secondary enzymolysis liquid after the secondary enzymolysis reaction is finished; carrying out microwave enzyme deactivation treatment on the secondary enzymatic hydrolysate, and obtaining enzyme-deactivated enzymatic hydrolysate after the microwave enzyme deactivation is finished;
(6) filtering with activated carbon: adding active carbon into the enzyme-deactivated enzymolysis liquid, wherein the adding amount of the active carbon is 3% of the mass of the enzyme-deactivated enzymolysis liquid, heating the enzyme-deactivated enzymolysis liquid to 90 ℃, and preserving the heat for 10 min; then cooling to 80 ℃, separating by diatomite, decoloring and removing fishy smell to obtain enzymatic hydrolysate;
(7) filtering with an inorganic nanofiltration ceramic membrane: filtering the enzymatic hydrolysate filtered by the activated carbon by using an inorganic nanofiltration ceramic membrane with the molecular weight cutoff of 800Da to obtain a permeate which is a high-purity bovine bone collagen peptide solution;
(8) concentration: controlling the material temperature at 60 ℃, concentrating the material fed into the concentrator in each batch for no more than 30 minutes under the vacuum degree of 0.07Mpa until the baume degree is 21 Be, and temporarily storing the concentrated solution in a concentrated solution storage tank;
(9) spray drying: the material temperature is 47 ℃, the baume degree is 21 Bee, the air inlet temperature of the spraying tower is adjusted to be 185 ℃, the air outlet temperature is adjusted to be 90 ℃, and the materials are dried into powder.
The filter element of the inorganic nanofiltration ceramic membrane in the step (7) is made of any one of siliceous material, aluminum material, magnesium material, silicon-aluminum material and silicon-magnesium material.
Example 3
A method for producing bovine bone collagen peptide comprises the following steps:
(1) pretreatment of raw materials: removing impurities on bones of the ox bones, crushing the ox bones into bone blocks of 2cm by using a bone crusher, cleaning the crushed ox bones, and crushing the ox bones into 50 meshes;
(2) raw material purification: placing the crushed bovine bone powder into 0.1mol/L NaOH solution with the mass 20 times of the crushed bovine bone powder, shaking for 3 hours at the temperature of 5 ℃ to remove non-collagen substances, filtering, repeatedly washing a bone sample to be neutral by using distilled water, draining, placing the bone sample into n-hexane solution with the concentration of 10% according to the material-liquid ratio of 1:8, shaking for degreasing for 3 hours at the temperature of 5 ℃ to remove fat, filtering, repeatedly washing the bone sample to be neutral by using distilled water, draining, adding the bone sample into 0.25mol/L disodium ethylenediamine tetraacetate concentrated solution according to the material-liquid ratio of 1: 10, shaking for decalcification for 3 hours at the temperature of 5 ℃, removing calcium, and freeze-drying to obtain purified bovine bone powder;
(3) placing the purified bovine bone meal into 0.5mol/L acetic acid solution according to the material-liquid ratio of 1: 10, extracting for 20 hours at the temperature of 5 ℃ by shaking, centrifuging and collecting supernatant to obtain bovine bone collagen solution;
(4) primary enzymolysis: adjusting the pH value of the bovine bone collagen solution to 9, and adding bone collagenase to carry out ultrasonic-assisted enzymolysis, wherein the primary enzymolysis temperature is 55 ℃, the primary enzymolysis time is 3 hours, and the adding amount of the bone collagenase is 0.3 percent of the mass of the bovine bone collagen; heating to 85 deg.C after enzymolysis, maintaining the temperature for 20min to inactivate enzyme to obtain primary enzymolysis solution;
(5) secondary enzymolysis: adjusting the pH value of the primary enzymolysis liquid to 7, adding a secondary compound enzyme for ultrasonic-assisted enzymolysis, wherein the secondary compound enzyme adopts pepsin, trypsin, papain and flavourzyme, and obtaining a secondary enzymolysis liquid after the secondary enzymolysis reaction is finished; carrying out microwave enzyme deactivation treatment on the secondary enzymatic hydrolysate, and obtaining enzyme-deactivated enzymatic hydrolysate after the microwave enzyme deactivation is finished;
(6) filtering with activated carbon: adding activated carbon into the enzyme-deactivated enzymolysis liquid, wherein the adding amount of the activated carbon is 4% of the mass of the enzyme-deactivated enzymolysis liquid, heating the enzyme-deactivated enzymolysis liquid to 100 ℃, and preserving the heat for 10 min; then cooling to 80 ℃, separating by diatomite, decoloring and removing fishy smell to obtain enzymatic hydrolysate;
(7) filtering with an inorganic nanofiltration ceramic membrane: filtering the enzymatic hydrolysate filtered by the activated carbon by using an inorganic nanofiltration ceramic membrane with the molecular weight cutoff of 800Da to obtain a permeate which is a high-purity bovine bone collagen peptide solution;
(8) concentration: controlling the material temperature at 65 ℃, concentrating the material fed into the concentrator in each batch for no more than 30 minutes under the vacuum degree of 0.08Mpa until the baume degree is 22 Be, and temporarily storing the concentrated solution in a concentrated solution storage tank;
(9) spray drying: the material temperature is 50 ℃, the baume degree is 22 Bee, the air inlet temperature of the spraying tower is adjusted to be 190 ℃, the air outlet temperature is 95 ℃, and the materials are dried into powder.
The filter element of the inorganic nanofiltration ceramic membrane in the step (7) is made of any one of siliceous material, aluminum material, magnesium material, silicon-aluminum material and silicon-magnesium material.
(1) And (3) detecting the enzymolysis effect of the high-efficiency compound enzyme preparation:
in examples 1 to 3, after the bovine bone is subjected to raw material pretreatment and oil-water separation, enzymolysis is performed by using a high-efficiency compound enzyme preparation under the conditions of no pH value adjustment and no temperature control, and in order to evaluate the enzymolysis effect, after the enzymolysis is finished, the method in appendix A of national standard GB/T22729-:
TABLE 1
The results in Table 1 show that the enzymolysis products of examples 1 to 3 have small and concentrated molecular weight, low free amino acid content (less than 200Da of less than 5%), a collagen peptide ratio of less than 1000Da of molecular weight of 100%, and a collagen peptide ratio of 200 to 1000Da of more than 95%. Therefore, the combination technical means of specific twice enzymolysis and high-efficiency complex enzyme enzymolysis provided by the invention can obviously improve the enzymolysis efficiency of the enzymolysis collagen.
(2) Detecting the water re-solubility of the finished product of the bovine bone collagen peptide and the light transmittance of the bovine bone collagen peptide solution:
and (3) respectively pouring 8g of the finished bovine bone collagen peptide powder obtained in the examples 1-3 into different cups, mixing with 300mL of warm boiled water at about 60 ℃, dissolving completely within 1s to obtain a bovine bone collagen peptide solution, and observing the solution by naked eyes to be clear and transparent without any precipitate. The light transmittance of the bovine bone collagen peptide solutions was measured at 620nm using an ultraviolet spectrophotometer, and the results are shown in the following table 4:
TABLE 2
| Example 1 | Example 2 | Example 3 | |
| Transmittance of item (%) | 96 | 94 | 95 |
From the results in table 2, it can be seen that the method adopts the technical means of inorganic nanofiltration ceramic membrane filtration to remove the substances which are not easy to dissolve, and then adopts the technical means of high-temperature and high-pressure treatment of peptide solution to further improve the solubility of the finished product, so that the obtained finished product of bovine bone collagen peptide is extremely easy to dissolve in water and has excellent water re-solubility, the dissolved solution after dissolving in water is clear and transparent, has no any precipitate and has high light transmittance, and when a consumer soaks the product, the product does not need to be stirred, is convenient to eat and has good eating experience.
(3) Shelf life test of the finished bovine bone collagen peptide product:
8g of the bovine bone collagen peptide finished product powder obtained in the examples 1-3 is respectively poured into a packaging bag, placed on an indoor display rack in an open mode at room temperature, and observed by naked eyes to obtain the caking time of the finished product, and the results are shown in the following table 3:
TABLE 3
| Example 1 | Example 2 | Example 3 | |
| Time (day) when the item caked | 56 | 54 | 53 |
Bovine bone collagen peptide produced by the prior art is easy to absorb moisture and agglomerate in the storage process, and the sale of products is influenced. The results in table 3 show that the method of the present invention using the inorganic nanofiltration ceramic membrane filtration technology can remove the sugar components that are easy to absorb moisture, so that the finished product is not easy to absorb moisture and agglomerate during storage, and is easy to store, which is a technical effect that the prior art cannot achieve.
Furthermore, it should be understood that although the present description refers to embodiments, not every embodiment may contain only a single embodiment, and such description is for clarity only, and those skilled in the art should integrate the description, and the embodiments may be combined as appropriate to form other embodiments understood by those skilled in the art.
Claims (3)
1. The production method of the bovine bone collagen peptide is characterized by comprising the following steps:
(1) pretreatment of raw materials: removing impurities on bones of the ox bones, crushing the ox bones into bone blocks of 2-3 cm by using a bone crusher, cleaning the crushed ox bones, and crushing the ox bones into 50 meshes;
(2) raw material purification: placing the crushed bovine bone meal into 0.1mol/L NaOH solution with the mass being 18-20 times of that of the crushed bovine bone meal, shaking for 1-3 hours at the temperature of 3-5 ℃ to remove non-collagen substances, filtering, repeatedly washing a bone sample with distilled water to be neutral, draining, placing the bone sample into n-hexane solution with the concentration of 10% according to the material-to-liquid ratio of 1: 6-8, shaking for degreasing for 1-3 hours at the temperature of 3-5 ℃ to remove fat, filtering, repeatedly washing the bone sample with distilled water to be neutral, draining, adding the bone sample into 0.25mol/L disodium ethylenediamine tetraacetate concentrated solution according to the material-to-liquid ratio of 1: 8-10, shaking for decalcification for 1-3 hours at the temperature of 3-5 ℃ to remove calcium, and freeze-drying to obtain purified bovine bone meal;
(3) placing the purified bovine bone meal into 0.5mol/L acetic acid solution according to the material-to-liquid ratio of 1: 8-10, extracting for 10-20h under shaking at the temperature of 3-5 ℃, centrifuging and collecting supernatant to obtain bovine bone collagen solution;
(4) primary enzymolysis: adjusting the pH value of the bovine bone collagen solution to 7-9, and adding bone collagenase to carry out ultrasonic-assisted enzymolysis, wherein the primary enzymolysis temperature is 50-55 ℃, the primary enzymolysis time is 1-3 h, and the addition amount of the bone collagenase is 0.1-0.3% of the mass of the bovine bone collagen; after enzymolysis, heating to 80-85 ℃, keeping the temperature for 10-20 min, and inactivating enzyme to obtain primary enzymolysis liquid;
(5) secondary enzymolysis: adjusting the pH value of the primary enzymolysis liquid to 5-7, adding a secondary compound enzyme for ultrasonic-assisted enzymolysis, wherein the secondary compound enzyme adopts pepsin, trypsin, papain and flavourzyme, and obtaining a secondary enzymolysis liquid after the secondary enzymolysis reaction is finished; carrying out microwave enzyme deactivation treatment on the secondary enzymatic hydrolysate, and obtaining enzyme-deactivated enzymatic hydrolysate after the microwave enzyme deactivation is finished;
(6) filtering with activated carbon: adding activated carbon into the enzyme-deactivated enzymolysis liquid, wherein the adding amount of the activated carbon is 2-4% of the mass of the enzyme-deactivated enzymolysis liquid, heating the enzyme-deactivated enzymolysis liquid to 80-100 ℃, and preserving the heat for 5-10 min; then cooling to 70-80 ℃, separating by diatomite, decoloring and removing fishy smell to obtain enzymatic hydrolysate;
(7) filtering with an inorganic nanofiltration ceramic membrane: filtering the enzymatic hydrolysate filtered by the activated carbon by using an inorganic nanofiltration ceramic membrane with the molecular weight cutoff of 800Da to obtain a permeate which is a high-purity bovine bone collagen peptide solution;
(8) concentration: controlling the material temperature to be 55-65 ℃, concentrating the material fed into the concentrator in each batch for no more than 30 minutes under the vacuum degree of 0.06-0.08 Mpa until the Baume degree is 20-22 Be, and temporarily storing the concentrated solution in a concentrated solution storage tank;
(9) spray drying: the material temperature is 45-50 ℃, the Baume degree is 20-22 Bee, the air inlet temperature of the spraying tower is adjusted to be 180-190 ℃, the air outlet temperature is 85-95 ℃, and the materials are dried into powder.
2. The method for producing bovine bone collagen peptide according to claim 1, wherein the filter core of the inorganic nanofiltration ceramic membrane in the step (7) is made of any one of silicon, aluminum, magnesium, silicon-aluminum and silicon-magnesium.
3. Bovine bone collagen peptide produced by the method of any one of claims 1 to 2.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202110142515.5A CN112724244A (en) | 2021-02-02 | 2021-02-02 | Bovine bone collagen peptide and production method thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202110142515.5A CN112724244A (en) | 2021-02-02 | 2021-02-02 | Bovine bone collagen peptide and production method thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN112724244A true CN112724244A (en) | 2021-04-30 |
Family
ID=75595509
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202110142515.5A Withdrawn CN112724244A (en) | 2021-02-02 | 2021-02-02 | Bovine bone collagen peptide and production method thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN112724244A (en) |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113088551A (en) * | 2021-05-25 | 2021-07-09 | 内蒙古蒙肽生物工程有限公司 | Preparation method of bone collagen peptide |
| CN113475618A (en) * | 2021-06-30 | 2021-10-08 | 内蒙古阿荣旗牧原康肽实业有限公司 | Method for preparing bovine bone collagen bone marrow peptide |
| CN113880942A (en) * | 2021-09-30 | 2022-01-04 | 吴伟 | Chicken bone collagen peptide with antioxidant activity and application thereof |
| CN114457138A (en) * | 2022-02-25 | 2022-05-10 | 浙江工业大学 | Method for removing type II collagen peptide polysaccharide |
| CN114903176A (en) * | 2022-05-09 | 2022-08-16 | 广州博厚健康科技有限公司 | Hypoallergenic polypeptide nutrition powder and preparation method thereof |
| CN115340595A (en) * | 2022-05-09 | 2022-11-15 | 湖南伍星生物科技有限公司 | Production method for preparing bovine cartilage collagen peptide by novel degreasing process |
| CN115353558A (en) * | 2022-05-13 | 2022-11-18 | 山东恒鑫生物科技有限公司 | Method for producing ossein peptide by using ossein |
| CN116640356A (en) * | 2023-06-05 | 2023-08-25 | 上海瑞邦生物材料有限公司 | Preparation method of enhanced bovine collagen sponge |
| CN116640823A (en) * | 2023-06-12 | 2023-08-25 | 上海瑞邦生物材料有限公司 | Preparation method of high-yield enzymolysis bovine collagen |
-
2021
- 2021-02-02 CN CN202110142515.5A patent/CN112724244A/en not_active Withdrawn
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113088551A (en) * | 2021-05-25 | 2021-07-09 | 内蒙古蒙肽生物工程有限公司 | Preparation method of bone collagen peptide |
| CN113088551B (en) * | 2021-05-25 | 2023-05-05 | 内蒙古蒙肽生物工程有限公司 | Preparation method of bone collagen peptide |
| CN113475618A (en) * | 2021-06-30 | 2021-10-08 | 内蒙古阿荣旗牧原康肽实业有限公司 | Method for preparing bovine bone collagen bone marrow peptide |
| CN113880942A (en) * | 2021-09-30 | 2022-01-04 | 吴伟 | Chicken bone collagen peptide with antioxidant activity and application thereof |
| CN114457138A (en) * | 2022-02-25 | 2022-05-10 | 浙江工业大学 | Method for removing type II collagen peptide polysaccharide |
| CN114903176A (en) * | 2022-05-09 | 2022-08-16 | 广州博厚健康科技有限公司 | Hypoallergenic polypeptide nutrition powder and preparation method thereof |
| CN115340595A (en) * | 2022-05-09 | 2022-11-15 | 湖南伍星生物科技有限公司 | Production method for preparing bovine cartilage collagen peptide by novel degreasing process |
| CN114903176B (en) * | 2022-05-09 | 2023-11-21 | 博厚健康科技股份有限公司 | Low-sensitization polypeptide nutrition powder and preparation method thereof |
| CN115353558A (en) * | 2022-05-13 | 2022-11-18 | 山东恒鑫生物科技有限公司 | Method for producing ossein peptide by using ossein |
| CN115353558B (en) * | 2022-05-13 | 2023-09-08 | 山东恒鑫生物科技有限公司 | Method for producing bone collagen peptide by using bone element |
| CN116640356A (en) * | 2023-06-05 | 2023-08-25 | 上海瑞邦生物材料有限公司 | Preparation method of enhanced bovine collagen sponge |
| CN116640823A (en) * | 2023-06-12 | 2023-08-25 | 上海瑞邦生物材料有限公司 | Preparation method of high-yield enzymolysis bovine collagen |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN112724244A (en) | Bovine bone collagen peptide and production method thereof | |
| CN109735591B (en) | Bovine bone collagen peptide and production method thereof | |
| CN103843970B (en) | Production method for preparing ossein oligopeptide meal, bone oil and bone meal | |
| CN105476030A (en) | Multi-functional composite oligopeptide nutrition powder | |
| CN105132498A (en) | Micromolecular sea cucumber peptide and preparation method thereof | |
| CN102994598B (en) | Weak bitter corn oligopeptide with high content of alanine and leucine, and preparation method thereof | |
| CN109897101B (en) | Collagen tripeptide and production method and application thereof | |
| CN101744090B (en) | Method for preparing small molecular peptides of soft-shelled turtle | |
| CN109722461B (en) | Deep sea fish collagen peptide and production method thereof | |
| CN101096697B (en) | Industrial production method of ovum protein polypeptide from fowl ovum by enzymatical process | |
| CN102643368A (en) | Method for synchronously extracting taurine, chitin and polypeptide from shrimp heads and shrimp leftovers | |
| CN102652829A (en) | Extraction method of ginseng peptide | |
| CN103636914A (en) | Oyster peptide extraction method | |
| CN1985852A (en) | Process of extracting sea cucumber polyose and other active components from boiled sea cucumber juice | |
| CN105077161B (en) | A kind of preparation method and application of the chicken powder rich in oligopeptides | |
| CN106748923B (en) | A kind of method that alliin is extracted from black garlic | |
| KR101883979B1 (en) | pomegranate drink comprising marine collagen and manufacturing method thereof | |
| CN101965897A (en) | Processing method for mussel isolated protein | |
| CN111938006A (en) | Cubilose collagen peptide tablet candy | |
| CN114605525A (en) | Tuna bone collagen peptide and production method thereof | |
| CN110669813A (en) | Yak rib small molecule peptide and extraction method thereof | |
| CN104844721A (en) | Extraction and separation method of Agrocybe aegirit polysaccharides | |
| CN106497741A (en) | A kind of processing method of sea cucumber different tissues low molecular weight polypeptide wine | |
| CN104131060B (en) | Corbicula fluminea anti-oxidative peptide and preparation method thereof | |
| CN115449535A (en) | Bone-derived collagen tripeptide and preparation method thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| WW01 | Invention patent application withdrawn after publication | ||
| WW01 | Invention patent application withdrawn after publication |
Application publication date: 20210430 |