A composition containing bovine bone collagen peptide, a preparation method and application thereof in treating osteoporosis

Abstract

The application discloses a kind of composition containing bovine bone collagen peptide, preparation method and its application in treating osteoporosis, it is related to collagen peptide extraction technical field.The composition containing bovine bone collagen peptide is made of the following weight parts of raw materials: bovine bone collagen peptide 40-65 parts, collagen peptide-calcium chelate 10-15 parts, maltodextrin 15-25 parts, chondroitin sulfate 3-5 parts, pregelatinized starch 8-12 parts, magnesium stearate 1-3 parts, functional peptide 5-10 parts.The composition containing bovine bone collagen peptide of the application, good taste, no bad smell, easy to be absorbed by human body, can effectively treat and improve osteoporosis, preparation method process operation is simple, and it is convenient for industrial production.

Description

Technical Field

[0001] This invention relates to the field of collagen peptide extraction technology, specifically to a composition containing bovine bone collagen peptides, its preparation method, and its application in the treatment of osteoporosis. Background Technology

[0002] Osteoporosis is a systemic metabolic disease characterized by decreased bone mass, deterioration of bone microstructure, and increased bone fragility, commonly seen in postmenopausal women and the elderly. Traditional nutritional interventions mainly focus on calcium and vitamin D supplementation, but these methods have the following problems: 1. Limited solubility and gastrointestinal tolerance; 2. Intestinal absorption efficiency is significantly affected by food environment and pH; 3. Poor long-term adherence and taste experience; 4. Unsatisfactory treatment and improvement effects.

[0003] Bovine bone collagen peptides are proteins extracted from bovine bones. They have the effects of enhancing skin elasticity, promoting bone health, improving joint function, maintaining muscle health, and promoting wound healing. As a nutritional supplement, it is suitable for a variety of people, especially those who need to improve their skin, bone, and joint health.

[0004] However, existing bovine bone collagen peptides and preparation methods cannot meet the requirements. Summary of the Invention

[0005] To address the shortcomings of existing technologies, this invention provides a composition containing bovine bone collagen peptides, a preparation method thereof, and its application in the treatment of osteoporosis, thus solving the problems raised in the background art.

[0006] To achieve the above objectives, the present invention provides the following technical solution:

[0007] In a first aspect, the present invention provides a composition containing bovine bone collagen peptides, which is made from the following raw materials in parts by weight: 40-65 parts bovine bone collagen peptides, 10-15 parts collagen peptide-calcium chelate, 15-25 parts maltodextrin, 3-5 parts chondroitin sulfate, 8-12 parts pregelatinized starch, 1-3 parts magnesium stearate, and 5-10 parts functional peptides.

[0008] Furthermore, the present invention provides a composition containing bovine bone collagen peptides, which is made from the following raw materials in parts by weight: 40 parts bovine bone collagen peptides, 10 parts collagen peptide-calcium chelate, 15 parts maltodextrin, 3 parts chondroitin sulfate, 8 parts pregelatinized starch, 1 part magnesium stearate, and 5 parts functional peptides.

[0009] Furthermore, the present invention provides a composition containing bovine bone collagen peptides, which is made from the following raw materials in parts by weight: 65 parts bovine bone collagen peptides, 15 parts collagen peptide-calcium chelate, 25 parts maltodextrin, 5 parts chondroitin sulfate, 12 parts pregelatinized starch, 3 parts magnesium stearate, and 10 parts functional peptides.

[0010] Furthermore, the present invention provides a composition containing bovine bone collagen peptides, which is made from the following raw materials in parts by weight: 55 parts bovine bone collagen peptides, 12 parts collagen peptide-calcium chelate, 22 parts maltodextrin, 4 parts chondroitin sulfate, 10 parts pregelatinized starch, 2 parts magnesium stearate, and 8 parts functional peptides.

[0011] Secondly, the present invention provides a method for preparing the above-mentioned composition containing bovine bone collagen peptides, the method comprising the following steps:

[0012] S1. Select fresh beef bones and clean them thoroughly. Put the beef bones into a solution containing 0.05-0.1 mol / L sodium hydroxide at a liquid-to-solid ratio of 10-20:1 and soak at room temperature for 3-6 hours. After soaking, take out the beef bones, clean them, and crush them into bone pieces of 1-2 cm size using a bone crusher. Add the bone pieces to water at a liquid-to-solid ratio of 8-12:1 and extract them in a sealed container at 120-135℃ for 1.5-3 hours.

[0013] S2. After cooking, stop heating and centrifuge the cooking liquid to remove the upper layer of floating oil and recover the lower layer of crude collagen solution.

[0014] S3. Add the crude collagen solution to the enzymatic hydrolysis equipment, adjust the pH to 7.0-7.2, and add a complex protease to the reaction solution for the first enzymatic hydrolysis reaction. The complex protease is composed of Protamex and Papain in a mass ratio of 2:1, and the amount added is 2% of the weight of the crude collagen solution. First, add 70% of the total amount of complex protease, and add the remaining amount after 30 minutes. The temperature of the first enzymatic hydrolysis is controlled at 55-58℃, and the reaction time is 1.5 hours, with slow stirring during the process. After the first enzymatic hydrolysis, adjust the pH of the hydrolysate to 6.8-7.0 with food-grade citric acid, and then add the protease Flavorzyme for the second enzymatic hydrolysis. The amount added is 0.1-0.3% of the solution weight, the reaction temperature is 52-55℃, and the reaction time of the second enzymatic hydrolysis is 2 hours, with slow stirring during the process. After the enzymatic hydrolysis is completed, inactivate the enzyme at 90-94℃, centrifuge, and collect the supernatant to obtain the final enzymatic hydrolysate.

[0015] S4. Using an ultrafiltration membrane with a molecular weight cutoff of 1000 Da, filter the final enzymatic hydrolysate at 10–15℃, controlling the operating pressure at 0.1–0.3 MPa. Collect the retentate, adjust the pH to 7.6–7.9, degas it under vacuum at 45–50℃, and prepare 0.8–1.0 mol / L CaCl2 with deionized water at the same temperature of 45–50℃. Add the retentate and CaCl2 solution dropwise over 10–20 min at a mass ratio of 1:0.1–0.3, followed by micro-titration with 0.5–1.0 mol / L NaOH. Maintain the pH at 7.6–7.9 using a closed-loop PID control system, monitoring free Ca2+ throughout the process.2+ Total Ca 2+ ≤25%, after the addition is complete, continue stirring at 50℃ for 20–30 min, slowly add 10% malic acid aqueous solution, adjust the pH of the system to 6.8–7.0, vacuum concentrate to a solid content of 25–35%, and spray dry for later use to obtain collagen peptide-calcium chelate;

[0016] S5. Collect the filtrate, add food-grade powdered activated carbon as a decolorizing agent, and decolorize at pH 4.0-7.0 and 35-50℃ for 50-60 minutes. After decolorization, centrifuge and collect the supernatant. Vacuum concentrate the supernatant to a solid content of 20-30% and then spray dry. Spray dry to obtain bovine bone collagen peptides.

[0017] S6. The functional peptide is prepared by solid-phase synthesis, and the amino acid sequence of the functional peptide is RGDAPFYRDHVK.

[0018] S7. Obtain the above-mentioned components by weight, mix them evenly, add excipients, and then prepare tablets or granules.

[0019] Thirdly, the present invention provides the use of the above-mentioned composition containing bovine bone collagen peptides in the preparation of a medicament for treating osteoporosis.

[0020] The present invention has the following beneficial effects:

[0021] (1) The composition of bovine bone collagen peptides of the present invention has a good taste, no unpleasant odor, is easily absorbed by the human body, and can effectively treat and improve osteoporosis.

[0022] (2) The method for preparing the bovine bone collagen peptide composition of the present invention has high extraction efficiency of bovine bone collagen peptide. The obtained bovine bone collagen peptide is the source of bone matrix and coordination sites. Collagen peptide-calcium chelate provides efficient calcium delivery and mineralization basis. Functional peptide provides osteogenic related signals / adhesion advantages. The process is simple and easy to industrialize.

[0023] (3) In the treatment of osteoporosis, the composition of the present invention has multiple components working together synergistically, resulting in stronger efficacy and more stable stratification.

[0024] Of course, any product implementing this invention does not necessarily need to achieve all of the advantages described above at the same time. Detailed Implementation

[0025] It should be noted that the embodiments described in this invention are merely some, not all, of the embodiments of this invention. All other embodiments obtained by those skilled in the art based on the embodiments of this invention without inventive effort are within the scope of protection of this invention.

[0026] Example 1

[0027] This invention provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 40g bovine bone collagen peptides, 10g collagen peptide-calcium chelate, 15g maltodextrin, 3g chondroitin sulfate, 8g pregelatinized starch, 1g magnesium stearate, and 5g functional peptides.

[0028] Example 2

[0029] This invention provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 65g bovine bone collagen peptides, 15g collagen peptide-calcium chelate, 25g maltodextrin, 5g chondroitin sulfate, 12g pregelatinized starch, 3g magnesium stearate, and 10g functional peptides.

[0030] Example 3

[0031] This invention provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 55g bovine bone collagen peptides, 12g collagen peptide-calcium chelate, 22g maltodextrin, 4g chondroitin sulfate, 10g pregelatinized starch, 2g magnesium stearate, and 8g functional peptides.

[0032] Example 4

[0033] This invention provides a method for preparing a composition containing bovine bone collagen peptides, the method comprising the following steps:

[0034] S1. Select fresh beef bones and clean them. Put the beef bones into a solution containing 0.05 mol / L sodium hydroxide at a liquid-to-solid weight ratio of 10:1 and soak at room temperature for 3 hours. After soaking, take out the beef bones, clean them, and crush them into 1 cm pieces using a bone crusher. Add the bone pieces to water at a liquid-to-solid weight ratio of 8:1 and extract them in a sealed container at 120°C for 1.5 hours.

[0035] S2. After cooking, stop heating and centrifuge the cooking liquid to remove the upper layer of floating oil and recover the lower layer of crude collagen solution.

[0036] S3. Add the crude collagen solution to the enzymatic hydrolysis equipment, adjust the pH to 7.0, and add a complex protease to the reaction solution for the first enzymatic hydrolysis reaction. The complex protease is composed of Protamex and Papain in a mass ratio of 2:1, and the amount added is 2% of the weight of the crude collagen solution. First, add 70% of the total amount of complex protease, and then add the remaining amount after 30 minutes. The temperature of the first enzymatic hydrolysis is controlled at 55℃, and the reaction time is 1.5 hours, with slow stirring during the process. After the first enzymatic hydrolysis, adjust the pH of the hydrolysate to 6.8 with food-grade citric acid, and then add the protease Flavorzyme for the second enzymatic hydrolysis. The amount added is 0.1% of the solution weight, the reaction temperature is 52℃, and the reaction time of the second enzymatic hydrolysis is 2 hours, with slow stirring during the process. After the enzymatic hydrolysis is completed, inactivate the enzyme at 90℃, centrifuge, and collect the supernatant to obtain the final enzymatic hydrolysate.

[0037] S4. Using an ultrafiltration membrane with a molecular weight cutoff of 1000 Da, filter the final enzymatic hydrolysate at 10℃, controlling the operating pressure at 0.1 MPa. Collect the retentate (i.e., the retentate, the side of the feed that did not permeate through ultrafiltration). Adjust the pH of the retentate to 7.6, degas it under vacuum at 45℃, and prepare 0.8 mol / L CaCl2 with deionized water at the same temperature of 45℃. Add the retentate and CaCl2 solution dropwise over 10 min at a mass ratio of 1:0.1 (retentate:CaCl2). Perform micro-titration with 0.5 mol / L NaOH. Maintain the pH at 7.6 using a closed-loop PID control system, monitoring free Ca2+ throughout the process. 2+ Total Ca 2+ ≤25%, after the addition is complete, continue stirring at 50℃ for 20 min, slowly add 10% malic acid aqueous solution, adjust the pH of the system to 6.8, vacuum concentrate to 25% solid content, and spray dry for later use to obtain collagen peptide-calcium chelate;

[0038] S5. Collect the filtrate (i.e., the permeate, the liquid that has passed through the ultrafiltration side), add food-grade powdered activated carbon as a decolorizing agent, and decolorize at pH 4.0 and 35℃ for 50 minutes. After decolorization, centrifuge and take the supernatant, vacuum concentrate to a solid content of 20%, and then spray dry to obtain bovine bone collagen peptides.

[0039] S6. The functional peptide is prepared by solid-phase synthesis, and the amino acid sequence of the functional peptide is RGDAPFYRDHVK.

[0040] S7. Obtain the components of the bovine bone collagen peptide composition of this application, mix them evenly, add excipients, and then prepare tablets or granules.

[0041] Example 5

[0042] This invention provides a method for preparing a composition containing bovine bone collagen peptides, the method comprising the following steps:

[0043] S1. Select fresh beef bones and clean them. Put the beef bones into a solution containing 0.1 mol / L sodium hydroxide at a liquid-to-solid weight ratio of 20:1 and soak at room temperature for 6 hours. After soaking, take out the beef bones, clean them, and crush them into 2 cm pieces using a bone crusher. Add the bone pieces to water at a liquid-to-solid weight ratio of 12:1 and extract them in a sealed container at 135°C for 3 hours.

[0044] S2. After cooking, stop heating and centrifuge the cooking liquid to remove the upper layer of floating oil and recover the lower layer of crude collagen solution.

[0045] S3. Add the crude collagen solution to the enzymatic hydrolysis equipment, adjust the pH to 7.2, and add a complex protease to the reaction solution for the first enzymatic hydrolysis reaction. The complex protease is composed of Protamex and Papain in a mass ratio of 2:1, and the amount added is 2% of the weight of the crude collagen solution. First, add 70% of the total amount of complex protease, and then add the remaining amount after 30 minutes. The temperature of the first enzymatic hydrolysis is controlled at 58℃, and the reaction time is 1.5 hours, with slow stirring during the process. After the first enzymatic hydrolysis, adjust the pH of the hydrolysate to 7.0 with food-grade citric acid, and then add the protease Flavorzyme for the second enzymatic hydrolysis. The amount added is 0.3% of the solution weight, the reaction temperature is 55℃, and the reaction time of the second enzymatic hydrolysis is 2 hours, with slow stirring during the process. After the enzymatic hydrolysis is completed, inactivate the enzyme at 94℃, centrifuge, and collect the supernatant to obtain the final enzymatic hydrolysate.

[0046] S4. Using an ultrafiltration membrane with a molecular weight cutoff of 1000 Da, the final enzymatic hydrolysate was filtered at 15°C under an operating pressure of 0.3 MPa. The retentate was collected, adjusted to pH 7.9, and degassed under vacuum at 50°C. A 1.0 mol / L CaCl2 solution was prepared with deionized water and kept at 50°C. This solution was continuously added dropwise over 20 minutes at a mass ratio of retentate:CaCl2 of 1:0.3, followed by micro-titration with 1.0 mol / L NaOH. The pH was maintained at 7.9 using a closed-loop PID control system, and free Ca2+ was monitored throughout the process. 2+ Total Ca 2+ ≤25%, after the addition is complete, continue stirring at 50℃ for 25 min, slowly neutralize with 10% malic acid dilute solution to pH 7.0, vacuum concentrate to solid content of 35%, set aside for spray drying to obtain collagen peptide-calcium chelate;

[0047] S5. Collect the filtrate, add food-grade powdered activated carbon as a decolorizing agent, and decolorize at pH 7.0 and 50℃ for 60 min. After decolorization, centrifuge and collect the supernatant. Vacuum concentrate to a solid content of 30% and then spray dry to obtain bovine bone collagen peptides.

[0048] S6. The functional peptide is prepared by solid-phase synthesis, and the amino acid sequence of the functional peptide is RGDAPFYRDHVK.

[0049] S7. Obtain the components of the bovine bone collagen peptide composition of this application, mix them evenly, add excipients, and then prepare tablets or granules.

[0050] Example 6

[0051] This invention provides a method for preparing a composition containing bovine bone collagen peptides, the method comprising the following steps:

[0052] S1. Select fresh beef bones and clean them. Put the beef bones into a solution containing 0.07 mol / L sodium hydroxide at a liquid-to-solid weight ratio of 15:1 and soak at room temperature for 4 hours. After soaking, take out the beef bones, clean them, and crush them into bone pieces of 1 cm size using a bone crusher. Add the bone pieces to water at a liquid-to-solid weight ratio of 10:1 and extract them in a sealed container at 130°C for 2 hours.

[0053] S2. After cooking, stop heating and centrifuge the cooking liquid to remove the upper layer of floating oil and recover the lower layer of crude collagen solution.

[0054] S3. Add the crude collagen solution to the enzymatic hydrolysis equipment, adjust the pH to 7.1, and add a complex protease to the reaction solution for the first enzymatic hydrolysis reaction. The complex protease is composed of Protamex and Papain in a mass ratio of 2:1, and the amount added is 2% of the weight of the crude collagen solution. First, add 70% of the total amount of complex protease, and then add the remaining amount after 30 minutes. The temperature of the first enzymatic hydrolysis is controlled at 56℃, and the reaction time is 1.5 hours, with slow stirring during the process. After the first enzymatic hydrolysis, adjust the pH of the hydrolysate to 6.9 with food-grade citric acid, and then add the protease Flavorzyme for the second enzymatic hydrolysis. The amount added is 0.2% of the solution weight, the reaction temperature is 53℃, and the reaction time of the second enzymatic hydrolysis is 2 hours, with slow stirring during the process. After the enzymatic hydrolysis is completed, inactivate the enzyme at 92℃, centrifuge, and collect the supernatant to obtain the final enzymatic hydrolysate.

[0055] S4. Using an ultrafiltration membrane with a molecular weight cutoff of 1000 Da, the final enzymatic hydrolysate was filtered at 12℃ with the operating pressure controlled at 0.2 MPa. The retentate was collected, adjusted to pH 7.8, and degassed under vacuum at 47℃. 0.9 mol / L CaCl2 was prepared with deionized water and kept at 47℃. The retentate was continuously added dropwise over 15 minutes at a mass ratio of 1:0.2 (retentate:CaCl2). The solution was then micro-titrated with 0.8 mol / L NaOH. The pH was maintained at 7.8 using a closed-loop PID control system, and free Ca2+ was monitored throughout the process. 2+ Total Ca 2+≤25%, after the addition is complete, continue stirring at 50℃ for 22 min, slowly add 10% malic acid aqueous solution, adjust the pH of the system to 6.9, vacuum concentrate to 30% solid content, and spray dry for later use to obtain collagen peptide-calcium chelate;

[0056] S5. Collect the filtrate, add food-grade powdered activated carbon as a decolorizing agent, and decolorize at pH 5.0 and 40℃ for 55 min. After decolorization, centrifuge and collect the supernatant. Vacuum concentrate to a solid content of 25% and then spray dry to obtain bovine bone collagen peptides.

[0057] S6. The functional peptide is prepared by solid-phase synthesis. The amino acid sequence of the functional peptide is RGDAPFYRDHVK, namely Arg–Gly–Asp–Ala–Pro–Phe–Tyr–Arg–Asp–His–Val–Lys.

[0058] S7. Obtain the components of the bovine bone collagen peptide composition of this application, mix them evenly, add excipients, and then prepare tablets or granules.

[0059] Comparative Example 1

[0060] Comparative Example 1 provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 30g bovine bone collagen peptides, 5g collagen peptide-calcium chelate, 22g maltodextrin, 4g chondroitin sulfate, 10g pregelatinized starch, 2g magnesium stearate, and 3g functional peptides.

[0061] Comparative Example 1 had a reduced ratio of bovine bone collagen peptides, collagen peptide-calcium chelates, and functional peptides, while the rest was the same as in Example 3.

[0062] Comparative Example 2

[0063] Comparative Example 2 provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 12g collagen peptide-calcium chelate, 22g maltodextrin, 4g chondroitin sulfate, 10g pregelatinized starch, 2g magnesium stearate, and 8g functional peptides.

[0064] Comparative Example 2 had bovine bone collagen peptides removed, but the rest was the same as in Example 3.

[0065] Comparative Example 3

[0066] Comparative Example 3 provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 55g bovine bone collagen peptides, 22g maltodextrin, 4g chondroitin sulfate, 10g pregelatinized starch, 2g magnesium stearate, and 8g functional peptides.

[0067] Comparative Example 3 omitted the collagen peptide-calcium chelate, otherwise it was the same as Example 3.

[0068] Comparative Example 4

[0069] Comparative Example 4 provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 55g bovine bone collagen peptides, 12g collagen peptide-calcium chelate, 22g maltodextrin, 4g chondroitin sulfate, 10g pregelatinized starch, and 2g magnesium stearate.

[0070] Comparative Example 4 had its functional peptide deleted, but the rest was the same as in Example 3.

[0071] Comparative Example 5

[0072] Comparative Example 5 provides a composition containing bovine bone collagen peptides, made from the following raw materials in grams by weight: 55g bovine bone collagen peptides, 12g collagen peptide-calcium chelate, 22g maltodextrin, 10g pregelatinized starch, 2g magnesium stearate, and 8g functional peptides.

[0073] Comparative Example 5 omitted chondroitin sulfate, but was otherwise identical to Example 3.

[0074] Experimental Case Study on Treatment of Osteoporosis

[0075] 1. Laboratory animals and grouping

[0076] Healthy female rats, 8–9 weeks old, were selected as experimental animals and acclimatized for one week before being randomly divided into groups for the experiment. To ensure statistical power, each group contained no fewer than 10 rats. Except for the blank control group, all rats underwent bilateral ovariectomy (OVX). After 3–4 weeks of postoperative stabilization, drug administration was initiated and continued for 12 weeks, administered once daily via gavage at a dose of 500 mg / kg. -1 ·d -1 The blank and model groups were filled with the same volume of distilled water. The grouping and treatment are as follows (11 groups in total):

[0077] Blank control group: Ovarian removal was not performed; only the ovary was exposed during the surgery but not removed, and no postoperative medication was given. Model control group: Ovulation was induced by OVX resection, and no postoperative treatment was given. Calcium control group: Calcium gluconate solution was administered by gavage after OVX surgery. Example 1 group: After OVX, a powder mixture prepared according to the composition of Example 1 of this invention containing bovine bone collagen peptides was given. Example 2 group: After OVX, a powder mixture prepared according to the composition of Example 2 of this invention containing bovine bone collagen peptides was given. Example 3 group: After OVX, a powder mixture prepared according to the composition of Example 3 of this invention containing bovine bone collagen peptides was given. The following are examples of the compounds: Comparative Example 1: A powdered mixture prepared by applying the composition containing bovine collagen peptides of Comparative Example 1 after OVX; Comparative Example 2: A powdered mixture prepared by applying the composition containing bovine collagen peptides of Comparative Example 2 after OVX; Comparative Example 3: A powdered mixture prepared by applying the composition containing bovine collagen peptides of Comparative Example 3 after OVX; Comparative Example 4: A powdered mixture prepared by applying the composition containing bovine collagen peptides of Comparative Example 4 after OVX; Comparative Example 5: A powdered mixture prepared by applying the composition containing bovine collagen peptides of Comparative Example 5 after OVX.

[0078] 2. Measurement of experimental data

[0079] DXA was used to measure the bone marrow diameter (BMD) of the lumbar spine (L4-L6) and left femur. Micro-CT was used to measure the bone marrow volume (BV / TV), tb.N, tb.Th, and tb.Sp in the cancellous bone.

[0080] 3. Experimental Data

[0081] Table 1 Bone mineral density (BMD, g / cm², mean ± SD; n=12)

[0082]

[0083] Table 2 Micro-CT parameters of cancellous bone (distal femur, mean ± SD; n=12)

[0084]

[0085] 4. Experimental Conclusions

[0086] After 12 weeks of oral administration, the composition of this invention significantly increased BMD compared to the control group, and also improved BV / TV, Tb.N, and Tb.Th, while decreasing Tb.Sp on micro-CT scans. Example 3 showed the best results, demonstrating optimal synergistic ratios and overall superiority over conventional calcium supplementation. Deletion or downregulation of key components resulted in a stepwise decline in efficacy, confirming that bovine collagen peptides are crucial, peptide-calcium and functional peptides provide synergy, and chondroitin is a supporting factor. Compared to comparative techniques, this invention exhibits significant technical advantages in controllable processes, synergistic formulation, and stable efficacy.

[0087] It should be noted that, in this document, relational terms such as "first" and "second" are used only to distinguish one entity or operation from another, and do not necessarily require or imply any such actual relationship or order between these entities or operations. Furthermore, the terms "comprising," "including," or any other variations thereof are intended to cover non-exclusive inclusion, such that a process, method, article, or apparatus that comprises a list of elements includes not only those elements but also other elements not expressly listed, or elements inherent to such process, method, article, or apparatus.

[0088] The preferred embodiments of the present invention disclosed above are merely illustrative of the invention. These preferred embodiments do not exhaustively describe all details, nor do they limit the invention to the specific implementations described. Clearly, many modifications and variations can be made based on the content of this specification. This specification selects and specifically describes these embodiments to better explain the principles and practical applications of the invention, thereby enabling those skilled in the art to better understand and utilize the invention. The invention is limited only by the claims and their full scope and equivalents.

Claims

1. A composition containing bovine bone collagen peptides, characterized in that, Made from the following parts by weight of raw materials: The formula contains 40-65 parts bovine bone collagen peptide, 10-15 parts collagen peptide-calcium chelate, 15-25 parts maltodextrin, 3-5 parts chondroitin sulfate, 8-12 parts pregelatinized starch, 1-3 parts magnesium stearate, and 5-10 parts functional peptides, wherein the amino acid sequence of the functional peptides is RGDAPFYRDHVK.

2. The composition containing bovine collagen peptides according to claim 1, characterized in that, Made from the following parts by weight of raw materials: 40 parts bovine bone collagen peptide, 10 parts collagen peptide-calcium chelate, 15 parts maltodextrin, 3 parts chondroitin sulfate, 8 parts pregelatinized starch, 1 part magnesium stearate, and 5 parts functional peptides.

3. The composition containing bovine collagen peptides according to claim 1, characterized in that, Made from the following parts by weight of raw materials: Bovine bone collagen peptides (65 parts), collagen peptide-calcium chelate (15 parts), maltodextrin (25 parts), chondroitin sulfate (5 parts), pregelatinized starch (12 parts), magnesium stearate (3 parts), and functional peptides (10 parts).

4. The composition containing bovine collagen peptides according to claim 1, characterized in that, Made from the following parts by weight of raw materials: 55 parts bovine bone collagen peptides, 12 parts collagen peptide-calcium chelate, 22 parts maltodextrin, 4 parts chondroitin sulfate, 10 parts pregelatinized starch, 2 parts magnesium stearate, and 8 parts functional peptides.

5. A method for preparing a composition containing bovine collagen peptides according to any one of claims 1-4, characterized in that, The method includes the following steps: S1. Select fresh beef bones and clean them thoroughly. Put the beef bones into a solution containing 0.05-0.1 mol / L sodium hydroxide at a liquid-to-solid ratio of 10-20:1 and soak at room temperature for 3-6 hours. After soaking, take out the beef bones, clean them, and crush them into bone pieces of 1-2 cm size using a bone crusher. Add the bone pieces to water at a liquid-to-solid ratio of 8-12:1 and extract them in a sealed container at 120-135℃ for 1.5-3 hours. S2. After cooking, stop heating and centrifuge the cooking liquid to remove the upper layer of floating oil and recover the lower layer of crude collagen solution. S3. Add the crude collagen solution to the enzymatic hydrolysis equipment, adjust the pH to 7.0-7.2, and add a complex protease to the reaction solution for the first enzymatic hydrolysis reaction. The complex protease is composed of Protamex and Papain in a mass ratio of 2:1, and the amount added is 2% of the weight of the crude collagen solution. First, add 70% of the total amount of complex protease, and add the remaining amount after 30 minutes. The temperature of the first enzymatic hydrolysis is controlled at 55-58℃, and the reaction time is 1.5 hours, with slow stirring during the process. After the first enzymatic hydrolysis, adjust the pH of the hydrolysate to 6.8-7.0 with food-grade citric acid, and then add the protease Flavorzyme for the second enzymatic hydrolysis. The amount added is 0.1-0.3% of the solution weight, the reaction temperature is 52-55℃, and the reaction time of the second enzymatic hydrolysis is 2 hours, with slow stirring during the process. After the enzymatic hydrolysis is completed, inactivate the enzyme at 90-94℃, centrifuge, and collect the supernatant to obtain the final enzymatic hydrolysate. S4. Using an ultrafiltration membrane with a molecular weight cutoff of 1000 Da, filter the final enzymatic hydrolysate at 10–15℃, controlling the operating pressure at 0.1–0.3 MPa. Collect the retentate, adjust the pH to 7.6–7.9, degas it under vacuum at 45–50℃, and prepare 0.8–1.0 mol / L CaCl2 with deionized water at the same temperature of 45–50℃. Add the retentate and CaCl2 solution dropwise over 10–20 min at a mass ratio of 1:0.1–0.3 for 10–20 min, and perform micro-titration with 0.5–1.0 mol / L NaOH. Maintain the pH at 7.6–7.9 using a closed-loop PID control system, monitoring free Ca2+ throughout the process. 2+ Total Ca 2+ ≤25%, after the addition is complete, continue stirring at 50℃ for 20–30 min, slowly add 10% malic acid aqueous solution, adjust the pH of the system to 6.8–7.0, vacuum concentrate to a solid content of 25–35%, and spray dry for later use to obtain collagen peptide-calcium chelate; S5. Collect the filtrate, add food-grade powdered activated carbon as a decolorizing agent, and decolorize at pH 4.0-7.0 and 35-50℃ for 50-60 minutes. After decolorization, centrifuge and collect the supernatant. Vacuum concentrate the supernatant to a solid content of 20-30% and then spray dry. Spray dry to obtain bovine bone collagen peptides. S6. The functional peptide is prepared by solid-phase synthesis. S7. Obtain the above-mentioned components by weight, mix them evenly, add excipients, and then prepare tablets or granules.

6. The use of the composition containing bovine bone collagen peptides according to claim 1 in the preparation of a medicament for treating osteoporosis.

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