CN111285777A - Energy-saving method for amino acid chelated calcium - Google Patents
Energy-saving method for amino acid chelated calcium Download PDFInfo
- Publication number
- CN111285777A CN111285777A CN202010082812.0A CN202010082812A CN111285777A CN 111285777 A CN111285777 A CN 111285777A CN 202010082812 A CN202010082812 A CN 202010082812A CN 111285777 A CN111285777 A CN 111285777A
- Authority
- CN
- China
- Prior art keywords
- amino acid
- calcium
- chelating
- reaction
- chelation
- 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.)
- Pending
Links
- 239000011575 calcium Substances 0.000 title claims abstract description 91
- 229910052791 calcium Inorganic materials 0.000 title claims abstract description 91
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 title claims abstract description 78
- 150000001413 amino acids Chemical class 0.000 title claims abstract description 71
- 238000000034 method Methods 0.000 title claims abstract description 28
- 238000006243 chemical reaction Methods 0.000 claims abstract description 48
- 230000009920 chelation Effects 0.000 claims abstract description 38
- -1 calcium amino acid Chemical class 0.000 claims abstract description 11
- 239000000843 powder Substances 0.000 claims description 15
- 239000000413 hydrolysate Substances 0.000 claims description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 8
- 241000251468 Actinopterygii Species 0.000 claims description 6
- 229940036811 bone meal Drugs 0.000 claims description 5
- 239000002374 bone meal Substances 0.000 claims description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 3
- 230000003301 hydrolyzing effect Effects 0.000 claims description 2
- 238000005903 acid hydrolysis reaction Methods 0.000 claims 1
- 230000035484 reaction time Effects 0.000 abstract description 10
- 239000013522 chelant Substances 0.000 description 14
- 239000000203 mixture Substances 0.000 description 14
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 12
- 230000015572 biosynthetic process Effects 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000000126 substance Substances 0.000 description 5
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 4
- 229910001424 calcium ion Inorganic materials 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 210000000988 bone and bone Anatomy 0.000 description 3
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 3
- 239000000920 calcium hydroxide Substances 0.000 description 3
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 229940106635 calcium amino acid chelate Drugs 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- UOXSXMSTSYWNMH-UHFFFAOYSA-L zinc;2-aminoacetate Chemical compound [Zn+2].NCC([O-])=O.NCC([O-])=O UOXSXMSTSYWNMH-UHFFFAOYSA-L 0.000 description 2
- 241000255789 Bombyx mori Species 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 239000004384 Neotame Substances 0.000 description 1
- 241000382353 Pupa Species 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229910052785 arsenic Inorganic materials 0.000 description 1
- RQNWIZPPADIBDY-UHFFFAOYSA-N arsenic atom Chemical compound [As] RQNWIZPPADIBDY-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000003851 biochemical process Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000004087 circulation Effects 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000002124 endocrine Effects 0.000 description 1
- 235000021321 essential mineral Nutrition 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- QSHDDOUJBYECFT-UHFFFAOYSA-N mercury Chemical compound [Hg] QSHDDOUJBYECFT-UHFFFAOYSA-N 0.000 description 1
- 229910052753 mercury Inorganic materials 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 230000004118 muscle contraction Effects 0.000 description 1
- HLIAVLHNDJUHFG-HOTGVXAUSA-N neotame Chemical compound CC(C)(C)CCN[C@@H](CC(O)=O)C(=O)N[C@H](C(=O)OC)CC1=CC=CC=C1 HLIAVLHNDJUHFG-HOTGVXAUSA-N 0.000 description 1
- 235000019412 neotame Nutrition 0.000 description 1
- 108010070257 neotame Proteins 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 230000000050 nutritive effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 238000013021 overheating Methods 0.000 description 1
- 230000008288 physiological mechanism Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 239000003488 releasing hormone Substances 0.000 description 1
- 230000033764 rhythmic process Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229910021654 trace metal Inorganic materials 0.000 description 1
- 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 1
- 238000005406 washing Methods 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C227/00—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton
- C07C227/28—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton from natural products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
- A23L33/175—Amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/195—Carboxylic acids, e.g. valproic acid having an amino group
- A61K31/197—Carboxylic acids, e.g. valproic acid having an amino group the amino and the carboxyl groups being attached to the same acyclic carbon chain, e.g. gamma-aminobutyric acid [GABA], beta-alanine, epsilon-aminocaproic acid or pantothenic acid
- A61K31/198—Alpha-amino acids, e.g. alanine or edetic acid [EDTA]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/40—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having five-membered rings with one nitrogen as the only ring hetero atom, e.g. sulpiride, succinimide, tolmetin, buflomedil
- A61K31/401—Proline; Derivatives thereof, e.g. captopril
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/41—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having five-membered rings with two or more ring hetero atoms, at least one of which being nitrogen, e.g. tetrazole
- A61K31/4164—1,3-Diazoles
- A61K31/4172—Imidazole-alkanecarboxylic acids, e.g. histidine
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K33/00—Medicinal preparations containing inorganic active ingredients
- A61K33/06—Aluminium, calcium or magnesium; Compounds thereof, e.g. clay
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/02—Nutrients, e.g. vitamins, minerals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C227/00—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton
- C07C227/14—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton from compounds containing already amino and carboxyl groups or derivatives thereof
- C07C227/18—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton from compounds containing already amino and carboxyl groups or derivatives thereof by reactions involving amino or carboxyl groups, e.g. hydrolysis of esters or amides, by formation of halides, salts or esters
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C277/00—Preparation of guanidine or its derivatives, i.e. compounds containing the group, the singly-bound nitrogen atoms not being part of nitro or nitroso groups
- C07C277/08—Preparation of guanidine or its derivatives, i.e. compounds containing the group, the singly-bound nitrogen atoms not being part of nitro or nitroso groups of substituted guanidines
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C319/00—Preparation of thiols, sulfides, hydropolysulfides or polysulfides
- C07C319/14—Preparation of thiols, sulfides, hydropolysulfides or polysulfides of sulfides
- C07C319/20—Preparation of thiols, sulfides, hydropolysulfides or polysulfides of sulfides by reactions not involving the formation of sulfide groups
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07D—HETEROCYCLIC COMPOUNDS
- C07D207/00—Heterocyclic compounds containing five-membered rings not condensed with other rings, with one nitrogen atom as the only ring hetero atom
- C07D207/02—Heterocyclic compounds containing five-membered rings not condensed with other rings, with one nitrogen atom as the only ring hetero atom with only hydrogen or carbon atoms directly attached to the ring nitrogen atom
- C07D207/04—Heterocyclic compounds containing five-membered rings not condensed with other rings, with one nitrogen atom as the only ring hetero atom with only hydrogen or carbon atoms directly attached to the ring nitrogen atom having no double bonds between ring members or between ring members and non-ring members
- C07D207/10—Heterocyclic compounds containing five-membered rings not condensed with other rings, with one nitrogen atom as the only ring hetero atom with only hydrogen or carbon atoms directly attached to the ring nitrogen atom having no double bonds between ring members or between ring members and non-ring members with hetero atoms or with carbon atoms having three bonds to hetero atoms with at the most one bond to halogen, e.g. ester or nitrile radicals, directly attached to ring carbon atoms
- C07D207/16—Carbon atoms having three bonds to hetero atoms with at the most one bond to halogen, e.g. ester or nitrile radicals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07D—HETEROCYCLIC COMPOUNDS
- C07D233/00—Heterocyclic compounds containing 1,3-diazole or hydrogenated 1,3-diazole rings, not condensed with other rings
- C07D233/54—Heterocyclic compounds containing 1,3-diazole or hydrogenated 1,3-diazole rings, not condensed with other rings having two double bonds between ring members or between ring members and non-ring members
- C07D233/64—Heterocyclic compounds containing 1,3-diazole or hydrogenated 1,3-diazole rings, not condensed with other rings having two double bonds between ring members or between ring members and non-ring members with substituted hydrocarbon radicals attached to ring carbon atoms, e.g. histidine
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Medicinal Chemistry (AREA)
- Epidemiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Obesity (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Mycology (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Inorganic Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Abstract
An energy-saving method for chelating amino acid into calcium, which at least comprises the following steps: providing an amino acid and a calcium source; and carrying out a chelation reaction on the amino acid and the calcium source by using a homogenizer to prepare the amino acid chelated calcium. The energy-saving method for chelating calcium amino acid can increase the chelating rate of amino acid and calcium source and shorten the chelating time. The traditional chelation reaction needs 80 minutes, and the rapid chelation by using a homogenizer only needs 30 minutes to achieve a chelation rate of more than 90 percent, so the invention can save 62.5 percent of reaction time, thereby meeting the requirement of energy saving.
Description
Technical Field
The present invention relates to a chelating method, and more particularly, to an energy-saving amino acid calcium chelating method.
Background
Calcium is an essential mineral nutrient for the human body, and accounts for about 1.5 to 2% of the body weight, more than 99% of calcium is present in bones and teeth, and the rest is scattered in body fluids and tissues and organs, and all cells require calcium to maintain normal physiological mechanisms. Calcium ions are the trigger of many biochemical and physiological processes in the organism, such as triggering muscle contraction, releasing hormones, delivering impulses, promoting blood clotting and regulating heart rhythm, and are particularly necessary for various higher organisms. Clinical studies in modern medicine also indicate that calcium ions are closely related to the functions of more than ten systems in vivo, such as immunity, nerves, endocrine, digestion, circulation, exercise, reproduction, and the like, and that calcium ions are important to the maintenance of vital functions.
The amino acid chelated calcium is a compound with a cyclic structure formed by reacting one or more amino acid groups with calcium metal. The amino acid chelated calcium has the characteristics of good chemical and biological stability, high biological effect and the like, and can achieve the double effects of supplementing amino acid and calcium.
Heretofore, the methods for producing amino acid chelated calcium include chemical synthesis, electrolytic semipermeable membrane method, ion exchange method, and the like. However, these methods have the following problems: slow reaction, long time, low yield, incomplete reaction and difficult removal of residual reactants not participating in the synthesis. Therefore, mass production is difficult and costly.
Disclosure of Invention
In view of the above, an objective of the present invention is to provide an energy-saving method for preparing amino acid chelated calcium, so as to solve the problem of the existing preparation method for amino acid chelated calcium.
To achieve the above object, the present invention provides an energy-saving method for chelating amino acid into calcium, which at least comprises the following steps: providing an amino acid and a calcium source; and adjusting the amino acid and calcium chelating reaction to generate amino acid chelating responses.
Wherein the mass ratio of the amino acid to the calcium source is substantially 1 to 1.
Wherein the rotation speed of the homogenizer is substantially 7 kilorevolutions per minute, the pH value of the chelation reaction is substantially 8, and the temperature is substantially 80 ℃.
Wherein the time required for the chelation reaction to reach a chelation rate of 90% is substantially 30 minutes.
Wherein the amino acid is compound amino acid, and the calcium source is fish bone meal hydrolysate.
Wherein, the pH value of the chelation reaction is adjusted by sodium hydroxide.
Wherein the fishbone powder hydrolysate is obtained by performing acidolysis on fishbone powder, and the fishbone powder contains calcium substantially 49.49% and water substantially 0.25%.
Wherein the fishbone powder hydrolysate is obtained by hydrolyzing fishbone powder with hydrochloric acid.
The traditional chelation reaction needs 80 minutes, and the rapid chelation by using a homogenizer only needs 30 minutes to achieve a chelation rate of more than 90 percent, so the invention can save 62.5 percent of reaction time, thereby meeting the requirement of energy saving. As mentioned above, the energy-saving method for chelating amino acid into calcium according to the present invention can have one or more of the following advantages:
(1) the energy-saving amino acid calcium chelating method of the invention improves the chelating reaction efficiency of amino acid and calcium source by the homogenizer, can improve the chelating rate of amino acid and calcium source, and shortens the chelating time to 30 minutes.
(2) The energy-saving amino acid calcium chelating method of the invention can increase the chelating rate of amino acid and calcium source to 90% and shorten the chelating time to 30 minutes by setting the homogenizer to a proper rotation speed and adjusting the chelating reaction of amino acid and calcium source to a proper pH value and temperature.
So that the manner in which the above recited features of the present invention can be understood and appreciated, a more particular description of the invention, briefly summarized above, may be had by reference to embodiments, some of which are illustrated in the appended drawings.
Drawings
FIG. 1 is a schematic flow chart of the energy-saving method for amino acid calcium chelation according to the invention.
FIG. 2 is a schematic diagram of the apparatus used in the energy-saving method for chelating amino acid into calcium.
Detailed Description
For the purpose of understanding the technical features, contents and advantages of the present invention and the effects achieved thereby, the present invention will be described in detail with reference to the accompanying drawings in the form of embodiments, wherein the drawings are provided for illustrative purposes and for supporting the specification, and are not necessarily to be construed as being true in scale and precise arrangement after the implementation of the present invention, and therefore, the scope of the present invention in practical implementation should not be read and limited by the scale and arrangement of the accompanying drawings. In addition, for the sake of easy understanding, the same components in the following embodiments are illustrated with the same reference numerals. The dimensional ratios of the components shown in the drawings are merely for convenience in explanation and are not intended to be limiting.
Furthermore, the words used throughout the specification and claims have the ordinary meaning as is usually accorded to each word or phrase in the art, in the context of this disclosure and in the context of particular integers, unless otherwise indicated. Certain terms used to describe the invention are discussed below or elsewhere in this specification to provide additional guidance to those skilled in the art in describing the invention.
Further, as used herein, the terms "comprising," "including," "having," "containing," and the like are open-ended terms, i.e., meaning including, but not limited to.
Referring to fig. 1 and fig. 2, fig. 1 is a schematic flow chart of the energy-saving calcium amino acid chelate method of the present invention, and fig. 2 is a schematic equipment diagram of the energy-saving calcium amino acid chelate method of the present invention. As shown in FIG. 1 and FIG. 2, the energy-saving method for amino acid calcium chelation at least comprises the following steps S10 and S20. Wherein, in step S10, an amino acid and a calcium source are provided. In step S20, a chelating reaction is performed, wherein in step S20, the amino acid and the calcium source are subjected to a chelating reaction by a homogenizer, thereby preparing the amino acid-chelated calcium.
The present invention utilizes a homogenizer 40 for chelation of amino acids with a calcium source, the homogenizer 40 being, for example, available from neotame, and being, for example, a HM-0025 homogenizer. The speed of operation of the homogenizer 40 may be controlled, for example, by a speed controller 60, which may adjust the rotational speed without a step, the rotational speed (RPM) of the homogenizer 40 may range from about 500 RPM to about 11,000 RPM, and preferably from about 4,000 RPM to about 8,000 RPM. Since the homogenizer 40 is prone to overheating at more than 8,000 rpm, the rotation speed is preferably not more than 8,000 rpm without increasing the cost (e.g., adding cooling equipment) and achieving a good chelating rate. However, in the present invention, the homogenizer 40 is preferably rotated at a speed of 7,000 rpm.
The homogenizer 40 may be provided with, for example, a safety clamp 42, the safety clamp 42 being configured to hold a reaction vessel 44, the reaction vessel 44 being configured to receive the amino acid and the calcium source to be reacted (i.e., the amino acid-calcium source mixture), and a rotor 46 of the homogenizer 40 extending into the reaction vessel 44 for homogenizing the amino acid and the calcium source. The invention uses the homogenizer 40 to promote the chelating efficiency of the amino acid and the calcium source, can improve the chelating rate of the amino acid and the calcium source, and shortens the chelating time.
In the present invention, any component substance containing an amino acid molecule/group is an amino acid claimed in the present invention. The amino acid may be, for example, a complex amino acid, but is not limited thereto, and the kind and content of the amino acid in the complex amino acid are not particularly limited. For example, the compound amino acid is obtained from Zhengzhou Furun bioengineering GmbH, and is in powder form, the total amino acid content is 80.9% (see the following ingredient table), the compound amino acid is extracted from silkworm pupa, the proportion of each amino acid is very close to the proportion of amino acid composition of human body, and the nutritive value is very high. The component types and contents of the above compound amino acids are only examples, and the user can select single component amino acids or compound amino acids with proper component types and contents according to actual needs.
Table of the composition of the various amino acids in the complex amino acids:
in the present invention, any substance containing a calcium component is a calcium source claimed in the present invention. For example, the calcium source can be, but is not limited to, fish bone meal hydrolysate. Fishbone powder is available from Huzhou bioengineering Limited company, for example, and has a calcium content of 49.49%, a water content of 0.25%, and trace metal elements (lead ≦ 1mg/Kg, mercury ≦ 0.5mg/Kg, and arsenic ≦ 0.5 mg/Kg). The types and contents of the calcium sources are only examples, and users can select the calcium sources with proper component types and contents according to actual requirements.
The fish bone meal is subjected to acidolysis reaction to obtain fish bone meal hydrolysate. For example, the salt bond and ester bond of collagen salt in fish bone powder are destroyed by hydrochloric acid to denature protein, and the calcium-containing substance is exposed and reacts with calcium phosphate and calcium hydroxide in the calcium-containing substance to convert bone calcium into soluble calcium. Preferably, 6mL of hydrochloric acid with concentration of 4mol/L is added into 1g of fishbone powder to act for 50 minutes at 100 ℃ so as to obtain fishbone powder hydrolysate with free calcium content of 75.65 mg/mL.
Then, the fishbone powder hydrolysate and the compound amino acid are mixed in a certain proportion in a homogenizer 40, and the pH value is adjusted by using sodium hydroxide, so that the compound amino acid and the fishbone powder hydrolysate can carry out chelation reaction under proper pH value. After the reaction is finished, performing centrifugal separation, washing the precipitate by adding absolute ethyl alcohol, concentrating the supernatant, freeze-drying and crushing to obtain the finished product of the compound amino acid chelated calcium.
The chelation ratio (%) in the present invention is W0×100/W1Wherein W is0Is the content of calcium in the chelate, W1The content of calcium in the reaction system.
The results of the chelation reaction of the amino acid-calcium source mixture at different pH values with the homogenizer are shown in the table. Wherein the nature and origin of the amino acid-calcium source mixture are as described above. The conditions of the chelation reaction were: the mass ratio of the amino acid to the calcium source is 1: 1, the reaction time is 30 minutes, the rotating speed of a homogenizer is 7,000 revolutions per minute, and the reaction temperature is 80 ℃. The amino acid-calcium source mixture with pH values of about 5, 6, 7, 8 and 9 respectively is subjected to chelation reaction for 30 minutes at a rotation speed of about 7,000 rpm by a homogenizer, and the chelation rates are detected to be about 65%, 70%, 80%, 90% and 76% respectively. From this graph, it can be seen that the amino acid-calcium source mixture has a chelating ratio of 90% at a pH of 8, and the effect is better.
Table one:
| pH value | 5 | 6 | 7 | 8 | 9 |
| Chelate ratio (%) | 65 | 70 | 80 | 90 | 76 |
As can be seen from the Table I, the chelation rate was low under acidic conditions, and high at pH 7 to 8. The reason for this is that when hydrogen ions (H) are present in the solution+) When present in large amounts, H+Can compete for electron-donating groups, and is not beneficial to the existence of chelate; and under alkaline conditions, OH-Compete for calcium ion to generate calcium hydroxide precipitate preferentially, and the calcium hydroxide precipitate is washed with anhydrous ethanol to be removed, and the amino acid is subjected to H+And OH-Has less influence, provides sufficient electron-donating groups, and further facilitates the formation of chelate by calcium through coordination bonds.
And the second table shows a table of the results of chelation reaction of the homogenizer with different mass ratios of amino acid and calcium source. The nature and source of the amino acid-calcium source mixture are as described above. The conditions of the chelation reaction were: the pH value of the amino acid-calcium source mixture is 8, the reaction time is 30 minutes, the rotating speed of a homogenizer is 7,000 revolutions per minute, and the reaction temperature is 80 ℃. The mixture is mixed by a homogenizer at a rotating speed of about 7,000 rpm in a mass ratio of about 1: 3. 1: 2. 1: 1. 2: 1. 3: 1 for 30 minutes, the chelating rate was about 74%, 81%, 90%, 80%, 79%. From this graph, it can be seen that the mass ratio of amino acids to calcium source is 1: the chelating rate can reach 90% when the chelating rate is 1, and the effect is better.
Watch two
| Mass ratio of the seed | 1:3 | 1:2 | 1:1 | 2:1 | 3:1 |
| Chelate ratio (%) | 74 | 81 | 90 | 80 | 79 |
As can be seen from the table II, when the mass ratio of the amino acid to the calcium source is small, the chelation rate is low; when the ratio becomes larger, the chelation rate gradually increases; when the mass ratio is 1: when 1, the chelation rate is the maximum; however, when the ratio is too large, the chelation rate decreases. The reason is that the amino acid and the calcium source coordinate to form a chelate in a certain proportion, and the chelating rate is influenced by more or less calcium content participating in the chelating reaction.
The third table shows the result chart of chelating reaction carried out by the homogenizer in cooperation with different reaction temperatures. The nature and source of the amino acid-calcium source mixture are as described above. The conditions of the chelation reaction were: the pH value of the amino acid-calcium source mixture is 8, the reaction time is 30 minutes, the rotating speed of the homogenizer is 7,000 revolutions per minute, and the mass ratio of the amino acid to the calcium source is 1 to 1. The chelating reaction is carried out for 30 minutes by a homogenizer at the rotation speed of about 7,000 r/min and the reaction temperature of about 50 ℃, 60 ℃, 70 ℃, 80 ℃ and 90 ℃, and the chelating rates are respectively 83%, 84%, 87%, 90% and 76% after detection. From this graph, it can be seen that the chelating rate is 90% at a reaction temperature of 80 ℃ and the effect is better.
Watch III
| Temperature (. degree.C.) | 50 | 60 | 70 | 80 | 90 |
| Chelate ratio (%) | 83 | 84 | 87 | 90 | 76 |
It is understood from the third table that the formation of chelate is not favored by too high a temperature, which may decompose the chelate or cause other reactions. The proper reaction temperature is favorable for the forward direction of chelation, and the temperature higher or lower is unfavorable for chelate formation.
The fourth table shows the results of chelation reaction with the homogenizer in combination with different reaction times. The nature and source of the amino acid-calcium source mixture are as described above. The conditions of the chelation reaction were: the pH value of the amino acid-calcium source mixture is 8, the rotating speed of the homogenizer is 7,000 revolutions per minute, the mass ratio of the amino acid to the calcium source is 1: 1, and the reaction temperature is 80 ℃. The chelating reaction is carried out by a homogenizer at the rotating speed of about 7,000 rpm and the reaction time of about 20 minutes, 25 minutes, 30 minutes, 35 minutes and 400 minutes respectively, and the chelating rates are respectively 78%, 84%, 90%, 85% and 80% after detection. As can be seen from the graph, the chelating ratio was 90% at a reaction time of 30 minutes, and the effect was excellent.
Watch four
| Induction (time) | 20 | 25 | 30 | 35 | 40 |
| Chelate ratio (%) | 78 | 84 | 90 | 85 | 80 |
As can be seen from Table IV, the chelating rate of the amino acid chelate compound increases with the increase of the reaction time, but the chelating rate decreases with the time exceeding 30 minutes. This indicates that the chelate is unstable and may be decomposed and changed with time, but the decomposition process is accompanied by new chelate synthesis, so the decomposition and synthesis will tend to be balanced, and the chelating rate will tend to decrease and change less and less.
The traditional chelation reaction needs 80 minutes, and the rapid chelation by using a homogenizer only needs 30 minutes to achieve a chelation rate of more than 90 percent, so the invention can save 62.5 percent of reaction time, thereby meeting the requirement of energy saving. In summary, the energy-saving method for chelating calcium with amino acid of the present invention utilizes the homogenizer to increase the chelating reaction efficiency of amino acid and calcium source, thereby increasing the chelating rate of amino acid and calcium source and shortening the chelating time to 30 minutes. The energy-saving amino acid calcium chelating method of the invention can increase the chelating rate of amino acid and calcium source to 90% and shorten the chelating time to 30 minutes by setting the homogenizer to a proper rotation speed and adjusting the chelating reaction of amino acid and calcium source to a proper pH value and temperature.
The foregoing is by way of example only, and not limiting. It is intended that all equivalent modifications or variations without departing from the spirit and scope of the present invention shall be included in the appended claims.
Description of the reference numerals
S10, S20: step 44: reaction vessel
40: the homogenizer 46: rotating member
42: the safety clamp 60: speed controller
Claims (5)
1. An energy-saving method for chelating amino acid into calcium, which at least comprises the following steps:
providing an amino acid and a calcium source; and
and (2) carrying out a chelation reaction on the amino acid and the calcium source by using a homogenizer to prepare the amino acid chelated calcium, wherein the mass ratio of the amino acid to the calcium source is substantially 1: 1, the rotating speed of the homogenizer is substantially 7 kilorevolutions per minute, the pH value of the chelation reaction is substantially 8, the temperature is substantially 80 ℃, and the time required for the chelation reaction to reach the chelation rate of 90% is substantially 30 minutes.
2. The energy-saving method for chelating calcium amino acid as claimed in claim 1, wherein the amino acid is a complex amino acid, and the calcium source is hydrolyzed solution of fishbone powder.
3. The method of claim 2, wherein the pH of the chelating reaction is adjusted with sodium hydroxide.
4. The method of claim 2 wherein the hydrolysate is prepared by acid hydrolysis of fishbone powder, and the fishbone powder contains calcium of 49.49% and water of 0.25%.
5. The method of claim 4 wherein the hydrolysate is prepared by hydrolyzing fish bone meal with hydrochloric acid.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010082812.0A CN111285777A (en) | 2020-02-07 | 2020-02-07 | Energy-saving method for amino acid chelated calcium |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010082812.0A CN111285777A (en) | 2020-02-07 | 2020-02-07 | Energy-saving method for amino acid chelated calcium |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN111285777A true CN111285777A (en) | 2020-06-16 |
Family
ID=71017009
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202010082812.0A Pending CN111285777A (en) | 2020-02-07 | 2020-02-07 | Energy-saving method for amino acid chelated calcium |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN111285777A (en) |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107485030A (en) * | 2017-07-31 | 2017-12-19 | 浦江县昂宝生物技术有限公司 | A kind of low value fish-bone polypeptide chelate calcium |
| CN110283090A (en) * | 2019-07-02 | 2019-09-27 | 广东海洋大学 | A kind of preparation method of L-phenylalanine chelating calcium powder and its L-phenylalanine of preparation chelate calcium tablet |
| TW202007682A (en) * | 2018-07-27 | 2020-02-16 | 崑山科技大學 | Method for rapidly chelating calcium by amino acid |
-
2020
- 2020-02-07 CN CN202010082812.0A patent/CN111285777A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107485030A (en) * | 2017-07-31 | 2017-12-19 | 浦江县昂宝生物技术有限公司 | A kind of low value fish-bone polypeptide chelate calcium |
| TW202007682A (en) * | 2018-07-27 | 2020-02-16 | 崑山科技大學 | Method for rapidly chelating calcium by amino acid |
| CN110283090A (en) * | 2019-07-02 | 2019-09-27 | 广东海洋大学 | A kind of preparation method of L-phenylalanine chelating calcium powder and its L-phenylalanine of preparation chelate calcium tablet |
Non-Patent Citations (2)
| Title |
|---|
| 吴霖等: "鱼骨粉制备复合氨基酸螯合钙工艺研究", 《食品与发酵科技》 * |
| 许先猛等: "猪皮胶原多肽螯合钙的制备及其结构表征", 《食品工业科技》 * |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN102172393A (en) | Calcium supplement of fish scale protein peptide calcium chelate and preparation method thereof | |
| CN102309008B (en) | Preparation method of collagen polypeptide chelated calcium | |
| CN102174073A (en) | Oyster protein peptide and zinc chelate and method for preparing same | |
| CN105012940B (en) | A kind of preparation method of nanometre collagen peptide chelated zinc | |
| CN1740143A (en) | Prepn process of metal-amino acid chelate | |
| IL127148A (en) | Creatine pyruvates, method for their production and physiologically compatible compositions containing them | |
| CN110642955B (en) | Esterified selenium polysaccharide and preparation method and application thereof | |
| Frost | Further studies on factor W | |
| CN101481336A (en) | Preparation of N-carbamoyl-aminoglutaric acid and sodium salt thereof | |
| CN100582090C (en) | Method for preparing N-carbamyl glutamic acid | |
| CN111285777A (en) | Energy-saving method for amino acid chelated calcium | |
| TWI690505B (en) | Method for rapidly chelating calcium by amino acid | |
| CN107712910A (en) | A kind of gelatin small peptide or collagen tripeptide chelating calcium and magnesium and preparation method thereof | |
| CN112300299A (en) | Preparation method and application of zinc and calcium polysaccharide complex | |
| CN111528480A (en) | Calcium nutritional supplement and preparation method thereof | |
| CN111979285B (en) | Preparation method of pearl peptide chelated calcium | |
| CN108484448A (en) | The method of one pot process N- carbamylglutamic acids | |
| CN114230500A (en) | Preparation method of vitamin D3 | |
| CN113841795A (en) | Self-assembled small peptide chelated copper feed additive and preparation method thereof | |
| CN111743034A (en) | Powdery feed for improving survival rate and weight gain rate of anguilla marmorata as well as preparation method and application of powdery feed | |
| WO2007136238A1 (en) | Method for producing a biologically active additive named 'active calcium' | |
| CN109970824B (en) | Preparation method of high-stability fructose calcium diphosphate | |
| CN1271048C (en) | Ion exchange resin purifying process for synthesizing calcium taurine | |
| CN115893459A (en) | Preparation method of multifunctional water-soluble nano magnesium hydroxide stock solution | |
| CN102041282A (en) | Method for preparing L-ornithine by utilizing enzyme method |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| WD01 | Invention patent application deemed withdrawn after publication | ||
| WD01 | Invention patent application deemed withdrawn after publication |
Application publication date: 20200616 |