CN107821726A - The purposes of grass carp anti-fatigue active peptide - Google Patents
The purposes of grass carp anti-fatigue active peptide Download PDFInfo
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- CN107821726A CN107821726A CN201711007753.5A CN201711007753A CN107821726A CN 107821726 A CN107821726 A CN 107821726A CN 201711007753 A CN201711007753 A CN 201711007753A CN 107821726 A CN107821726 A CN 107821726A
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- grass carp
- active peptide
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- enzymolysis
- fatigue active
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 76
- 241000252230 Ctenopharyngodon idella Species 0.000 title claims abstract description 55
- 230000002929 anti-fatigue Effects 0.000 title claims abstract description 40
- 238000004332 deodorization Methods 0.000 claims abstract description 20
- 238000001728 nano-filtration Methods 0.000 claims abstract description 16
- 238000001556 precipitation Methods 0.000 claims abstract description 11
- 238000000746 purification Methods 0.000 claims abstract description 11
- 230000036541 health Effects 0.000 claims abstract description 9
- 239000002537 cosmetic Substances 0.000 claims abstract description 8
- 239000003814 drug Substances 0.000 claims abstract description 8
- 235000013305 food Nutrition 0.000 claims abstract description 8
- 238000002360 preparation method Methods 0.000 claims abstract description 7
- 238000005227 gel permeation chromatography Methods 0.000 claims abstract description 6
- 239000007791 liquid phase Substances 0.000 claims abstract description 6
- 239000002253 acid Substances 0.000 claims abstract 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 53
- 239000012153 distilled water Substances 0.000 claims description 30
- 108090000145 Bacillolysin Proteins 0.000 claims description 24
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 claims description 21
- 230000000975 bioactive effect Effects 0.000 claims description 20
- 241000251468 Actinopterygii Species 0.000 claims description 15
- 102000004190 Enzymes Human genes 0.000 claims description 15
- 108090000790 Enzymes Proteins 0.000 claims description 15
- 239000007788 liquid Substances 0.000 claims description 12
- GVJHHUAWPYXKBD-UHFFFAOYSA-N (±)-α-Tocopherol Chemical compound OC1=C(C)C(C)=C2OC(CCCC(C)CCCC(C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-UHFFFAOYSA-N 0.000 claims description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 10
- 239000012141 concentrate Substances 0.000 claims description 10
- 230000009849 deactivation Effects 0.000 claims description 10
- 239000000706 filtrate Substances 0.000 claims description 10
- 230000007062 hydrolysis Effects 0.000 claims description 10
- 238000006460 hydrolysis reaction Methods 0.000 claims description 10
- 238000011068 loading method Methods 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 7
- 239000000047 product Substances 0.000 claims description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- 102000004169 proteins and genes Human genes 0.000 claims description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 6
- 244000063299 Bacillus subtilis Species 0.000 claims description 5
- 235000004347 Perilla Nutrition 0.000 claims description 5
- 229920005654 Sephadex Polymers 0.000 claims description 5
- 239000012507 Sephadex™ Substances 0.000 claims description 5
- 206010042674 Swelling Diseases 0.000 claims description 5
- 102000004142 Trypsin Human genes 0.000 claims description 5
- 108090000631 Trypsin Proteins 0.000 claims description 5
- 229930003427 Vitamin E Natural products 0.000 claims description 5
- 238000002835 absorbance Methods 0.000 claims description 5
- 235000015165 citric acid Nutrition 0.000 claims description 5
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid group Chemical class C(CC(O)(C(=O)O)CC(=O)O)(=O)O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 5
- 238000001514 detection method Methods 0.000 claims description 5
- 230000029087 digestion Effects 0.000 claims description 5
- 238000007865 diluting Methods 0.000 claims description 5
- 239000003480 eluent Substances 0.000 claims description 5
- WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 claims description 5
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 5
- 239000012071 phase Substances 0.000 claims description 5
- 239000002244 precipitate Substances 0.000 claims description 5
- 238000000926 separation method Methods 0.000 claims description 5
- 230000008961 swelling Effects 0.000 claims description 5
- 239000012588 trypsin Substances 0.000 claims description 5
- 235000019165 vitamin E Nutrition 0.000 claims description 5
- 229940046009 vitamin E Drugs 0.000 claims description 5
- 239000011709 vitamin E Substances 0.000 claims description 5
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 claims description 4
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 3
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 claims description 3
- 239000011780 sodium chloride Substances 0.000 claims description 3
- 230000007935 neutral effect Effects 0.000 claims description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims 2
- 244000124853 Perilla frutescens Species 0.000 claims 1
- 229910021529 ammonia Inorganic materials 0.000 claims 1
- 230000005611 electricity Effects 0.000 claims 1
- 238000000034 method Methods 0.000 claims 1
- 238000010025 steaming Methods 0.000 claims 1
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 abstract description 12
- 210000003743 erythrocyte Anatomy 0.000 abstract description 10
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 abstract description 8
- 229910052760 oxygen Inorganic materials 0.000 abstract description 8
- 239000001301 oxygen Substances 0.000 abstract description 8
- -1 ketone acids Chemical class 0.000 abstract description 7
- 230000004060 metabolic process Effects 0.000 abstract description 7
- 210000000056 organ Anatomy 0.000 abstract description 7
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 abstract description 6
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 abstract description 6
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 abstract description 6
- 235000004279 alanine Nutrition 0.000 abstract description 6
- 235000013922 glutamic acid Nutrition 0.000 abstract description 6
- 239000004220 glutamic acid Substances 0.000 abstract description 6
- 238000007833 oxidative deamination reaction Methods 0.000 abstract description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 abstract description 6
- 229940107700 pyruvic acid Drugs 0.000 abstract description 6
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- 230000006641 stabilisation Effects 0.000 abstract description 4
- 238000011105 stabilization Methods 0.000 abstract description 4
- 238000007654 immersion Methods 0.000 abstract 1
- GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical group CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 12
- 239000000243 solution Substances 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 8
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- 230000000694 effects Effects 0.000 description 7
- 230000009182 swimming Effects 0.000 description 7
- 102000035195 Peptidases Human genes 0.000 description 6
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- 239000004365 Protease Substances 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 235000019419 proteases Nutrition 0.000 description 6
- 244000025254 Cannabis sativa Species 0.000 description 5
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- 229910052708 sodium Inorganic materials 0.000 description 4
- 239000011734 sodium Substances 0.000 description 4
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
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- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
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- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 240000000560 Citrus x paradisi Species 0.000 description 1
- MQQLYEHXSBJTRK-FXQIFTODSA-N Cys-Val-Cys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](CS)N MQQLYEHXSBJTRK-FXQIFTODSA-N 0.000 description 1
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- SFTZWNJFZYOLBD-ZDLURKLDSA-N Ser-Gly-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H](N)CO SFTZWNJFZYOLBD-ZDLURKLDSA-N 0.000 description 1
- YDWLCDQXLCILCZ-BWAGICSOSA-N Thr-His-Tyr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O YDWLCDQXLCILCZ-BWAGICSOSA-N 0.000 description 1
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- BVKZGUZCCUSVTD-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O BVKZGUZCCUSVTD-UHFFFAOYSA-N 0.000 description 1
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Classifications
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/04—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from fish or other sea animals
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
- A61K38/012—Hydrolysed proteins; Derivatives thereof from animals
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/10—General cosmetic use
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Abstract
The invention provides a kind of purposes of grass carp anti-fatigue active peptide, for the purposes in health products, food, cosmetics or medicine.The preparation method of grass carp anti-fatigue active peptide, including immersion deodorization, stepwise discretization, isoelectric precipitation, nanofiltration, gel chromatography and high-efficient liquid phase chromatogram purification.The grass carp anti-fatigue active peptide being prepared can promote red blood cell to restore, improve red blood cell oxygen carrying capacity, and the oxidative deamination in musculature, on the one hand corresponding α ketone acids are generated into tricarboxylic acid cycle oxidation energy supply, on the other hand the amino taken off is coupled with pyruvic acid or glutamic acid, form alanine and amide glutaminate, there is provided energy.Contribute to the stabilization of interior environment, adjust the function of organ comprehensively, and be smoothed out metabolic process, be advantageous to the raising of body ability to work.
Description
Technical field
The invention belongs to biological technical field, specifically a kind of purposes of grass carp anti-fatigue active peptide.
Background technology
Modern nutriology research finds that peptide has the spies such as specific ionization Amino Acid Absorption is fast, absorptivity is good, biological value is high
Point, it is the active material with different physiological roles.Wherein, antifatigue peptide, which has, significantly improves human body ability to work, strengthens flesh
Meat content and strength, the locomitivity of body, and quick dispelling fatigue are maintained or improve, it is rapid to recover and strengthen the work(such as muscle power
Effect, helps to maintain health under movement environment.Therefore, antifatigue peptide, which turns into, is engaged in physical, mental, sports et al.
A kind of important functional food ingredient of group.
The content of the invention
It is an object of the invention to provide a kind of grass carp for the purposes being used in health products, food, cosmetics or medicine to resist
Anti-fatigue activity peptide.Above-mentioned grass carp anti-fatigue active peptide contributes to the stabilization of interior environment, adjusts the function of organ comprehensively, and makes metabolism
Process is smoothed out, and is advantageous to the raising of body ability to work, and its preparation method is simple, cost is cheap, with short production cycle.
The present invention is directed to the problem of being mentioned in background technology, and the technical scheme taken is：The use of grass carp anti-fatigue active peptide
On the way, for the purposes in health products, food, cosmetics or medicine.
The preparation method of grass carp anti-fatigue active peptide, comprises the following steps：
1）Soak deodorization：The grass carp flesh of fish is cleaned with clear water, 1 ~ 4h in deodorization liquid is soaked in, drains；
2）Stepwise discretization：Add distilled water in the grass carp flesh of fish to be homogenized, the mass volume ratio of the grass carp flesh of fish and distilled water is 1g：5~
15ml。
Homogenate is placed in 25 ~ 40 DEG C of isoperibol, adds trypsin digestion, enzymolysis terminates rear enzyme deactivation, adds
Bacillus subtilis neutral protease and bioactive peptide enzymolysis, enzymolysis terminate rear enzyme deactivation, filter to take filtrate；
3）Isoelectric precipitation：It is 5.5 ~ 6.5 to adjust filtrate pH, and centrifuging and taking precipitates after standing；
4）Nanofiltration：In precipitation plus it is placed in after distilled water dissolving in distilled water and concentrates 24 ~ 36h of nanofiltration；
5）Gel chromatography：Post will be filled after Sephadex G-15 gel swellings with distilled water, checks loading after post uniformity, with certainly
Dynamic sampler collects eluent, surveys ultraviolet absorptivity under 280nm, does curve；Loading is repeated, is collected and divided according to absorbance curve
From solution；Load solution is that 10 ~ 20 times of nanofiltration concentrate distilled water diluting obtains；
6）High-efficient liquid phase chromatogram purification：High performance liquid chromatography separation purification condition is：Chromatographic column：1.7 μm of BEH C18 chromatograms
Post；Mobile phase：0 ~ 5min, water；5 ~ 16min, 60 ~ 70% water, 30 ~ 40% acetonitriles；16 ~ 30min, 40 ~ 60% water, 40 ~ 60% acetonitriles；
30 ~ 40min, acetonitrile；Flow velocity：0.7 ~ 1.3ml/min, 25 ~ 35 DEG C of column temperature, Detection wavelength are 254 nm and 280 nm, collect master
Chromatographic peak is wanted, it is lyophilized to obtain grass carp anti-fatigue active peptide.Above-mentioned grass carp anti-fatigue active peptide can promote red blood cell to restore, and improve red
Cell oxygen carrying capacity, and the oxidative deamination in musculature, on the one hand generate corresponding 2-ketoacid and enter tricarboxylic acid cycle oxygen
Change energy supply, the amino on the other hand taken off is coupled with pyruvic acid or glutamic acid, forms alanine and amide glutaminate, there is provided energy
Amount.Contribute to the stabilization of interior environment, adjust the function of organ comprehensively, and be smoothed out metabolic process, be advantageous to body work
The raising of ability.
Deodorization liquid composition and its parts by weight are：5 ~ 10 parts of citric acids, 10 ~ 18 parts of extractive of perilla, 0.1 ~ 0.3 part of chlorination
Sodium, 0.5 ~ 0.8 part of sodium acid carbonate, 20 ~ 30 parts of ethanol and 0.2 ~ 0.4 part of vitamin E.Fishy smell material property composition with grass carp
It is trimethylamine, above-mentioned deodorization liquid can react to form quaternary ammonium salt with trimethylamine, and can dissolving trimethylamine, and deodorization effect ten is clearly demarcated
It is aobvious.
The addition of trypsase be homogenate quality 0.2 ~ 0.7%, enzymolysis pH be 7.5 ~ 9.0, hydrolysis temperature be 25 ~
40 DEG C, enzymolysis time is 2 ~ 4h.The addition of Bacillus subtilis neutral protease is the 0.1 ~ 0.5% of homogenate quality, active
The addition of small peptide be Bacillus subtilis neutral protease quality 1 ~ 5%, enzymolysis pH be 7.0 ~ 7.8, hydrolysis temperature be 35 ~
50 DEG C, enzymolysis time is 10 ~ 30min.Using trypsase and Bacillus subtilis neutral protease stepwise discretization, by homogenate
In big grass carp fish protein enzymolysis into the less active material of molecular weight.Trypsase and Bacillus subtilis neutral protease
Enzymatic hydrolysis condition is different, causes the enzymolysis efficiency of two kinds of protease to be in higher state by the way of stepwise discretization.Active peptide
Bioactivity depend on peptide chain amino acid sequence and length and its space structure, it means that different protease hydrolytics obtain
Active peptide biological function it is different.Single protease is few to the restriction enzyme site of protein, and obtained polypeptide amount is few, more hatching eggs
The white enzyme polypeptide amount that enzymolysis protein matter obtains simultaneously is big, but is easily destroyed polypeptide active, is allowed to lose bioactivity, above-mentioned substep
Enzymolysis operation can at utmost digest to obtain grass carp anti-fatigue active peptide.
The amino acid sequence of bioactive peptide is：HSHCVCSGTTHYVLHCVNCSR.Above-mentioned bioactive peptide is to bacillus subtilis
Bacterium neutral proteinase has activation, i.e., under bioactive peptide existence condition, the enzymolysis effect of Bacillus subtilis neutral protease
Rate significantly improves, and reduces the addition of Bacillus subtilis neutral protease and shortens enzymolysis time.
Compared with prior art, the advantage of the invention is that：
1. grass carp anti-fatigue active peptide prepared by the present invention can promote red blood cell to restore, raising red blood cell oxygen carrying capacity, and
Oxidative deamination in musculature, corresponding 2-ketoacid is on the one hand generated into tricarboxylic acid cycle oxidation energy supply, is on the other hand taken off
The amino come is coupled with pyruvic acid or glutamic acid, forms alanine and amide glutaminate, there is provided energy.Contribute to the steady of interior environment
It is fixed, the function of organ is adjusted comprehensively, and metabolic process is smoothed out, be advantageous to the raising of body ability to work, for health care
Purposes in product, food, cosmetics or medicine；
2. trypsase and Bacillus subtilis neutral protease stepwise discretization are used, and Bacillus subtilis neutral albumen
The bioactive peptide that amino acid sequence is HSHCVCSGTTHYVLHCVNCSR is added when enzyme digests.Above-mentioned bioactive peptide is to withered grass bud
Spore bacillus neutral proteinase has activation, i.e., under bioactive peptide existence condition, the enzyme of Bacillus subtilis neutral protease
Solution efficiency significantly improves, and reduces the addition of Bacillus subtilis neutral protease and shortens enzymolysis time.
Embodiment
The present invention program is described further below by embodiment：
Embodiment 1：
The purposes of grass carp anti-fatigue active peptide, for the purposes in health products, food, cosmetics or medicine.
The preparation method of grass carp anti-fatigue active peptide, comprises the following steps：
1）Soak deodorization：The grass carp flesh of fish is cleaned with clear water, 1 ~ 4h in deodorization liquid is soaked in, drains；
2）Stepwise discretization：Add distilled water in the grass carp flesh of fish to be homogenized, the mass volume ratio of the grass carp flesh of fish and distilled water is 1g：5~
15ml。
Homogenate is placed in 25 ~ 40 DEG C of isoperibol, adds trypsin digestion, enzymolysis terminates rear enzyme deactivation, adds
Bacillus subtilis neutral protease and bioactive peptide enzymolysis, enzymolysis terminate rear enzyme deactivation, filter to take filtrate；
3）Isoelectric precipitation：It is 5.5 ~ 6.5 to adjust filtrate pH, and centrifuging and taking precipitates after standing；
4）Nanofiltration：In precipitation plus it is placed in after distilled water dissolving in distilled water and concentrates 24 ~ 36h of nanofiltration；
5）Gel chromatography：Post will be filled after Sephadex G-15 gel swellings with distilled water, checks loading after post uniformity, with certainly
Dynamic sampler collects eluent, surveys ultraviolet absorptivity under 280nm, does curve；Loading is repeated, is collected and divided according to absorbance curve
From solution；Load solution is that 10 ~ 20 times of nanofiltration concentrate distilled water diluting obtains；
6）High-efficient liquid phase chromatogram purification：High performance liquid chromatography separation purification condition is：Chromatographic column：1.7 μm of BEH C18 chromatograms
Post；Mobile phase：0 ~ 5min, water；5 ~ 16min, 60 ~ 70% water, 30 ~ 40% acetonitriles；16 ~ 30min, 40 ~ 60% water, 40 ~ 60% acetonitriles；
30 ~ 40min, acetonitrile；Flow velocity：0.7 ~ 1.3ml/min, 25 ~ 35 DEG C of column temperature, Detection wavelength are 254 nm and 280 nm, collect master
Chromatographic peak is wanted, it is lyophilized to obtain grass carp anti-fatigue active peptide.Above-mentioned grass carp anti-fatigue active peptide can promote red blood cell to restore, and improve red
Cell oxygen carrying capacity, and the oxidative deamination in musculature, on the one hand generate corresponding 2-ketoacid and enter tricarboxylic acid cycle oxygen
Change energy supply, the amino on the other hand taken off is coupled with pyruvic acid or glutamic acid, forms alanine and amide glutaminate, there is provided energy
Amount.Contribute to the stabilization of interior environment, adjust the function of organ comprehensively, and be smoothed out metabolic process, be advantageous to body work
The raising of ability.
Deodorization liquid composition and its parts by weight are：5 ~ 10 parts of citric acids, 10 ~ 18 parts of extractive of perilla, 0.1 ~ 0.3 part of chlorination
Sodium, 0.5 ~ 0.8 part of sodium acid carbonate, 20 ~ 30 parts of ethanol and 0.2 ~ 0.4 part of vitamin E.Fishy smell material property composition with grass carp
It is trimethylamine, above-mentioned deodorization liquid can react to form quaternary ammonium salt with trimethylamine, and can dissolving trimethylamine, and deodorization effect ten is clearly demarcated
It is aobvious.
The addition of trypsase be homogenate quality 0.2 ~ 0.7%, enzymolysis pH be 7.5 ~ 9.0, hydrolysis temperature be 25 ~
40 DEG C, enzymolysis time is 2 ~ 4h.The addition of Bacillus subtilis neutral protease is the 0.1 ~ 0.5% of homogenate quality, active
The addition of small peptide be Bacillus subtilis neutral protease quality 1 ~ 5%, enzymolysis pH be 7.0 ~ 7.8, hydrolysis temperature be 35 ~
50 DEG C, enzymolysis time is 10 ~ 30min.Using trypsase and Bacillus subtilis neutral protease stepwise discretization, by homogenate
In big grass carp fish protein enzymolysis into the less active material of molecular weight.Trypsase and Bacillus subtilis neutral protease
Enzymatic hydrolysis condition is different, causes the enzymolysis efficiency of two kinds of protease to be in higher state by the way of stepwise discretization.Active peptide
Bioactivity depend on peptide chain amino acid sequence and length and its space structure, it means that different protease hydrolytics obtain
Active peptide biological function it is different.Single protease is few to the restriction enzyme site of protein, and obtained polypeptide amount is few, more hatching eggs
The white enzyme polypeptide amount that enzymolysis protein matter obtains simultaneously is big, but is easily destroyed polypeptide active, is allowed to lose bioactivity, above-mentioned substep
Enzymolysis operation can at utmost digest to obtain grass carp anti-fatigue active peptide.
The amino acid sequence of bioactive peptide is：HSHCVCSGTTHYVLHCVNCSR.Above-mentioned bioactive peptide is to bacillus subtilis
Bacterium neutral proteinase has activation, i.e., under bioactive peptide existence condition, the enzymolysis effect of Bacillus subtilis neutral protease
Rate significantly improves, and reduces the addition of Bacillus subtilis neutral protease and shortens enzymolysis time.
Embodiment 2：
The purposes of grass carp anti-fatigue active peptide, for the purposes in health products, food, cosmetics or medicine.
The preparation method of grass carp anti-fatigue active peptide, comprises the following steps：
1）Soak deodorization：The grass carp flesh of fish is cleaned with clear water, 2h in deodorization liquid is soaked in, drains；
2）Stepwise discretization：Add distilled water in the grass carp flesh of fish to be homogenized, the mass volume ratio of the grass carp flesh of fish and distilled water is 1g：
10ml。
Homogenate is placed in 30 DEG C of isoperibol, adds trypsin digestion, enzymolysis terminates rear enzyme deactivation, adds withered grass
Subtilis neutral pro-tease and bioactive peptide enzymolysis, enzymolysis terminate rear enzyme deactivation, filter to take filtrate；
3）Isoelectric precipitation：It is 6.0 to adjust filtrate pH, and centrifuging and taking precipitates after standing；
4）Nanofiltration：In precipitation plus it is placed in after distilled water dissolving in distilled water and concentrates nanofiltration 24h；
5）Gel chromatography：Post will be filled after Sephadex G-15 gel swellings with distilled water, checks loading after post uniformity, with certainly
Dynamic sampler collects eluent, surveys ultraviolet absorptivity under 280nm, does curve；Loading is repeated, is collected and divided according to absorbance curve
From solution；Load solution is that nanofiltration concentrate is obtained again with distilled water diluting 15；
6）High-efficient liquid phase chromatogram purification：High performance liquid chromatography separation purification condition is：Chromatographic column：1.7 μm of BEH C18 chromatograms
Post；Mobile phase：0 ~ 5min, water；5 ~ 16min, 60% water, 40% acetonitrile；16 ~ 30min, 40% water, 60% acetonitrile；30 ~ 40min, second
Nitrile；Flow velocity：1.0ml/min, 30 DEG C of column temperature, Detection wavelength are 254 nm and 280 nm, collect main chromatographic peak, lyophilized to obtain grass
Fish anti-fatigue active peptide.Above-mentioned grass carp anti-fatigue active peptide can promote red blood cell to restore, raising red blood cell oxygen carrying capacity, and
Oxidative deamination in musculature, corresponding 2-ketoacid is on the one hand generated into tricarboxylic acid cycle oxidation energy supply, is on the other hand taken off
The amino come is coupled with pyruvic acid or glutamic acid, forms alanine and amide glutaminate, there is provided energy.Contribute to the steady of interior environment
It is fixed, the function of organ is adjusted comprehensively, and metabolic process is smoothed out, be advantageous to the raising of body ability to work.
Deodorization liquid composition and its parts by weight are：8 parts of citric acids, 16 parts of extractive of perilla, 0.2 part of sodium chloride, 0.4 part of carbonic acid
Hydrogen sodium, 25 parts of ethanol and 0.3 part of vitamin E.
The addition of trypsase is the 0.5% of homogenate quality, and enzymolysis pH is 8.0, and hydrolysis temperature is 30 DEG C, during enzymolysis
Between be 2h.The addition of Bacillus subtilis neutral protease is the 0.2% of homogenate quality, and the addition of bioactive peptide is withered
The 3% of careless subtilis neutral pro-tease quality, enzymolysis pH are 7.5, and hydrolysis temperature is 45 DEG C, enzymolysis time 15min.
The amino acid sequence of bioactive peptide is：HSHCVCSGTTHYVLHCVNCSR.
Embodiment 3：
The purposes of grass carp anti-fatigue active peptide, for the purposes in health products, food, cosmetics or medicine.
The preparation method of grass carp anti-fatigue active peptide, comprises the following steps：
1）Soak deodorization：The grass carp flesh of fish is cleaned with clear water, 2h in deodorization liquid is soaked in, drains；
2）Stepwise discretization：Add distilled water in the grass carp flesh of fish to be homogenized, the mass volume ratio of the grass carp flesh of fish and distilled water is 1g：
8ml。
Homogenate is placed in 30 DEG C of isoperibol, adds trypsin digestion, enzymolysis terminates rear enzyme deactivation, adds withered grass
Subtilis neutral pro-tease and bioactive peptide enzymolysis, enzymolysis terminate rear enzyme deactivation, filter to take filtrate；
3）Isoelectric precipitation：It is 6.0 to adjust filtrate pH, and centrifuging and taking precipitates after standing；
4）Nanofiltration：In precipitation plus it is placed in after distilled water dissolving in distilled water and concentrates nanofiltration 24h；
5）Gel chromatography：Post will be filled after Sephadex G-15 gel swellings with distilled water, checks loading after post uniformity, with certainly
Dynamic sampler collects eluent, surveys ultraviolet absorptivity under 280nm, does curve；Loading is repeated, is collected and divided according to absorbance curve
From solution；Load solution is that nanofiltration concentrate is obtained again with distilled water diluting 15；
6）High-efficient liquid phase chromatogram purification：High performance liquid chromatography separation purification condition is：Chromatographic column：1.7 μm of BEH C18 chromatograms
Post；Mobile phase：0 ~ 5min, water；5 ~ 16min, 60% water, 40% acetonitrile；16 ~ 30min, 40% water, 60% acetonitrile；30 ~ 40min, second
Nitrile；Flow velocity：1.0ml/min, 30 DEG C of column temperature, Detection wavelength are 254 nm and 280 nm, collect main chromatographic peak, lyophilized to obtain grass
Fish anti-fatigue active peptide.Above-mentioned grass carp anti-fatigue active peptide can promote red blood cell to restore, raising red blood cell oxygen carrying capacity, and
Oxidative deamination in musculature, corresponding 2-ketoacid is on the one hand generated into tricarboxylic acid cycle oxidation energy supply, is on the other hand taken off
The amino come is coupled with pyruvic acid or glutamic acid, forms alanine and amide glutaminate, there is provided energy.Contribute to the steady of interior environment
It is fixed, the function of organ is adjusted comprehensively, and metabolic process is smoothed out, be advantageous to the raising of body ability to work.
Deodorization liquid composition and its parts by weight are：10 parts of citric acids, 17 parts of extractive of perilla, 0.1 part of sodium chloride, 0.5 part of carbon
Sour hydrogen sodium, 25 parts of ethanol and 0.3 part of vitamin E.
The addition of trypsase is the 0.5% of homogenate quality, and enzymolysis pH is 8.0, and hydrolysis temperature is 30 DEG C, during enzymolysis
Between be 2h.The addition of Bacillus subtilis neutral protease is the 0.2% of homogenate quality, and the addition of bioactive peptide is withered
The 3% of careless subtilis neutral pro-tease quality, enzymolysis pH are 7.5, and hydrolysis temperature is 45 DEG C, enzymolysis time 15min.
The amino acid sequence of bioactive peptide is：HSHCVCSGTTHYVLHCVNCSR.
Embodiment 4：
Tested using classical mouse anti-reflecting fatigue.Before experiment, mouse is randomly divided into 4 groups, every group 8, daily gavage 1 time, with life
Reason salt solution is control group, respectively with 5,10,30mg/kg dosage for experimental group, continuous gavage 7d, and after last gavage 30min,
The galvanized wire of the body weight of mouse tail root load 5%, is placed in the depth of water（30±1cm）Water temperature（25±1℃）In swimming trunk, water is stirred frequently,
Mouse four limbs are made to keep motion；Record mouse from swimming to the dead time（min）For its swimming time.
Influence of the pomelo peel ethyl acetate layer extract of table 1 to mice burden swimming（x±s）
*p<0.05, * * p<0.01.
Fatigue refers to that its function can not be maintained at a certain specified level or can not maintain a certain predetermined exercise intensity, table by body
Energy system power output and muscle strength decline or the decline of internal organs function when now to move, and it is motility that power, which exhausts,
The special shape of fatigue.Swimming time is the important indicator of exercise tolerance when reflection is tired, is usually used in evaluation experimental animal
Exercise tolerance and improve experimental animal exercise tolerance measure effect.Experimental result shows, grass carp anti-fatigue active peptide is low, in
, high 3 kinds of concentration before being administered and physiological saline but compared with, the swimming time of mouse can be increased, wherein, high concentration can be brighter
Increase the swimming time of mouse aobviously, that is, strengthen the fatigue resistance (P of mouse<0.01).
Routine operation in the operating procedure of the present invention is well known to those skilled in the art, herein without repeating.
Technical scheme is described in detail embodiment described above, it should be understood that it is described above only
For the specific embodiment of the present invention, it is not intended to limit the invention, all any modifications made in the spirit of the present invention,
Supplement or similar fashion replacement etc., should be included in the scope of the protection.
Sequence table
<110>Pujiang County Ou Li Bioisystech Co., Ltd
<120>The purposes of grass carp anti-fatigue active peptide
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 21
<212> PRT
<213>Artificial synthesized (Mytilus coruscus)
<400> 1
His Ser His Cys Val Cys Ser Gly Thr Thr His Tyr Val Leu His Cys
1 5 10 15
Val Asn Cys Ser Arg
20
Claims (8)
1. the purposes of grass carp anti-fatigue active peptide, it is characterised in that for the purposes in health products, food, cosmetics or medicine.
2. the purposes of grass carp anti-fatigue active peptide according to claim 1, it is characterised in that：The preparation of described active peptide
Method comprises the following steps：
1）Soak deodorization：The grass carp flesh of fish is cleaned with clear water, 1 ~ 4h in deodorization liquid is soaked in, drains；
2）Stepwise discretization：Distilled water homogenate is added in the grass carp flesh of fish, homogenate is placed in 25 ~ 40 DEG C of isoperibol, added
Enter trypsin digestion, enzymolysis terminates rear enzyme deactivation, adds Bacillus subtilis neutral protease and bioactive peptide enzymolysis, enzymolysis knot
Enzyme deactivation after beam, filters to take filtrate；
3）Isoelectric precipitation：The isoelectric point that filtrate pH is target protein is adjusted, centrifuging and taking precipitates after standing；
4）Nanofiltration：In precipitation plus it is placed in after distilled water dissolving in distilled water and concentrates 24 ~ 36h of nanofiltration；
5）Gel chromatography：Post will be filled after Sephadex G-15 gel swellings with distilled water, checks loading after post uniformity, with certainly
Dynamic sampler collects eluent, surveys ultraviolet absorptivity under 280nm, does curve；Loading is repeated, is collected and divided according to absorbance curve
From solution；Load solution is that 10 ~ 20 times of nanofiltration concentrate distilled water diluting obtains；
6）High-efficient liquid phase chromatogram purification：High performance liquid chromatography separation purification condition is：Chromatographic column：1.7 μm of BEH C18 chromatograms
Post；Mobile phase：0 ~ 5min, water；5 ~ 16min, 60 ~ 70% water, 30 ~ 40% acetonitriles；16 ~ 30min, 40 ~ 60% water, 40 ~ 60% acetonitriles；
30 ~ 40min, acetonitrile；Flow velocity：0.7 ~ 1.3ml/min, 25 ~ 35 DEG C of column temperature, Detection wavelength are 254 nm and 280 nm, collect master
Chromatographic peak is wanted, it is lyophilized to obtain grass carp anti-fatigue active peptide.
3. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：Described deodorization liquid composition and
Its parts by weight is：5 ~ 10 parts of citric acids, 10 ~ 18 parts of extractive of perilla, 0.1 ~ 0.3 part of sodium chloride, 0.5 ~ 0.8 part of sodium acid carbonate,
20 ~ 30 parts of ethanol and 0.2 ~ 0.4 part of vitamin E.
4. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：The described grass carp flesh of fish is with steaming
The mass volume ratio of distilled water is 1g：5~15ml.
5. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：Described trypsase adds
Enter 0.2 ~ 0.7% that amount is homogenate quality, enzymolysis pH is 7.5 ~ 9.0, and hydrolysis temperature is 25 ~ 40 DEG C, and enzymolysis time is 2 ~ 4h.
6. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：Described bacillus subtilis
The addition of neutral proteinase is the 0.1 ~ 0.5% of homogenate quality, and the addition of bioactive peptide is Bacillus subtilis neutral egg
The 1 ~ 5% of white enzyme quality, enzymolysis pH are 7.0 ~ 7.8, and hydrolysis temperature is 35 ~ 50 DEG C, and enzymolysis time is 10 ~ 30min.
7. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：The ammonia of described bioactive peptide
Base acid sequence is：HSHCVCSGTTHYVLHCVNCSR.
8. the purposes of grass carp anti-fatigue active peptide according to claim 2, it is characterised in that：Described target protein etc.
Electricity is put：5.5~6.5.
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| CN108935912A (en) * | 2018-06-21 | 2018-12-07 | 中国农业大学 | A kind of fish protein peptide and preparation method thereof inhibited with DPP-IV with anti-fatigue effect |
| CN111374219A (en) * | 2020-05-10 | 2020-07-07 | 江西师范大学 | Preparation method of black carp fish high-oxidation-resistance anticancer peptide |
| CN113373196A (en) * | 2021-06-11 | 2021-09-10 | 福建农林大学 | Processing method of anti-fatigue peptide of anoectochilus formosanus |
| CN114158621A (en) * | 2021-12-10 | 2022-03-11 | 宁夏九宝生态农业科技发展有限公司 | Composition of wolfberry fruit oil and walnut oil and application thereof |
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| CN108935912A (en) * | 2018-06-21 | 2018-12-07 | 中国农业大学 | A kind of fish protein peptide and preparation method thereof inhibited with DPP-IV with anti-fatigue effect |
| CN108935912B (en) * | 2018-06-21 | 2021-04-23 | 中国农业大学 | Fish meat protein peptide with DPP-IV inhibition and anti-fatigue functions and preparation method thereof |
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| CN113373196A (en) * | 2021-06-11 | 2021-09-10 | 福建农林大学 | Processing method of anti-fatigue peptide of anoectochilus formosanus |
| CN113373196B (en) * | 2021-06-11 | 2023-10-31 | 福建农林大学 | Processing method of anti-fatigue peptide of anoectochilus formosanus |
| CN114158621A (en) * | 2021-12-10 | 2022-03-11 | 宁夏九宝生态农业科技发展有限公司 | Composition of wolfberry fruit oil and walnut oil and application thereof |
| CN114158621B (en) * | 2021-12-10 | 2024-03-26 | 宁夏九宝生态农业科技发展有限公司 | A composition containing oleum Lycii and oleum Juglandis and its application |
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