WO2006101301A1 - Calcium binding amino acid - Google Patents
Calcium binding amino acid Download PDFInfo
- Publication number
- WO2006101301A1 WO2006101301A1 PCT/KR2005/003848 KR2005003848W WO2006101301A1 WO 2006101301 A1 WO2006101301 A1 WO 2006101301A1 KR 2005003848 W KR2005003848 W KR 2005003848W WO 2006101301 A1 WO2006101301 A1 WO 2006101301A1
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- WIPO (PCT)
- Prior art keywords
- calcium
- amino acid
- bone
- bound
- peptides
- Prior art date
Links
- 150000001413 amino acids Chemical class 0.000 title claims abstract description 44
- 102000005701 Calcium-Binding Proteins Human genes 0.000 title claims description 8
- 108010045403 Calcium-Binding Proteins Proteins 0.000 title claims description 8
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims abstract description 86
- 239000011575 calcium Substances 0.000 claims abstract description 86
- 229910052791 calcium Inorganic materials 0.000 claims abstract description 86
- 210000000988 bone and bone Anatomy 0.000 claims abstract description 62
- 241000251468 Actinopterygii Species 0.000 claims abstract description 45
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 42
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 37
- 238000002360 preparation method Methods 0.000 claims abstract description 19
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 claims abstract description 11
- 239000011574 phosphorus Substances 0.000 claims abstract description 11
- 229910052698 phosphorus Inorganic materials 0.000 claims abstract description 11
- 241000283690 Bos taurus Species 0.000 claims abstract description 8
- 241001465754 Metazoa Species 0.000 claims abstract description 5
- 235000019688 fish Nutrition 0.000 claims description 43
- 150000007524 organic acids Chemical class 0.000 claims description 13
- 239000000463 material Substances 0.000 claims description 7
- 102000004169 proteins and genes Human genes 0.000 claims description 7
- 108090000623 proteins and genes Proteins 0.000 claims description 7
- 102000008186 Collagen Human genes 0.000 claims description 5
- 108010035532 Collagen Proteins 0.000 claims description 5
- 229920001436 collagen Polymers 0.000 claims description 5
- 238000003756 stirring Methods 0.000 claims description 5
- 239000006228 supernatant Substances 0.000 claims description 5
- 241001454694 Clupeiformes Species 0.000 claims description 4
- 235000019513 anchovy Nutrition 0.000 claims description 4
- 210000001519 tissue Anatomy 0.000 claims description 4
- 241000251730 Chondrichthyes Species 0.000 claims description 3
- 241000287828 Gallus gallus Species 0.000 claims description 3
- 210000000845 cartilage Anatomy 0.000 claims description 3
- 238000004108 freeze drying Methods 0.000 claims description 2
- 230000002797 proteolythic effect Effects 0.000 claims description 2
- 238000001694 spray drying Methods 0.000 claims description 2
- 239000000843 powder Substances 0.000 abstract description 15
- 238000010521 absorption reaction Methods 0.000 abstract description 14
- 239000000126 substance Substances 0.000 abstract description 8
- 239000003795 chemical substances by application Substances 0.000 abstract description 6
- 230000001737 promoting effect Effects 0.000 abstract description 6
- 108010001441 Phosphopeptides Proteins 0.000 abstract description 5
- 239000005018 casein Substances 0.000 abstract description 5
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 abstract description 5
- 235000021240 caseins Nutrition 0.000 abstract description 5
- 230000026731 phosphorylation Effects 0.000 abstract description 5
- 238000006366 phosphorylation reaction Methods 0.000 abstract description 5
- 102000002322 Egg Proteins Human genes 0.000 abstract description 4
- 108010000912 Egg Proteins Proteins 0.000 abstract description 4
- 210000003278 egg shell Anatomy 0.000 abstract description 4
- 208000001132 Osteoporosis Diseases 0.000 abstract description 3
- 235000014653 Carica parviflora Nutrition 0.000 abstract description 2
- 241000243321 Cnidaria Species 0.000 abstract description 2
- 230000000694 effects Effects 0.000 abstract description 2
- 230000001939 inductive effect Effects 0.000 abstract description 2
- 230000000295 complement effect Effects 0.000 abstract 1
- 235000015872 dietary supplement Nutrition 0.000 abstract 1
- 235000013373 food additive Nutrition 0.000 abstract 1
- 239000002778 food additive Substances 0.000 abstract 1
- 230000002787 reinforcement Effects 0.000 abstract 1
- 229960005069 calcium Drugs 0.000 description 68
- 238000000034 method Methods 0.000 description 16
- 239000000047 product Substances 0.000 description 16
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 15
- 238000000605 extraction Methods 0.000 description 13
- 230000007062 hydrolysis Effects 0.000 description 11
- 238000006460 hydrolysis reaction Methods 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 239000000203 mixture Substances 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 7
- 102000004157 Hydrolases Human genes 0.000 description 7
- 108090000604 Hydrolases Proteins 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 6
- 102000011632 Caseins Human genes 0.000 description 5
- 108010076119 Caseins Proteins 0.000 description 5
- 239000001506 calcium phosphate Substances 0.000 description 5
- 229910000389 calcium phosphate Inorganic materials 0.000 description 5
- 235000011010 calcium phosphates Nutrition 0.000 description 5
- 230000015556 catabolic process Effects 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 5
- 238000001035 drying Methods 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 238000011282 treatment Methods 0.000 description 4
- 102000008934 Muscle Proteins Human genes 0.000 description 3
- 108010074084 Muscle Proteins Proteins 0.000 description 3
- 102000057297 Pepsin A Human genes 0.000 description 3
- 108090000284 Pepsin A Proteins 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 3
- 229910000019 calcium carbonate Inorganic materials 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 3
- 235000013372 meat Nutrition 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 3
- 229940111202 pepsin Drugs 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 235000013361 beverage Nutrition 0.000 description 2
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 2
- 239000001639 calcium acetate Substances 0.000 description 2
- 235000011092 calcium acetate Nutrition 0.000 description 2
- 229960005147 calcium acetate Drugs 0.000 description 2
- FNAQSUUGMSOBHW-UHFFFAOYSA-H calcium citrate Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O.[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O FNAQSUUGMSOBHW-UHFFFAOYSA-H 0.000 description 2
- 239000001354 calcium citrate Substances 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000002329 infrared spectrum Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000000813 small intestine Anatomy 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- 235000019640 taste Nutrition 0.000 description 2
- 235000013337 tricalcium citrate Nutrition 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 208000017667 Chronic Disease Diseases 0.000 description 1
- 208000035150 Hypercholesterolemia Diseases 0.000 description 1
- 208000031226 Hyperlipidaemia Diseases 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000001354 calcination Methods 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229960004256 calcium citrate Drugs 0.000 description 1
- MKJXYGKVIBWPFZ-UHFFFAOYSA-L calcium lactate Chemical compound [Ca+2].CC(O)C([O-])=O.CC(O)C([O-])=O MKJXYGKVIBWPFZ-UHFFFAOYSA-L 0.000 description 1
- 239000001527 calcium lactate Substances 0.000 description 1
- 229960002401 calcium lactate Drugs 0.000 description 1
- 235000011086 calcium lactate Nutrition 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 235000015165 citric acid Nutrition 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- -1 coral calcium Chemical compound 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 210000001198 duodenum Anatomy 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 210000003608 fece Anatomy 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 239000000413 hydrolysate Substances 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 238000011221 initial treatment Methods 0.000 description 1
- 229910021432 inorganic complex Inorganic materials 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 239000011147 inorganic material Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 230000031146 intracellular signal transduction Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 210000004877 mucosa Anatomy 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000004118 muscle contraction Effects 0.000 description 1
- 235000003715 nutritional status Nutrition 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
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- 235000019515 salmon Nutrition 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof
- A23L17/65—Addition of, or treatment with, microorganisms or enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/16—Inorganic salts, minerals or trace elements
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2200/00—Function of food ingredients
- A23V2200/30—Foods, ingredients or supplements having a functional effect on health
Definitions
- Calcium is the most abundant inorganic element in human body, and is contained in an amount of about 1200 g, which is about 2% of the body weight of an average adult. Calcium is distributed in the body such that 99% is used to form the skeleton and teeth, while only 1% is used in the physiological activity regulating functions such as contraction and relaxation of muscles, regular heartbeat, blood coagulation, activation of enzymes, and intracellular signal transduction for stimulation and excitation.
- calcium takes an important role of reducing the occurrence of osteoporosis as well as chronic diseases such as hypercholesterolemia, arterial sclerosis, hyperlipidemia, hypertension and the like, and thus the nutritional status of calcium should be always maintained at an appropriate level.
- the daily recommended calcium intake is approximately 700 mg, and this implies that calcium intake through food ingestion is very important.
- the calcium absorption rate in the body is so low that, in an adult, only 30% or less on the average, and 45% at the maximum, of the daily recommended intake is substantially taken in.
- calcium in order for calcium to be absorbed in the body, calcium must exist in a soluble form upon passing through the mucosal cells in the small intestine where calcium is absorbed, and calcium can be absorbed only in an ionic state.
- the pH environment in the small intestine is mildly basic, and it is almost impossible for inorganic calcium to exist in the ionic state.
- calcium can maintain the ionic state in the mucosa only by means of a specially structured material.
- the ions generated in the stomach fail to be protected by compounds having particular structures, the ions bind with an excess of phosphoric acid while passing through the duodenum, so as to form non-absorbable inorganic calcium phosphate, which is excreted with feces.
- Representative commercial calcium formulations are supplied as chemically synthesized products in the forms of non-soluble calcium salts such as calcium carbonate and calcium phosphate, and of soluble salts such as calcium chloride, calcium citrate and calcium acetate, and as natural calcium formulations in the form of simply processed non-soluble calcium obtained by pulverization and calcination of bovine bone powder, fish bone powder, egg shell powder, clam shell powder, coral powder and the like.
- 6-319487 suggests a method for preparing water-soluble calcium by immersing fish bone in acetic acid to soften the bone.
- this method involves complicated processes, and the product can be used only in liquid type beverages, thus limiting the use. Accordingly, the method is not widely used.
- CPP casein phosphopeptide
- USP 4,358,465 (1982) Japanese Published Patent Application No. 2-7616 (1990) and the like.
- These technologies are substantially identical in the principle and fundamental process, with slight differences lying only in the types of the enzymes that are used for breakdown of casein sodium, and in the separation and purification methods.
- the fundamental process consists of the steps of hydrolysis, separation and purification, and the step of artificially inducing the binding of chemically synthesized calcium with CPP and then drying.
- Natural calcium materials that are currently used for commercial purposes include calcium carbonate such as coral calcium, clam shell calcium and egg shell calcium, and calcium phosphate such as cattle bone power and fish bone powder; however, cattle bone powder is substantially out of use because of the mad cow disease, and egg shell calcium and clam shell calcium are under the same circumstances because of the warnings by FDA and the like on heavy metal contamination, and the problem of absorption rate.
- Sparingly soluble calcium products such as calcium carbonate and calcium phosphate that are used as synthetic chemical products, precipitate upon addition into milk or the like, thus revealing the defective stability of the product
- water-soluble calcium products such as calcium lactate, calcium citrate and calcium acetate cause a serious change in taste upon addition of certain amounts, and reveal critical disadvantages such as generation of aggregates, increase in the viscosity during heat treatment processes, and increase in the bitter taste due to gelation, all resulting from the reaction of calcium with the casein protein in milk.
- CPP casein phosphopeptide
- CPP casein phosphopeptide
- the basic type CPP which is a peptide for absorption promotion
- the upgraded type CPP which is the basic type CPP bound with artificially added calcium.
- these CPP products are limited in use because of complicated production processes and expensive prices.
- the present invention provides a preparation of amino acid-bound calcium as a safety-verified natural calcium material, which is water-soluble, and upon addition to a milk product, does not cause any change in taste or any changes affecting the product stability such as precipitation or binding, and which can be produced by a simple and efficient process.
- the amino acid-bound calcium preparation according to the invention is a natural calcium preparation of high concentration which can be produced from fish bone frame, a natural calcium material, in the form of amino acid-bound calcium having excellent absorption rate in human body, and which does not require combined use of a calcium absorption promoting agent.
- Fig. 1 is a graph indicating the degrees of hydrolysis under different conditions to determine the optimal conditions for extracting inorganic calcium and amino acid peptides from fish bone frame.
- Fig. 2 is a graph indicating the calcium recovery rates under different conditions to determine the optimal conditions for preparing amino acid-bound calcium from fish bone frame.
- Fig. 3 is a graph indicating the IR spectral result verifying the presence or absence of phosphorylation of amino acid peptides to confirm the binding ability of extracted calcium and the amino peptides.
- the present invention provides an amino acid-bound calcium preparation which is produced by simultaneously reacting fish bone frame with an edible organic acid and a protein hydrolase, so as to dissolve out phosphorus and calcium from the fish bone frame and to break down protein to amino acid peptides.
- the amino acid peptides thus generated then binds with the extracted phosphorus to be phosphorylated, and subsequently the phosphorylated amino acid peptides in turn binds with the calcium.
- 1% of the fish bone frame relative to a 1 to 10% solution of the organic acid, and 1% of the hydrolase relative to the amount of the fish bone frame, in the reaction with stirring for 4 to 12 hours.
- 1% of the fish bone frame relative to a 1 to 10% solution of the organic acid, and 1% of the hydrolase relative to the amount of the fish bone frame, in the reaction with stirring for 4 to 12 hours.
- 1% (based on dry weight) of wet pulverized fish (hoki) bone frame relative to a 10% acetic acid solution (pH 2.0 to 2.2), and 1% (relative to the amount of the fish bone frame) of an enzyme (pepsin) were introduced into a reactor equipped with a stirrer. The mixture was allowed to react at 40 0 C for 12 hours with mild stirring, and then filtered and centrifuged to separate the supernatant, thereby preparing a hydrolyzed peptide composition containing a large amount of inorganic substances.
- a control group to which the enzyme was not added and another control group to which the organic acid was not added were established under the same reaction conditions except the components not added, and the degrees of hydrolysis and the calcium recovery rates were compared.
- the degree of hydrolysis of the fish bone frame was about 25% and about 40% for the cases of treatment with the organic acid and treatment with the hydrolase, respectively, while about 70% of hydrolysis occurred in the case of combined treatment with the organic acid and the enzyme.
- a composition of non-phosphorylated peptides was prepared under the same reaction conditions as described above, using a substrate consisting only of muscle proteins (hoki, meat only), with the fish bone component completely removed.
- the IR spectra of the prepared compositions were compared to verify the phosphorylation status.
- the difference between the non-phosphorylated peptides and the phosphorylated peptides was found in the region of 1 ,000 to 1 ,300 cm " ' of the IR spectrum corresponding to the presence of phosphoric acid group, and the peaks appeared in the spectrum of the phosphorylated peptides but not in the spectrum of the non-phosphorylated peptides.
- the present invention can also make use of shark cartilage, cattle bone, pig bone, chicken bone, fresh anchovy, dried anchovy and the like, in addition to the fish bone frame.
- the fish bone frame (fish bone with muscle proteins attached) used in the present invention as a raw material for natural calcium was mainly composed of the fish bone and muscle proteins attached thereto after a primary treatment of fish in a fish processing factory (removal of fish meat for fish cutlet products, removal of fish meat from tuna, salmon and the like for sashimi), and was used after storage in a freezer at - 30 0 C.
- the bone in living organisms consists of collagen, non-collagenous proteins and inorganic complex hydroxyapatite (Ca ⁇ 0 (PO 4 ) 6 (OH) 2 ).
- the collagen constituting the bone forms a strong complex with the inorganic constituent hydroxyapatite and thus can be hardly broken down by general enzymes, but the organic acid makes it possible to dissolve out calcium and phosphorus, which are the main constituents of hydroxyapatite.
- acetic acid facilitates extraction of collagen, thus leading to effective breakdown of muscle and bone proteins, and easy recovery of calcium together with the protein breakdown products.
- the edible organic acid to be used in the present invention is not limited, but is most preferably acetic acid (5 to 10%, pH 2-3).
- Other useful examples include edible lactic acid, citric acid, formic acid and the like.
- the hydrolase used for the hydrolysis together with the organic acid may be any enzyme that does not undergo deactivation in an acidic environment which satisfies the above-described conditions, and examples thereof include pepsin and trypsin.
- the concentration of substrate may be suitably 1 to 10%
- the concentration of enzyme to be introduced may be 1 to 5% relative to the concentration of the substrate
- the time required for hydrolysis and extraction may be 4 to 12 hours, while these conditions may be appropriately determined within the ranges described above in consideration of economic aspects.
- the phosphorus dissolved out during the extraction process becomes directly involved in phosphorylation of the amino acid peptides which are a partial hydrolysate of proteins generated through enzymatic breakdown, immediately after their dissolution, so as to form phosphorylated amino acid peptides.
- the strong affinity of the formed phosphorylated amino acid peptides adsorb calcium which has been dissolved out together with the phosphorus during the extraction process, so as to form amino acid- bound calcium.
- the calcium-binding phosphopeptides (CBPP) formed through the extraction and binding processes described above are separate and purified by filtration, and only the fraction of calcium-binding phosphopeptides having a molecular weight of 10,000 Da or less is collected and subjected to freeze drying or spray drying.
- the CBPP prepared by the method according to the present invention is a natural water-soluble calcium preparation of high concentration in the form of inorganic substances such as calcium binding with amino acids.
- the calcium preparation is a material excellent in the safety aspect, and can be used per se as a raw material for beverages, diet supplements and pharmaceutical products, without the necessity of combined use of a calcium absorption promoting agent.
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Abstract
There is provided a functional preparation of amino acid-bound calcium comprising natural calcium bound with amino acid peptides, which is prepared by simultaneously extracting amino acid peptides and natural inorganic substances such as calcium and phosphorus from animal bone tissues, particularly fresh fish bone frame, and then inducing phosphorylation of the amino acid peptides as well as binding of the resulting phosphorylated amino acid peptides with the extracted calcium. The amino acid-bound calcium preparation thus produced contains water-soluble calcium; therefore, it solves the problem of calcium absorption rate of the conventional natural calcium preparations (claim shell powder, egg shell powder, fish bone powder, cattle bone powder, coral powder, etc.) due to their insolubility and at the same time, satisfies per se the effect of addition of casein phosphopeptides that are widely used as a commercial calcium absorption promoting agent to complement the low absorption rate problem. Thus, the amino acid-bound calcium preparation of the invention can be widely used as an agent for treating osteoporosis, and as a food supplement and a food additive for calcium reinforcement that are effective for osteoporosis.
Description
CALCIUM BINDING AMINO ACID
TECHNICAL FIELD
Calcium is the most abundant inorganic element in human body, and is contained in an amount of about 1200 g, which is about 2% of the body weight of an average adult. Calcium is distributed in the body such that 99% is used to form the skeleton and teeth, while only 1% is used in the physiological activity regulating functions such as contraction and relaxation of muscles, regular heartbeat, blood coagulation, activation of enzymes, and intracellular signal transduction for stimulation and excitation.
In particular, calcium takes an important role of reducing the occurrence of osteoporosis as well as chronic diseases such as hypercholesterolemia, arterial sclerosis, hyperlipidemia, hypertension and the like, and thus the nutritional status of calcium should be always maintained at an appropriate level. The daily recommended calcium intake is approximately 700 mg, and this implies that calcium intake through food ingestion is very important. However, even though food containing calcium is taken in, the calcium absorption rate in the body is so low that, in an adult, only 30% or less on the average, and 45% at the maximum, of the daily recommended intake is substantially taken in.
According to a general theory of calcium intake, in order for calcium to be absorbed in the body, calcium must exist in a soluble form upon passing through the
mucosal cells in the small intestine where calcium is absorbed, and calcium can be absorbed only in an ionic state. However, the pH environment in the small intestine is mildly basic, and it is almost impossible for inorganic calcium to exist in the ionic state. Thus, calcium can maintain the ionic state in the mucosa only by means of a specially structured material. That is, when the water-soluble mineral ions generated in the stomach fail to be protected by compounds having particular structures, the ions bind with an excess of phosphoric acid while passing through the duodenum, so as to form non-absorbable inorganic calcium phosphate, which is excreted with feces.
BACKGROUND ART
Representative commercial calcium formulations are supplied as chemically synthesized products in the forms of non-soluble calcium salts such as calcium carbonate and calcium phosphate, and of soluble salts such as calcium chloride, calcium citrate and calcium acetate, and as natural calcium formulations in the form of simply processed non-soluble calcium obtained by pulverization and calcination of bovine bone powder, fish bone powder, egg shell powder, clam shell powder, coral powder and the like.
It has been found that the breakdown product resulting from trypsin-mediated hydrolysis of casein, a milk protein, binds to metal ions such as calcium and iron to form a soluble complex, thus exerting an effect of preventing the formation of insoluble substances such as calcium phosphate which is excreted out from the body (Reeves et al, Science. 128:474 (1958)).
Among patented technologies in the related art, for example, there are known methods for preparing fish bone powder by separating bones from fish and drying them
(Japanese Laid-Open Patent Applications No. 2-231059 and No. 4-121166), but large quantities of energy are needed for drying moisture. Also known is a method for preparing fish bone powder by washing the central bone part of fish with high-pressure water, hydrolyzing any remaining protein with proteases, removing the hydrolysis product by washing, drying the resulting substance by vacuum heating evaporation and grinding (Japanese Laid-Open Patent Application No. 2-231059), but the product thus prepared has low content of calcium. On the other hand, in order to solve the problems described above, Japanese Laid-Open Patent Application No. 6-319487 suggests a method for preparing water-soluble calcium by immersing fish bone in acetic acid to soften the bone. However, this method involves complicated processes, and the product can be used only in liquid type beverages, thus limiting the use. Accordingly, the method is not widely used.
Among Korean patented technologies in the related art, methods for preparing fish bone powder, water-soluble calcium and calcium absorption promoting peptides are disclosed in KP 10-0403284, KP 10-0399722 and the like. However, processes such as extraction of specific hydrolases from tuna guts are complicated, and water-soluble calcium preparations are of low product yield, thus it being difficult for the products to be widely used from an economical viewpoint.
In addition, prior art technologies for preparing CPP (casein phosphopeptide), which is a calcium absorption promoting agent widely used over the world, include USP 4,358,465 (1982), Japanese Published Patent Application No. 2-7616 (1990) and the like. These technologies are substantially identical in the principle and fundamental process, with slight differences lying only in the types of the enzymes that are used for breakdown of casein sodium, and in the separation and purification methods. The
fundamental process consists of the steps of hydrolysis, separation and purification, and the step of artificially inducing the binding of chemically synthesized calcium with CPP and then drying.
DETAILED DESCRIPTION OF THE INVENTION
Natural calcium materials that are currently used for commercial purposes include calcium carbonate such as coral calcium, clam shell calcium and egg shell calcium, and calcium phosphate such as cattle bone power and fish bone powder; however, cattle bone powder is substantially out of use because of the mad cow disease, and egg shell calcium and clam shell calcium are under the same circumstances because of the warnings by FDA and the like on heavy metal contamination, and the problem of absorption rate. Sparingly soluble calcium products such as calcium carbonate and calcium phosphate that are used as synthetic chemical products, precipitate upon addition into milk or the like, thus revealing the defective stability of the product, whereas water-soluble calcium products such as calcium lactate, calcium citrate and calcium acetate cause a serious change in taste upon addition of certain amounts, and reveal critical disadvantages such as generation of aggregates, increase in the viscosity during heat treatment processes, and increase in the bitter taste due to gelation, all resulting from the reaction of calcium with the casein protein in milk.
Meanwhile, CPP (casein phosphopeptide) is the only available material widely used for commercial purposes as a water-soluble calcium absorption promoting agent. There are two types of CPP, namely, the basic type CPP which is a peptide for absorption promotion, and the upgraded type CPP which is the basic type CPP bound with artificially added calcium. However, these CPP products are limited in use
because of complicated production processes and expensive prices.
DISCLOSURE OF THE INVENTION
It is an object of the present invention to solve the problems described above, and thus the present invention provides a preparation of amino acid-bound calcium as a safety-verified natural calcium material, which is water-soluble, and upon addition to a milk product, does not cause any change in taste or any changes affecting the product stability such as precipitation or binding, and which can be produced by a simple and efficient process.
As described above, the amino acid-bound calcium preparation according to the invention is a natural calcium preparation of high concentration which can be produced from fish bone frame, a natural calcium material, in the form of amino acid-bound calcium having excellent absorption rate in human body, and which does not require combined use of a calcium absorption promoting agent.
BRIEF DESCRIPTION OF DRAWINGS
Fig. 1 is a graph indicating the degrees of hydrolysis under different conditions to determine the optimal conditions for extracting inorganic calcium and amino acid peptides from fish bone frame.
Fig. 2 is a graph indicating the calcium recovery rates under different conditions to determine the optimal conditions for preparing amino acid-bound calcium from fish bone frame.
Fig. 3 is a graph indicating the IR spectral result verifying the presence or absence of phosphorylation of amino acid peptides to confirm the binding ability of
extracted calcium and the amino peptides.
Best Mode For Carrying Out The Invention
In order to achieve the objects described above, the present invention provides an amino acid-bound calcium preparation which is produced by simultaneously reacting fish bone frame with an edible organic acid and a protein hydrolase, so as to dissolve out phosphorus and calcium from the fish bone frame and to break down protein to amino acid peptides. The amino acid peptides thus generated then binds with the extracted phosphorus to be phosphorylated, and subsequently the phosphorylated amino acid peptides in turn binds with the calcium.
It is preferable to use 1% of the fish bone frame relative to a 1 to 10% solution of the organic acid, and 1% of the hydrolase relative to the amount of the fish bone frame, in the reaction with stirring for 4 to 12 hours.
It is preferable to use 1% of the fish bone frame relative to a 1 to 10% solution of the organic acid, and 1% of the hydrolase relative to the amount of the fish bone frame, in the reaction with stirring for 4 to 12 hours.
Furthermore, it is also preferable to filter the phosphorylated amino acid peptides that are bound with calcium, to centrifuge the filtrate and take the supernatant, and then to freeze-dry or spray-dry the supernatant.
It is also preferable to use any one selected from shark cartilage, cattle bone, pig bone and chicken bone, instead of the fish bone frame.
EXAMPLE 1
Preparation of hydrolyzed peptides and extraction of calcium from fish bone
frame
1% (based on dry weight) of wet pulverized fish (hoki) bone frame relative to a 10% acetic acid solution (pH 2.0 to 2.2), and 1% (relative to the amount of the fish bone frame) of an enzyme (pepsin) were introduced into a reactor equipped with a stirrer. The mixture was allowed to react at 400C for 12 hours with mild stirring, and then filtered and centrifuged to separate the supernatant, thereby preparing a hydrolyzed peptide composition containing a large amount of inorganic substances.
Meanwhile, in order to determine the optimal hydrolysis conditions and inorganic substance extraction conditions, a control group to which the enzyme was not added and another control group to which the organic acid was not added (distilled water. pH adjusted) were established under the same reaction conditions except the components not added, and the degrees of hydrolysis and the calcium recovery rates were compared.
As shown by the results indicated in Fig. 1 , the degree of hydrolysis of the fish bone frame was about 25% and about 40% for the cases of treatment with the organic acid and treatment with the hydrolase, respectively, while about 70% of hydrolysis occurred in the case of combined treatment with the organic acid and the enzyme.
On the other hand, the rates of calcium recovery from the fish bone frame were compared as shown in Fig. 2, and the highest calcium content and calcium yield were obtained in the case of combining treatments with the organic acid and the enzyme. EXAMPLE 2
Preparation of calcium extracted from fish bone frame, and phosphorylated amino acid peptides from phosphorus and hydrolyzed amino acid peptides (calcium binding peptide: amino acid peptide: CBPP)
1% of (based on dry weight) of wet pulverized fish (hoki) bone frame relative to a 10% acetic acid solution (pH 2.0 to 2.2) and 1% (relative to the amount of the fish bone frame) of an enzyme (pepsin) were introduced into a reactor equipped with a stirrer. The mixture was allowed to react at 400C for 12 hours with mild stirring, and then filtered and centrifuged to separate the supernatant, thereby preparing a phosphorylated peptide composition containing a large amount of inorganic substances.
In addition to that, in order to establish a control group for non-phosphorylated peptides, a composition of non-phosphorylated peptides was prepared under the same reaction conditions as described above, using a substrate consisting only of muscle proteins (hoki, meat only), with the fish bone component completely removed.
Since the calcium binding ability of the hydrolyzed amino acid peptides is determined by the presence or absence of phosphorylation of amino acid peptides, the IR spectra of the prepared compositions were compared to verify the phosphorylation status.
As shown in Fig. 3, the difference between the non-phosphorylated peptides and the phosphorylated peptides was found in the region of 1 ,000 to 1 ,300 cm"' of the IR spectrum corresponding to the presence of phosphoric acid group, and the peaks appeared in the spectrum of the phosphorylated peptides but not in the spectrum of the non-phosphorylated peptides. The absorption band for the P=O bond appeared at around 1 ,300 cm"', that of the P-O-C bond appeared at around 1 ,100 to 1,200 cm"', and that of the -O-P group bonded to an alkyl group appeared at around 1,000 cm"1. These absorption bands were not confirmed in the non-phosphorylated peptides, but were confirmed in all samples of phosphorylated peptides.
The present invention can also make use of shark cartilage, cattle bone, pig
bone, chicken bone, fresh anchovy, dried anchovy and the like, in addition to the fish bone frame.
According to the present invention, it is also possible to prepare using animal bone tissues as well as skin tissues, amino acid-bound calcium containing amino acid peptides derived from collagen, which is a component constituting the animal bone tissues and skin tissues.
INDUSTRIAL APPLICABILITY
The fish bone frame (fish bone with muscle proteins attached) used in the present invention as a raw material for natural calcium, was mainly composed of the fish bone and muscle proteins attached thereto after a primary treatment of fish in a fish processing factory (removal of fish meat for fish cutlet products, removal of fish meat from tuna, salmon and the like for sashimi), and was used after storage in a freezer at - 300C.
In the present invention, extraction of inorganic calcium and phosphorus, and extraction of organic amino acid peptides were carried out simultaneously in a combined extraction process for dissolution of calcium and phosphorus by an edible organic acid and for extraction of amino acid peptides by a proteolytic hydrolase. The bone in living organisms consists of collagen, non-collagenous proteins and inorganic complex hydroxyapatite (Caι0(PO4)6(OH)2). The collagen constituting the bone forms a strong complex with the inorganic constituent hydroxyapatite and thus can be hardly broken down by general enzymes, but the organic acid makes it possible to dissolve out calcium and phosphorus, which are the main constituents of hydroxyapatite. In particular, acetic acid facilitates extraction of collagen, thus leading to effective
breakdown of muscle and bone proteins, and easy recovery of calcium together with the protein breakdown products.
The edible organic acid to be used in the present invention is not limited, but is most preferably acetic acid (5 to 10%, pH 2-3). Other useful examples include edible lactic acid, citric acid, formic acid and the like.
The hydrolase used for the hydrolysis together with the organic acid may be any enzyme that does not undergo deactivation in an acidic environment which satisfies the above-described conditions, and examples thereof include pepsin and trypsin.
During the processes of hydrolysis of fish bone frame and extraction of inorganic materials, the concentration of substrate may be suitably 1 to 10%, the concentration of enzyme to be introduced may be 1 to 5% relative to the concentration of the substrate, and the time required for hydrolysis and extraction may be 4 to 12 hours, while these conditions may be appropriately determined within the ranges described above in consideration of economic aspects.
The phosphorus dissolved out during the extraction process becomes directly involved in phosphorylation of the amino acid peptides which are a partial hydrolysate of proteins generated through enzymatic breakdown, immediately after their dissolution, so as to form phosphorylated amino acid peptides. The strong affinity of the formed phosphorylated amino acid peptides adsorb calcium which has been dissolved out together with the phosphorus during the extraction process, so as to form amino acid- bound calcium.
The calcium-binding phosphopeptides (CBPP) formed through the extraction and binding processes described above are separate and purified by filtration, and only the fraction of calcium-binding phosphopeptides having a molecular weight of 10,000
Da or less is collected and subjected to freeze drying or spray drying.
The CBPP prepared by the method according to the present invention is a natural water-soluble calcium preparation of high concentration in the form of inorganic substances such as calcium binding with amino acids. The calcium preparation is a material excellent in the safety aspect, and can be used per se as a raw material for beverages, diet supplements and pharmaceutical products, without the necessity of combined use of a calcium absorption promoting agent.
Claims
1. An amino acid-bound calcium preparation produced by simultaneously reacting fish bone frame with an edible organic acid and a proteolytic hydrolase to dissolve out phosphorus and calcium from the fish bone frame and to break down the proteins to amino acid peptides, thus resulting in binding of the amino acid peptides with the phosphorus to phosphorylate the amino acid peptides and subsequent binding of the phosphorylated amino acid peptides with the calcium.
2. The amino acid-bound calcium preparation according to claim 1, wherein 1 % of the fish bone frame relative to a 1 to 10% solution of the organic acid, and 1% of the hydrolase relative to the amount of the fish bone frame are reacted with stirring for 4 to 12 hours.
3. The amino acid-bound calcium preparation according to claim 1 or 2, wherein the calcium-binding phosphorylated amino acid peptides are filtered and centrifuged, and the supernatant obtained therefrom is subjected to freeze-drying or spray-drying.
4. The amino acid-bound calcium preparation according to claim 1, wherein a material selected from shark cartilage, cattle bone, pig bone, chicken bone, fresh anchovy and dried anchovy is used instead of the fish bone frame.
5. The amino acid-bound calcium preparation according to claim 1, wherein the preparation is prepared using animal bone tissues and skin tissues instead of the fish bone frame so as to contain amino acid peptides derived from collagen, which is a component constituting the animal bone tissues and skin tissues.
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| KR20050023889 | 2005-03-03 | ||
| KR10-2005-0023889 | 2005-03-23 |
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Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103211229A (en) * | 2013-04-25 | 2013-07-24 | 福建永生活力生物工程有限公司 | Health food for increasing bone mineral density and preparation method thereof |
| CN104982937A (en) * | 2015-07-31 | 2015-10-21 | 中科和素（天津）医药科技有限公司 | Composition for promoting sclerotin and periosteum repairing and preparation method thereof |
| CN105211892A (en) * | 2015-11-14 | 2016-01-06 | 中国海洋大学 | A kind of fish-bone calcium peptide chelate complex and preparation method thereof |
| CN110604313A (en) * | 2019-09-30 | 2019-12-24 | 浙江海洋大学 | Method for preparing high-protein high-calcium supplement by using mussel waste materials |
| CN111165827A (en) * | 2020-02-26 | 2020-05-19 | 福建鼍龙实业有限责任公司 | Crocodile peptide chelated calcium and preparation method and application thereof |
| CN112006287A (en) * | 2020-07-30 | 2020-12-01 | 华中农业大学 | High-calcium high-collagen food and preparation method thereof |
| KR20210133826A (en) * | 2020-04-29 | 2021-11-08 | 주식회사 대호 | Manufacturing method of growth promoters for livestock |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN109123062A (en) * | 2018-06-22 | 2019-01-04 | 青岛海洋生物医药研究院股份有限公司 | A kind of preparation method and application of peptide calcium chelate |
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| JPH0416165A (en) * | 1990-05-08 | 1992-01-21 | Snow Brand Milk Prod Co Ltd | Preparation of bone-fortifying food, feed and medicine and bone peptide and protein mixture to be used therein |
| KR20020019784A (en) * | 2000-09-07 | 2002-03-13 | 김세권 | Preparation of fish bone powder and calcium absorption accelerating peptide using the enzyme from fish processing waste |
| KR20020019783A (en) * | 2000-09-07 | 2002-03-13 | 한영호 | A method for extracting water-soluble calcium from fish bone |
| KR20040074598A (en) * | 2003-02-19 | 2004-08-25 | 나카가와모모키 | Method of producing protein hydrolysates from fish scale |
-
2005
- 2005-11-14 KR KR1020077000101A patent/KR20070069123A/en not_active Application Discontinuation
- 2005-11-14 WO PCT/KR2005/003848 patent/WO2006101301A1/en active Application Filing
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0416165A (en) * | 1990-05-08 | 1992-01-21 | Snow Brand Milk Prod Co Ltd | Preparation of bone-fortifying food, feed and medicine and bone peptide and protein mixture to be used therein |
| KR20020019784A (en) * | 2000-09-07 | 2002-03-13 | 김세권 | Preparation of fish bone powder and calcium absorption accelerating peptide using the enzyme from fish processing waste |
| KR20020019783A (en) * | 2000-09-07 | 2002-03-13 | 한영호 | A method for extracting water-soluble calcium from fish bone |
| KR20040074598A (en) * | 2003-02-19 | 2004-08-25 | 나카가와모모키 | Method of producing protein hydrolysates from fish scale |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103211229A (en) * | 2013-04-25 | 2013-07-24 | 福建永生活力生物工程有限公司 | Health food for increasing bone mineral density and preparation method thereof |
| CN104982937A (en) * | 2015-07-31 | 2015-10-21 | 中科和素（天津）医药科技有限公司 | Composition for promoting sclerotin and periosteum repairing and preparation method thereof |
| CN105211892A (en) * | 2015-11-14 | 2016-01-06 | 中国海洋大学 | A kind of fish-bone calcium peptide chelate complex and preparation method thereof |
| CN105211892B (en) * | 2015-11-14 | 2017-12-19 | 中国海洋大学 | A kind of fish-bone calcium peptide chelate complex and preparation method thereof |
| CN110604313A (en) * | 2019-09-30 | 2019-12-24 | 浙江海洋大学 | Method for preparing high-protein high-calcium supplement by using mussel waste materials |
| CN111165827A (en) * | 2020-02-26 | 2020-05-19 | 福建鼍龙实业有限责任公司 | Crocodile peptide chelated calcium and preparation method and application thereof |
| KR20210133826A (en) * | 2020-04-29 | 2021-11-08 | 주식회사 대호 | Manufacturing method of growth promoters for livestock |
| KR102437393B1 (en) | 2020-04-29 | 2022-08-30 | 주식회사 대호 | Manufacturing method of growth promoters for livestock |
| CN112006287A (en) * | 2020-07-30 | 2020-12-01 | 华中农业大学 | High-calcium high-collagen food and preparation method thereof |
| CN112006287B (en) * | 2020-07-30 | 2023-02-28 | 华中农业大学 | High-calcium high-collagen food and preparation method thereof |
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| KR20070069123A (en) | 2007-07-02 |
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