CN1552892A - Physiological active buck peptide by compound proteinase catalysis and use of products thereby - Google Patents
Physiological active buck peptide by compound proteinase catalysis and use of products thereby Download PDFInfo
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Abstract
This invention relates to preparation of deer peptide with biological activity by composite protease catalysis and its uses in human immunity, fatigue resistance and hypoxia tolerance. Products are obtained by heating deer meat paste as raw material, which is screened with 80 mesh, to 48-52 deg.C, regulating pH 6.8-7.2 with NaOH solution, stirring and adding neutral protease, papoid or trypsin, then adding fragrant protease after protein hydrolysis to 28-33%, controlling reaction with standard 2M NaOH to make protein hydrolysis to 34 -42%, heating enzymolysed liquid to 114-116 deg.C for 10-15 minutes, sharply cooling to atmosphere, solid-liquid separating, concentrating, and drying to obtain yellow powder or granular products of deer peptide.
Description
Technical field
The invention belongs to biochemical field, be specifically related to a kind of enzymatic method hydrolysis of conjugated protein venison of using and prepare deer peptide product, and this deer peptide product is in the application of aspects such as enhance immunity power, enhancing anti-fatigue ability and hypoxia-bearing capability with physiologically active.
Background technology
Physiologically active peptide is that popular topic is the most studied by current food educational circles, is generally made through the enzyme effect by protein, because of the difference of material protein, hydrolase, separation and refining method can arrive different products; The peptide class, particularly some oligopeptides not only have than the better performance of digesting and assimilating of protein, exciting is to it is found that some peptide class also has such as the physiologically active of regulating human physiological functions, disease resistance, found low antigen so far, promoted lipid metabolism, the absorption of reducing cholesterol, promotion mineral substance, hypotensive, anti-oxidant, improve a series of physiological functions such as immunizing power, and they have acid preferably, thermostability, water-soluble, viscosity with advantage such as change in concentration is blunt, are with a wide range of applications at aspects such as functional foodstuff, medicines.The acquisition of bioactive peptide has 3 kinds of approach, and at present the maximum of usefulness are the protease hydrolysis methods.Enzyme hydrolysis method is in gentleness or gentle relatively condition, and by selecting the kind of enzyme, the control reaction process comes the hydrolysis natural protein, obtains the given activity peptide.
In recent years, the progress of polypeptide protein is very rapid, and the immunomodulatory of polypeptide, characteristic such as anti-oxidant, hypotensive, antibiotic and antiviral have been described in many researchs.For example: immunomodulatory peptides: newborn source property immunomodulatory peptides can stimulate the mouse peritoneal macrophages to engulf sheep red blood cell (SRBC) under conditions in vitro.Intravenous injection can strengthen the ability of mouse to pneumococcal infection.Make detection architecture with mouse macrophage, visible immune-active peptides has the effect that stimulates the macrophage phagocytic ability.Equally, also can produce by suitable enzymolysis as the proteic soybean protein of human foods and rice protein and to have immunocompetent peptide, and some peptide can also suppress the growth of tumour cell except having the phagocytic activity that stimulates scavenger cell.These immune-active peptides can combine Lymphoid tissue with intestinal mucosa and interact, also can be free by the intestines wall directly and periphery lymphocyte have an effect.The bioactive peptide that derives from animal can strengthen the function of scavenger cell, increases the non-specific resistance reaction to many cause of diseases, has antitumor, antivirus action.
China is spotted deer big producing country, supports ten thousand of the about 50-60 of deer livestock on hand at present.The deer product is generally acknowledged it is the product with abundant nutrition value and medicinal function.But because limited in one's ability, thereby limited the processing and utilization of development, the especially venison of deer product to the understanding and the deep processing of deer product.Venison is the nutritious delicious food that people generally acknowledge always.For a long time, venison just as a kind of delicacies of low fat high protein, reduces its using value greatly.Because contained protein and physiologically active ingredient and general animal is different in the venison, prove after deliberation and contain profuse aminoacid component in the venison, except containing the non-essential amino acid composition, contain also that human body can not synthesize and 7 kinds of indispensable amino acids that must from food, obtain.In addition hydrolysis of protein in the venison, and obtain segmental polypeptide of all size and aminoacid component, then can improve added value of product greatly, satisfy the needs in market.Contained physiologically active peptide has effects such as the immunizing power of raising, hypoxia tolerance, antifatigue in the what is more important venison range of hydrolysed peptides.
Summary of the invention
The purpose of this invention is to provide the proteic method of a kind of conjugated protein enzymatic hydrolysis venison, thereby prepare the biological activity deer peptide that has the enhance immunity function, has raising body fatigue resistance function and anoxia tolerance function, this activity deer peptide can be widely used in preparation various protective foodss, makeup and medicine.
Conjugated protein enzymatic process of the present invention comprises the steps:
(1): raw materials pretreatment
1. starting material: the starting material that the present invention uses are that healthy spotted deer is through slaughtering the fresh or refrigerated venison that obtains.
2. pre-treatment: the refrigerated venison is thawed in cold water or directly use fresh venison, reject bone, lymph and manadesma and fat, be twisted into meat gruel with mincer, the deionized water (protein is about 11-13%) that adds venison weight 1/3rd, handled 15-20 minute in 120-122 ℃, be twisted into the meat slurry with colloidal mill then, the meat slurry is by 80 mesh standard sieves.
3. various proteolytic enzyme are standby with 8-12 times of frozen water dissolving respectively.The detail file of the proteolytic enzyme that uses see the following form:
| Title | The source | Usage quantity |
| 1398 neutral proteinase (Neutral proteinase) | Fangshan zymin head factory | 600-1000(u/gPr) |
| Compound protease (Flavourzyme 500MG) | Letter Bioprocessors Corp. of Novi | 25-30(LAPU/gPr) |
| Papoid (Papain) | Nanning Pang Bo biotechnology company limited | 800-1200(u/gPr) |
| Trypsin Trysin) | Jiangmen Biotechnology Development Centre, Guangdong Prov. | 1000-1500(u/gPr) |
4. prepare standard N aOH solution (2M).
(2): enzymolysis
1, the meat slurry by 80 mesh standard sieves adds in the isothermal reaction jar, is heated to 48-52 ℃, regulates the pH value to 6.8-7.2 with standard NaOH solution;
2, (rotating speed 100-130rpm/min) adds different types of proteolytic enzyme (neutral protease, papoid or trypsinase respectively in stirring, add different enzymes and can obtain having the deer peptide product of different physiologically actives), with standard NaOH solution control reaction process, make protein degree between 28～33%, add flavor protease again, continue to make protein degree between 34～42% with standard NaOH solution control reaction process;
3, the temperature of rising enzymolysis solution was kept 10-15 minute to 114-116 ℃, rapidly temperature was reduced to room temperature.
Using pH-Stat method control protein degree in the enzymic hydrolysis process, in the proteolysis process, is initial pH value with the NaOH solution control hydrolysis liquid pH value of demarcating concentration promptly, converses proteinic degree of hydrolysis in the solution by following formula.
DH＝(V*N)/(1.36*M)
Wherein:
DH-venison degree of hydrolysis;
The volume (L) of the standard NaOH solution that V--adds;
The volumetric molar concentration (mol/L) of the standard NaOH solution that N--adds;
The quality of fresh venison (kg) in the M--reaction system.
(3): solid-liquid separation
Use centrifugal or filtering method to remove residue, collect supernatant liquor, measure soluble solid content (Abbe refractometer or hand-held saccharometer).Test-results shows, uses filtering method can remove insoluble substance to a greater extent.
(4): concentrate
Mode concentrated supernatant with concentrating under reduced pressure makes soluble solid content reach 24-26%.
Use the content of Abbe refractometer or hand-held saccharometer monitoring soluble solid.Test-results shows, can produce a small amount of flocks (flocks is that soluble solid self flocculation produces) after concentrating, and this precipitation can not influence the physiologically active of deer peptide.In addition, can adopt filtration or centrifugation method that precipitation is disposed.If adopt filtering method, must add the diatomite of 2-4% in the filtrate; If the use centrifugation method, then centrifugal force will reach more than the 8000g, and centrifugation time is 20 minutes.
(5): drying
The deer peptide that is applied to protective foods can adopt the method for spraying drying, lyophilize or microwave drying to carry out drying, resulting deer peptide product is faint yellow to xanchromatic powder or particle (drying means difference, the outward appearance of product can be different), the moisture absorption very easily.Said spray drying process is to add a certain amount of Zulkovsky starch in the enzymolysis concentrated solution, carries out spraying drying after the stdn; Said lyophilize is that the enzymolysis concentrated solution directly carries out drying in freeze drying equipment; Said method for microwave drying is that the enzymolysis concentrated solution directly carries out drying in microwave dryer.
(6): detect
The present invention adopts micro-Kjeldahl determination testing product protein content
(7): deer peptide physiologically active detects:
This experimental observation the influence of venison hydrolyzate to mouse immune adjusting, antifatigue, hypoxia tolerance physiological potency.The result shows, this product is after taking 15 days continuously, the thymus index of mouse, the phagocytic index of mononuclear macrophage all there are tangible influence, prolong hypoxia endurance time, swimming time, reduction swimming back and the blood lactic acid value of mouse, can strengthen hypoxia tolerance and the anti-fatigue ability of mouse.Disclosed the effect that deer peptide product that the combinative enzyme hydrolysis venison obtains has certain immunoregulation effect to mouse and strengthens antifatigue and hypoxia-bearing capability.
Test materials:
1, tried thing: the lyophilize powder of the conjugated protein protease hydrolysate of Cervus nippon meat (being respectively A, B, three kinds of conjugated protein protease hydrolysates of C) is provided by this laboratory.
2, animal: Kunming mouse body weight 18-20g, male and female half and half.Changchun Biological Products Institute provides.
3, instrument and medicine: analytical balance (100,000/), Cary50 ultraviolet spectrophotometer, 250mL port grinding bottle, treadmill (diameter 30cm, dark 40cm), thermometer, stopwatch.
Test method:
The mouse of each test group is divided into 4 groups at random, every group quantity identical (10 or 20), and blank group gives distilled water, and high low dose group according to dosage gives the venison hydrolyzate, and positive control gives corresponding Zadaxin or Radix Panacis Quinquefolii saponin.Each treated animal (Zadaxin is pressed 0.2mL/20g body weight tail vein injection) except that Zadaxin is pressed the 0.5mL/20g body weight and is irritated stomach, and once a day, continuous 15 days, last was given and tried to begin test behind the 30min behind the thing.
1, the mensuration animal of thymus index and spleen index gives sample after 15 days continuously, and every mouse is weighed, and the cervical vertebra dislocation is put to death, and gets thymus gland, spleen is weighed, and calculates thymus index and spleen index (the milligram number of the thymus gland of every 10g mouse body weight or spleen) respectively.
2, the carbon clearance of mononuclear macrophage experiment successive administration is 15 days, 30min after the last administration, tail vein injection China prepared Chinese ink 5mL/kg body weight.Injection back 2min and 15min socket of the eye venous blood collection 20 μ L are dissolved in 2mL, 1g/L Na
2CO
3In the solution, measure OD value at 721 type spectrophotometer 650nm wavelength places, and cut open get Mouse Liver, spleen is weighed, and calculates phagocytic rate K (K=injects the pitch time of the logarithmic difference of the OD value of twice measurement behind the prepared Chinese ink/twice) and phagocytic index α
3, mouse normal pressure hypoxia tolerance experiment successive administration is 15 days, and last is given and tried 30min behind the thing, and mouse is placed the 250mL port grinding bottle, seals bottleneck with Vaseline, and the record mouse is from going into the bottle beginning to the dead time, as the hypoxia endurance time (min) of mouse.
4, mouse swimming with a load attached to the body experiment successive administration is 15 days, last is given and to be tried 30min behind the thing, place the swimming case to swim mouse, the depth of water is no less than 30cm, 25 ℃ ± 0.5 ℃ of water temperature, the bear a heavy burden sheet lead of 4% body weight of mouse root afterbody, record mouse from the swimming beginning to the dead time, as the swimming time (min) of mouse.
5, after blood lactic acid content mensuration last was tried thing 30min before and after the mouse swimming, respectively at before the swimming and behind swimming (bearing a heavy burden 2% in 25-30 ℃ of 60min) the rest 15min, a rear vein beard was got blood, adopts sulfuric acid colorimetric method for determining blood lactic acid content then.
Test-results:
Table 1, venison hydrolyzate A are to the influence of thymus index and spleen index
The dosage number of animals
Group thymus index spleen index
(g/kg.d) (only)
Blank---20 0.0188 ± 0.0116 0.0435 ± 0.0117
High dose group 10 20 0.0257 ± 0.0115
*0.0472 ± 0.0226
*
Low dose group 1 20 0.0237 ± 0.0151
*0.0361 ± 0.0179
*
Zadaxin group 0.005 20 0.0314 ± 0.0191
*0.0478 ± 0.0212
*
*P＜0.05，
**P＞0.05
By can showing in the table 1 that the thymus index of venison hydrolyzate A to mouse has tangible influence, and to the not significantly influence of spleen index of mouse.Illustrate that the venison hydrolyzate has the effect of the growth that promotes immune organ thymus gland, and to the not influence of spleen organ.The immunoregulation effect that shows the venison hydrolyzate may realize by the T cell, and irrelevant with the B cell.
The carbon clearance experiment of table 2, the venison hydrolyzate A mouse monokaryon scavenger cell of feeding
The dosage number of animals
Group phagocytic rate K phagocytic index α
(g/kg.d) (only)
Blank---20 0.0036 ± 0.0028 2.7908 ± 1.2152
High dose group 10 20 0.0181 ± 0.0187 4.2513 ± 1.2205
*
Low dose group 1 20 0.0158 ± 0.0133 4.8839 ± 1.8901
*
Zadaxin group 0.005 20 0.0090 ± 0.0037 3.7198 ± 0.7721
*
*P＜0.05
In the table 2, the high dose group of the venison hydrolyzate A that feeds and low dose group are organized with blank the phagocytic index of carbon granules the mononuclear macrophage of mouse evident difference.
The mouse normal pressure hypoxia tolerance experiment of table 3, the venison hydrolyzate B that feeds
Dosage number of animals P value is (with blank
The group survival time (min)
(g/kg.d) (only) compares)
Blank---10 29.3077 ± 4.9562
High dose group 2.5 10 41.8889 ± 12.0566 0.0437
Low dose group 0.5 10 32.2000 ± 0.4859 0.0873
Radix Panacis Quinquefolii saponin 2.5 10 53.6364 ± 3.8542 0.0125
The data of table 3 show, the high dose group of the venison hydrolyzate B mouse of feeding and the blank group of hypoxia-bearing capability (P＜0.05) that can obviously strengthen under the mouse normal pressure, and low dose group is not effect then.Therefore should take high relatively dosage at enhancing hypoxia tolerance vigor.
The swimming with a load attached to the body experiment of table 4, the venison hydrolyzate C mouse of feeding
Dosage number of animals P value is (with the blank ratio
Group swimming time (min)
(g/kg.d) (only))
Blank---10 6.75 ± 4.03
High dose group 2.5 10 11.50 ± 5.68 0.021
Low dose group 0.5 10 9.80 ± 9.16 0.050
Radix Panacis Quinquefolii saponin 2.5 10 16.90 ± 2.85 0.010
Table 4 data show that the high dose group of the venison hydrolyzate C that feeds and low dose group can make the swimming time of mouse obviously prolong.And have relation is necessarily arranged with the dosage that gives of venison hydrolyzate.
Blood lactic acid content measurement result before and after table 5, the venison hydrolyzate C mouse of the feeding swimming
Blood lactic acid difference before and after the dosage swimming
Group number of animals (only)
(g/kg.d)????????????????????(mmol/L)
Blank---20 0.8496 ± 0.3722
High dose group 2.5 20 0.2876 ± 0.1732
*
Low dose group 0.5 20 0.2756 ± 0.1844
*
Radix Panacis Quinquefolii saponin 2.5 20 0.2817 ± 0.1915
*
*P＜0.01 shows the venison hydrolyzate C that feeds, and can obviously reduce the production rate of blood lactic acid behind the mouse swimming exercise.
Above-mentioned experimental result shows, mouse is taken 15 days continuously under doses after, the thymus index of mouse, the phagocytic index of mononuclear macrophage are all had tangible influence, and hypoxia endurance time and swimming time under the normal pressure of prolongation mouse reduce the blood lactic acid value after mouse is swum.Point out three kinds of venison hydrolyzate A, B, C, mouse is had the effect of certain immunoregulation effect and enhancing antifatigue and hypoxia-bearing capability.
It is protein raw material that the present invention adopts the venison of spotted deer, produces the deer peptide of biologically active, and its advantage is the source that has not only enlarged biological activity deer peptide, and has improved the value of venison.
It is catalyzer that the present invention adopts compound protease, action condition gentleness not only, and rate of recovery height, and utilize the selective action of different proteolytic enzyme to prlmary structure of protein hydrolysis site, obtain having the deer peptide of different physiologically actives by the different proportionings of proteolytic enzyme.
The present invention adopts pH-Stat method control protein degree, and its advantage is to control proteinic degree of hydrolysis easily, avoids the influence of factors such as temperature, materials variance, stir speed (S.S.) to hydrolytic process, is convenient to industrial application.
Description of drawings
The invention provides three accompanying drawings
Fig. 1 is the process flow sheet of example venison hydrolyzate A of the present invention
Fig. 2 is the process flow sheet of example venison hydrolyzate B of the present invention
Fig. 3 is the process flow sheet of example venison hydrolyzate C of the present invention
Embodiment
Example 1: technical process is with reference to accompanying drawing 1
80 kilograms of inputs of pretreated venison slurry are gone in the retort, are heated with stirring to 50 ℃, regulate pH value to 7.0.(rotating speed 120rpm/min) adds frozen water dissolved neutral protease earlier in stirring, with standard NaOH solution control reaction process, make protein degree reach 28%, add frozen water dissolved food flavor enzyme then and proceed hydrolysis reaction, make proteinic degree of hydrolysis reach 38%, the temperature to 115 of enzymolysis solution ℃ was kept 15 minutes, rapidly temperature was reduced to room temperature.Concentrating under reduced pressure is to solid content 25%, lyophilize then.Promptly obtain having about 8 kilograms of the deer peptides (protein recovery is about 70%) that improve the immunizing power physiological function.
Example 2: technical process is with reference to accompanying drawing 2
80 kilograms of inputs of pretreated venison slurry are gone in the retort, are heated with stirring to 50 ℃, regulate pH value to 7.0.(rotating speed 120rpm/min) adds frozen water dissolved trypsinase earlier in stirring, with standard NaOH solution control reaction process, make protein degree reach 33%, add frozen water dissolved food flavor enzyme then and proceed hydrolysis reaction, make proteinic degree of hydrolysis reach 41%, the temperature to 115 of enzymolysis solution ℃ was kept 15 minutes, rapidly temperature was reduced to room temperature.Concentrating under reduced pressure is to solid content 25%, lyophilize then.Promptly obtain having about 8.5 kilograms of the deer peptides (protein recovery is about 72%) of hypoxia tolerance.
Example 3: technical process is with reference to accompanying drawing 3
80 kilograms of inputs of pretreated venison slurry are gone in the retort, are heated with stirring to 50 ℃, regulate pH value to 7.0 ± 0.1.(rotating speed 120rpm/min) adds frozen water dissolved papoid earlier in stirring, with standard NaOH solution control reaction process, make protein degree reach 31%, add frozen water dissolved food flavor enzyme then and proceed hydrolysis reaction, make proteinic degree of hydrolysis reach 42%, the temperature to 115 of enzymolysis solution ℃ was kept 15 minutes, rapidly temperature was reduced to room temperature.Concentrating under reduced pressure is to solid content 25%, lyophilize then.Promptly obtain having about 8 kilograms of the deer peptides (protein recovery is about 70%) of antifatigue physiological function.
The process characteristic of example 1,2,3 is:
1. adopt different proteolytic enzyme with a graded hydrolysis Cervus nippon meat respectively, utilized the recognition reaction of different proteolytic enzyme to prlmary structure of protein, hydrolysis produces the polypeptide fragments with specific physiologically active.
2. with pH-Stat method control protein degree, can control proteinic degree of hydrolysis easily, avoid of the influence of factors such as temperature, materials variance, stir speed (S.S.) hydrolytic process.
3. the active deer peptide of gained can be widely used in preparing industry fields such as medicine with enhance immunity power, hypoxia-bearing capability, antifatigue physiological function, healthcare products, food.
Claims (7)
1, a kind of physiologically active deer peptide of compound protease catalytic preparation is to be protein raw material with the venison,, comprises raw materials pretreatment, enzymolysis, concentrates, unit operations such as drying, preparation as lytic enzyme with proteolytic enzyme, the steps include:
(1) the refrigerated venison is thawed in cold water or directly use fresh venison, reject bone, lymph and manadesma and fat, be twisted into meat gruel with mincer, the deionized water that adds venison weight 1/3rd, handled 15-20 minute in 120-122 ℃, be twisted into the meat slurry with colloidal mill then, the meat slurry is by 80 mesh standard sieves;
(2) the meat slurry is put into the isothermal reaction jar, be heated to 48-52 ℃, regulate the pH value to 6.8-7.2 with the 2M NaOH solution of standard, the neutral protease that under the stirring velocity of rotating speed 100-130rpm/min, adds 600-1000u/gPr, the papoid of 800-1200u/gPr or the trypsinase of 1000-1500u/gPr, 2M NaOH solution control reaction process with standard, make protein degree between 28～33%, the flavor protease that adds 25-30LAPU/gPr again, continue 2M NaOH solution control reaction process, make protein degree between 34～42% with standard; The temperature of enzymolysis solution raise again to 114-116 ℃, kept 10-15 minute, rapidly temperature is reduced to room temperature;
(3) enzymolysis solution through solid-liquid separation, concentrate after making soluble solid content reach 24-26% and drying faint yellowly to xanchromatic powder or particle deer peptide product.
2, the physiologically active deer peptide of compound protease catalytic preparation as claimed in claim 1 is characterized in that: can adopt centrifugal or filtering method to remove residue, collect supernatant liquor, realize solid-liquid separation.
3, the physiologically active deer peptide of compound protease catalytic preparation as claimed in claim 1, it is characterized in that: with the mode concentrated supernatant of concentrating under reduced pressure, make soluble solid content reach 24-26%, can adopt filtration or centrifugation method that precipitation is disposed to a small amount of flocks that concentrates the back generation, must add the diatomite of 2-4% during filtration in the filtrate; When centrifugal then centrifugal force to reach more than the 8000g, centrifugation time is 20 minutes.
4, the physiologically active deer peptide of compound protease catalytic preparation as claimed in claim 1 is characterized in that: can adopt the method for spraying drying, lyophilize or microwave drying to carry out drying.
5, any one described physiologically active deer peptide of claim 1-4 is in the application that is used for aspect the enhance immunity power.
6, any one described physiologically active deer peptide of claim 1-4 is in the application that is used for aspect the enhancing body anti-fatigue ability.
7, any one described physiologically active deer peptide of claim 1-4 is in the application that is used to improve aspect the body's hypoxia tolerance.
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Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102669669A (en) * | 2012-05-30 | 2012-09-19 | 吉林大学 | Deer spleen extract preparation and preparation method thereof |
| CN102919863A (en) * | 2012-10-31 | 2013-02-13 | 吉林大学 | Sika deer liver/heart powder or particle and preparation method and application thereof |
| CN103805418A (en) * | 2013-10-28 | 2014-05-21 | 山东常生源食品科技有限公司 | Sea cucumber wine |
| CN104324357A (en) * | 2014-11-05 | 2015-02-04 | 吉林大学 | Application of sika deer spleen extract in anti-fatigue medicaments |
| CN105982078A (en) * | 2015-02-09 | 2016-10-05 | 田德军 | Deep processing method of deer meat |
| CN110812310A (en) * | 2019-11-14 | 2020-02-21 | 融致丰生制药有限公司 | Deer fetus extract and composition for preventing alopecia, nourishing and growing hair, and preparation method and application thereof |
| CN110897160A (en) * | 2019-12-18 | 2020-03-24 | 广东凤凰高科生物科技有限公司 | Cordyceps militaris tortoise deer protein peptide oral liquid and preparation method thereof |
| CN111812333A (en) * | 2020-06-29 | 2020-10-23 | 吉林省东北亚生物科技有限公司 | Method for comparing activity of ligamentum cervi natural peptide and enzymatic hydrolysis peptide on resisting rheumatoid arthritis |
-
2003
- 2003-12-19 CN CNA2003101159642A patent/CN1552892A/en active Pending
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102669669A (en) * | 2012-05-30 | 2012-09-19 | 吉林大学 | Deer spleen extract preparation and preparation method thereof |
| CN102669669B (en) * | 2012-05-30 | 2013-09-18 | 吉林大学 | Deer spleen extract preparation and preparation method thereof |
| CN102919863A (en) * | 2012-10-31 | 2013-02-13 | 吉林大学 | Sika deer liver/heart powder or particle and preparation method and application thereof |
| CN102919863B (en) * | 2012-10-31 | 2013-12-04 | 吉林大学 | Sika deer liver/heart powder or particle and preparation method and application thereof |
| CN103805418A (en) * | 2013-10-28 | 2014-05-21 | 山东常生源食品科技有限公司 | Sea cucumber wine |
| CN104324357A (en) * | 2014-11-05 | 2015-02-04 | 吉林大学 | Application of sika deer spleen extract in anti-fatigue medicaments |
| CN104324357B (en) * | 2014-11-05 | 2016-05-18 | 吉林大学 | The application of sika deer deer spleen extract in anti-fatigue medicament |
| CN105982078A (en) * | 2015-02-09 | 2016-10-05 | 田德军 | Deep processing method of deer meat |
| CN110812310A (en) * | 2019-11-14 | 2020-02-21 | 融致丰生制药有限公司 | Deer fetus extract and composition for preventing alopecia, nourishing and growing hair, and preparation method and application thereof |
| CN110897160A (en) * | 2019-12-18 | 2020-03-24 | 广东凤凰高科生物科技有限公司 | Cordyceps militaris tortoise deer protein peptide oral liquid and preparation method thereof |
| CN111812333A (en) * | 2020-06-29 | 2020-10-23 | 吉林省东北亚生物科技有限公司 | Method for comparing activity of ligamentum cervi natural peptide and enzymatic hydrolysis peptide on resisting rheumatoid arthritis |
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