CN114958946A - Preparation method of fermented red date chelated peptide iron - Google Patents
Preparation method of fermented red date chelated peptide iron Download PDFInfo
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- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 title claims abstract description 113
- 229910052742 iron Inorganic materials 0.000 title claims abstract description 59
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 37
- 238000002360 preparation method Methods 0.000 title claims abstract description 14
- 239000000047 product Substances 0.000 claims abstract description 26
- 238000000855 fermentation Methods 0.000 claims abstract description 20
- 230000004151 fermentation Effects 0.000 claims abstract description 20
- 239000007788 liquid Substances 0.000 claims abstract description 17
- 241001247821 Ziziphus Species 0.000 claims abstract description 16
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 16
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 16
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 13
- 108010059892 Cellulase Proteins 0.000 claims abstract description 12
- 108091005804 Peptidases Proteins 0.000 claims abstract description 12
- 239000004365 Protease Substances 0.000 claims abstract description 12
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 12
- 229940106157 cellulase Drugs 0.000 claims abstract description 12
- 241000186660 Lactobacillus Species 0.000 claims abstract description 9
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 9
- 229940039696 lactobacillus Drugs 0.000 claims abstract description 9
- 238000004537 pulping Methods 0.000 claims abstract description 7
- 238000001035 drying Methods 0.000 claims abstract description 5
- 238000000265 homogenisation Methods 0.000 claims abstract description 5
- 241001465754 Metazoa Species 0.000 claims abstract description 4
- 108010009736 Protein Hydrolysates Proteins 0.000 claims abstract description 3
- 239000000413 hydrolysate Substances 0.000 claims description 10
- 238000000034 method Methods 0.000 claims description 8
- 108010089792 Hemeproteins Proteins 0.000 claims description 7
- 102000008015 Hemeproteins Human genes 0.000 claims description 7
- 210000003743 erythrocyte Anatomy 0.000 claims description 7
- 210000004369 blood Anatomy 0.000 claims description 5
- 239000008280 blood Substances 0.000 claims description 5
- 238000001694 spray drying Methods 0.000 claims description 5
- 238000000926 separation method Methods 0.000 claims description 4
- 102000001554 Hemoglobins Human genes 0.000 claims description 3
- 108010054147 Hemoglobins Proteins 0.000 claims description 3
- 230000010100 anticoagulation Effects 0.000 claims description 2
- 238000001556 precipitation Methods 0.000 claims description 2
- 238000010521 absorption reaction Methods 0.000 abstract description 10
- 239000010836 blood and blood product Substances 0.000 abstract description 2
- 229940125691 blood product Drugs 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 13
- -1 iron ion Chemical class 0.000 description 7
- 210000004027 cell Anatomy 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 238000010438 heat treatment Methods 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 150000004032 porphyrins Chemical group 0.000 description 4
- 238000003756 stirring Methods 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 239000013589 supplement Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 150000003278 haem Chemical class 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- CWYNVVGOOAEACU-UHFFFAOYSA-N Fe2+ Chemical compound [Fe+2] CWYNVVGOOAEACU-UHFFFAOYSA-N 0.000 description 2
- 102000015636 Oligopeptides Human genes 0.000 description 2
- 108010038807 Oligopeptides Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 229910001448 ferrous ion Inorganic materials 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 102000018146 globin Human genes 0.000 description 2
- 108060003196 globin Proteins 0.000 description 2
- 125000004433 nitrogen atom Chemical group N* 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- VZGDMQKNWNREIO-UHFFFAOYSA-N tetrachloromethane Chemical compound ClC(Cl)(Cl)Cl VZGDMQKNWNREIO-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- KSFOVUSSGSKXFI-GAQDCDSVSA-N CC1=C/2NC(\C=C3/N=C(/C=C4\N\C(=C/C5=N/C(=C\2)/C(C=C)=C5C)C(C=C)=C4C)C(C)=C3CCC(O)=O)=C1CCC(O)=O Chemical compound CC1=C/2NC(\C=C3/N=C(/C=C4\N\C(=C/C5=N/C(=C\2)/C(C=C)=C5C)C(C=C)=C4C)C(C)=C3CCC(O)=O)=C1CCC(O)=O KSFOVUSSGSKXFI-GAQDCDSVSA-N 0.000 description 1
- ZZZCUOFIHGPKAK-UHFFFAOYSA-N D-erythro-ascorbic acid Natural products OCC1OC(=O)C(O)=C1O ZZZCUOFIHGPKAK-UHFFFAOYSA-N 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 229930003268 Vitamin C Natural products 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 102000038379 digestive enzymes Human genes 0.000 description 1
- 108091007734 digestive enzymes Proteins 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 125000001041 indolyl group Chemical group 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 235000003170 nutritional factors Nutrition 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 229950003776 protoporphyrin Drugs 0.000 description 1
- 125000000168 pyrrolyl group Chemical group 0.000 description 1
- 230000037384 skin absorption Effects 0.000 description 1
- 231100000274 skin absorption Toxicity 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 238000009210 therapy by ultrasound Methods 0.000 description 1
- 238000004704 ultra performance liquid chromatography Methods 0.000 description 1
- 238000007738 vacuum evaporation Methods 0.000 description 1
- 235000019154 vitamin C Nutrition 0.000 description 1
- 239000011718 vitamin C Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
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- Life Sciences & Earth Sciences (AREA)
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- Genetics & Genomics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
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Abstract
The invention belongs to the technical field of animal blood products, and relates to a preparation method of fermented red date chelated peptide iron, which comprises the following steps: pulping red dates, adding cellulase for enzymolysis to obtain a jujube pulp enzymolysis liquid; adding haematochrome protein into the jujube pulp enzymatic hydrolysate, and performing homogenization treatment; inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 1-3 d; adding protease into the fermented solution for enzymolysis for 2-4 h; then concentrating and drying to prepare a finished product; the product prepared by the invention is rich in two components of peptide iron and chelating peptide iron, so that the active iron content of the product is greatly improved, and the absorption efficiency of iron elements is effectively improved.
Description
Technical Field
The invention belongs to the technical field of animal blood products, and relates to a preparation method of fermentation type red date chelated peptide iron.
Background
Hemoproteins are a large group of metal proteins containing protoporphyrin IX as a prosthetic group, and perform different biological functions according to different protein molecule composition modes of connecting proteins and metal ions on the prosthetic group of the hemoprotein and wrapping heme by a protein polypeptide chain. Ferrohemoglobin, the most prominent component of red blood cells, is composed of globin and heme. The heme molecule is a small molecule with a porphyrin structure, nitrogen atoms on four pyrrole rings in porphyrin are coordinately bound with a ferrous ion at the center of the porphyrin molecule, and nitrogen atoms on indole side chains in histidine residue at the 8 th position in a globin peptide chain are coordinately bound with the ferrous ion from the upper part of the plane of the porphyrin molecule.
The protein is finally decomposed into oligopeptides and free amino acids by the action of digestive enzymes of the gastrointestinal tract. Oligopeptides are more advantageous in absorption than free amino acids and can be absorbed intact into the blood. The polypeptide-porphyrin iron which is the decomposition product of the hemoprotein has strong iron supplementing effect, strong oxidation resistance and health care function. The polypeptide is used as a nutritional factor with multiple functional properties such as oxidation resistance, fatigue resistance and the like, and can also promote the absorption of non-chelated iron.
The red dates are one of recognized foods with the functions of iron supplement and blood supplement, each hundred grams of red dates contain 2.3mg of iron, and simultaneously contain rich vitamin C, but the iron in the red dates is not easy to be utilized and absorbed by human bodies, in the existing products, the red date products are directly mixed with iron chelating peptides to prepare iron supplement products, but the chelated protein peptides are difficult to further promote the absorption of iron elements contained in the red dates, so that part of plant source iron in the products can not be fully absorbed.
Disclosure of Invention
The invention overcomes the defects of the prior art, provides a preparation method of the fermentation type red date chelated peptide iron, solves the problem that the iron element in the red dates is not easy to absorb, and improves the unit content and the utilization rate of the iron supplement product iron by utilizing the combination of the polypeptide of the decomposition product of the existing hemoprotein-porphyrin iron and the iron element in the red dates.
In order to achieve the above object, the present invention is achieved by the following technical solutions.
A preparation method of fermentation type red date chelated peptide iron comprises the following steps:
1) pulping red dates, adding cellulase for enzymolysis to obtain a jujube pulp enzymolysis liquid;
2) adding haematochrome protein into the jujube pulp enzymatic hydrolysate, and performing homogenization treatment;
3) inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 1-3 d;
4) adding protease into the fermented solution for enzymolysis for 2-4 h; then concentrating and drying to obtain the finished product.
Preferably, the mass percent of the cellulase is 0.5-2.5%.
Preferably, the enzymolysis time in the step 1) is 2-6 h.
Preferably, the hemoglobin protein is obtained by subjecting animal blood to anticoagulation treatment, centrifugal separation of erythrocytes, erythrocyte breakage, isoelectric point precipitation and centrifugal separation.
Preferably, the homogenization treatment is to homogenize the date pulp enzymolysis liquid added with the haematochrome protein by a homogenizer for 1-2 h.
Preferably, the mass ratio of the jujube pulp enzymolysis liquid to the hemoprotein is 1: 1.5-2.5.
Preferably, the pH of the homogenized mixed liquid is adjusted to 5.0-6.0.
Preferably, after enzymolysis by protease, heating to 70-85 ℃, and treating for 15-30 min; and then filtered.
Preferably, the drying is spray drying.
Compared with the prior art, the invention has the following beneficial effects:
the mechanism of the preparation method of the fermentation type red date chelated iron peptide is as follows: firstly, red dates are subjected to wall breaking pulping, so that plant fibers in the red dates are fully softened, and meanwhile, sugar and protein components are fully dissolved out; further enzymolysis of fibrous components with cellulase to release iron ion and dissolve in the pulp; adding heme protein and homogenizing to break heme protein into finer structures, wherein red date pulp and broken heme protein are fully mixed in the process, iron ions in the date pulp are further chelated with exposed polypeptide after breaking to form stable iron chelated protein, the activity of iron elements in plants is fully activated, and the iron absorption efficiency of the iron elements is improved by chelation with micro-protein; finally, carrying out enzymolysis on the chelated protein obtained by physical treatment by using protease to further carry out enzymolysis on the peptide iron product; the final product is rich in two components of peptide iron and chelating peptide iron, so that the active iron content of the product is greatly improved, and the absorption efficiency of iron elements is effectively improved.
Detailed Description
In order to make the technical problems, technical solutions and advantageous effects to be solved by the present invention more clearly apparent, the present invention is further described in detail with reference to the embodiments. It should be understood that the specific embodiments described herein are merely illustrative of the invention and are not intended to limit the invention. The technical solutions of the present invention are described in detail below with reference to examples, but the scope of protection is not limited thereto.
Example 1
A preparation method of fermentation type red date chelated peptide iron comprises the following specific steps:
1. crushing fresh red dates, adding water accounting for 30% of the mass of the red dates, stirring, pulping, and then adding cellulase into obtained date pulp for enzymolysis to obtain date pulp enzymatic hydrolysate; the cellulase is purchased from Shandong Longman bioengineering Co Ltd, the addition amount is 1.5%, and the enzymolysis temperature is 28-34 ℃.
2. Adding 2 times of heme protein into the jujube pulp enzymatic hydrolysate subjected to enzymolysis;
preparation of hemoprotein: adding anticoagulant into fresh pig blood, centrifuging at 2500r/min for 15min, and removing supernatant to obtain erythrocyte. Adding erythrocyte into 3 times volume of normal saline, centrifuging for 20min after fully stirring, discarding the supernatant, adding normal saline, repeatedly washing, centrifuging for 20min at 3000r/min for the last time, and pouring out the supernatant to obtain solid. Adding equal volume of distilled water and 0.5 volume times of carbon tetrachloride into the solid, performing ultrasonic treatment for 10min, centrifuging at 3000r/min for 15min, pouring out supernatant, performing vacuum evaporation to obtain hemoglobin solid, and storing in a refrigerator at 4 deg.C.
3. Homogenizing the jujube pulp enzymatic hydrolysate added with the haematochrome protein by adopting a homogenizer for 2 h; adjusting the pH value of the homogenized mixed liquid to 5.0-6.0.
4. Inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 1-3 d; the fermentation temperature is 30-32 ℃, and the yeast and the lactobacillus are the conventional commercial strains purchased in the conventional market.
5. After fermentation is finished, adding protease into the fermented solution for enzymolysis for 4 hours; the protease is a commercial strain purchased in the conventional market, and can also be specifically subjected to enzymolysis by using a restriction enzyme; the temperature of enzymolysis is 34-37 ℃;
6. heating to 70-85 deg.C after enzymolysis, and treating for 15-30 min; then filtering and concentrating, and carrying out spray drying to prepare a finished product.
Example 2
A preparation method of fermentation type red date chelated peptide iron comprises the following specific steps:
1. crushing fresh red dates, adding water accounting for 30% of the mass of the red dates, stirring, pulping, and then adding cellulase into obtained date pulp for enzymolysis to obtain date pulp enzymatic hydrolysate; the cellulase is purchased from Shandong Longman bioengineering Co Ltd, the addition amount is 1%, and the enzymolysis temperature is 28-34 ℃.
2. Adding 2 times of heme protein into the jujube pulp enzymatic hydrolysate subjected to enzymolysis;
the hemoprotein was prepared as in example 1.
3. Homogenizing the jujube pulp enzymatic hydrolysate added with the haematochrome protein by a homogenizer for 1.5 h; adjusting the pH value of the homogenized mixed liquid to 5.0-6.0.
4. Inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 2 d; the fermentation temperature is 30-32 ℃, and the yeast and the lactobacillus are the conventional commercial strains purchased in the conventional market.
5. After fermentation is finished, adding protease into the fermented solution for enzymolysis for 3 hours; the protease is a commercial strain purchased in the conventional market, and can also be specifically subjected to enzymolysis by using a restriction enzyme; the temperature of enzymolysis is 34-37 ℃;
6. heating to 70-85 deg.C after enzymolysis, and treating for 15-30 min; then filtering and concentrating, and carrying out spray drying to prepare a finished product.
Example 3
A preparation method of fermentation type red date chelated peptide iron comprises the following specific steps:
1. crushing fresh red dates, adding water accounting for 20% of the mass of the red dates, stirring, pulping, and then adding cellulase into obtained date pulp for enzymolysis to obtain date pulp enzymatic hydrolysate; the cellulase is purchased from Shandong Longman bioengineering Co Ltd, the addition amount is 2.5%, and the enzymolysis temperature is 32-34 ℃.
2. Adding 1 time of heme protein into the jujube pulp enzymatic hydrolysate subjected to enzymolysis;
the hemoprotein was prepared as in example 1.
3. Homogenizing the jujube pulp enzymatic hydrolysate added with the haematochrome protein by a homogenizer for 1.5 h; adjusting the pH value of the homogenized mixed liquid to 5.0-6.0.
4. Inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 3 d; the fermentation temperature is 32 ℃, and the yeast and the lactobacillus are the conventional commercial strains purchased in the conventional market.
5. After fermentation is finished, adding protease into the fermented solution for enzymolysis for 1.5 h; the protease is a commercial strain purchased in the conventional market, and can also be specifically subjected to enzymolysis by using a restriction enzyme; the temperature of enzymolysis is 37 ℃;
6. after the enzymolysis is finished, heating to 85 ℃, and treating for 30 min; then filtering and concentrating, and carrying out spray drying to prepare a finished product.
Experimental examples comparative experiments were conducted on the products obtained in examples 1 to 3, with the currently marketed iron peptide products and the products obtained by adding jujube pulp to the iron peptide products, and the Caco-2 cell model absorption experiments showed that the products had a definite iron absorption utilization rate higher than that of iron peptide and the mixed products of iron peptide and jujube pulp.
Materials and methods
Caco-2 cell line, china type culture collection; caco-2 cells at 25 cm 2 The cell culture medium (DMEM high-sugar medium containing 10% fetal calf serum, 100 U.mL-1 penicillin, 100 U.mL-1 streptomycin, 2 mmol.L-1L-glutamine, target sample) was used in a culture flask at 37 deg.C and 5% CO 2 Culturing in an incubator. Determination of Caco-2 simulated intestinal skin absorption rate: collecting iron ions on the surface of Caco-2 cells, and determining the absorptivity of the iron ions by UPLC.
After the products of examples 1-3 are added, the activity of Caco-2 cells is improved, the iron ions obtained after the simulated digestion of the target sample are absorbed by the Caco-2 cells, the absorption rate of the iron ions is improved along with the prolonging of the transport time, and the absorption rate of the iron ions of example 3 is 1.56 times that of the peptide iron product and is 1.52 times that of the mixed product of the peptide iron and the jujube pulp.
While the invention has been described in further detail with reference to specific preferred embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention as defined by the appended claims.
Claims (9)
1. A preparation method of fermentation type red date chelated peptide iron is characterized by comprising the following steps:
1) pulping red dates, adding cellulase for enzymolysis to obtain a jujube pulp enzymolysis liquid;
2) adding haematochrome protein into the jujube pulp enzymatic hydrolysate, and performing homogenization treatment;
3) inoculating yeast and lactobacillus into the homogenized mixed liquid for fermentation for 1-3 d;
4) adding protease into the fermented solution for enzymolysis for 2-4 h; then concentrating and drying to obtain the finished product.
2. The method for preparing the fermented red date chelated peptide iron as claimed in claim 1, wherein the cellulase is 0.5-2.5% by mass.
3. The preparation method of the fermented red date chelated peptide iron as claimed in claim 1 or 2, wherein the enzymolysis time in step 1) is 2-6 h.
4. The method for preparing the fermented red date chelated peptide iron according to claim 1, characterized in that the hemoglobin protein is obtained by subjecting animal blood to anticoagulation treatment, centrifugal separation of erythrocytes, erythrocyte disruption, isoelectric point precipitation and centrifugal separation.
5. The method for preparing fermented red date chelated peptide iron as claimed in claim 1, wherein the homogenization treatment is to homogenize the red date pulp enzymolysis liquid added with haematochrome protein by using a homogenizer for 1-2 h.
6. The method for preparing fermented red date chelated iron peptide according to claim 1, wherein the mass ratio of the red date pulp enzymatic hydrolysate to the heme protein is 1: 1.5-2.5.
7. The method for preparing fermented red date chelated peptide iron as claimed in claim 1, wherein the pH value of the homogenized mixed liquid is adjusted to 5.0-6.0.
8. The preparation method of the fermented red date chelated peptide iron according to claim 1, characterized in that, after enzymolysis by protease, the temperature is raised to 70-85 ℃, and the treatment is carried out for 15-30 min; and then filtered.
9. The method for preparing the fermented red date chelated peptide iron according to claim 1, characterized in that the drying is spray drying.
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Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008020260A2 (en) * | 2006-08-16 | 2008-02-21 | R-Ko-N Kft. | Use of siderophores in prevention of vascular diseases, production of siderophores and qualifying siderophore containing meat-products |
| CN101664543A (en) * | 2009-09-02 | 2010-03-10 | 张滨 | Hemokinin-iron oral liquid |
| CN105420323A (en) * | 2015-12-23 | 2016-03-23 | 吉林大学 | Phytochelatin iron supplementation powder containing iron and preparation method of phytochelatin iron supplementation powder |
| CN105561286A (en) * | 2016-01-20 | 2016-05-11 | 吉林大学 | Red date iron replenishment drink containing peptide and iron-chelating peptide and preparation method |
| CN107048361A (en) * | 2017-04-12 | 2017-08-18 | 塔里木大学 | A kind of big rue granatum composite enzyme of jujube and preparation method thereof |
| CN107361270A (en) * | 2016-05-12 | 2017-11-21 | 洛阳华清天木生物科技有限公司 | A kind of preparation method of jujube enzyme beverage |
| CN108576317A (en) * | 2018-04-05 | 2018-09-28 | 安徽陆泰电气科技有限公司 | A kind of richness iron chelating stone flower tea powder and preparation method thereof |
| CN114010762A (en) * | 2021-11-01 | 2022-02-08 | 杭州佰倍优生物科技有限公司 | Preparation for improving anemia symptoms and preparation method thereof |
-
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Patent Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008020260A2 (en) * | 2006-08-16 | 2008-02-21 | R-Ko-N Kft. | Use of siderophores in prevention of vascular diseases, production of siderophores and qualifying siderophore containing meat-products |
| CN101664543A (en) * | 2009-09-02 | 2010-03-10 | 张滨 | Hemokinin-iron oral liquid |
| CN105420323A (en) * | 2015-12-23 | 2016-03-23 | 吉林大学 | Phytochelatin iron supplementation powder containing iron and preparation method of phytochelatin iron supplementation powder |
| CN105561286A (en) * | 2016-01-20 | 2016-05-11 | 吉林大学 | Red date iron replenishment drink containing peptide and iron-chelating peptide and preparation method |
| CN107361270A (en) * | 2016-05-12 | 2017-11-21 | 洛阳华清天木生物科技有限公司 | A kind of preparation method of jujube enzyme beverage |
| CN107048361A (en) * | 2017-04-12 | 2017-08-18 | 塔里木大学 | A kind of big rue granatum composite enzyme of jujube and preparation method thereof |
| CN108576317A (en) * | 2018-04-05 | 2018-09-28 | 安徽陆泰电气科技有限公司 | A kind of richness iron chelating stone flower tea powder and preparation method thereof |
| CN114010762A (en) * | 2021-11-01 | 2022-02-08 | 杭州佰倍优生物科技有限公司 | Preparation for improving anemia symptoms and preparation method thereof |
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