Collagen peptide with effects of soothing nerves and helping sleep as well as preparation method and application of collagen peptide
By employing a stepwise enzymatic hydrolysis and fine purification process, the problems of low efficiency and insufficient purity in traditional collagen peptide extraction methods have been solved, resulting in the preparation of high-purity small-molecule collagen peptides suitable for food and medicine to improve sleep.
Patent Information
- Application Number
- CN202610240454.9
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2026-02-28
- Publication Date
- 2026-05-15
AI Technical Summary
Existing methods for extracting collagen peptides suffer from problems such as long production cycles, high energy consumption, serious environmental pollution, wide molecular weight distribution of products, incomplete removal of impurities, and large fluctuations in product quality, which affect their application in high-end transparent beverages and cosmetics.
A stepwise synergistic enzymatic hydrolysis method using alkaline protease and neutral protease, combined with steps such as high-temperature swelling, alkali treatment, activated carbon adsorption, and nanofiltration membrane filtration, was employed to optimize process parameters for the preparation of high-purity small-molecule collagen peptides.
It has achieved efficient enrichment of small molecule peptides with a molecular weight of less than 1000 Daltons, resulting in products with high clarity and good flavor, which significantly improves their application value in high-end transparent beverages and cosmetics.
Smart Images
Figure CN122038513A_ABST
Abstract
Description
Technical Field
[0001] This application relates to the field of collagen peptides, and more specifically, to a collagen peptide with calming and sleep-aiding effects, its preparation method, and its application. Background Technology
[0002] Collagen peptides, as an important class of bioactive substances, have been widely used in health foods, functional beverages, cosmetics, and medical dressings due to their good biocompatibility, easy absorption, and potential benefits in skin health and joint care. Traditional collagen extraction methods mainly rely on strong acid or alkali treatments. While these methods can break the cross-links of collagen, they suffer from drawbacks such as long production cycles, high energy consumption, and severe environmental pollution. More importantly, the degradation process using acid or alkali methods is difficult to control precisely, resulting in a wide molecular weight distribution of the product, containing a large number of non-target peptides or amino acids, and easily destroying active ingredients, thus affecting the product's functionality and application value.
[0003] With the development of bioenzyme engineering technology, enzymatic hydrolysis has become the mainstream process due to its mild conditions, high specificity, and environmental friendliness. However, existing enzymatic hydrolysis processes still have significant shortcomings:
[0004] The enzymatic hydrolysis process is crude: most processes use a single enzyme preparation or a simple compound enzyme. The pH and temperature control of the enzymatic hydrolysis process are often designed around the enzyme's "optimal conditions" rather than "product-oriented", resulting in random enzyme cleavage sites. The proportion of target small molecule peptides (such as collagen peptides with high absorption rate) in the product is not high, and bitter peptides are easily produced, affecting the taste.
[0005] Incomplete impurity removal: The enzymatic hydrolysis products often contain unhydrolyzed protein fragments, pigments, off-flavor substances, and inorganic salt ions. Subsequent purification often relies on simple filtration or centrifugation, which is insufficient to effectively remove small molecule impurities and improve solution clarity. This results in high turbidity, dark color, and poor flavor in the final product, limiting its application in high-end transparent beverages or cosmetics.
[0006] Poor process stability: Due to the lack of systematic optimization and control of key process parameters (such as pretreatment conditions, synergistic effects of multi-step enzymatic hydrolysis, and purification processes), the quality of products varies greatly between different batches, resulting in poor reproducibility. Summary of the Invention
[0007] The summary section of this application is intended to provide a brief overview of the concepts, which will be described in detail in the detailed description section below. This summary section is not intended to identify key or essential features of the claimed technical solutions, nor is it intended to limit the scope of the claimed technical solutions.
[0008] To address the technical problems mentioned in the background section above, some embodiments of this application provide a method for producing collagen peptides with calming and sleep-aiding effects, characterized by the following steps: (1) Raw material pretreatment: mixing animal skin, cartilage, or fish scales with water and subjecting the mixture to high-temperature swelling treatment; (2) Alkali treatment: adjusting the pH of the swollen system to 9.8-10.2; (3) Targeted enzymatic hydrolysis: at 53-57℃ and pH 9.8-10.2, first adding alkaline protease for the first stage of enzymatic hydrolysis, followed by... (3) Add neutral protease for the second enzymatic hydrolysis; (4) Acid treatment and inactivation: Adjust the pH of the system after enzymatic hydrolysis to 4.8-5.2, and then heat to 88-92℃ to inactivate the enzyme; (5) Neutralization: Adjust the pH of the system after enzyme inactivation to 5.8-6.2; (6) Adsorption decolorization and filtration: Add activated carbon for adsorption, and then filter to obtain primary clarified liquid; (7) Membrane separation: Filter the primary clarified liquid through a nanofiltration membrane to obtain concentrated peptide liquid; (8) Sterilization: Perform ultra-high temperature instantaneous sterilization on the concentrated peptide liquid.
[0009] Further, the directional enzymatic hydrolysis in step (3) specifically involves: first adding alkaline protease at a weight of 0.5%-1.0% of the raw material and hydrolyzing for 15-25 minutes; then adding neutral protease at a weight of 0.2%-0.4% of the raw material and hydrolyzing for 150-170 minutes.
[0010] Further, the high-temperature swelling treatment in step (1) is as follows: animal skin or cartilage or fish scales are mixed with purified water at a mass ratio of 1:(6-10), heated at 90-97℃ for 2-4 hours, then cold water is added to adjust the total water-to-material ratio to 1:(4-5), and the temperature is lowered to 53-57℃.
[0011] Furthermore, the alkaline regulator used in step (2) is sodium hydroxide solution; the acidic regulator used in step (4) is glacial acetic acid solution or food-grade hydrochloric acid solution.
[0012] Further, the adsorption conditions in step (6) are as follows: at 48-52°C, add activated carbon accounting for 8%-12% of the weight of the raw material, and stir for 25-35 minutes for adsorption.
[0013] Further, the filtration in step (6) includes sequential activated carbon pre-coating filtration and precision filtration, wherein the turbidity of the primary clarified liquid is controlled below 1.0 NTU.
[0014] A collagen peptide, characterized in that the collagen peptide is prepared by the method according to any one of claims 1 to 9.
[0015] The application of a collagen peptide in the preparation of foods or medicines that improve sleep quality, prolong sleep time, or shorten sleep latency.
[0016] The beneficial effects of this application are as follows:
[0017] A strategy of "alkaline pretreatment + stepwise synergistic enzymatic hydrolysis by alkaline and neutral proteases" was adopted. First, collagen was fully denatured and swollen under alkaline conditions, creating an optimal environment for alkaline proteases to perform preliminary, selective cleavage. Then, under neutral conditions, neutral proteases were used for deep, gradual enzymatic hydrolysis. This targeted enzymatic hydrolysis process is not random degradation, but rather tends to hydrolyze specific peptide bonds in collagen, thereby efficiently and specifically enriching small molecule peptides (such as collagen peptides) with a molecular weight less than 1000 Daltons. As shown in comparative experiments, using the method of this invention, the proportion of small molecule peptides can stably reach over 95%, while the traditional single enzymatic hydrolysis method only achieves about 85%, demonstrating significant advantages. Attached Figure Description
[0018] The accompanying drawings, which form part of this application, are used to provide a further understanding of the application and to make other features, objects, and advantages of the application more apparent. The illustrative embodiments and descriptions of this application are used to explain the application and do not constitute an undue limitation of the application.
[0019] Furthermore, throughout the accompanying drawings, the same or similar reference numerals denote the same or similar elements. It should be understood that the drawings are schematic, and the elements are not necessarily drawn to scale.
[0020] In the attached diagram:
[0021] Figure 1 This is a schematic diagram of the overall framework according to an embodiment of this application;
[0022] Figure 2 This is a structural schematic diagram of a part of the embodiment, mainly showing the structure of the hydrolysis device;
[0023] Figure 3 This is a structural schematic diagram of a part of the embodiment, mainly showing... Figure 1 The local structure.
[0024] Figure label:
[0025] 1. Hydrolysis tank; 2. Stirring shaft; 3. Stirring rod; 4. Drive component; 5. First heating structure; 6. Second heating structure; 7. Dispersion column. Detailed Implementation
[0026] Embodiments of this disclosure will now be described in more detail with reference to the accompanying drawings. While some embodiments of this disclosure are shown in the drawings, it should be understood that this disclosure can be implemented in various forms and should not be construed as limited to the embodiments set forth herein. Rather, these embodiments are provided to provide a more thorough and complete understanding of this disclosure. It should be understood that the accompanying drawings and embodiments of this disclosure are for illustrative purposes only and are not intended to limit the scope of protection of this disclosure.
[0027] It should also be noted that, for ease of description, only the parts relevant to the invention are shown in the accompanying drawings. Unless otherwise specified, the embodiments and features described in this disclosure can be combined with each other.
[0028] It should be noted that the concepts of "first" and "second" mentioned in this disclosure are used only to distinguish different devices, modules or units, and are not used to limit the order of functions performed by these devices, modules or units or their interdependencies.
[0029] It should be noted that the terms "a" and "a plurality of" used in this disclosure are illustrative rather than restrictive, and those skilled in the art should understand that, unless otherwise expressly indicated in the context, they should be understood as "one or more".
[0030] Unless otherwise specified, all experiments used 100 kg of pre-treated (degreasing, washing) pigskin from the same batch as raw materials. The basic process followed the procedure of Example 1 of this invention, with adjustments made only for the single variable to be investigated. The final product testing indicators included: (1) molecular weight distribution (using high-performance gel permeation chromatography to calculate the percentage of peptides with a molecular weight <1000 Daltons in the total peptide content); (2) product turbidity (NTU value); (3) sensory evaluation (blind evaluation of color, odor, and taste by 3 professional tasters).
[0031] This disclosure will now be described in detail with reference to the accompanying drawings and embodiments.
[0032] Reference Figure 1 ,
[0033] A method for developing collagen peptides with calming and sleep-aiding effects, characterized by comprising the following steps:
[0034] (1) Raw material pretreatment: Mix animal skin, cartilage or fish scales with water and perform high-temperature swelling treatment;
[0035] (2) Alkali treatment: Adjust the pH of the swollen system to 9.8-10.2;
[0036] (3) Targeted enzymatic hydrolysis: Under the conditions of 53-57℃ and pH 9.8-10.2, alkaline protease is added first for the first stage of enzymatic hydrolysis, and then neutral protease is added for the second stage of enzymatic hydrolysis;
[0037] (4) Acid treatment and inactivation: Adjust the pH of the system after enzymatic hydrolysis to 4.8-5.2, and then heat to 88-92℃ to inactivate the enzyme;
[0038] (5) Neutralization: Adjust the pH of the enzyme-inactivated system to 5.8-6.2;
[0039] (6) Adsorption decolorization and filtration: Activated carbon is added for adsorption, and then filtered to obtain a primary clear liquid;
[0040] (7) Membrane separation: The primary clarified liquid is filtered through a nanofiltration membrane to obtain a concentrated peptide solution;
[0041] (8) Sterilization: The concentrated peptide solution is subjected to ultra-high temperature instantaneous sterilization.
[0042] Further, the directional enzymatic hydrolysis in step (3) specifically involves: first adding alkaline protease at a weight of 0.5%-1.0% of the raw material and hydrolyzing for 15-25 minutes; then adding neutral protease at a weight of 0.2%-0.4% of the raw material and hydrolyzing for 150-170 minutes.
[0043] Further, the high-temperature swelling treatment in step (1) is as follows: animal skin or cartilage or fish scales are mixed with purified water at a mass ratio of 1:(6-10), heated at 90-97℃ for 2-4 hours, then cold water is added to adjust the total water-to-material ratio to 1:(4-5), and the temperature is lowered to 53-57℃.
[0044] Furthermore, the alkaline regulator used in step (2) is sodium hydroxide solution; the acidic regulator used in step (4) is glacial acetic acid solution or food-grade hydrochloric acid solution.
[0045] Further, the adsorption conditions in step (6) are as follows: at 48-52°C, add activated carbon accounting for 8%-12% of the weight of the raw material, and stir for 25-35 minutes for adsorption.
[0046] Further, the filtration in step (6) includes sequential activated carbon pre-coating filtration and precision filtration, wherein the turbidity of the primary clarified liquid is controlled below 1.0 NTU.
[0047] A collagen peptide, characterized in that the collagen peptide is prepared by the method according to any one of claims 1 to 9.
[0048] The application of a collagen peptide in the preparation of foods or medicines that improve sleep quality, prolong sleep time, or shorten sleep latency.
[0049] Case 1: Optimization of Enzyme Addition Ratio and Time in Two Steps of Targeted Enzymatic Hydrolysis
[0050] Experimental objective: To verify the necessity of the two-step directional enzymatic hydrolysis strategy of "alkali enzyme first, then neutral enzyme" and its specific parameters (enzyme amount, time).
[0051] Experimental plan:
[0052] The present invention group (Example A): was carried out entirely according to the parameters of claim 2. At 55°C and pH 10.0, 0.7% alkaline protease was added first, and enzymatic hydrolysis was carried out for 20 minutes; then 0.3% neutral protease was added, and enzymatic hydrolysis was carried out for 160 minutes.
[0053] Comparative Example B (single enzymatic hydrolysis): using only 1.0% neutral protease, enzymatic hydrolysis was performed at pH 7.0 and 55°C for 180 minutes.
[0054] Comparative Example C (enzyme addition order reversed): At pH 7.0 and 55℃, first add 0.3% neutral protease for 80 minutes of enzymatic hydrolysis, then adjust the pH to 10.0 and add 0.7% alkaline protease for 100 minutes of enzymatic hydrolysis.
[0055] Comparative Example D (enzyme amount outside the range): At pH 10.0 and 55℃, 1.5% alkaline protease was added first for 20 minutes of enzymatic hydrolysis, followed by 0.8% neutral protease for 160 minutes of enzymatic hydrolysis.
[0056] Experimental results:
[0057] Group <1000Da peptide proportion Turbidity (NTU) Sensory evaluation Example A 96.2% 0.8 Light yellow, clear, no bitter taste, pure collagen characteristic flavor. Comparative Example B 84.5% 2.5 Yellow, slightly cloudy, with a distinctly bitter aftertaste. Comparative Example C 88.1% 1.9 Yellow, slightly cloudy, with a slight odor. Comparative Example D 95.8% 3.2 Dark yellow, cloudy, with a strong burnt and bitter smell.
[0058] Experimental conclusion:
[0059] The two-step targeted enzymatic hydrolysis (Group A) under alkaline pretreatment environment used in this invention can most effectively cut collagen into target small molecule peptides, with a yield significantly higher than that of traditional single enzymatic hydrolysis (Group B).
[0060] The order of enzymatic digestion is crucial. The process of first enzymatically digesting alkaline enzymes and then neutral enzymes (Group A) is superior to the reverse order (Group C), indicating that opening the protein's spatial structure in an alkaline environment is a key step.
[0061] The enzyme dosage must be strictly controlled within the range specified in this invention. While excessive enzyme use (Group D) also produced small molecule peptides, over-enzymatic hydrolysis led to an increase in bitter peptides and may have disrupted the activated carbon adsorption process, resulting in abnormally high turbidity, darker color, and deteriorated flavor. This demonstrates that the enzyme dosage range determined in this invention (0.5-1.0% for alkaline enzymes and 0.2-0.4% for neutral enzymes) represents the optimal balance between efficiency and quality.
[0062] Case Study 2: Effects of Water-to-Material Ratio and Temperature on Raw Material Pretreatment (Swelling)
[0063] Experimental objective: To verify the effects of water-to-material ratio and temperature during the high-temperature swelling stage on subsequent enzymatic hydrolysis efficiency and product clarity.
[0064] Experimental plan:
[0065] The present invention group (Example E): using the preferred parameters of claim 3, the water-to-material ratio is 1:6, heated at 94°C for 3 hours, and then cold water is added to adjust the total water-to-material ratio to 1:4.
[0066] Comparative Example F (water-to-material ratio too low): water-to-material ratio 1:3, heated at 94℃ for 3 hours. Due to the excessively high viscosity, subsequent stirring and heat transfer became difficult.
[0067] Comparative Example G (excessive water-to-material ratio): Water-to-material ratio 1:15, heated at 94℃ for 3 hours. Energy consumption increased significantly.
[0068] Comparative Example H (temperature too low): water-to-material ratio 1:6, but only heated at 70°C for 3 hours.
[0069] Experimental results (mainly examining the initial state of the enzyme hydrolysate and the final product):
[0070] Group Material status after profit increase <1000Da peptide proportion Terminal turbidity (NTU) Example E It expands fully and forms a homogeneous suspension. 95.5% 0.9 Comparative Example F It formed a sticky clump and was not mixed evenly. 81.3% 5.0 (Difficult to filter) Comparative Example G Thin, low proportion of raw materials 90.1% 1.2 (but with low yield and high energy consumption) Comparative Example H Insufficient expansion, some raw materials remain hard. 87.6% 2.1
[0071] Experimental conclusion:
[0072] The preferred water-to-material ratio (1:6-10) and high-temperature (90-97℃) swelling conditions (Group E) of this invention ensure sufficient swelling and denaturation of collagen, laying the foundation for subsequent homogenization and efficient enzymatic hydrolysis. A water-to-material ratio that is too low (Group F) makes the operation impossible; a ratio that is too high (Group G) is uneconomical; and insufficient temperature (Group H) results in incomplete pretreatment, directly affecting the final degree of hydrolysis and product clarity.
[0073] Case Study 3: Optimization of Activated Carbon Adsorption Dosage and Conditions
[0074] Experimental objective: To verify the key role of activated carbon dosage in decolorization, impurity removal, and product clarity.
[0075] Experimental plan:
[0076] After completing the aforementioned enzymatic hydrolysis, inactivation, and neutralization steps, five portions of the same mass of the enzymatic hydrolysate were taken and subjected to adsorption at 50°C:
[0077] Example 1 of this invention: Add 10% of the weight of the raw material of activated carbon and stir for 30 minutes.
[0078] Comparative Example J (insufficient dosage): Add 5% activated carbon by weight of raw materials and stir for 30 minutes.
[0079] Comparative example K (excessive dosage): Add 20% of the raw material weight of activated carbon and stir for 30 minutes.
[0080] Comparative Example L (temperature too low): Add 10% of the raw material weight of activated carbon, but stir at 30°C for 30 minutes.
[0081] Comparative Example M (no adsorption step): No activated carbon was added; the mixture was filtered directly.
[0082] Experimental results:
[0083] Group Decolorization effect Terminal turbidity (NTU) Odor removal status Example I Good, light yellow 0.8 Complete removal Comparative Example J Generally, it is yellow. 1.8 Some residue Comparative example K Excellent, nearly colorless 0.5 Complete removal Comparative Example L Poor quality, yellowish-brown 2.5 Incomplete removal Comparative Example M None, dark brown >10.0 The odor is obvious.
[0084] Experimental conclusion:
[0085] The activated carbon adsorption step is crucial for reducing product turbidity and improving sensory quality (compare Group I and Group M).
[0086] The dosage range (8-12%) and temperature (48-52℃) selected in this invention are key to achieving the best balance between efficiency and economy. Insufficient dosage (Group J) or excessively low temperature (Group L) both result in substandard purification effects; while excessive use (Group K) can improve the indicators, it will significantly increase costs and may also lead to the excessive adsorption and loss of the target peptide, which does not meet the requirements of industrial production.
[0087] Overall Conclusion
[0088] The comparative experiments described above clearly demonstrate that in the preparation method provided by this invention, the key parameters (such as ratio, temperature, pH, and time) defined in each step of the complete process chain—from raw material pretreatment (swelling) → directional enzymatic hydrolysis (two-step method) → purification (activated carbon adsorption)—are interconnected and synergistically related. Deviation from any key parameter may lead to a significant decrease in yield, purity, or sensory properties of the final product. This strongly proves that the technical solution of this invention is not a simple patchwork of existing technologies or a routine parameter adjustment, but a deeply optimized, inventive invention that produces outstanding comprehensive effects.
[0089] The following examples aim to illustrate the potential efficacy of the collagen peptides prepared by the method of the present invention in improving sleep through in vitro activity testing, animal behavioral experiments, and preliminary human trials. All collagen peptide samples used were prepared according to the process described in Example 1 (corresponding to the parameter combinations of Examples A / E / I in the aforementioned cases).
[0090] Example 4: In vitro simulated digestive stability and prediction of γ-aminobutyric acid (GABA) receptor binding activity
[0091] Objective: To evaluate the stability of the collagen peptides of this invention in the digestive system and to predict their potential interaction with the GABA_A receptor, a key target for sleep aid, using computer simulations. Methods:
[0092] Simulated gastrointestinal digestion: Samples were sequentially placed in systems containing pepsin (pH 2.0, 37℃, 2h) and trypsin (pH 7.5, 37℃, 2h). Changes in peptide molecular weight distribution before and after digestion were analyzed by high-performance liquid chromatography (HPLC).
[0093] Molecular docking simulation: Three characteristic peptides (such as Gly-Pro-Hyp, Pro-Hyp-Gly, and Hyp-Gly-Pro) with high content were screened from the collagen peptide mixture prepared in this invention. Using AutoDockVina software, molecular docking was performed between these peptides and the classical benzodiazepine binding site of the GABA_A receptor (PDBID: 6HUJ), and the binding energy (kcal / mol) was calculated. Results:
[0094] Digestive stability: After simulating gastrointestinal digestion, the proportion of peptides with a molecular weight <1000Da in the sample changed from 96.2% to 95.1%, indicating that the collagen peptides prepared in this invention have excellent digestive stability and most of the active peptides can be effectively absorbed.
[0095] Molecular docking results: All three collagen characteristic peptides can form hydrogen bonds and hydrophobic interactions with the GABA_A receptor binding cavity. The predicted binding energy is between -7.2 and -8.5 kcal / mol, showing moderate to strong binding potential, suggesting that they may exert physiological effects by regulating the GABAergic system.
[0096] Example 5: Synergistic effect of spontaneous activity in mice and sodium pentobarbital
[0097] Objective: To verify the sedative and synergistic hypnotic effects of the collagen peptides of this invention through animal experiments. Methods: Sixty healthy male ICR mice were randomly divided into 5 groups (n=12): blank control group (equal volume of physiological saline), positive control group (diazepam, 1 mg / kg BW), low-dose collagen peptide group (100 mg / kg BW), medium-dose group (200 mg / kg BW), and high-dose group (400 mg / kg BW). The peptides were administered by gavage once daily for 28 consecutive days.
[0098] Spontaneous activity experiment: 30 minutes after the last administration, mice were placed in a spontaneous activity recorder and the number of mouse movements (horizontal movement grids) was recorded within 10 minutes.
[0099] Synergistic sleep experiment with sodium pentobarbital: A subthreshold dose of sodium pentobarbital (35 mg / kg BW) was administered intraperitoneally 30 minutes after the last administration. Sleep latency (time from injection to the disappearance of the righting reflex) and sleep duration (time from the disappearance to the recovery of the righting reflex) were recorded. Results:
[0100] Group Number of independent activities (times / 10min) Sleep latency (seconds) Sleep duration (minutes) Blank control group 352±41 Not falling asleep / Few falling asleep 4.2±1.5 Diazepam Group 255±28 312±45 68.5±12.3 Low-dose collagen peptide group 225±38 285±62 35.1±1.8 Medium dose group of collagen peptides 188±35 185±52 22.4±6.7 High-dose collagen peptide group 140±32 110±48 21.6±8.1
[0101] Conclusion: Medium and high doses of the collagen peptides of this invention can significantly inhibit spontaneous activity in mice, and significantly shorten the sleep latency induced by sodium pentobarbital and prolong sleep time, showing certain sedative and synergistic hypnotic effects in a dose-dependent manner.
[0102] Reference Figure 2-3 ,
[0103] The enzymatic hydrolysis reaction is achieved using an enzymatic hydrolysis device. The enzymatic hydrolysis device includes:
[0104] The system consists of an enzymatic hydrolysis tank 1, a stirring shaft 2, a stirring rod 3, a drive unit 4, and a heating element. The raw materials to be hydrolyzed are placed into the enzymatic hydrolysis tank 1. The stirring shaft 2 is located inside the tank. The drive unit 4 rotates the stirring shaft, and the stirring rod 3 is fixed to the stirring shaft 2. This system effectively stirs the raw materials in the enzymatic hydrolysis tank 1, ensuring thorough mixing and a more complete reaction. The heating element maintains the temperature of the enzymatic hydrolysis tank 1 at 50-80℃.
[0105] The heating element includes a first heating structure 5 and a second heating structure 6; the enzymatic hydrolysis device also includes a dispersion column 7, which is disposed on the side of the stirring shaft 2, and the stirring rod 3 is located between multiple dispersion columns 7. A first cavity is formed in the stirring shaft 2, and a second cavity is formed on the dispersion column 7. The first heating structure 5 is disposed in the first cavity, and multiple second heating structures 6 are disposed, each placed in one of the multiple second cavities of the dispersion column 7.
[0106] Both the first heating structure 5 and the second heating structure 6 are pipelines filled with water at a temperature of 50-80℃. This keeps the main rotating shaft and the dispersion column 7 at a relatively high temperature, thus achieving a larger heating range within the enzymatic hydrolysis tank 1 and more uniform heating of the raw materials in the enzymatic hydrolysis process.
[0107] The dispersion column 7 is fixed to the mixing tank, and the second heating structure 6 is fixed to the inner wall of the second cavity. The second cavity has an inlet 61, an outlet 62, and a drain 63. An external water pump heating system is connected to the inlet 61 and outlet 62, allowing hot water to circulate in the pipeline, exchanging heat with the dispersion column 7 and heating the raw materials in the enzymatic hydrolysis tank 1. Simultaneously, the dispersion column 7 also disperses the raw materials after stirring by the stirring rod 3, further increasing the efficiency of uniform mixing.
[0108] Specifically, the first heating structure 5 is the same as the second heating structure 6. The first heating structure 5 is inserted into the first cavity and exchanges heat with the stirring shaft 2. Thus, the stirring shaft 2 exchanges heat with the raw materials in the enzymatic hydrolysis tank 1, further increasing the uniformity of heating of the raw materials.
[0109] The outlet 63 of the second heating structure 6 is fixed to the dispersion column 7. A through-hole is provided on the dispersion column 7, and the outlet 63 connects to the through-hole. Since the dispersion column 7 is fixed, this facilitates the connection between the outlet 63 and the through-hole. A control valve is installed at the outlet 63. After the reaction in the enzymatic hydrolysis tank 1 is completed, the control valve can be opened, and hot water will be discharged from the outlet 63 into the enzymatic hydrolysis tank 1. The jet force of the water discharged from the outlet 63 can be used to better spray onto the inner wall of the enzymatic hydrolysis tank 1, increasing the cleaning effect of the enzymatic hydrolysis tank 1.
[0110] The above description is merely a selection of preferred embodiments of this disclosure and an explanation of the technical principles employed. Those skilled in the art should understand that the scope of the invention involved in the embodiments of this disclosure is not limited to technical solutions formed by specific combinations of the above-described technical features, but should also cover other technical solutions formed by arbitrary combinations of the above-described technical features or their equivalents without departing from the above-described inventive concept. For example, technical solutions formed by substituting the above-described features with (but not limited to) technical features with similar functions disclosed in the embodiments of this disclosure.
Claims
1. A method for developing a collagen peptide with calming and sleep-aiding effects, characterized in that, Includes the following steps: (1) Raw material pretreatment: Mix animal skin, cartilage or fish scales with water and perform high-temperature swelling treatment; (2) Alkali treatment: Adjust the pH value of the swollen system to 9.8-10.2; (3) Targeted enzymatic hydrolysis: Under the conditions of 53-57℃ and pH 9.8-10.2, first add alkaline protease for the first stage of enzymatic hydrolysis, and then add neutral protease for the second stage of enzymatic hydrolysis; (4) Acid treatment and inactivation: Adjust the pH value of the system after enzymatic hydrolysis to 4.8-5.2, and then raise the temperature to 88-92℃ to inactivate the enzyme; (5) Neutralization: Adjust the pH value of the system after enzyme inactivation to 5.8-6.2; (6) Adsorption decolorization and filtration: Add activated carbon for adsorption, and then filter to obtain primary clarified liquid; (7) Membrane separation: Filter the primary clarified liquid through nanofiltration membrane to obtain concentrated peptide liquid; (8) Sterilization: Perform ultra-high temperature instantaneous sterilization on the concentrated peptide liquid.
2. The method according to claim 1, characterized in that, The directional enzymatic hydrolysis in step (3) is as follows: first, add alkaline protease accounting for 0.5%-1.0% of the raw material weight and hydrolyze for 15-25 minutes; then add neutral protease accounting for 0.2%-0.4% of the raw material weight and hydrolyze for 150-170 minutes.
3. The method according to claim 1 or 2, characterized in that, The high-temperature swelling treatment in step (1) is as follows: animal skin or cartilage or fish scales are mixed with purified water at a mass ratio of 1:(6-10), heated at 90-97℃ for 2-4 hours, then cold water is added to adjust the total water-to-material ratio to 1:(4-5), and the temperature is lowered to 53-57℃.
4. The method according to claim 1, characterized in that, The alkaline regulator used in step (2) is sodium hydroxide solution; the acidic regulator used in step (4) is glacial acetic acid solution or food-grade hydrochloric acid solution.
5. The method according to claim 1, characterized in that, The adsorption conditions described in step (6) are as follows: at 48-52℃, add activated carbon accounting for 8%-12% of the weight of the raw material, and stir for 25-35 minutes for adsorption.
6. The method according to claim 1, characterized in that, The filtration in step (6) includes activated carbon pre-coating filtration and precision filtration performed sequentially, and the turbidity of the primary clarified liquid is controlled below 1.0 NTU.
7. A collagen peptide, characterized in that, The collagen peptides are prepared by the method described in any one of claims 1 to 9.
8. The use of the collagen peptide as described in claim 7 in the preparation of a food or medicine that improves sleep quality, prolongs sleep time, or shortens sleep latency.