CN115010803A - Preparation of hemoglobin polypeptide rich in heme iron - Google Patents
Preparation of hemoglobin polypeptide rich in heme iron Download PDFInfo
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- OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 2
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- PMVSDNDAUGGCCE-TYYBGVCCSA-L Ferrous fumarate Chemical compound [Fe+2].[O-]C(=O)\C=C\C([O-])=O PMVSDNDAUGGCCE-TYYBGVCCSA-L 0.000 description 1
- DKKCQDROTDCQOR-UHFFFAOYSA-L Ferrous lactate Chemical compound [Fe+2].CC(O)C([O-])=O.CC(O)C([O-])=O DKKCQDROTDCQOR-UHFFFAOYSA-L 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 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
- OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
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- MDXRFOWKIZPNTA-UHFFFAOYSA-L butanedioate;iron(2+) Chemical compound [Fe+2].[O-]C(=O)CCC([O-])=O MDXRFOWKIZPNTA-UHFFFAOYSA-L 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- FAPWYRCQGJNNSJ-UBKPKTQASA-L calcium D-pantothenic acid Chemical compound [Ca+2].OCC(C)(C)[C@@H](O)C(=O)NCCC([O-])=O.OCC(C)(C)[C@@H](O)C(=O)NCCC([O-])=O FAPWYRCQGJNNSJ-UBKPKTQASA-L 0.000 description 1
- 229960002079 calcium pantothenate Drugs 0.000 description 1
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- 238000000605 extraction Methods 0.000 description 1
- 210000001105 femoral artery Anatomy 0.000 description 1
- 210000003191 femoral vein Anatomy 0.000 description 1
- 229960002089 ferrous chloride Drugs 0.000 description 1
- 239000011773 ferrous fumarate Substances 0.000 description 1
- 229960000225 ferrous fumarate Drugs 0.000 description 1
- 235000002332 ferrous fumarate Nutrition 0.000 description 1
- 235000013924 ferrous gluconate Nutrition 0.000 description 1
- 239000004222 ferrous gluconate Substances 0.000 description 1
- 229960001645 ferrous gluconate Drugs 0.000 description 1
- 239000004225 ferrous lactate Substances 0.000 description 1
- 235000013925 ferrous lactate Nutrition 0.000 description 1
- 229940037907 ferrous lactate Drugs 0.000 description 1
- 229960001604 ferrous succinate Drugs 0.000 description 1
- 229960000304 folic acid Drugs 0.000 description 1
- 235000019152 folic acid Nutrition 0.000 description 1
- 239000011724 folic acid Substances 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
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- 238000007710 freezing Methods 0.000 description 1
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- 238000001727 in vivo Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- NMCUIPGRVMDVDB-UHFFFAOYSA-L iron dichloride Chemical compound Cl[Fe]Cl NMCUIPGRVMDVDB-UHFFFAOYSA-L 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- VRIVJOXICYMTAG-IYEMJOQQSA-L iron(ii) gluconate Chemical compound [Fe+2].OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O.OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O VRIVJOXICYMTAG-IYEMJOQQSA-L 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
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- 229960003512 nicotinic acid Drugs 0.000 description 1
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- 230000000050 nutritive effect Effects 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
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- 239000011734 sodium Substances 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/795—Porphyrin- or corrin-ring-containing peptides
- C07K14/805—Haemoglobins; Myoglobins
-
- 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
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a preparation method of hemoglobin polypeptide rich in heme iron. The method takes fresh animal blood as a raw material, and obtains the hemoglobin polypeptide rich in heme iron by a biological enzymolysis technology. The hemoglobin polypeptide obtained by the invention has the characteristics of high polypeptide content, high heme iron content, small molecular weight, good water solubility, good taste and the like, has a good curative effect on improving iron deficiency anemia, and can be widely applied to the fields of food, medicine and the like.
Description
Technical Field
The invention relates to the field of animal polypeptides, and in particular relates to preparation of hemoglobin polypeptide rich in heme iron.
Background
Common iron supplements on the market comprise ferrous sulfate, ferrous chloride, ferrous gluconate, ferrous lactate, ferrous succinate, ferrous fumarate and the like, and although the iron content of the iron supplements is high, the iron supplements have low utilization rate in vivo, large toxic and side effects and special metal rust taste, and are difficult to eat for a long time. The heme iron is a biological iron, can be directly absorbed by intestinal mucosa cells, does not produce any digestive tract stimulation symptom, has high bioavailability, and is a more ideal iron supplement. Heme iron is an important nutrient in blood, the main source of which is animal blood. The animal blood is the first byproduct obtained after slaughtering, and is an animal protein resource with high nutritive value and great development and utilization value. However, the utilization rate of blood for animal slaughtering in China is very low, wherein a part of blood is used in the form of primary processing such as blood powder or blood bean curd, and the like, and a considerable part of blood is discharged or discarded in the form of sewage, the utilization rate is less than 10%, so that a large amount of precious nutrient resources are lost, and serious environmental pollution is caused. Therefore, the utilization of animal blood to develop the functional foods of biological peptides, food additives and the like can not only improve the utilization rate of blood and the added value of animal products, but also have important significance for prolonging the industrial chain of industrial production of animal blood products, increasing the economic income of farmers and herders and protecting the ecological environment.
At present, hemoglobin polypeptide products in the market are not rich in heme iron and have serious bitter taste and fishy smell. Hemoglobin polypeptide rich in heme iron is not found because heme iron is easily oxidized in the enzymolysis process, incomplete protein shearing can be caused by insufficient enzymolysis in the enzymolysis process, and excessive precipitation can be caused by excessive enzymolysis. The prior patents related to the preparation application of the blood peptide include, for example, "preparation method of deer blood peptide and anti-fatigue effect thereof" with application publication number CN107164446A, "preparation method of enzymatic hydrolyzed tuna blood protein antihypertensive peptide" with application publication number CN105063150A, "preparation method of camel blood protein polypeptide" with application publication number CN107557423A, "extraction method of pig blood peptide" with application publication number CN102367465A, "industrial production method of enzymatic hydrolysis of pig whole blood into oligopeptide and amino acid" with application publication number CN103589770B, and preparation of hemoglobin polypeptide rich in heme iron is not seen in the prior patents. Aiming at the current research and development situation, the invention provides a preparation method of hemoglobin polypeptide rich in heme iron.
Disclosure of Invention
The invention aims to provide a preparation method of hemoglobin polypeptide rich in heme iron.
The technical scheme adopted by the invention is as follows:
a method for preparing hemoglobin polypeptide rich in heme iron comprises the following steps:
(1) treating raw materials: after fresh bovine blood is collected from a slaughterhouse, quickly adding sodium citrate for anticoagulation, centrifuging to remove blood plasma, and collecting red blood cells; high-shear cell membrane crushing is carried out by adopting a high-pressure homogenizer; heating at 50 deg.C for 30min in dark condition to obtain hemoglobin.
(2) Enzymolysis: adding protease into the mixture at a certain temperature and pH according to a certain feed-liquid ratio for enzymolysis;
(3) and (3) ultrafiltration concentration: the cut-off molecular weight of the ultrafiltration membrane is 6000-;
(4) and (3) drying: a spray drying method is adopted.
Wherein the blood in the step (1) is mainly bovine blood or sheep blood.
The enzymolysis method in the step (2) comprises the following steps: adding a proper amount of purified water according to the feed-liquid ratio of 1: 10-20, adding trypsin and flavourzyme with the enzyme dosage of 5.0-10.0 per mill of the weight of the fresh animal blood, carrying out enzymolysis for 8 hours, wherein the enzymolysis temperature is 45 ℃ in the first 6 hours, the pH is 7.5, the enzymolysis temperature is 55 ℃ in the last 2 hours, the pH is 7, boiling for 0.5 hour, and inactivating the enzyme.
The spray drying conditions in the step (4) are that the air inlet temperature is 160-180 ℃ and the air outlet temperature is 80-100 ℃.
Compared with the existing blood protein polypeptide patent, the invention has the following advantages and beneficial effects:
(1) the invention adopts a special raw material treatment mode: the high-shear cell membrane is crushed by adopting a high-pressure homogenizer, so that the efficiency is improved, and the protein content is also improved; further combining with physical denaturation method, heating at 50 deg.C for 30min in dark condition to remove denatured impurity protein, and obtaining relatively pure hemoglobin with hemoglobin content of above 90%.
(2) The invention screens special enzyme for enzymolysis to obtain hemoglobin polypeptide rich in heme iron, which can be directly absorbed by intestinal mucosa cells without generating any digestive tract stimulation symptom compared with the traditional iron supplement.
Detailed Description
The following detailed description of the embodiments of the present invention is provided for illustrative purposes, and is not intended to limit the scope of the present invention.
Comparative example 1 feedstock treatment
The bovine blood and the sheep blood are subjected to wall breaking treatment by adopting a water swelling method, a high shear crushing method and a normal saline washing and wall breaking method respectively, and test results are shown in tables 1 and 2.
TABLE 1 bovine hemoglobins (BHb g/L) obtained by different wall-breaking treatments
TABLE 2 sheep blood hemoglobin (BHb g/L) obtained by different wall breaking treatment methods
As can be seen from the data in tables 1 and 2, compared with the traditional water swelling method for wall breaking of red blood cells and normal saline washing for wall breaking of red blood cells, the high shear crushing method is more convenient, rapid and effective in wall breaking, the sodium content of the product is controlled, the energy consumption in the production process is reduced, and the hemoglobin content is increased. Meanwhile, by further combining a physical denaturation method, denatured hybrid protein is removed on the basis of ensuring the biological activity of hemoglobin, so that the content of the hemoglobin is up to more than 90%.
The method combines the dissolved amount of the hemoglobin and the actual production efficiency and adopts a high-shear cell membrane breaking method to carry out pretreatment on the animal blood.
Comparative example 2 comparison of enzymatic Effect and iron content of hemoglobin in different enzyme preparations
In order to obtain the optimal enzyme preparation of hemoglobin polypeptide rich in heme iron by screening, the enzymolysis effect of trypsin, flavourzyme and papain on bovine blood is respectively considered, and the content of polypeptide, the clarity and the iron content are taken as indexes. Table 3 shows the polypeptide content and the heme iron content obtained after the enzymatic treatment of different enzyme preparations. As can be seen from the data in Table 3, under the respective optimal hydrolysis conditions, the content of polypeptide, clarity and iron content after the enzymolysis treatment by trypsin and flavourzyme are the highest, and the effect is the best. By combining test data and adopting trypsin and flavourzyme to carry out enzymolysis on the bovine hemoglobin, the obtained polypeptide content and the iron content of the product are relatively highest, the clarity of the solution is optimal, and the method is suitable for industrial production.
TABLE 3 enzymolysis effect and heme iron content of different enzyme preparations
Example 1
A method for preparing hemoglobin polypeptide rich in heme iron comprises the following steps:
(1) raw material treatment: after fresh bovine blood is collected from a slaughterhouse, quickly adding sodium citrate for anticoagulation, centrifuging to discard blood plasma, and collecting red blood cells; high-shear cell membrane crushing is carried out by adopting a high-pressure homogenizer; heating at 50 deg.C for 30min in dark condition to obtain hemoglobin.
(2) Enzymolysis: adding a proper amount of purified water according to the material-liquid ratio of 1: 10, uniformly stirring, adjusting the temperature of the solution to be 45 ℃, adding trypsin with the pH value of 7.5 being 6.0 per mill of the weight of the fresh animal blood, carrying out enzymolysis treatment for 6 hours, then adding flavourzyme with the weight of 8.0 per mill of the weight of the fresh animal blood under the conditions that the temperature of the solution is 55 ℃ and the pH value is 7, carrying out enzymolysis for 2 hours, finishing the enzymolysis, boiling for 0.5 hour, and inactivating the enzyme.
(3) And an ultrafiltration membrane with the membrane aperture of 10KD is adopted for molecular interception.
(4) And (4) performing single-effect concentration on the ultrafiltered enzymolysis solution until the concentration is 30-50.
(5) And (3) drying: a spray drying method is adopted, wherein the air inlet temperature is 160 ℃, and the air outlet temperature is 85 ℃.
The obtained hemoglobin polypeptide has 88.26% of iron content 2659.86mg/kg
Example 2
A method for preparing hemoglobin polypeptide rich in heme iron comprises the following steps:
(1) treating raw materials: after fresh bovine blood is collected from a slaughterhouse, quickly adding sodium citrate for anticoagulation, centrifuging to remove blood plasma, and collecting red blood cells; high-shear cell membrane crushing is carried out by adopting a high-pressure homogenizer; heating at 50 deg.C for 30min in dark condition to obtain hemoglobin.
(2) Enzymolysis: adding a proper amount of purified water according to the material-liquid ratio of 1: 20, uniformly stirring, adjusting the temperature of the solution to be 45 ℃, adding trypsin with the pH value of 7.5 being 5.0 per mill of the weight of the fresh animal blood, carrying out enzymolysis treatment for 6 hours, then adding flavourzyme with the weight being 5.0 per mill 3 percent of the weight of the fresh animal blood under the conditions that the temperature of the solution is 55 ℃ and the pH value is 7, carrying out enzymolysis for 2 hours, finishing enzymolysis, boiling for 0.5 hour, and inactivating enzyme.
(3) And (3) performing molecular interception by using an ultrafiltration membrane with the membrane pore diameter of 10 KD.
(4) And performing single-effect concentration on the ultrafiltered enzymolysis liquid until the concentration is 30-50.
(5) And (3) drying: a spray drying method is adopted, wherein the air inlet temperature is 170 ℃, and the air outlet temperature is 85 ℃.
The obtained hemoglobin polypeptide has 90.06% of iron content 2785.58mg/kg
Comparative example 3 detection of iron content of commercially available different hemoglobin polypeptide stocks
Table 4 shows the results of measuring the iron content of the commercial hemoglobin polypeptide peptide raw materials, wherein the hemoglobin polypeptide No. 1 is the product of the present invention, i.e., intra-mongolia sky-based biotechnology limited company, and the hemoglobin polypeptides No. 2, 3, 4, 5, and 6 are other commercial products. The result shows that the iron content in the product is 2579.84mg/kg, which is far higher than other products, and the product is hemoglobin polypeptide rich in heme iron.
TABLE 4 iron content of commercial hemoglobin polypeptide materials and iron supplement products
Example 4 experiment of hemoglobin Polypeptides on iron deficiency anemia animals
The intervention of the blood protein polypeptide in the invention on IDA rats is carried out, and the research on three aspects of blood indexes, body weight and protein nutrition is carried out to research the prevention effect of the blood protein polypeptide on the IDA of the rats.
1. Experimental materials and instruments
1.1 Experimental materials
1.1.1 Experimental animals
The Wistar strain rat is 4 weeks old, 60 +/-6 g in weight, half male and half female, and good in health condition.
1.1.2 iron element
A blood protein polypeptide: the blood protein used in the experiment is mostly a sample provided by inner Mongolia Tianqi biotechnology limited in the same batch, and the iron content of the sample is 2650.25 mg/kg.
Ferrous sulfate: zhengzhou repup bioengineering limited.
1.1.3 Low-iron feed
And (3) measuring the iron content in the feed by an atomic absorption method by referring to the AOAC low-iron base material, wherein the iron content is 7 mg/kg. The formulation is shown in Table 5.
TABLE 5 Low iron feed formulations
Note: 1. mixed minerals (no iron), whose composition is (%): MnSO 4 ·H 2 O，6.65；ZnSO 4 ·H 2 O，3.39；CuSO 4 ·H 2 O, 0.97; KI (containing I, 0.65%), 1.23; corn starch, 87.76. Mixed vitamins consisting of (per kg): VA: 4000 IU; VD 3 ：1000IU；VE：50IU；VK 3 ：50μg；VB 1 ：6mg；VB 2 ：6mg；VB 6 : 7 mg; nicotinic acid: 30 mg; calcium pantothenate: 15 mg; 2mg of folic acid; biotin: 0.2 mg.
The iron pollution is strictly controlled in the feed preparation process, all the tools for holding the feed are soaked overnight by nitric acid, and are repeatedly washed clean by deionized water.
1.2 Experimental instruments
Microsyrinths (MC, shanghai anting microsyrinths); stainless steel electric heating plates (DB-III, Shandong Yucheng Jiade apparatus factory); muffle furnace (science instruments and Equipment factory, Tianjin); an automatic hemocytometer (sysmef-820, hismeton, japan); atomic absorption spectrophotometer (model AA-6200, Shimadzu corporation, Japan); analytical balance (model a5003N, shanghai analytical electronic balance plant); centrifuge (model LD4-2, Beijing medical centrifuge Mill).
2. Experimental method
2.1 feeding conditions: stainless steel mouse cages are adopted, distilled water is drunk, natural lighting is realized, free food taking is realized, the room temperature is 22 +/-2 ℃, the humidity is 50% -60%, the stainless steel mouse cages, enamel food basins and glass water feeders are adopted, all utensils are soaked in 10% nitric acid solution to ensure that animals are in a strict iron-free environment, and the pollution of external iron is strictly prevented in experiments. The experimental rats are fed with distilled water and other animals are fed according to the operating rules of experimental animal feeding
2.2 Experimental groups
Experimental animals were randomly divided into 5 groups of 10 animals each. Respectively a normal control group, a ferrous sulfate group, a blood protein polypeptide high-dose group, a blood protein polypeptide low-dose group and a model control group.
2.3 animal model preparation and administration method
Control group: feeding basic feed and feeding 10mL/kg of deionized water;
iron deficiency model group: feeding low-iron feed and 10mL/kg of deionized water for intragastric administration;
high dose fibrin polypeptid set: feeding low-iron feed and gavage 200mg/kg d blood protein polypeptide containing 2.0mg/kg d iron;
low dose fibrin polypeptid set: feeding low-iron feed and gavage 100mg/kg d blood protein polypeptide solution containing 1.0mg/kg d iron;
ferrous sulfate group: feeding low-iron feed and a gastric lavage 5.5 mg/kg.d ferrous sulfate solution containing 2.0 mg/kg.d iron;
each group of rats had free access to food and drinking deionized water.
3. Detecting an object
Respectively collecting blood from tail vein before molding and after 5 weeks, collecting about 0.1mL of blood from one tube of the two tubes of blood from each rat, performing anticoagulation treatment, and measuring hemoglobin and erythrocyte amount; collecting the rest blood into a 5.0mL centrifuge tube, preserving the heat for 30min in a 37 ℃ water bath box, preparing serum by centrifugation, freezing and storing the serum for detection of Serum Iron (SI). Hb content was measured by an automatic blood cell analyzer. Meanwhile, taking femoral artery and vein blood to measure blood, measuring the total serum protein, albumin, globulin level and Serum Iron (SI) iron by a full-automatic blood biochemical analyzer conventionally and measuring by an atomic absorption method.
4. Statistical analysis
Statistical analysis was performed using SPSS 19.0. Performing single-factor variance analysis on all indexes, and performing comparison among groups by using an LSD method; and (4) adopting a rank sum test on data which is not normal or has uneven variance.
5. Results of the experiment
5.1 Effect of hemoglobin Polypeptides on rat hemoglobin
Before the experiment, the hemoglobin difference of each group of rats has no statistical significance (P is more than 0.05); at the end of the experiment, compared with the control group, the hemoglobin content of the iron deficiency model group is obviously reduced (P is less than 0.05); compared with the iron deficiency model group, the hemoglobin concentrations of the high-dose hemoglobin polypeptide group, the low-dose hemoglobin polypeptide group and the ferrous sulfate group are all obviously increased (P is less than 0.05); the concentration of the hemoglobin is not significantly different from that of the hemoglobin before modeling (P is more than 0.05), and the hemoglobin concentration is not significantly different between the high-dose hemoglobin polypeptide group and the low-dose hemoglobin polypeptide group and between the high-dose hemoglobin polypeptide group and the ferrous sulfate group (P is more than 0.05), and detailed results are shown in a table 6.
Table 6 effect of hemoglobin polypeptides on rat hemoglobin (n-10,
)
note: p < 0.05 compared to normal group; comparison of P < 0.01 with normal group
Comparison of P & lt 0.05 with the model group; the comparison of a tangle-solidup with the model group P is less than 0.01
P is less than 0.05 compared with the ferrous sulfate group; it is rather than the high dose group, P < 0.01
□ comparison P < 0.05 compared to before experiment; □ □ comparison with high dose group P < 0.01
5.2 Effect of the hemoglobin Polypeptides on the number of Red blood cells in rats
Before the experiment, the difference of the number of the red blood cells of each group of rats has no statistical significance (P is more than 0.05); at the end of the experiment, the red blood cell number content of the iron-deficiency model group is obviously reduced (P is less than 0.05) compared with that of the control group; compared with the iron deficiency model group, the red blood cell number of the high-dose blood protein polypeptide group, the low-dose blood protein polypeptide group and the ferrous sulfate group is obviously increased (P is less than 0.05); the number of the red blood cells is not significantly different from that of the red blood cells before model building (P is more than 0.05), and the results are shown in a table 7, wherein the three groups are a high-dose blood protein polypeptide group, a low-dose blood protein polypeptide group and ferrous sulfate.
TABLE 7 Effect of blood protein Polypeptides on the number of Red blood cells in rats (× 10) 12 /L，n＝10，
)
Note: p < 0.05 compared to normal group; comparison of P < 0.01 with the abnormal group
Comparison of P & lt 0.05 with the model group; the comparison of a tangle-solidup with the model group P is less than 0.01
P is less than 0.05 compared with ferrous sulfate group; it is rather than the high dose group, P < 0.01
□ comparison P < 0.05 compared to before experiment; □ □ comparison with high dose group P < 0.01
5.3 Effect of the hemoglobin Polypeptides on the hematocrit of rats
Before the experiment, the difference of the hematocrit of the rats in each group has no statistical significance (P is more than 0.05); at the end of the experiment, compared with a control group, the hematocrit content of the iron-deficiency model group is obviously reduced (P is less than 0.05); compared with the iron deficiency model group, the haematocrit of the high-dose blood protein polypeptide group, the low-dose blood protein polypeptide group and the ferrous sulfate group is obviously increased (P is less than 0.05); the erythrocyte volume is not significantly different from that before modeling (P is more than 0.05), and is not significantly different among the high-dose blood protein polypeptide group, the low-dose blood protein polypeptide group and the ferrous sulfate (P is more than 0.05), and the results are shown in a table 8.
Table 8 effect of blood protein polypeptides on rat hematocrit (n-10,
)
note: p < 0.05 compared to normal group; comparison of P < 0.01 with normal group
Comparison of P & lt 0.05 with the model group; the comparison of a tangle-solidup with the model group P is less than 0.01
P is less than 0.05 compared with ferrous sulfate group; it is much better than the high dose group than P < 0.01
□ comparison P < 0.05 compared to before experiment; □ □ comparison with high dose group P < 0.01
5.4 Effect of hemoglobin Polypeptides on rat serum iron concentration
Before the experiment, the difference of the serum iron concentration of rats in each group has no statistical significance (P is more than 0.05); at the end of the experiment, compared with a control group, the serum iron concentration content of the iron-deficiency model group is obviously reduced (P is less than 0.05); compared with the iron deficiency model group, the serum iron concentrations of the high-dose blood protein polypeptide group, the low-dose blood protein polypeptide group and the ferrous sulfate group are obviously increased (P is less than 0.05); the serum iron concentration before the model building is not significantly different (P is more than 0.05), and the serum iron concentration is not significantly different among a high-dose blood protein polypeptide group, a low-dose blood protein polypeptide group and ferrous sulfate (P is more than 0.05), and the results are shown in a table 9.
Table 9 effect of hemoglobin polypeptides on rat serum iron concentration (n ═ 10, x ± s
)
Note: p < 0.05 compared to normal group; comparison of P < 0.01 with normal group
Comparison of P & lt 0.05 with the model group; the comparison of a tangle-solidup with the model group P is less than 0.01
P is less than 0.05 compared with ferrous sulfate group; it is rather than the high dose group, P < 0.01
□ comparison P < 0.05 compared to before experiment; □ □ comparison with high dose group P < 0.01
The study observed the effects of hemoglobin polypeptides on serum iron content, hemoglobin, red blood cell count and hematocrit in an anemic rat model, and compared to ferrous sulfate. The results show that the high-dose histone and the low-dose histone can obviously improve the serum iron content, the hemoglobin, the erythrocyte number and the hematocrit (P is less than 0.05); has no significant difference (P is more than 0.05) with that before molding. And after 5 weeks of administration, no significant difference exists among the high-dose blood protein polypeptide group, the low-dose blood protein polypeptide group and the ferrous sulfate group (P is more than 0.05). The hemoglobin polypeptide obtained by the invention has better curative effect on improving iron deficiency anemia.
Claims (9)
1. The preparation method of the hemoglobin polypeptide rich in heme iron comprises the following steps: (1) processing raw materials; (2) enzyme treatment; (3) ultrafiltration and concentration; (4) and (5) drying to obtain the product.
2. The method for preparing hemoglobin polypeptide rich in heme iron according to claim 1, wherein the raw material of step (1) is processed by collecting fresh animal blood from slaughter house, adding sodium citrate for anticoagulation, centrifuging to remove blood plasma, and collecting red blood cells; high-shear cell membrane crushing is carried out by adopting a high-pressure homogenizer; heating at 50 deg.C for 30min in dark condition to obtain hemoglobin.
3. The preparation method of the heme iron-rich hemoglobin polypeptide of claim 1, wherein the enzymolysis treatment in step (2) comprises adding purified water to the pretreated hemoglobin at a ratio of 1: 10-20, wherein trypsin and flavourzyme are added in an amount of 5.0-10.0% of the weight of the fresh blood of the animal, and the enzymolysis time is 8 hours, wherein the enzymolysis temperature in the first 6 hours is 45 ℃, the pH value is 7.5, the enzymolysis temperature in the second 2 hours is 55 ℃, the pH value is 7, and the enzyme is deactivated after boiling for 0.5 hour.
4. The method for preparing hemoglobin polypeptide containing abundant heme iron as claimed in claim 1, wherein the ultrafiltration membrane of step (3) has a cut-off molecular weight of 6000-30000, and is concentrated by single-effect concentration.
5. The method for preparing hemoglobin polypeptide rich in heme iron according to claim 2, wherein the drying method in the step (4) is a spray drying method, and the spray drying conditions are that the air inlet temperature is 160-180 ℃ and the air outlet temperature is 80-100 ℃.
6. The method of claim 2, wherein the feed-to-liquid ratio is preferably 1: 15.
7. The method for preparing hemoglobin polypeptide of claim 2, wherein the trypsin is preferably used in an amount of 5.0% by weight of the fresh blood of the animal, and the flavourzyme is preferably used in an amount of 8.0% by weight of the fresh blood of the animal.
8. The method of any one of claims 1-6, wherein the amount of said hemoglobin polypeptide is greater than 85%, and wherein the iron content is greater than 2600 mg/kg.
9. The use of a blood protein peptide according to any one of claims 1-7 for ameliorating iron deficiency anemia.
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