CN107573405B - Mussel polypeptide extract and preparation method thereof - Google Patents
Mussel polypeptide extract and preparation method thereof Download PDFInfo
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Abstract
The invention provides a method for preparing mussel polypeptide by using nano enzyme technology, and mussel polypeptide extract and mussel polypeptide monomer PEPTIDE-S which are prepared by the method and have the function of regulating blood fat, and the amino acid sequence is as follows: Gly-Ile-Ala-Val-Pro-Val-Trp.
Description
Technical Field
The invention belongs to the field of biological medicines, and particularly relates to a mussel polypeptide extract and a preparation method thereof.
Background
Blood lipids are a general term for neutral fats and lipids in plasma, the main components of blood lipids are triglyceride TG and cholesterol TC, and hyperlipidemia is called when the blood lipid concentration exceeds the normal high limit (tg1.81mm, tc5.95mm). Hyperlipidemia can induce many cardiovascular and cerebrovascular diseases and metabolic diseases, such as hypertension, atherosclerosis, diabetes and the like. The prevention and treatment of hyperlipidemia has important significance for preventing complications thereof, especially cardiovascular and cerebrovascular diseases. One of the methods for preventing hyperlipidemia is to limit the intake of high cholesterol foods such as high calorie foods, animal fats and oils, and liver. The method can cause insufficient acquisition of protein and lipid in vivo to cause physical deterioration of weak people and damage to health; the second method is drug therapy, which inhibits the absorption and synthesis of cholesterol by inhibiting the synthesis and enhancing the clearance of Low Density Lipoprotein (LDL) and Very Low Density Lipoprotein (VLDL). The drug therapy can generate a plurality of toxic and side effects, and the blood fat can rise quickly after the drug taking is stopped.
Therefore, how to develop a pure natural lipid-lowering product which is safe, non-toxic, free of side effects, significant in lipid-lowering efficacy and free of rebound after use becomes a hot spot in the industry at present.
Mussels are commonly known as rainbow, a marine mollusk. Mussels have a high nutritional value and a certain medicinal value. Mussel meat has a protein content of about 60% and is rich in amino acids essential to the human body (up to 49%), which is far superior to other meat products. In addition, it contains vitamins, trace elements and unsaturated fatty acids such as DHA, BPA, etc. beneficial to human body. The fresh mussels are popular seafood products and have high nutritional value, but are not easy to store after being harvested, and are processed into dried mussels after being cooked, so that the nutritional value of the mussels is greatly reduced, great waste is caused, and the development of the mussel industry in China is limited. At present, there are mussel deep processing technologies, such as the chinese patent invention "preparation method of mussel active polypeptide (No. CN 10175598B)". However, the invention adopts a common enzymolysis method, the utilization rate of enzyme is low, and the obtained mussel polypeptide has no function of regulating blood fat of human body.
How to improve the utilization efficiency of enzyme, reduce industrial production cost, improve production technology to obtain a marine mussel peptide with blood lipid regulating activity, promote the development and utilization of mussels is a realistic problem which needs to be solved urgently by the research in the industry at present.
Disclosure of Invention
Aiming at the problems in the prior art, the invention provides a method for preparing mussel polypeptide by using a nano-enzyme technology, and a mussel polypeptide extract and a mussel polypeptide monomer which are prepared by the method and have the effect of regulating blood fat.
The invention provides a preparation method of a mussel polypeptide extract, which adopts immobilized nanoenzyme to carry out enzymolysis on mussel freeze-dried powder to obtain the mussel polypeptide extract.
The preparation method according to any one of the first aspect of the present invention, wherein the mussel lyophilized powder is mussel powder obtained by mincing, freeze-drying and degreasing fresh mussel meat. Wherein, the particle size of the mussel lyophilized powder is not specially required, preferably 10-200 μm, more preferably 50-150 μm, and most preferably 80-100 μm. The degreasing treatment can be performed by various methods known in the art, preferably by using a supercritical extraction device to degrease the mussel powder, wherein the supercritical extraction pressure is preferably 30-50MPa, more preferably 35-40MPa, and most preferably about 35 MPa; the supercritical extraction temperature is preferably from 30 to 50 deg.C, more preferably from 35 to 45 deg.C, and most preferably about 35 deg.C; the supercritical extraction time is preferably 100-300min, more preferably 150-250min, and most preferably about 200 min.
The production method according to any one of the first aspect of the present invention, wherein the immobilized nanoenzyme used is a flavourzyme. Immobilized nanoenzymes of various particle sizes can be used in the present invention, preferably the particle size of the immobilized nanoenzyme is 100-1000nm, preferably 200-800 nm. The immobilized nanoenzyme used in the invention can be obtained commercially, and preferably is a flavor protease meeting the food-grade enzyme preparation standard recommended by FAO/WHO/JECFA/FCC.
The preparation method according to any one of the first aspect of the present invention, wherein the immobilized nanoenzyme is added in an amount of 0.005-5%, preferably 0.01-1%, more preferably 0.05-0.5%, and most preferably about 0.1% (the percentage is mass percentage) of the mussel lyophilized powder. The enzymolysis time is 2-6h, preferably 3-5h, and most preferably about 4 h. The temperature of the enzymatic hydrolysis is 40-68 deg.C, preferably 50-65 deg.C, more preferably 55-62 deg.C, and most preferably about 60 deg.C. The pH value of the enzymolysis reaction system is 7.5-10, more preferably 8.5-9.5, and most preferably 9. The pH value of the enzymatic reaction system may be adjusted using various pH adjusting agents commonly used in the art, preferably, the pH value of the reaction system is adjusted using an aqueous NaOH solution and an aqueous HCl solution, more preferably, the pH value of the reaction system is adjusted using an aqueous NaOH solution of 0.5 to 2mol/L and an aqueous HCl solution of 0.5 to 2mol/L, and most preferably, the pH value of the reaction system is adjusted using an aqueous NaOH solution of about 1mol/L and an aqueous HCl solution of about 1 mol/L.
The preparation method according to any one of the first aspect of the present invention further comprises a step of purifying the enzymatic hydrolysate, specifically removing pigment from the enzymatic hydrolysate, wherein the method for removing pigment adopts various methods known in the art, preferably adopts an activated carbon adsorption method, specifically: centrifuging the enzymolysis solution, taking the supernatant, adding active carbon, adsorbing pigment by magnetic stirring, and centrifuging to remove the precipitate. Wherein the adding amount of the active carbon is 0.1-10% of the mussel freeze-dried powder, preferably 0.5-5%, more preferably 1-3%, and most preferably about 2% (the percentage is mass percentage); the temperature of the activated carbon for adsorbing the pigment is 20-65 deg.C, more preferably 30-50 deg.C, and most preferably about 42 deg.C. Preferably, the pigment is adsorbed by magnetic stirring at 50-200rpm for 10-120min, more preferably at 80-160rpm for 20-60min, and most preferably at 120rpm for about 30 min. The refined enzymolysis liquid is obtained by centrifuging for 0.5-2h, preferably 0.8-1.5h, and most preferably about 1h with a tubular centrifuge. Preferably, the tubular centrifuge has a centrifugation factor of 6000-.
In a second aspect, the present invention provides a mussel polypeptide extract prepared by the above preparation method. The extract contains polypeptide 70-80%, amino acids 10-18%, mucopolysaccharide 3.5-6%, and trace elements such as calcium, iron, zinc, manganese, phosphorus, and other nutrients such as vitamins. The polypeptide component in the extract mainly comprises 2-10 peptides (with molecular weight of 0.2-1.5 kDa), and accounts for about 80% of the total peptide content.
In a third aspect, the invention provides an active polypeptide PEPTIDE-S, wherein the amino acid sequence of the polypeptide is shown as SEQ ID NO: 1, specifically: Gly-Ile-Ala-Val-Val-Pro-Trp, molecular weight 740.89 Da.
The active polypeptide PEPTIDE-S can be obtained by refining and purifying the mussel polypeptide extract: intercepting components with molecular weight less than or equal to 1000Da from mussel polypeptide extract with 1000Da ultrafiltration membrane; separating with Sephadex column chromatography, and collecting the component with highest absorbance value at 560 nm; finally separating by C18 column chromatography to obtain active polypeptide PEPTIDE-S.
The active polypeptide PEPTIDE-S can be prepared by other methods known in the art, such as a solid phase synthesis method, a biological engineering method, and the like, in addition to the above-mentioned method provided by the present invention.
In the fourth aspect, the invention provides an application of the mussel polypeptide extract or the active polypeptide PEPTIDE-S in preparing medicines or health products for treating and/or preventing diseases related to hyperlipidemia. The diseases associated with hyperlipidemia include, but are not limited to, hypertension, atherosclerosis, diabetes, cerebrovascular disease, pancreatitis, lithiasis, fatty liver, etc.
In a fifth aspect, the present invention provides a pharmaceutical composition, which comprises an active ingredient mussel polypeptide extract and/or active polypeptide PEPTIDE-S and pharmaceutically acceptable excipients.
The pharmaceutical compositions of the present invention may be formulated in a form conventional in the art, including, but not limited to, powders, tablets (including various coated tablets, sustained-release or controlled-release tablets), lozenges, capsules (including soft and hard capsules), granules, pills, dispersible powders, aqueous or oily suspensions, aqueous or oily solutions, emulsions, elixirs, syrups and the like, suitable for oral use, creams, ointments, gels, aqueous or oily solutions, aqueous or oily suspensions, and the like; a powder or liquid aerosol suitable for inhalation use; suitable for parenteral administration, intravenous, subcutaneous or intramuscular injection, sterile aqueous or oily injection or lyophilized powder injection, suppository and the like.
The pharmaceutically acceptable excipients include, but are not limited to, excipients, lubricants, binders, disintegrants, water-soluble polymers, inorganic salts, solvents, dissolution aids, suspending agents, isotonic agents, buffers, preservatives, antioxidants, coloring agents, sweetening agents, acidulants, foaming agents, flavoring agents, and the like.
The pharmaceutical compositions of the invention may also contain other active ingredients, for example other active ingredients with antioxidant activity, such as other active ingredients capable of lowering blood pressure. The person skilled in the art is able to determine suitable amounts of mussel polypeptide extract or PEPTIDE-S of the invention and various adjuvants and/or other active ingredients in pharmaceutical and nutraceutical compositions according to conventional methods.
In the present invention, various mussels such as Mytilus edulis (mytilus chilus) and Mytilus galloprovincialis (mytilus gallophovingia), preferably Mytilus edulis. Generally speaking, the Mytilus edulis of various sizes can be used, with a large shell of 14-16cm in length, a shell of 5-6cm in height, and a weight of 30-40 g.
The invention has the beneficial effects that:
1. the raw material used in the invention is the deep sea mussel which is generally used as food directly, and the original activity and/or nutritional value of the mussel are greatly lost after being treated in the using process. The invention greatly improves the use value of the mussels and expands the use range of the mussels.
2. The enzymolysis method of the invention uses the immobilized nanometer flavor protease to greatly reduce the consumption of the enzyme and obtain the polypeptide with biological activity. The immobilized nanoenzyme can be recycled, can always keep higher enzyme activity, for example, the enzyme activity can be recycled for 10 times, and the enzyme activity of the immobilized nanoenzyme can be kept above 95 percent, so that the industrial cost can be greatly saved.
3. The enzymatic polypeptide extract and the polypeptide single product PEPTIDE-S have the activity of regulating blood fat but not only have good effect on diseases caused by hyperlipidemia, such as but not limited to hypertension, atherosclerosis, diabetes and the like.
Drawings
FIG. 1 is an MS map of the polypeptide PEPTIDE-S.
Detailed Description
In order to make the objects, technical solutions and advantages of the present invention more apparent, the present invention is further described in detail with reference to the following embodiments. It should be understood that the specific embodiments described herein are merely illustrative of the invention and do not limit the invention in any way.
Example 1 preparation of mussel polypeptide extract
(1) Cleaning live deep sea mussel, removing shell, vacuum freeze drying, and pulverizing into powder with particle size of 80-100 μm. Weighing 10kg of perna canaliculus powder, placing the perna canaliculus powder in an extraction kettle of a supercritical extraction device for degreasing treatment, wherein the extraction pressure is 35MPa, the extraction temperature is 35 ℃, the extraction time is about 200min, and separating under normal pressure to obtain 9.4kg of degreased perna canaliculus powder.
(2) Taking 9.4kg of degreased perna canaliculus powder, adding 150L of deionized water, uniformly mixing, grinding and homogenizing for 5 times by using a colloid mill, and filtering the obtained slurry by using a 100-mesh screen; putting the filtrate in a reaction kettle, adding water to the total volume of 372L to ensure that the mass/volume percentage of the raw materials in the suspension is 5%, adding immobilized nano flavourzyme (Novexin biotechnology Co., Ltd., product number PW431145M) into the reaction kettle, wherein the temperature of the reaction kettle is 60 ℃, the pH value of the reaction system is adjusted to be about 9, the pH value of the reaction system is monitored at any time in the enzymolysis process, the pH value of the reaction system is adjusted by using 1mol/L NaOH aqueous solution and 1mol/L HCl aqueous solution to keep the pH value of the reaction system to be about 9, the stirring speed of the reaction kettle is 100rpm, and the enzymolysis process lasts for 4 hours; adsorbing and removing the immobilized nano enzyme from the enzymolysis reaction system by using a magnet to obtain enzymolysis crude liquid; recovering immobilized nanometer flavor protease, soaking in dilute alkali solution for 20min, washing with distilled water to neutrality, vacuum filtering, purifying immobilized nanometer enzyme, storing at 4 deg.C, and performing enzymolysis again.
(3) Centrifuging the enzymolysis crude solution at room temperature at 5000rpm for 15min, collecting supernatant, adding 185g of active carbon, and magnetically stirring at 42 deg.C and 120rpm for about 30min to adsorb pigment; and then centrifuging for 1h by a tubular centrifuge, setting the centrifugation factor to 10000, removing the precipitate and reserving clear liquid to obtain refined enzymolysis liquid.
(4) The refined enzymolysis liquid is spray-dried to obtain 1kg of the common mussel polypeptide extract, and the yield is 10%. The inlet temperature of the pressure spray dryer is 180 ℃, the outlet temperature is 80 ℃ and the pressure is 1.6 Mpa.
Example 2 isolation of polypeptide PEPTIDE-S having blood lipid modulating Activity
Taking 50ml of refined enzymolysis liquid prepared in the step (3) in the embodiment 1, and intercepting components with the molecular weight less than or equal to 1000Da through ultrafiltration (selecting 1000Da by a filter membrane); then separating and purifying by using a chromatographic column, wherein the filler is Sephadex G-250, the mobile phase is aqueous solution, the column temperature is room temperature, the detection wavelength is 560nm, collecting according to time, collecting for 20 minutes per tube, and collecting components for freeze-drying. The activity of cholesterol (TC)/Triglyceride (TG) reducing activity of each tube of freeze-dried powder is determined, the specific determination method is shown in example 3, and one tube with the most obvious effect of reducing The Cholesterol (TC)/Triglyceride (TG) is used as a pure product of the potential lipid-lowering active peptide.
Separating and purifying the tube with the best blood fat reduction by RP-HPLC, using a C18 column, wherein a mobile phase A liquid is a TFA aqueous solution with the volume percentage of 0.1 percent, performing ultrasonic degassing before using, a mobile phase B liquid is acetonitrile, the detection wavelength is 215nm, the column temperature is room temperature, the injection volume is 20ul-40ul, and performing gradient elution by adopting a gradient elution method: after 0-50 min, the liquid A is linearly reduced by 100-0%, and the liquid B is linearly increased by 0-100%; 50-60 min, 0% of the solution A and 100% of the solution B, and collecting the eluent with the retention time of 40-50 min. The eluent is the monopeptide solution with antioxidant activity. The polypeptide component with good hypolipidemic activity is obtained by separation and named PEPTIDE-S, and the yield of the single PEPTIDE is about 1 percent of that of the polypeptide extract. The molecular weight of the peptide was determined to be 740.89Da by high performance liquid-electrospray tandem mass spectrometry (HPLC-ESI-MS). The mass spectrum is shown in figure 1. The amino acid sequence of the polypeptide PEPTIDE-S is determined to be Gly-Ile-Ala-Val-Pro-Val-Trp by an amino acid automatic sequencer (adopting a German-Mannheim model A300 full-automatic amino acid sequencer), and the molecular weight of the polypeptide PEPTIDE-S is 740.89 Da.
EXAMPLE 3 in vitro Activity assay for polypeptide extracts and PEPTIDEs for modulating blood lipid levels
After the HepG2 cells are normally passaged, the HepG2 cells grow in a culture medium containing 10% fetal calf serum for 24 hours, the original culture medium is discarded, the culture medium is changed into 1% BSA for culture, 10ug/ml cholesterol and 1ug/ml 25-hydroxy cholesterol are added for 24 hours, the cholesterol in the cells is obviously increased through determination, and the establishment of a high cholesterol (TC) cell model is successful. HepG2 grows in a culture medium containing 10% fetal calf serum, the original culture medium is discarded after 24 hours, the culture is changed to 1% BSA for culture, 50 mu mol/L oleic acid is added for acting for 24 hours, the absorption rate of free fatty acid in the culture solution is about 40%, the intracellular triglyceride has the increasing trend through determination, and the cell model with high Triglyceride (TG) is successful.
Grouping experiments: negative control group: cells were treated with 0.1% DMSO for 24 h; positive control group: 0.5umol/ml simvastatin was used as a positive control; high, medium, low dose groups of polypeptide extracts: taking the polypeptide extract prepared in the example 1, wherein the dosages are 400, 200 and 100mg/ml respectively; high, medium, and low dose groups of mussel PEPTIDE monomer PEPTIDE-S: taking the mussel PEPTIDE monomer PEPTIDE-S prepared in example 2, wherein the dosages are 400, 200 and 100mg/ml respectively; the positive control group and the experimental group treated the cells with simvastatin and polypeptide extract and PEPTIDE-S at different concentrations for 24h, after the cells were treated, they were digested with pancreatin, centrifuged at 2000rpm for 10min and the cells were collected and resuspended in 1ml PBS solution. Cells were harvested by centrifugation at 200. mu.l, and 30. mu.l of cell lysate was added to measure the total protein by the Bradford method. Another 800ul cell suspension was centrifuged, the supernatant was discarded and resuspended in 1ml isopropanol, disrupted by sonication for 20min, centrifuged at 12000rpm for 10min, the supernatant was transferred to another new 1.5ml centrifuge tube and vacuum dried. The Cholesterol (TC)/Triglyceride (TG) content was measured using a cholesterol measurement kit (cat # SB1985, Beijing Solebao technologies)/triglyceride measurement kit (cat # BC0147, Beijing Solebao technologies). The results are expressed as Total Cholesterol (TC)/Triglyceride (TG) (g/kg) contained in cells containing 1g of total protein.
The results are shown in Table 1.
TABLE 1 results of experiments on the in vitro activity of polypeptide extract and PEPTIDE-S for regulating blood lipid
| Group of | Dosage form | TC(g/kg) | TG(g/kg) |
| Negative control group | 0 | 55.86 | 161.35 |
| Positive control group | 0.5μmol/L | 41.33** | 115.64** |
| High dosage of polypeptide extract | 400mg/ml | 50.25* | 147.35* |
| Dosage in polypeptide extract | 200mg/ml | 53.48* | 151.76* |
| Low dosage of polypeptide extract | 100mg/ml | 54.33* | 155.32* |
| High dose of PEPTIDE-S | 400mg/ml | 44.63** | 121.48** |
| PEPTIDE-S MEDIUM DOSAGE | 200mg/ml | 46.89** | 131.94** |
| Low dose of PEPTIDE-S | 100mg/ml | 53.01* | 138.18** |
P < 0.05 indicated significant differences from the negative control group;
p < 0.01 indicates a very significant difference in the values compared to the negative control group.
The results show that different doses of the polypeptide extract reduced the total cholesterol level and the total triglyceride level in HepG2 cells to different degrees. After 24 hours of treatment of high cholesterol and high triglyceride model cells of HepG2 cells with different doses of mussel PEPTIDE monomer PEPTIDE-S, total cholesterol levels and total triglyceride levels in HepG2 cells were significantly reduced to different extents, and both were expressed as P < 0.01.
EXAMPLE 4 in vivo Activity-regulating experiments of polypeptide extracts and PEPTIDEs of PEPTIDE-S
90 SPF male Wistar rats with a body weight of about 200 + -10 g were selected. Rats were acclimatized for 3 days and randomized into 9 groups: normal control group, high-fat model group, positive control simvastatin group, high, medium and low dose polypeptide extract group (using the polypeptide extract prepared in example 1), high, medium and low dose mussel PEPTIDE-S group (using the mussel PEPTIDE-S prepared in example 2), 10 per group. Each group of rats had free access to water and 8 groups were given high fat diet, except for the normal control group. After feeding for 2 weeks, blood is taken from venous plexus behind eyeballs of rats in a normal group and rats in a high-fat feed group, the concentration of TC and TG in serum of the rats in a high-fat model group is more than 2 times that of the rats in a normal control group, and the difference level of TC and TG in the rats in two groups is obvious (P is less than 0.01), which indicates that the molding is successful. From the 3 rd week of experiment, rats of each group are still raised according to the previous method, and the normal control group and the model group are subjected to intragastric perfusion according to 10mL/kg of physiological saline; the experimental groups are respectively given corresponding doses of mussel PEPTIDE polypeptide extracts (high, medium and low doses respectively equal to 10000, 5000 and 2500mg/kg of the amount of crude drugs) or mussel PEPTIDE monomer PEPTIDE-S (high, medium and low doses respectively equal to 100, 50 and 25mg/kg of the amount of crude drugs) to be suspended and then are fed by gastric administration at 10 mL/kg; the positive control simvastatin (simvastatin) group was administered by gastric gavage with 10mL/kg simvastatin tablet suspension (5mg/kg)1 time per day. After feeding (administration) continuously for 6 weeks, rats of each group were anesthetized by intraperitoneal injection of 10mL/kg of 5% chloral hydrate, blood was taken from the abdominal aorta, the blood was allowed to stand for 30min, the blood serum was separated by centrifugation at 5000rpm and 4 ℃ for 15min, and TC, TG and HDL-C, LDL-C levels were measured by a biochemical analyzer.
The results are shown in Table 2.
TABLE 2 results of experiments on the regulation of blood lipid activity in vivo by polypeptide extracts and PEPTIDEs-S
△P < 0.01 shows that the normal group has very significant difference compared with the high fat model group;
p < 0.05 indicated significant differences from the model group values;
p < 0.01 indicates a very significant difference from the model group compared values.
The results show that the serum TC, TG and LDL-C of the rats in the model group with four detection results of the blood fat are obviously increased (P is less than 0.05) compared with the serum TC, TG and LDL-C of the rats in the normal group; compared with a model group, the serum TC, TG and LDL-C values of rats in a positive control group are obviously reduced (P is less than 0.01), and the serum HDL-C value of rats is obviously recovered after simvastatin/high-dose mussel PEPTIDE extract or mussel PEPTIDE monomer PEPTIDE-S is used.
Sequence listing
<110> Beijing Bo peptide unknown Biotechnology Limited
<120> mussel polypeptide extract and preparation method thereof
<160>1
<170>PatentIn Version 3.3
<210>1
<211>7
<212>PRT
<213> Artificial sequence
<400>1
Gly Ile Ala Val Val Pro Trp 7
Claims (3)
1. An active polypeptide PEPTIDE-S, wherein the amino acid sequence of said polypeptide is as set forth in SEQ ID NO: 1 is shown.
2. Use of the active polypeptide PEPTIDE-S as claimed in claim 1 for the preparation of a medicament or health product for the treatment and/or prevention of diseases associated with hyperlipidemia.
3. A pharmaceutical composition is characterized by comprising an active ingredient polypeptide-S and pharmaceutically acceptable auxiliary materials; the amino acid sequence of the PEPTIDE-S is shown as SEQ ID NO: 1 is shown.
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| CN113041263B (en) * | 2021-03-15 | 2023-07-25 | 青岛大学 | Application of mussel functional lipid in preparation of products for treating type 2 diabetes |
| CN113604531A (en) * | 2021-08-23 | 2021-11-05 | 大连工业大学 | Method for simultaneously preparing mussel functional lipid and active polypeptide |
| CN114044807B (en) * | 2021-11-19 | 2023-08-22 | 浙江海洋大学 | Mussel hypolipidemic oligopeptide for treating hyperlipidemia |
| CN116004418A (en) * | 2022-07-19 | 2023-04-25 | 江苏海洋大学 | Bacillus bailii Z-1 and application thereof in preparation of hydrolysate |
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| CN102952838A (en) * | 2011-08-23 | 2013-03-06 | 浙江海洋学院 | Preparation method of immune-enhancing mussel enzymatic hydrolytic polypeptide and preparation method of corresponding tablet thereof |
| CN103204906A (en) * | 2013-01-29 | 2013-07-17 | 浙江海洋学院 | Mussel meat protein antioxidative peptide and preparation method thereof |
| CN103710414A (en) * | 2013-08-07 | 2014-04-09 | 江苏大学 | Preparation method and application of mussel oligopeptide |
| CN105420331A (en) * | 2016-01-15 | 2016-03-23 | 北京博肽未名生物技术有限公司 | Method for extracting polypeptide through tadpole enzymolysis and polypeptide prepared by method |
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| CN102952838A (en) * | 2011-08-23 | 2013-03-06 | 浙江海洋学院 | Preparation method of immune-enhancing mussel enzymatic hydrolytic polypeptide and preparation method of corresponding tablet thereof |
| CN103204906A (en) * | 2013-01-29 | 2013-07-17 | 浙江海洋学院 | Mussel meat protein antioxidative peptide and preparation method thereof |
| CN103710414A (en) * | 2013-08-07 | 2014-04-09 | 江苏大学 | Preparation method and application of mussel oligopeptide |
| CN105420331A (en) * | 2016-01-15 | 2016-03-23 | 北京博肽未名生物技术有限公司 | Method for extracting polypeptide through tadpole enzymolysis and polypeptide prepared by method |
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