US20150203891A1 - Method of Making Collagen Powder From Marine Cartilage and Skin - Google Patents
Method of Making Collagen Powder From Marine Cartilage and Skin Download PDFInfo
- Publication number
- US20150203891A1 US20150203891A1 US14/157,609 US201414157609A US2015203891A1 US 20150203891 A1 US20150203891 A1 US 20150203891A1 US 201414157609 A US201414157609 A US 201414157609A US 2015203891 A1 US2015203891 A1 US 2015203891A1
- Authority
- US
- United States
- Prior art keywords
- mixture
- mixing
- tank
- marine
- 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.)
- Abandoned
Links
- 102000008186 Collagen Human genes 0.000 title claims abstract description 26
- 108010035532 Collagen Proteins 0.000 title claims abstract description 26
- 229920001436 collagen Polymers 0.000 title claims abstract description 26
- 239000000843 powder Substances 0.000 title claims abstract description 24
- 210000000845 cartilage Anatomy 0.000 title claims abstract description 18
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 11
- 239000000203 mixture Substances 0.000 claims abstract description 37
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 17
- 108090000790 Enzymes Proteins 0.000 claims abstract description 13
- 102000004190 Enzymes Human genes 0.000 claims abstract description 13
- 102000000503 Collagen Type II Human genes 0.000 claims abstract description 8
- 108010041390 Collagen Type II Proteins 0.000 claims abstract description 8
- 229920002774 Maltodextrin Polymers 0.000 claims abstract description 7
- 239000005913 Maltodextrin Substances 0.000 claims abstract description 7
- 210000000988 bone and bone Anatomy 0.000 claims abstract description 7
- 229940035034 maltodextrin Drugs 0.000 claims abstract description 7
- 239000013049 sediment Substances 0.000 claims abstract description 7
- 108091005804 Peptidases Proteins 0.000 claims abstract description 6
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 6
- 238000000034 method Methods 0.000 claims description 21
- 239000007788 liquid Substances 0.000 claims description 16
- 229940088598 enzyme Drugs 0.000 claims description 11
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- 241000251730 Chondrichthyes Species 0.000 claims description 8
- 230000029087 digestion Effects 0.000 claims description 8
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 7
- 102000012422 Collagen Type I Human genes 0.000 claims description 5
- 108010022452 Collagen Type I Proteins 0.000 claims description 5
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 claims description 4
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 claims description 3
- 229920002567 Chondroitin Polymers 0.000 claims description 3
- DLGJWSVWTWEWBJ-HGGSSLSASA-N chondroitin Chemical compound CC(O)=N[C@@H]1[C@H](O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@H](O)C=C(C(O)=O)O1 DLGJWSVWTWEWBJ-HGGSSLSASA-N 0.000 claims description 3
- 229920002674 hyaluronan Polymers 0.000 claims description 3
- 229960003160 hyaluronic acid Drugs 0.000 claims description 3
- 102000004169 proteins and genes Human genes 0.000 claims description 3
- 108090000623 proteins and genes Proteins 0.000 claims description 3
- 229920002683 Glycosaminoglycan Polymers 0.000 claims description 2
- 108090000526 Papain Proteins 0.000 claims description 2
- 238000010438 heat treatment Methods 0.000 claims 3
- 238000001035 drying Methods 0.000 claims 1
- 238000000227 grinding Methods 0.000 claims 1
- -1 marine skin Substances 0.000 claims 1
- 238000001694 spray drying Methods 0.000 claims 1
- 239000007921 spray Substances 0.000 abstract description 4
- 239000000126 substance Substances 0.000 description 4
- 206010028980 Neoplasm Diseases 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000009849 deactivation Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 108091005508 Acid proteases Proteins 0.000 description 1
- 108090000145 Bacillolysin Proteins 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 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
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 210000001188 articular cartilage Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 210000003035 hyaline cartilage Anatomy 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 208000015122 neurodegenerative disease Diseases 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000010451 perlite Substances 0.000 description 1
- 235000019362 perlite Nutrition 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000003319 supportive effect Effects 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
Images
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
Definitions
- This invention is directed to a method of making collagen powder. More particularly, this invention is directed to a method of making hydrolyzed Type II collagen from marine cartilage and hydrolyzed Type I collagen from marine skin.
- Collagen is a fibrous protein that forms insoluble fibers of high tensile strength, which contains the unique amino acids hyroxyproline and hydrosylysine. It is rich in glycine, but lacks cysteine and tryptophan, and has an unusually regular amino-acid domain. It is a natural nontoxic substance that in prior studies showed positive beneficial results for treating degenerative diseases such as osteoarthritis and rheumatoid arthritis and other inflammatory diseases/conditions. It was also associated as a substance with cancer combating properties, research later backed up that claim. Collagen has been found to block a tumor's angiogenesis—the growth of new blood vessels that feed a tumor and help it grow.
- angiogenesis the growth of new blood vessels that feed a tumor and help it grow.
- Type II collagen is the principal component of extracellular matrix of articular/hyaline cartilage. It is composed of 15-25% of the wet weight, about half the dry weight and 90-95% of the total collagen content in the cartilage. Type II Collagen from shark cartilage induces a cytokine response in human leukocytes, but the main bio-active components remain somewhat elusive. Medical research tends to group all collagen together as unique but equal substances. Collagen can be difficult to digest and breakdown when taken orally. Because of this, it does not allow the release and breakdown of essential components that benefit the body.
- An objective of the present invention is to provide a method of making collagen powder that raises a bodies pH levels from acid to more neutral range.
- Another objective of the present invention is to provide a method of making a collagen powder consumed in capsule form to improve flexibility and reduce pain.
- a method of making hydrolyzed marine Type II collagen includes the mixing of marine cartilage, water, an enzyme and a protease enzyme for an extended period of time. Once mixed, the mixture is heated for a period of time at 150° F. Once heated, the enzymes are deactivated, the bone sediment separated, and the fat removed. Next, maltodextrin is added to the mixture and finally the mixture is spray dried to form a collagen powder.
- FIG. 1 is a flow diagram of a method of making collagen powder
- FIG. 2 is a schematic drawing of an environment for making collagen powder
- FIG. 3 is a flow diagram of a method of making collagen powder
- FIG. 4 is a schematic drawing of an environment for making collagen powder.
- the process of making hydrolyzed marine Type II collagen begins at step 100 by placing marine cartilage 10 into a digestion vessel or tank 12 .
- marine cartilage 10 Preferably shark cartilage in a range between 500 to 3,000 pounds is provided (and optimally 1,000 pounds of shark cartilage) to the digestion tank 12 .
- the cartilage 10 is frozen or dried.
- step 110 between 500 and 2,500 pounds of water 14 is added to the digestion tank 12 and optimally 1,025 pounds of water 14 is added.
- an enzyme 16 such as a bromalain or (ficen) is added to the digestion tank 12 .
- the enzyme 16 is papain in a range of 500 mLs to 20 L and optimally 4,800 mLs of 200 tyrosine units (T.U.) is added.
- a neutral or alkaline protease enzyme 18 is added to the digestion tank. Preferably between 10 mLs and 20 L is added and optimally 14 L is added.
- an actuator 20 in the digestion tank 12 mixes the contents while the mixture 22 is heated at a temperature of approximately 150° F. for a period of 30 minutes to 48 hours. This process turns the cartilage 10 in the mixture 22 into a liquid 26 .
- the mixture 22 is heated to a temperature of between 180° F. and 200° F. for a period of between 5 and 30 minutes at step 150 . Deactivation may occur in the digestion tank 12 or the mixture 22 may be transferred to another reactor 23 . Also, the deactivation step 150 may occur immediately after step 140 or after the mixture 22 has cooled at least partially.
- the bone sediment 24 from the marine cartilage 10 is separated from the liquid 26 at step 160 . Separation may occur by decanting, filtering, or centrifuging.
- any fat 28 in the liquid 26 is removed and/or separated from the liquid 26 in any conventional manner at step 170 .
- the liquid 26 is transferred to a second tank 30 and heated or cooled to a temperature of between 140° F. to 170° F. at step 180 .
- step 190 maltodextrin 32 , at a 1% to 60% weight of the mixture, is added to second tank 30 to help take away moisture from the liquid 26 .
- the maltodextrin 32 is added at between 30% and 32% weight.
- step 200 the liquid 26 is spray dried in hot air such that the liquid evaporates and a collagen powder 33 drops and is then packaged at step 210 .
- the collagen powder 33 has a molecular weight in a range between 18,000 and 180,000 Daltons. Also, preferably, the collagen powder 33 includes a minimum of 4% hyaluronic acid and typically 11%, a minimum of 5% chondroitin, between 20% and 45% of mucopolysaccharide, and a minimum of 10% protein. In one test, the collagen powder 33 included:
- the bone sediment 24 is dried at step 220 , ground to a powder at step 230 and then packaged at step 240 .
- a similar method is used to make hydrolyzed marine Type I collagen.
- step 300 approximately 18 L of water 14 is added to a tank or vessel 34 .
- marine skin 36 is added to the water 14 in the tank 34 .
- the marine skin 36 is approximately 1,285 grams shark skin cut into squares between 0.25 and 1.5 square inches (and optimally 1 square inch).
- sodium hydroxide 38 is added to the tank 34 to form a mixture 40 .
- 72 mLs of 50% sodium hydroxide 38 is added.
- the mixture 40 is then mixed for approximately 40 minutes and at step 340 , the liquid 42 is drained from the skin 36 .
- the liquid 42 is drained from the skin 36 .
- approximately 18 L of water 14 is added to tank 34 and mixed for 10 minutes.
- the liquid 42 is drained from the skin 36 to wash or rinse the skin. Steps 350 and 360 are repeated preferably three times. At this point, the pH of the mixture 40 is approximately 8.0.
- step 370 18 L of water 14 is added to the tank 34 .
- step 380 32 mLs of sulfuric acid 44 is added to the tank 34 and then mixed for approximately 40 minutes.
- the liquid 42 is drained from the tank 34 such that the skin 36 is retained at step 390 .
- 18 L of water 14 and 180 grams of citric acid 46 are added to the tank 34 and mixed for approximately 40 minutes at step 400 .
- step 410 again the liquid 42 is drained while retaining the skin 36 .
- step 420 18 L of water 14 is added to the tank 34 and mixed for about 10 minutes.
- step 430 the liquid 42 is drained while retaining the skin 36 .
- the pH level is between 2.8 and 3.4.
- step 440 18 L of water 14 is added to the tank 34 , the mixture 40 is heated to 113° F., and the mixture 40 is mixed for about 18 hours.
- step 450 the mixture 40 is centrifuged followed by filtering the mixture 40 at step 460 through filter pads and perlite. Once filtered, the mixture 40 is heated between 131° F. and 194° F. to evaporate the liquid 42 such that the mixture 40 is 7% to 50% solids at step 470 .
- the Type I collagen 50 and Type II collagen 33 powder may be blended at a 10% to 90% ratio and preferably a 50% to 50% ratio at step 520 .
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
Description
- This invention is directed to a method of making collagen powder. More particularly, this invention is directed to a method of making hydrolyzed Type II collagen from marine cartilage and hydrolyzed Type I collagen from marine skin.
- Shark cartilage is no longer controversial throughout medical, allied medical or participant supportive treatment circles today. The main beneficial attributes that this substance delivers have been well established over the past number of years. The active combination of the elements responsible for triggering such beneficial action is still somewhat unknown.
- Collagen is a fibrous protein that forms insoluble fibers of high tensile strength, which contains the unique amino acids hyroxyproline and hydrosylysine. It is rich in glycine, but lacks cysteine and tryptophan, and has an unusually regular amino-acid domain. It is a natural nontoxic substance that in prior studies showed positive beneficial results for treating degenerative diseases such as osteoarthritis and rheumatoid arthritis and other inflammatory diseases/conditions. It was also associated as a substance with cancer combating properties, research later backed up that claim. Collagen has been found to block a tumor's angiogenesis—the growth of new blood vessels that feed a tumor and help it grow.
- Type II collagen is the principal component of extracellular matrix of articular/hyaline cartilage. It is composed of 15-25% of the wet weight, about half the dry weight and 90-95% of the total collagen content in the cartilage. Type II Collagen from shark cartilage induces a cytokine response in human leukocytes, but the main bio-active components remain somewhat elusive. Medical research tends to group all collagen together as unique but equal substances. Collagen can be difficult to digest and breakdown when taken orally. Because of this, it does not allow the release and breakdown of essential components that benefit the body.
- An objective of the present invention is to provide a method of making collagen powder that raises a bodies pH levels from acid to more neutral range.
- Another objective of the present invention is to provide a method of making a collagen powder consumed in capsule form to improve flexibility and reduce pain.
- A method of making hydrolyzed marine Type II collagen includes the mixing of marine cartilage, water, an enzyme and a protease enzyme for an extended period of time. Once mixed, the mixture is heated for a period of time at 150° F. Once heated, the enzymes are deactivated, the bone sediment separated, and the fat removed. Next, maltodextrin is added to the mixture and finally the mixture is spray dried to form a collagen powder.
-
FIG. 1 is a flow diagram of a method of making collagen powder; -
FIG. 2 is a schematic drawing of an environment for making collagen powder; -
FIG. 3 is a flow diagram of a method of making collagen powder; and -
FIG. 4 is a schematic drawing of an environment for making collagen powder. - Referring to the Figures, the process of making hydrolyzed marine Type II collagen begins at
step 100 by placingmarine cartilage 10 into a digestion vessel ortank 12. Preferably shark cartilage in a range between 500 to 3,000 pounds is provided (and optimally 1,000 pounds of shark cartilage) to thedigestion tank 12. Thecartilage 10 is frozen or dried. - At
step 110, between 500 and 2,500 pounds ofwater 14 is added to thedigestion tank 12 and optimally 1,025 pounds ofwater 14 is added. In addition, atstep 120 anenzyme 16 such as a bromalain or (ficen) is added to thedigestion tank 12. - Preferably, the
enzyme 16 is papain in a range of 500 mLs to 20 L and optimally 4,800 mLs of 200 tyrosine units (T.U.) is added. Finally, atstep 130, a neutral oralkaline protease enzyme 18 is added to the digestion tank. Preferably between 10 mLs and 20 L is added and optimally 14 L is added. - Next, at
step 140, anactuator 20 in thedigestion tank 12 mixes the contents while themixture 22 is heated at a temperature of approximately 150° F. for a period of 30 minutes to 48 hours. This process turns thecartilage 10 in themixture 22 into aliquid 26. - To deactivate the
16 and 18 afterenzymes step 140, themixture 22 is heated to a temperature of between 180° F. and 200° F. for a period of between 5 and 30 minutes atstep 150. Deactivation may occur in thedigestion tank 12 or themixture 22 may be transferred to anotherreactor 23. Also, thedeactivation step 150 may occur immediately afterstep 140 or after themixture 22 has cooled at least partially. - Once the
16 and 18 are deactivated, theenzymes bone sediment 24 from themarine cartilage 10 is separated from theliquid 26 atstep 160. Separation may occur by decanting, filtering, or centrifuging. - After the
bone sediment 24 is separated from theliquid 26, anyfat 28 in theliquid 26 is removed and/or separated from theliquid 26 in any conventional manner atstep 170. Once thefat 28 is removed, theliquid 26 is transferred to asecond tank 30 and heated or cooled to a temperature of between 140° F. to 170° F. atstep 180. - Next, at
step 190,maltodextrin 32, at a 1% to 60% weight of the mixture, is added tosecond tank 30 to help take away moisture from theliquid 26. Preferably, themaltodextrin 32 is added at between 30% and 32% weight. Finally, atstep 200, theliquid 26 is spray dried in hot air such that the liquid evaporates and acollagen powder 33 drops and is then packaged atstep 210. - Preferably, the
collagen powder 33 has a molecular weight in a range between 18,000 and 180,000 Daltons. Also, preferably, thecollagen powder 33 includes a minimum of 4% hyaluronic acid and typically 11%, a minimum of 5% chondroitin, between 20% and 45% of mucopolysaccharide, and a minimum of 10% protein. In one test, thecollagen powder 33 included: -
Analyte Mucoploysaccharide 43.2% Hyaluronic acid 10.71% Chondroitin 23.5% - In addition to making the
collagen powder 33, afterstep 160, thebone sediment 24 is dried atstep 220, ground to a powder atstep 230 and then packaged atstep 240. - A similar method is used to make hydrolyzed marine Type I collagen. To begin, at
step 300 approximately 18 L ofwater 14 is added to a tank orvessel 34. Atstep 310,marine skin 36 is added to thewater 14 in thetank 34. Preferably themarine skin 36 is approximately 1,285 grams shark skin cut into squares between 0.25 and 1.5 square inches (and optimally 1 square inch). Next, atstep 320,sodium hydroxide 38 is added to thetank 34 to form amixture 40. Preferably 72 mLs of 50%sodium hydroxide 38 is added. - The
mixture 40, atstep 330, is then mixed for approximately 40 minutes and atstep 340, theliquid 42 is drained from theskin 36. Once drained, atstep 350, approximately 18 L ofwater 14 is added totank 34 and mixed for 10 minutes. Once mixed, atstep 360, theliquid 42 is drained from theskin 36 to wash or rinse the skin. 350 and 360 are repeated preferably three times. At this point, the pH of theSteps mixture 40 is approximately 8.0. - Next, at
step 370, 18 L ofwater 14 is added to thetank 34. At 380, 32 mLs ofstep sulfuric acid 44 is added to thetank 34 and then mixed for approximately 40 minutes. When the mixing is completed, the liquid 42 is drained from thetank 34 such that theskin 36 is retained atstep 390. Once drained, 18 L of 14 and 180 grams ofwater citric acid 46 are added to thetank 34 and mixed for approximately 40 minutes atstep 400. - At
step 410, again the liquid 42 is drained while retaining theskin 36. Then, atstep 420, 18 L ofwater 14 is added to thetank 34 and mixed for about 10 minutes. Again atstep 430, the liquid 42 is drained while retaining theskin 36. At this point, the pH level is between 2.8 and 3.4. - Next, at
step 440, 18 L ofwater 14 is added to thetank 34, themixture 40 is heated to 113° F., and themixture 40 is mixed for about 18 hours. Upon completion, atstep 450, themixture 40 is centrifuged followed by filtering themixture 40 atstep 460 through filter pads and perlite. Once filtered, themixture 40 is heated between 131° F. and 194° F. to evaporate the liquid 42 such that themixture 40 is 7% to 50% solids atstep 470. - Once evaporated 0.1% w/w of fungal or
bacterial acid protease 48 is added to themixture 40 atstep 480 and heated at 131° F. for approximately 4 to 5 hours. Next, themixture 40 is heated to 149° F. to deactivate theenzyme 48 atstep 490. Atstep 500, themixture 40 is spray dried with or withoutmaltodextrin 32 and is packaged atstep 510. The result is a Type I collagen powder 50 with less than 10% moisture and 90% to 100% protein. - The Type I collagen 50 and
Type II collagen 33 powder may be blended at a 10% to 90% ratio and preferably a 50% to 50% ratio atstep 520.
Claims (20)
Priority Applications (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14/157,609 US20150203891A1 (en) | 2014-01-17 | 2014-01-17 | Method of Making Collagen Powder From Marine Cartilage and Skin |
| CA2877546A CA2877546A1 (en) | 2014-01-17 | 2015-01-13 | Method of making collagen powder from marine cartilage and skin |
| US14/623,718 US20150203569A1 (en) | 2014-01-17 | 2015-02-17 | Method of making collagen powder from marine cartilage and skin |
| US15/234,712 US10752671B2 (en) | 2014-01-17 | 2016-08-11 | Method of making collagen powder from marine cartilage and skin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14/157,609 US20150203891A1 (en) | 2014-01-17 | 2014-01-17 | Method of Making Collagen Powder From Marine Cartilage and Skin |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US14/623,718 Division US20150203569A1 (en) | 2014-01-17 | 2015-02-17 | Method of making collagen powder from marine cartilage and skin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| US20150203891A1 true US20150203891A1 (en) | 2015-07-23 |
Family
ID=53544208
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US14/157,609 Abandoned US20150203891A1 (en) | 2014-01-17 | 2014-01-17 | Method of Making Collagen Powder From Marine Cartilage and Skin |
| US14/623,718 Abandoned US20150203569A1 (en) | 2014-01-17 | 2015-02-17 | Method of making collagen powder from marine cartilage and skin |
| US15/234,712 Active 2035-05-23 US10752671B2 (en) | 2014-01-17 | 2016-08-11 | Method of making collagen powder from marine cartilage and skin |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US14/623,718 Abandoned US20150203569A1 (en) | 2014-01-17 | 2015-02-17 | Method of making collagen powder from marine cartilage and skin |
| US15/234,712 Active 2035-05-23 US10752671B2 (en) | 2014-01-17 | 2016-08-11 | Method of making collagen powder from marine cartilage and skin |
Country Status (2)
| Country | Link |
|---|---|
| US (3) | US20150203891A1 (en) |
| CA (1) | CA2877546A1 (en) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106755191A (en) * | 2016-11-30 | 2017-05-31 | 无锡甜丰食品有限公司 | A kind of utilization Chinese yam starch makes the preparation method of maltodextrin |
| US20190100785A1 (en) * | 2017-10-03 | 2019-04-04 | Robert den Hoed | Method of producing undenatured collagen from cartilage with low temperature hydrolysis |
| CN114106152B (en) * | 2022-01-26 | 2022-04-19 | 广州创尔生物技术股份有限公司 | A kind of method for preparing triple helix structure collagen by spray drying |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020018229A1 (en) * | 2000-07-26 | 2002-02-14 | Motohiro Nakamaki | Printer, printer control method, program therefor, and recording medium storing the program |
| US20020182290A1 (en) * | 2001-05-01 | 2002-12-05 | Novozymes A/S | Method for processing fish material |
| US6780841B2 (en) * | 2001-11-13 | 2004-08-24 | Biocell Technology, Llc | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
| US20070004629A1 (en) * | 2001-01-24 | 2007-01-04 | Stiles Terri L | K9 and equine joint health food supplement and method of administering |
| US20070000462A1 (en) * | 2005-06-30 | 2007-01-04 | Jongmin Lee | Method and apparatus for setting bias spring load during assembly of a camshaft phaser |
| US20130003547A1 (en) * | 2011-06-29 | 2013-01-03 | Cisco Technology, Inc. | Detecting and Mitigating Overload on Switches by Wireless Mobile Client Devices |
| US20130035473A1 (en) * | 2011-08-03 | 2013-02-07 | Dana Summers | Collagen mixture and method of making the same |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL87344A (en) * | 1988-08-04 | 1992-03-29 | Univ Bar Ilan | Process for the production of gelatin from fish skins |
-
2014
- 2014-01-17 US US14/157,609 patent/US20150203891A1/en not_active Abandoned
-
2015
- 2015-01-13 CA CA2877546A patent/CA2877546A1/en not_active Abandoned
- 2015-02-17 US US14/623,718 patent/US20150203569A1/en not_active Abandoned
-
2016
- 2016-08-11 US US15/234,712 patent/US10752671B2/en active Active
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020018229A1 (en) * | 2000-07-26 | 2002-02-14 | Motohiro Nakamaki | Printer, printer control method, program therefor, and recording medium storing the program |
| US20070004629A1 (en) * | 2001-01-24 | 2007-01-04 | Stiles Terri L | K9 and equine joint health food supplement and method of administering |
| US20020182290A1 (en) * | 2001-05-01 | 2002-12-05 | Novozymes A/S | Method for processing fish material |
| US6780841B2 (en) * | 2001-11-13 | 2004-08-24 | Biocell Technology, Llc | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
| US20070000462A1 (en) * | 2005-06-30 | 2007-01-04 | Jongmin Lee | Method and apparatus for setting bias spring load during assembly of a camshaft phaser |
| US20130003547A1 (en) * | 2011-06-29 | 2013-01-03 | Cisco Technology, Inc. | Detecting and Mitigating Overload on Switches by Wireless Mobile Client Devices |
| US20130035473A1 (en) * | 2011-08-03 | 2013-02-07 | Dana Summers | Collagen mixture and method of making the same |
Non-Patent Citations (1)
| Title |
|---|
| Wong et al., Collagen in the egg shell membranes of the hen, Abstract, Developmental Biology, Vol. 104, Issue 1, July 1984, pages 28-36 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2877546A1 (en) | 2015-07-17 |
| US20150203569A1 (en) | 2015-07-23 |
| US20160347820A1 (en) | 2016-12-01 |
| US10752671B2 (en) | 2020-08-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8470975B2 (en) | Collagen mixture and method of making the same | |
| US10752671B2 (en) | Method of making collagen powder from marine cartilage and skin | |
| CN109022527A (en) | A kind of quinoa polypeptide and preparation method thereof with hypotensive activity | |
| CN109371088A (en) | A kind of preparation method of sea cucumber active peptide | |
| CN103689212A (en) | Method for extracting small molecule peptide from fresh animal bone | |
| US20230050896A1 (en) | Marine-based gelatin powders and methods of making | |
| KR102214600B1 (en) | Functional composition comprsing low molecular collagen peptide extract from skate skin and Functional food comprising the same | |
| CN104774895B (en) | The method for preparing wood frog collagen | |
| US20130137854A1 (en) | Collagen mixture and method of making the same | |
| JP5044166B2 (en) | Method for producing extract of stem and / or branch of Ekokogi | |
| KR20150102865A (en) | Biocompatible Collagen and Methods for Preparing the Same | |
| CN115109816A (en) | Method for preparing elastin peptide, elastin peptide prepared thereby and uses thereof | |
| KR101462366B1 (en) | Preparing method of low-salted anchovy | |
| CN106942652A (en) | It is a kind of to improve immunity, strengthen the health-preserving food of resistance against diseases | |
| KR100887538B1 (en) | Manufacturing method of softening agent mixed with mushroom extract and kiwi | |
| CN106720801B (en) | Burdock tea rich in inulin | |
| CN105002246A (en) | Fish polypeptide with uniform molecular weight distribution, and preparation method thereof | |
| KR20200132276A (en) | Method for Separating Sericin Protein for Preventing or Treating Bone Diseases and Uses Thereof | |
| CN103305578B (en) | Method for preparing antihypertensive substances from visceral connective tissue of abalone | |
| RU2562581C1 (en) | Method of producing biologically active agent from sea cucumber, having general tonic and immunomodulating properties | |
| CN108887588B (en) | A kind of method that utilizes enzymatic method to prepare sheep bone meal | |
| KR101998647B1 (en) | A method for producing a dentifrice composition, and a dentifrice composition | |
| US20130217631A1 (en) | Collagen mixture and method of making the same | |
| CN110089616A (en) | A kind of processing method of selenium-rich hydrolysis rice protein cream and powder | |
| RU2816703C1 (en) | Method of producing fermented velvet antlers extract by three-step treatment |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: FINAL REJECTION MAILED |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: DOCKETED NEW CASE - READY FOR EXAMINATION |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: NON FINAL ACTION MAILED |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: RESPONSE TO NON-FINAL OFFICE ACTION ENTERED AND FORWARDED TO EXAMINER |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: FINAL REJECTION MAILED |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: DOCKETED NEW CASE - READY FOR EXAMINATION |
|
| STPP | Information on status: patent application and granting procedure in general |
Free format text: NON FINAL ACTION MAILED |
|
| STCB | Information on status: application discontinuation |
Free format text: ABANDONED -- FAILURE TO RESPOND TO AN OFFICE ACTION |