CN116987178A - Preparation method of fish bone collagen polypeptide chelated calcium powder - Google Patents

Preparation method of fish bone collagen polypeptide chelated calcium powder Download PDF

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CN116987178A
CN116987178A CN202310991004.XA CN202310991004A CN116987178A CN 116987178 A CN116987178 A CN 116987178A CN 202310991004 A CN202310991004 A CN 202310991004A CN 116987178 A CN116987178 A CN 116987178A
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powder
polypeptide
fishbone
fish bone
enzymolysis
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李帅
李珊珊
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Qiqihar University
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Qiqihar University
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    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/06Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products

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Abstract

The invention discloses a preparation method of fish bone collagen polypeptide chelated calcium powder, which aims to solve the problems that the existing bone polypeptide has low chelation rate with calcium ions, the antioxidation activity is required to be improved, and the like. The preparation method comprises the following steps: 1. pre-treating fish bones; 2. immersing the fishbone powder into lactic acid solution for acidolysis treatment to obtain decalcified fishbone powder; 3. adding decalcified fishbone powder into water, and adding papain for enzymolysis; 4. mixing fishbone powder and the fishbone powder after enzymolysis, adding the fishbone powder into water, and adding compound protease for enzymolysis treatment; 5. lyophilizing the mixed polypeptide solution to obtain polypeptide powder; 6. polypeptide powder and CaCl 2 Adding the above materials into calcium solution for chelation reaction. The invention takes fish bones as raw materials and adopts papaya eggsThe method comprises the steps of carrying out enzymolysis treatment on decalcified fish bone powder by using white enzyme, and then treating and mixing the fish bone powder by using compound protease. The chelation rate of the polypeptide powder and calcium ions reaches more than 70%, and the proliferation rate of the fish bone collagen polypeptide chelated calcium powder to osteoblasts is about 160%.

Description

Preparation method of fish bone collagen polypeptide chelated calcium powder
Technical Field
The invention relates to a preparation method of a bone collagen polypeptide calcium chelate.
Background
The fishery cultivation yield of China accounts for 70% of the global cultivation yield, and is the only country with the cultivation yield exceeding the fishing yield in the main fishery countries in the world. Along with the development of fishery in China, fishery processing is also attracting more and more attention. A large amount of offal including fish head, fish skin, fish fin, fish tail, fish bone and residual fish meat can be produced in the processing process of the fish product, and if the protein and nutrient elements in the offal can be fully utilized, the additional value can be improved, and the environmental pollution can be reduced.
The fish bone has the characteristics of high protein and low fat, the calcium content is obviously higher than that of livestock bones such as cattle, pigs, sheep, chickens and the like, and the calcium-phosphorus ratio is close to the optimal absorption ratio of 2:1. In recent years, research on the fishbone shows that the fishbone can be used for preparing active calcium, fishbone food, extracting collagen, chondroitin and other components, and also can be used for wastewater treatment and the like. Ogawa extracts acid-soluble collagen, which is typically type I collagen, from bones and scales of black drum fish, sheep sea bream, and can be used in functional foods, cosmetics, and biopharmaceuticals.
The fish bone contains abundant collagen components, and is an excellent resource for developing fish collagen. Collagen in bones can be effectively utilized through enzymolysis, and is hydrolyzed into collagen polypeptide and amino acid, so that the collagen polypeptide and amino acid are easier to digest and absorb by human bodies, the unique nutrition effect is exerted, and the functional characteristics of the collagen polypeptide and amino acid can be improved. The collagen polypeptide is an enzymolysis product of collagen, and has a molecular weight much lower than that of collagen, and researches show that the collagen polypeptide has good functional characteristics such as solubility, oil absorption, foamability, water absorption and the like, and the hydrolysate of the fish bone protein also has a certain oxidation resistance.
Disclosure of Invention
The invention aims to solve the problems that the existing bone polypeptide has low chelation rate with calcium ions, has antioxidant activity and has to be improved on osteoblast proliferation activity, and the like, and provides a preparation method of fish bone collagen polypeptide chelated calcium powder.
The preparation method of the fish bone collagen polypeptide chelated calcium powder is realized according to the following steps:
1. putting the fish bones with the fish meat removed into water, steaming at high pressure at a temperature of more than 100 ℃, cooling, grinding, and drying to obtain the fish bone powder;
2. immersing fishbone powder into a lactic acid solution with the mass fraction of 1.5-2%, carrying out water bath reaction at the temperature of 50-60 ℃, filtering and respectively collecting calcium-dissolving liquid and bone powder after water bath, and washing and drying the bone powder after water bath to obtain decalcified fishbone powder;
3. adding decalcified fishbone powder into water, regulating the pH value of the system to be 7, then adding papain, carrying out enzymolysis treatment for 1.5-3 h at the temperature of 40-55 ℃, inactivating enzyme, cooling, and respectively collecting hydrolysate and the fishbone powder after enzymolysis;
4. mixing the fishbone powder obtained in the first step with the fishbone powder obtained after enzymolysis, adding the fishbone powder into water, adjusting the pH value of a system to be 7, adding compound protease, carrying out enzymolysis at the temperature of 40-55 ℃ for 2.5-3.5 hours, inactivating enzyme, cooling, and collecting enzymolysis liquid;
5. mixing the enzymolysis liquid and the hydrolysis liquid in the step three, filtering by an ultrafiltration membrane to obtain a mixed polypeptide solution, and carrying out freeze-drying treatment on the mixed polypeptide solution to obtain polypeptide powder;
6. polypeptide powder and CaCl 2 Adding the mixture into the calcium solution in the second step, carrying out chelation reaction at the temperature of 55-65 ℃, cooling, adding absolute ethyl alcohol for alcohol precipitation, and freeze-drying the precipitate to obtain the fish bone collagen polypeptide chelated calcium powder;
wherein the addition amount of papain in the third step is 2500-3000U/g; in the fourth step, the compound protease consists of neutral protease and flavourzyme, and the adding amount of the compound protease is controlled to be 3000-4000U/g.
The method for preparing the polypeptide chelated calcium powder takes fish bones as raw materials, and the pretreated fish bones are immersed into lactic acid solution for acidolysis, so that calcium components in the fish bones are dissolved out to form free calcium, the biological activity of the free calcium in the calcium solution is better and the free calcium is easier to absorb, and meanwhile, the collagen can be primarily hydrolyzed by acidolysis. Then, carrying out enzymolysis treatment on the decalcified fishbone powder by adopting papain, wherein the digestion capacity of the papain is moderate, and the enzymolysis treatment time is required to be controlled at the moment so as to obtain collagen polypeptide with proper molecular weight; mixing the fishbone powder obtained in the first step with the fishbone powder obtained after enzymolysis, and performing advanced enzymolysis with compound protease, wherein the compound protease comprises neutral protease and flavourzyme, the neutral protease is endopeptidase, and the flavourzyme contains exo-proteaseThe peptidase can provide various enzyme cutting sites, more polypeptides with molecular weight below 3kDa can be obtained through deep enzymolysis, and meanwhile, the flavor protease can also improve the peculiar smell of the fish bone collagen polypeptide. Finally, polypeptide powder and CaCl are added 2 Adding into calcium-dissolving solution together, and adding CaCl into the solution simultaneously 2 The provided calcium ions and active calcium generated by acidolysis are combined with the polypeptide with low molecular weight, so that the chelation rate of the calcium is improved, and the chelation rate is up to more than 70%.
The chelation rate of the polypeptide powder prepared by the invention and calcium ions reaches more than 70%, and the proliferation rate of the fish bone collagen polypeptide chelated calcium powder to osteoblasts is about 160%.
Detailed Description
The first embodiment is as follows: the preparation method of the fish bone collagen polypeptide chelated calcium powder of the embodiment is implemented according to the following steps:
1. putting the fish bones with the fish meat removed into water, steaming at high pressure at a temperature of more than 100 ℃, cooling, grinding, and drying to obtain the fish bone powder;
2. immersing fishbone powder into a lactic acid solution with the mass fraction of 1.5-2%, carrying out water bath reaction at the temperature of 50-60 ℃, filtering and respectively collecting calcium-dissolving liquid and bone powder after water bath, and washing and drying the bone powder after water bath to obtain decalcified fishbone powder;
3. adding decalcified fishbone powder into water, regulating the pH value of the system to be 7, then adding papain, carrying out enzymolysis treatment for 1.5-3 h at the temperature of 40-55 ℃, inactivating enzyme, cooling, and respectively collecting hydrolysate and the fishbone powder after enzymolysis;
4. mixing the fishbone powder obtained in the first step with the fishbone powder obtained after enzymolysis, adding the fishbone powder into water, adjusting the pH value of a system to be 7, adding compound protease, carrying out enzymolysis at the temperature of 40-55 ℃ for 2.5-3.5 hours, inactivating enzyme, cooling, and collecting enzymolysis liquid;
5. mixing the enzymolysis liquid and the hydrolysis liquid in the step three, filtering by an ultrafiltration membrane to obtain a mixed polypeptide solution, and carrying out freeze-drying treatment on the mixed polypeptide solution to obtain polypeptide powder;
6. polypeptide powder and CaCl 2 Added together in step twoPerforming chelation reaction in the calcium-dissolving liquid at 55-65 ℃, cooling, adding absolute ethyl alcohol for alcohol precipitation, and freeze-drying the precipitate to obtain fish bone collagen polypeptide chelated calcium powder;
wherein the addition amount of papain in the third step is 2500-3000U/g; in the fourth step, the compound protease consists of neutral protease and flavourzyme, and the adding amount of the compound protease is controlled to be 3000-4000U/g.
The fish bone used in the first step of the present embodiment may be salmon bone, cod bone, weever bone, silver carp bone, plaice bone, tuna bone, or the like.
The enzymolysis treatment time of the third and fourth steps of the embodiment affects the distribution of the molecular mass of the polypeptide in the mixed polypeptide solution. In the fifth step, the polypeptide with molecular mass in the range of 1 KD-2 KD in the mixed polypeptide solution accounts for 50% -70% of the total mass of the polypeptide, and the polypeptide with preferential molecular mass in the range of 1 KD-2 KD accounts for 58% -70% of the total mass of the polypeptide.
The second embodiment is as follows: the first difference between the present embodiment and the specific embodiment is that the particle size of the fishbone powder in the first step is 100-300 μm.
And a third specific embodiment: the difference between the present embodiment and the first or second embodiment is that the water bath reaction time in the second step is 1.5-3 hours.
The specific embodiment IV is as follows: the difference between the present embodiment and one to three embodiments is that the enzymolysis treatment is performed for 2 hours at 45 ℃ in the third step.
Fifth embodiment: the embodiment is different from the first to fourth embodiments in that the mass ratio of the fishbone powder to the decalcified fishbone powder in the third step is 1.5-5:1.
Specific embodiment six: the difference between the present embodiment and one to fifth embodiments is that the enzyme deactivation treatment in the third step is an enzyme deactivation treatment at 100℃for 10min.
Seventh embodiment: the difference between the embodiment and the first to sixth embodiments is that the mass ratio of the fishbone powder in the fourth step to the fishbone powder after enzymolysis is (2-3): 1.
Eighth embodiment: the difference between the present embodiment and one to seven embodiments is that the enzymolysis treatment is performed at 50 ℃ for 2.5 to 3.5 hours in the fourth step.
Detailed description nine: this embodiment differs from one to eight of the embodiments in the polypeptide powder and CaCl in step six 2 The mass ratio of (2-3) is 1.
Detailed description ten: this embodiment differs from one of the first to ninth embodiments in that the chelation reaction is performed at 60℃for 60 to 80 minutes in the sixth step.
Embodiment one: the preparation method of the fishbone collagen polypeptide chelated calcium powder is implemented according to the following steps:
1. placing salmon bone with fish meat removed into water, steaming at 100deg.C under high pressure, cooling, grinding, and drying to obtain fish bone powder;
2. immersing fishbone powder into 2% lactic acid solution, reacting in water bath at 60deg.C for 2 hr, filtering to collect calcium-soluble solution and water-bath bone powder, washing and drying to obtain decalcified fishbone powder;
3. adding decalcified fishbone powder into water, regulating pH=7, adding papain, performing enzymolysis in water bath at 50deg.C for 1.5 hr, inactivating enzyme, cooling, and collecting hydrolysate and hydrolyzed fishbone powder;
4. mixing the fishbone powder obtained in the first step and the fishbone powder obtained after enzymolysis according to the mass ratio of 2.5:1, adding the mixture into water, adjusting the pH value of a system to be 7, adding compound protease, carrying out water bath enzymolysis for 2.5 hours at the temperature of 50 ℃, inactivating enzyme, cooling, and collecting enzymolysis liquid;
5. mixing the enzymolysis liquid and the hydrolysis liquid in the step three, filtering by an ultrafiltration membrane with the molecular weight cut-off of 5kDa to obtain a mixed polypeptide solution, and carrying out freeze-drying treatment on the mixed polypeptide solution to obtain polypeptide powder;
6. polypeptide powder and CaCl are mixed according to the mass ratio of 2:1 2 Adding into the calcium solution in the second step, chelating at 60deg.C for 1 hr, cooling, adding anhydrous ethanol, precipitating with ethanol, and collecting precipitateFreeze drying to obtain fish bone collagen polypeptide chelated calcium powder;
wherein the addition amount of papain in the third step is 2500U/g; in the fourth step, the composite protease consists of neutral protease and flavourzyme, and the adding amount of the composite protease is controlled to be 4000U/g.
1. Determination of component force and quantity distribution of fishbone collagen polypeptide
The acetonitrile in the mobile phase of the column was 40% vol and the water was 60% vol by high performance liquid chromatography.
In the fishbone collagen polypeptide obtained in the step five of the embodiment, the polypeptide with the molecular mass of 1 KD-2 KD accounts for 66% of the total mass of the polypeptide, the polypeptide with the molecular mass of less than 1KD accounts for 21% of the total mass of the polypeptide, and the molecular mass of the rest polypeptides is more than 2KD.
2. Determination of fish bone collagen polypeptide chelation rate
The chelation reaction time was 1h, and the chelation rate of the fish bone collagen polypeptide obtained in step five of this example was 73.5% at ph=7 of the system.
3. Determination of the ability of the fishbone collagen polypeptide to scavenge hydroxyl free radicals
Hydroxyl radical is generated by metabolism of organism, is the most active radical, and can cause protein crosslinking deformation, nucleic acid damage, membrane peroxidation and the like, and has the greatest toxicity to human body. Therefore, the detection of hydroxyl radicals (. OH) is of great importance in antioxidant studies. In this example, a Fenton reaction system was used for the test, and H was used 2 O 2 With Fe 3+ The reaction generates hydroxyl radicals (. OH), for a specific method reference is made to the Barry Hallifell method.
Through testing, the fish bone collagen polypeptide sample obtained in the fifth embodiment has the removal rate of 28.8% of the hydroxy free radical when the concentration is 2mg/ml, and the IC of the fish bone collagen polypeptide sample 50 =5.3mg/ml。
4. Determination of osteoblast proliferation Activity of fishbone collagen polypeptide chelated calcium powder
The present embodiment employs MTT assay to measure cell proliferation. MC3T3-E1 cells were grown at 5X 10 3 Density of individual/well was inoculated on 96-well plate, cultured for 24 hours, and then usedThe fish bone collagen polypeptide chelated calcium culture solution (100 mu L) with the concentration of 0.1mg/ml is cultured for 48 hours. At the end of the incubation, 10. Mu. LMTT solution was added to each well and incubated for another 4 hours. 150 μl of DMSO was added to each well, and the absorbance of each well was measured using an microplate reader after shaking for 10min.
As a result of testing, the proliferation rate of osteoblasts was 160% when the fish bone collagen polypeptide chelate calcium culture solution was used at a concentration of 0.1 mg/ml.
Embodiment two: the embodiment is different from the first embodiment in that step three, decalcified fishbone powder is added into water, the pH=7 of the system is adjusted, then papain is added, and the enzymolysis treatment is carried out in a water bath at 50 ℃ for 3 hours; and step four, mixing the fishbone powder obtained in the step one and the fishbone powder obtained after enzymolysis according to the mass ratio of 2.5:1, adding the mixture into water, adjusting the pH value of a system to be 7, adding compound protease, and carrying out water bath enzymolysis at the temperature of 50 ℃ for 3.5 hours.
The polypeptide with molecular mass smaller than 1KD in the fishbone collagen polypeptide obtained in the embodiment accounts for 32% of the total mass of the polypeptide, the polypeptide with molecular mass of 1 KD-2 KD accounts for 58% of the total mass of the polypeptide, the chelation rate of the fishbone collagen polypeptide is 76.5%, but the proliferation rate of the fishbone collagen polypeptide chelated calcium sample to osteoblasts is reduced to 148%. If the enzymolysis treatment time of the third step and the fourth step is further increased, the chelation rate of the fish bone collagen polypeptide is not obviously changed, but the proliferation activity of osteoblasts is further reduced.

Claims (10)

1. The preparation method of the fish bone collagen polypeptide chelated calcium powder is characterized by comprising the following steps:
1. putting the fish bones with the fish meat removed into water, steaming at high pressure at a temperature of more than 100 ℃, cooling, grinding, and drying to obtain the fish bone powder;
2. immersing fishbone powder into a lactic acid solution with the mass fraction of 1.5-2%, carrying out water bath reaction at the temperature of 50-60 ℃, filtering and respectively collecting calcium-dissolving liquid and bone powder after water bath, and washing and drying the bone powder after water bath to obtain decalcified fishbone powder;
3. adding decalcified fishbone powder into water, regulating the pH value of the system to be 7, then adding papain, carrying out enzymolysis treatment for 1.5-3 h at the temperature of 40-55 ℃, inactivating enzyme, cooling, and respectively collecting hydrolysate and the fishbone powder after enzymolysis;
4. mixing the fishbone powder obtained in the first step with the fishbone powder obtained after enzymolysis, adding the fishbone powder into water, adjusting the pH value of a system to be 7, adding compound protease, carrying out enzymolysis at the temperature of 40-55 ℃ for 2.5-3.5 hours, inactivating enzyme, cooling, and collecting enzymolysis liquid;
5. mixing the enzymolysis liquid and the hydrolysis liquid in the step three, filtering by an ultrafiltration membrane to obtain a mixed polypeptide solution, and carrying out freeze-drying treatment on the mixed polypeptide solution to obtain polypeptide powder;
6. polypeptide powder and CaCl 2 Adding the mixture into the calcium solution in the second step, carrying out chelation reaction at the temperature of 55-65 ℃, cooling, adding absolute ethyl alcohol for alcohol precipitation, and freeze-drying the precipitate to obtain the fish bone collagen polypeptide chelated calcium powder;
wherein the addition amount of papain in the third step is 2500-3000U/g; in the fourth step, the compound protease consists of neutral protease and flavourzyme, and the adding amount of the compound protease is controlled to be 3000-4000U/g.
2. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein the particle size of the fish bone powder in the first step is 100-300 micrometers.
3. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein the water bath reaction time in the second step is 1.5-3 h.
4. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein in the third step, the enzymolysis treatment is performed at 45 ℃ for 2 hours.
5. The method for preparing the fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein the mass ratio of the fish bone powder to the decalcified fish bone powder in the third step is 1.5-5:1.
6. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein the enzyme deactivation treatment in the step three is an enzyme deactivation treatment at 100 ℃ for 10min.
7. The method for preparing the fishbone collagen polypeptide chelated calcium powder according to claim 1, wherein the mass ratio of the fishbone powder to the fishbone powder after enzymolysis in the fourth step is (2-3): 1.
8. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein in the fourth step, enzymolysis is performed at 50 ℃ for 2.5-3.5 h.
9. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, characterized in that in step six, polypeptide powder and CaCl are used 2 The mass ratio of (2-3) is 1.
10. The method for preparing fish bone collagen polypeptide chelated calcium powder according to claim 1, wherein in the step six, the chelation reaction is performed at 60 ℃ for 60-80 min.
CN202310991004.XA 2023-08-08 2023-08-08 Preparation method of fish bone collagen polypeptide chelated calcium powder Pending CN116987178A (en)

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN117562979A (en) * 2023-11-20 2024-02-20 山东大学齐鲁医院 Biological agent for treating preeclampsia syndrome

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN117562979A (en) * 2023-11-20 2024-02-20 山东大学齐鲁医院 Biological agent for treating preeclampsia syndrome
CN117562979B (en) * 2023-11-20 2024-05-28 山东大学齐鲁医院 Biological agent for treating preeclampsia syndrome

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