CN108017701A - A kind of biologically active polypeptide FPKYPVEPF and its preparation method and application - Google Patents
A kind of biologically active polypeptide FPKYPVEPF and its preparation method and application Download PDFInfo
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- CN108017701A CN108017701A CN201711125053.6A CN201711125053A CN108017701A CN 108017701 A CN108017701 A CN 108017701A CN 201711125053 A CN201711125053 A CN 201711125053A CN 108017701 A CN108017701 A CN 108017701A
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- fpkypvepf
- biologically active
- active polypeptide
- polypeptide
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4732—Casein
-
- 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
- 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
-
- 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
- A61Q19/08—Anti-ageing preparations
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Epidemiology (AREA)
- Birds (AREA)
- Gastroenterology & Hepatology (AREA)
- Dermatology (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The present invention relates to albumen field, and in particular to its amino acid sequence of a kind of biologically active polypeptide FPKYPVEPF and its preparation method and application, biologically active polypeptide FPKYPVEPF is Phe Pro Lys Tyr Pro Val Glu Pro Phe.By the experiment of ion vitro immunization function point analysis, internal Antisenility Experiment, demonstrating polypeptide FPKYPVEPF has preferable immunoloregulation function and activity of fighting against senium, on the one hand, the biologically active polypeptide FPKYPVEPF of the present invention can strengthen the in-vitro multiplication ability of lymphocyte and macrophage, the ability that body resists extraneous pathogenic infection is improved, reduces body incidence；On the other hand, the vigor of internal anti-peroxidation enzyme system can be improved, strengthen the function of body resistance external source sexual stimulus, so as to reduce organism aging process, aging and sick probability, exploitation is of great significance with immunoloregulation function, the food of anti-senescence function, health products and medicine tool.
Description
Technical field
The present invention relates to albumen field, more particularly, to a kind of biologically active polypeptide FPKYPVEPF and preparation method thereof and
Using.
Background technology
During cow's milk is through lactobacillus-fermented, a part of protein in cow's milk is metabolized by lactic acid bacteria to be utilized, concurrently
A series of biochemical reactions have been given birth to, protein is changed into polypeptide or free amino acid, is digested or passes through
The absorption and transport of intestinal epithelial cell is directly entered the blood circulation of human body.In these polypeptides, some is with special
Physiological function, is referred to as " biologically active peptide ".
It is particularly important that safe biologically active peptide is found in natural food source.In recent years, it has been found that some foods
The polypeptides matter in thing source has good bioactivity, such as corn small peptide, soybean peptide, cow's milk polypeptide.These polypeptides can
To be obtained by number of ways such as microbial fermentation, digestion enzymolysis, and biologically active polypeptide is by 2~20 mostly
Amino acid residue forms, and molecular weight is less than 6000Da, contains a certain amount of hydrophobic amino acid, aromatic amino acid.
Immune-active peptides are to obtain and prove that one kind biology of its physiological activity is living from breast first after opioid peptides discovery
Property polypeptide.Jolles in 1981 et al. has found first, using trypsin hydrolysis people lactoprotein, can obtain an amino acid sequence
The hexapeptide of Val-Glu-Pro-Ile-Pro-Tyr is classified as, experiment in vitro proves that the peptide can strengthen Turnover of Mouse Peritoneal Macrophages pair
The phagocytosis of sheep red blood cell (SRBC).Migliore-Samour et al. has found the hexapeptide Thr-Thr-Met-Pro- from casein
Leu-Trp can stimulate phagocytosis and enhancing of the sheep erythrocyte to mouse peritoneal macrophages for kerekou pneumonia primary
The resistance of bacterium.Li Su duckweeds et al. find rat peritoneal macrophages with newborn source immunomodulatory peptides (PGPIPN) the feeding rat of synthesis
Phagocytosis and the relevant immunoloregulation function of red blood cell have significant enhancing.
Research shows that immune-active peptides can not only strengthen immunity of organisms, stimulates the propagation of body lymphocyte, enhancing
The phagocytic function of macrophage, promotes the release of cell factor, improves the ability that body resists extraneous pathogenic infection, reduce machine
Body incidence, and the immunological rejection of body will not be caused.
Aging is a natural phenomena, and process is often accompanied by the change of antioxidant levels, organ-tissue, immune factor, its
The change of complexity, the trend that such as proinflammatory cytokine IL-6, IL-4, TNF-α presentation increase, IL-6 occur for middle cell factor
It is all considered to play an important role in the generating process of geriatric disease with TNF-a.With science of heredity and molecular biology
Development, the research of biological decay mechanism achieve gratifying progress.Researcher by using some model organisms, as mouse,
The term single gene mutating experiment of drosophila and C. Elegans Automatic Screening etc., it is found that some genes can dramatically increase service lifes of these organisms and reach
As many as 6 times.
Anti-aging peptide in terms of physiological function there is amino acid cannot compare excellent as a kind of emerging antidotal agent
Gesture, it can produce promotion or inhibitory action to the enzyme in organism, improve absorption and the profit to mineral matter and other nutrients
With, removing interior free yl, the resistance to oxidation of enhancing body itself, to slow down aging.Therefore, the nutrition and health care of biologically active peptide
Effect has become the emphasis of domestic and foreign scholars' subject study.Qiu Juan et al. pass through experimental studies have found that, milk-derived bioactive micro peptide
Life span of drosophila melanogaster can effectively be extended, delay its aging, and also there is preferable antioxidation, thus it is speculated that be probably wherein to be rich in coloured glaze
Base peptides.SOD vigor in serum, reduces its lipid in discovery bovine colostrum extract energy conspicuousness raising the elderly's body such as the brightness in week
Peroxide and enhancing body resistance to oxidation, have certain anti-senescence function.
The research on biologically active polypeptide has much at present, for example Chinese patent CN105254738A discloses one kind and comes
The milk-derived biologically active polypeptide DELQDKIH of beta-casein is come from, Chinese patent CN105254739A discloses one kind and derives from
The milk-derived biologically active polypeptide GTQYTD of α s1- caseins, Chinese patent CN105254740A, which are disclosed, a kind of derives from α s2-
The milk-derived biologically active polypeptide NQFYQKF of casein.
The content of the invention
It is an object of the invention to provide a kind of biologically active polypeptide FPKYPVEPF and its preparation method and application.
The purpose of the present invention can be achieved through the following technical solutions：
First aspect present invention, there is provided a kind of biologically active polypeptide FPKYPVEPF, its amino acid sequence are Phe-Pro-
Lys-Tyr-Pro-Val-Glu-Pro-Phe, such as SEQ ID NO：Shown in 1.
Preferably, the biologically active polypeptide is milk-derived.Beta-casein is derive specifically from, and is beta-casein variation
The amino acid residue that B is the 111st~119.Beta-casein variation B amino acid sequences such as SEQ ID NO：Shown in 3.
The amino acid sequence of beta-casein and corresponding nucleotides sequence are classified as existing technology, encoding ss-casein variation B
The biologically active polypeptide FPKYPVEPF of the nucleotide fragments energy encoding mature of 111st~119 amino acids residue.
Preferably, the biologically active polypeptide has immunoloregulation function and anti-senescence function.
Second aspect of the present invention, there is provided encode the nucleotide fragments of the biologically active polypeptide FPKYPVEPF, its sequence
For：5 '-ttt cct aaa tat cca gtt gag ccc ttt-3 ', such as SEQ ID NO：Shown in 2.
Third aspect present invention, there is provided the preparation method of the biologically active polypeptide FPKYPVEPF, can pass through gene
The method of engineering is artificial synthesized, can be directly obtained from dairy products by the method isolated and purified, can directly pass through chemistry
It is synthetically prepared.
Fourth aspect present invention, there is provided the biologically active polypeptide FPKYPVEPF has immunoloregulation function in preparation
Food, health products, the application in medicine or cosmetics.
Fifth aspect present invention, there is provided the biologically active polypeptide FPKYPVEPF is being prepared with anti-senescence function
Application in food, health products or medicine.
Sixth aspect present invention, there is provided the biologically active polypeptide FPKYPVEPF is being prepared while had immunological regulation
Application in the food of function and anti-senescence function, health products or medicine.
Specifically, biologically active polypeptide FPKYPVEPF of the invention, which can be used for preparing, reduces free radical to skin wound
The harmful medicine of cosmetics, preparation with immunological regulation and/or anti-aging；And due to the biologically active polypeptide of the present invention
Product after FPKYPVEPF is degraded by intestines and stomach still has bioactivity, thus can be also used for preparing the food such as Yoghourt,
Adjust the health products of immunity, and the oral medicine being used to prepare with immunological regulation and/or anti-aging.
Seventh aspect present invention, there is provided a kind of immunological regulation product, including the biologically active polypeptide FPKYPVEPF or
The derivative of the biologically active polypeptide FPKYPVEPF；The immunological regulation product includes immunological regulation food, immunological regulation
Health products, immunoregulation medicament or immunological regulation cosmetics；The derivative of the biologically active polypeptide FPKYPVEPF, refers to
On the amino acid side groups of biologically active polypeptide FPKYPVEPF, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Eighth aspect present invention, there is provided a kind of anti-aging product, including the biologically active polypeptide FPKYPVEPF or institute
State the derivative of biologically active polypeptide FPKYPVEPF；The anti-aging product include antisenility cistanche food, antisenescence health product or
Antiaging agent；The derivative of the biologically active polypeptide FPKYPVEPF, refers to the ammonia in biologically active polypeptide FPKYPVEPF
On base acid side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, ester
The modification such as change or glycosylation, obtained polypeptide derivative.
Ninth aspect present invention, there is provided product a kind of while that there is immunoloregulation function and anti-senescence function, including
The derivative of the biologically active polypeptide FPKYPVEPF or described biologically active polypeptides FPKYPVEPF；With immunoloregulation function
Include food, health products or medicine with the product of anti-senescence function；The derivative of the biologically active polypeptide FPKYPVEPF, is
Refer on the amino acid side groups of biologically active polypeptide FPKYPVEPF, aminoterminal or c-terminus carry out hydroxylating, carboxylated,
Be carbonylated, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Biologically active polypeptide FPKYPVEPF's of the present invention has the beneficial effect that：The milk-derived biologically active polypeptide of the present invention
FPKYPVEPF has preferable adjusting immunity of organisms activity and activity of fighting against senium；On the one hand, biologically active polypeptide of the invention
FPKYPVEPF can strengthen the in-vitro multiplication ability of lymphocyte and macrophage, improve body and resist extraneous pathogenic infection
Ability, reduce body incidence；On the other hand, it is possible to increase the vigor of internal anti-peroxidation enzyme system, enhancing body resistance are outer
The function of source sexual stimulus, so as to reduce organism aging process, aging and sick probability, to exploitation with immunoloregulation function and anti-ageing
Dairy products and the health products tool of old function are of great significance.
Brief description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=563.288)；
Fig. 2：Mass-to-charge ratio is the second order ms figure of 563.288 fragment；
Fig. 3：Mass-to-charge ratio is 563.288 polypeptide az, by crack conditions；
Fig. 4：Influence situations of the biologically active polypeptide FPKYPVEPF to drosophila survival rate；
Fig. 5：Hydrogen peroxide (H2O2) acute experiment.
Embodiment
Before specific embodiments of the present invention are further described, it should be appreciated that protection scope of the present invention is not limited to down
State specific specific embodiment；It is also understood that the term used in the embodiment of the present invention is specific specific in order to describe
Embodiment, the protection domain being not intended to be limiting of the invention.
When embodiment provides number range, it should be appreciated that except non-invention is otherwise noted, two ends of each number range
Any one numerical value can be selected between point and two endpoints.Unless otherwise defined, in the present invention all technologies for using and
Scientific terminology is identical with the normally understood meaning of those skilled in the art of the present technique.Except used in embodiment specific method, equipment,
Outside material, according to grasp of the those skilled in the art to the prior art and the record of the present invention, it can also use and this
Any method, equipment and the material of the similar or equivalent prior art of method, equipment described in inventive embodiments, material come real
The existing present invention.
Unless otherwise stated, disclosed in this invention experimental method, detection method, preparation method using this technology lead
Molecular biology, biochemistry, chromatin Structure and the analysis of domain routine, analytical chemistry, cell culture, recombinant DNA technology and
The routine techniques of association area.These technologies existing perfect explanation in the prior art, for details, reference can be made to Sambrook etc.
MOLECULAR CLONING：A LABORATORY MANUAL, Second edition, Cold Spring Harbor
Laboratory Press, 1989and Third edition, 2001；Ausubel etc., CURRENT PROTOCOLS IN
MOLECULAR BIOLOGY, John Wiley＆Sons, New York, 1987and periodic updates；the
Series METHODS IN ENZYMOLOGY, Academic Press, San Diego；Wolffe, CHROMATIN
STRUCTURE AND FUNCTION, Third edition, Academic Press, San Diego, 1998；METHODS IN
ENZYMOLOGY, Vol.304, Chromatin (P.M.Wassarman and A.P.Wolffe, eds.), Academic
Press, San Diego, 1999；With METHODS IN MOLECULAR BIOLOGY, Vol.119, Chromatin
Protocols (P.B.Becker, ed.) Humana Press, Totowa, 1999 etc..
The present invention is described in detail with specific embodiment below in conjunction with the accompanying drawings.
1 active peptide FPKYPVEPF's of embodiment is artificial synthesized
First, the synthesis of biologically active peptide
1. RINK resin 3g (substitution value 0.3mmol/g) are weighed in the reactor of 150ml, with the dichloromethane of 50ml
(DCM) soak.
2.2 it is small when after, wash resin with nitrogen-dimethylformamide (DMF) of 3 times of resin volumes, then drain, so weight
It is four times multiple, resin is drained rear stand-by.
3. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4,v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.Washed four times with the DMF of 3 times of resin volumes after having taken off protection,
Then drain.
4. take the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
5. weigh amino acid Phe in right amount and 1- hydroxyls-benzene a pair of horses going side by side triazole (HOBT) is in right amount in the centrifuge tube of 50ml, addition
The DMF of 20ml is dissolved, and then adds the N of 3ml, and N diisopropylcarbodiimide (DIC) vibration shakes up 1min, treats that solution is clear
It is added to after clear in reactor, then reactor is placed in 30 DEG C of shaking table and is reacted.
6.2 it is small when after, with a certain amount of acetic anhydride end socket (acetic anhydride:DIEA:DCM=1:1:2,v:v:V) half an hour, so
Washed four times, drained stand-by with the DMF of 3 times of resin volumes afterwards.
7. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4, v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.Washed four times with DMF after having taken off protection, then drained.
8. take the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
9. weighing second amino acid next in right amount and HOBT being in right amount in the centrifuge tube of 50ml, the DMF generals of 25ml are added
It is dissolved, and the DIC vibrations for then adding 2.5ml shake up 1min, are added to after solution clarification in reactor, then by reactor
It is placed in 30 DEG C of shaking table and reacts.
10.1 it is small when after, take a small amount of resin to detect, (each two drop of inspection A, inspection B, 100 DEG C of reactions detected with ninhydrin method
1min), if resin is colourless, illustrate that the reaction was complete；If resin has color, illustrate that condensation is incomplete, the reaction was continued.
11. after complete reaction, washing resin four times with DMF, then drain, a certain amount of 20% is added into reactor
Piperidines (piperidines/DMF=1:4,v:V), it is placed on decolorization swinging table and rocks 20min, the Fmoc protection groups on resin is sloughed with this
Group.Washed four times with DMF after having taken off protection, then drain whether detection protection sloughs.
12. amino acid Pro, Lys, Tyr, Pro, Val, Glu, Pro and Phe are connected successively according to step 9-11.
13. after last amino acid is connected, protection is sloughed, is washed four times with DMF, is then taken out resin with methanol
It is dry.Then with 95 cutting liquid (trifluoroacetic acids:1,2 dithioglycols:3, isopropyl base silane:Water=95:2:2:1, v:v:V) by polypeptide
Cut down from resin (every gram of resin adds 10ml cutting liquids), and with ice ether (cutting liquid：Ether=1:9,v:V) centrifugation is heavy
Drop four times.
So far, artificial synthesized biologically active peptide FPKYPVEPF.
2nd, the confirmation of biologically active peptide
1) UPLC is analyzed
UPLC conditions are as follows：
Instrument：Waters ACQUITY UPLC ultra high efficiency liquid phase-electron spray-level Four bar-time of-flight mass spectrometer
Chromatographic column specification：BEH C18 chromatographic columns
Flow velocity：0.4mL/min
Temperature：50℃
Ultraviolet detection wavelength：210nm
Sample size：2μL
Gradient condition：A liquid：Water containing 0.1% formic acid (v/v), B liquid：Acetonitrile containing 0.1% formic acid (v/v)
2) mass spectral analysis
Mass Spectrometry Conditions are as follows：
Ionic means：ES+
Mass range (m/z)：100-1000
Capillary voltage (Capillary) (kV)：3.0
Sampling spiroid (V)：35.0
Ion source temperature (DEG C)：115
Remove solvent temperature (DEG C)：350
Go solvent stream (L/hr)：700.0
Collision energy (eV)：4.0
Sweep time (sec)：0.25
Interior sweep time (sec)：0.02
According to above analysis method, using ultra high efficiency liquid phase-electron spray-level Four bar-flight time mass spectrum, to bioactivity
Peptide FPKYPVEPF carries out chromatography and mass spectral analysis, its mass chromatography extraction figure is as shown in Figure 1, extract the two level matter at this peak
As shown in Figures 2 and 3, the polypeptide mass-to-charge ratio that can obtain this peak is 563.288Da, and retention time is for spectrogram and az, by crack conditions
64.7min。
3) result
From the figure 3, it may be seen that situation about being broken according to az, by, calculates by Mascot software analysis, obtains mass-to-charge ratio
The fragment sequence of 563.288Da is Phe-Pro-Lys-Tyr-Pro-Val-Glu-Pro-Phe (FPKYPVEPF), is denoted as SEQ
ID NO：1.The residue sequence of the fragment and beta-casein variation B the 111st~119 is corresponding, beta-casein amino acid sequence
GenBank numbering be AAA30431.1, sequence is shown in SEQ ID NO：3.
The adjusting immunity of organisms activity experiment of 2 biologically active peptide of embodiment
First, the vitro lymphocyte proliferation capacity experimental of mtt assay measure biologically active polypeptide FPKYPVEPF
1. experiment material and instrument：
Reagent and material：Experimental animal balb/c mouse (male 6-8 week old, Shanghai Communications University's agricultural and biological institute
Animal experimental center)；The milk-derived biologically active polypeptide FPKYPVEPF that embodiment 1 obtains；(the purchase of mouse lymphocyte extracting solution
From Suo Laibao companies)；RPMI1640 culture mediums (are purchased from GIBCO companies)；3- (4,5- dimethylthiazole -2) -2,5- diphenyl four
Nitrogen azoles bromide (MTT, purchased from Amresco companies)；ConA (ConA, purchased from Sigma companies)；Bovine serum albumin(BSA)
(BSA, purchased from Genebase companies)；Pepsin (is purchased from Sigma companies)；Pancreatin (Corolase PP, purchased from AB companies).
Instrument and equipment：LRH-250F biochemical cultivation cases, Shanghai perseverance Science and Technology Ltd.；GL-22M high speed freezing centrifuges,
Shanghai Lu Xiang instrument centrifuges Instrument Ltd.；Hera cell 150CO2 incubators, Heraeus companies；Dragon
Wellscan MK3 microplate reader, Labsystems companies；ALPHA 1-2-LD vacuum freeze driers, Christ companies；Superelevation
Effect liquid phase chromatogram-quadrupole rod time of-flight mass spectrometer, waters companies.
2. experimental method：
Mouse spleen is taken under aseptic condition, mouse lymphocyte is extracted with lymphocyte extracting solution, carries out Yuan Dynasty's culture.With
Cell density is adjusted to 2.5 × 10 by complete RPMI1640 nutrient solutions6A/mL.Sequentially added in 96 porocyte culture plates：
100 μ L mouse lymphocyte suspensions, 100 μ L RPMI1640 complete culture solutions, 20 μ L ConAs, 100 μ L samples.In addition,
Blank control group (PBS of pH7.2~7.4,3mol/L) and negative control group (500 μ g/mL BSA) are set, and research shows that its is right
Do not influenced in vitro lymphocyte proliferation.Every group of 3 parallel laboratory test samples.In 5%CO2After 68h being cultivated in 37 DEG C of incubators,
20 μ L MTT are added under aseptic condition per hole, continue to cultivate 4h, careful abandoning supernatant, 100 μ L dimethyl sulfoxide (DMSO)s are added per hole,
37 DEG C of biochemical cultivation cases hatch 10min, shake up, light absorption value is measured at 570nm with microplate reader.
Vitro lymphocyte proliferation ability represents that computational methods are as follows with stimulus index：
In formula：A1For blank control at the 570nm under light absorption value；A2For negative control group at the 570nm under extinction
Value, A3For experimental group at the 570nm under light absorption value.
3. experimental result and analysis：
Influences of the 1 biologically active polypeptide FPKYPVEPF of table to vitro lymphocyte proliferation
| Experiment packet | Stimulus index SI |
| Negative control group | 1 |
| FPKYPVEPF | 1.175±0.072* |
Note：* labelled notation is compared with negative control, there is significant difference (P ＜ 0.05).
Experimental result is shown in Table 1.As shown in Table 1, the bar for being 100 μ g/mL in the mass concentration of biologically active peptide FPKYPVEPF
Under part, the stimulus index of milk-derived biologically active peptide FPKYPVEPF is more than BSA, illustrates that FPKYPVEPF can be stimulated to a certain extent
The propagation of external mouse lymphocyte.And the stimulus index of FPKYPVEPF has reached 1.175, and negative control group is with aobvious
Write difference (P<0.05).Therefore, it can be assumed that active peptides FPKYPVEPF, which has, remarkably promotes mouse lymphocyte propagation
Ability, can be used as a kind of health products or additive to eat, it is possible to increase the immunity of animal and human body.
2nd, the macrophages in vitro multiplication capacity experiment of mtt assay measure biologically active polypeptide FPKYPVEPF
1) experiment reagent and instrument
Reagent：Experimental animal balb/c mouse (male 6-8 week old) Shanghai Communications University agricultural and biological institute animal reality
Test center；The milk-derived biologically active polypeptide FPKYPVEPF that embodiment 1 obtains；3- (4,5- dimethylthiazole -2) -2,5- hexichol
Base tetrazole bromide (MTT) Amresco companies；LPS (lipopolysaccharides) Sigma companies；Bovine serum albumin(BSA) (Bovine Serum
Albumin, BSA) Genebase companies；Three lysates, the water containing 10%SDS, 5% isobutanol and 0.012mol/L HCl
Solution.
Instrument and equipment：LRH-250F biochemical cultivation cases Shanghai perseverance Science and Technology Ltd.；On GL-22M high speed freezing centrifuges
Hai Luxiang instrument centrifuges Instrument Ltd.；Hera cell 150CO2Incubator Heraeus companies；Dragon Wellscan
MK3 microplate reader Labsystems companies.
2) test method：
2% (w/w) the sterilizing starch solutions of balb/c mouse peritoneals injection 2ml, continuous injection three days, last time is injected
24 it is small when after break neck put to death.Skin of abdomen is peelled off, 4 DEG C of phosphate buffers (PBS) is drawn with syringe and rinses abdominal cavity repeatedly, from
After heart pipe collects flushing liquor, supernatant is abandoned in centrifugation (1000rpm, 4 DEG C) after ten minutes, (is contained with 4 DEG C of RPMI1640 complete culture solutions
10%FBS) wash twice, cell viability examination is done in the dyeing of 0.2% trypan blue solution, confirms the vibrant macrophage collected
Account for more than 95%.After cell counting count board reading, adjustment cell concentration to suitable concentration.
It will blow and beat to the cell suspension to suspend completely and added 96 porocyte culture plates, 37 DEG C, 5%CO with suitable volumes2
After when culture 4 is small under environment, liquid in hole is abandoned in suction, and cell culture plate well is carefully cleaned with 37 DEG C of RPMI1640 complete culture solutions
Bottom, washes away not adherent cell and cell fragment, obtains adherent peritoneal macrophage after purification.0.2ml is added per hole
RPMI1640 complete mediums, experiment add after being dissolved in culture medium in advance with small peptide sample and LPS, start cell culture.
After obtaining adherent peritoneal macrophage after purification, experimental group adds dissolved with biologically active polypeptide per hole
The 200 μ l/ holes of RPMI1640 complete culture solutions (10%FBS) of FPKYPVEPF (1mg/ml), continuously cultivate 48h；Negative control group
Add the 200 μ l/ holes of RPMI1640 complete culture solutions (10%FBS) dissolved with BSA (500 μ g/mL) per hole；Blank group is added
200 μ l/ holes of RPMI1640 complete culture solutions (10%FBS), continuously cultivate 48h.Also, experimental group, negative control group and blank
Group sets normal group and inflammation group respectively again；Inflammation group adds LPS to final concentration of 100ng/ml when 24h is arrived in culture；Normal group
It is not added with LPS；And normally group and inflammation group add 20 μ l/ holes of 5%MTT in 44h；Cell culture adds 100 μ after reaching 48h
Three lysates in l/ holes are to terminate culture, after dissolving overnight, survey the absorbance in each hole with microplate reader under wavelength 570nm
(OD570), the calculation formula of growth index (Growth Indices) is as follows：
Wherein, blank nutrient solution is the RPMI1640 complete culture solutions containing 10%FBS.
3) experimental result and analysis
The influence that 2 biologically active polypeptide FPKYPVEPF of table breeds macrophages in vitro
| Experiment packet | Normal group GI | Inflammation group GI |
| Negative control group | 1 | 1 |
| FPKYPVEPF(1mg/ml) | 1.0851±0.0728** | 1.1574±0.0427** |
Note：* represent compared with negative control, there is significant difference (P ＜ 0.05)；* represent compared with negative control group,
There is significant difference (P ＜ 0.01)
Experimental result is shown in Table 2, as shown in Table 2, under conditions of 1mg/ml biologically active polypeptides FPKYPVEPF is added, just
Often the macrophage of group and inflammation group has propagation.And compared with negative control group, there is significant difference (P ＜ 0.01).
Illustrate that biologically active polypeptide FPKYPVEPF has significant proliferation function to macrophages in vitro.
The activity of fighting against senium experiment of 3 biologically active peptide of embodiment
First, biologically active polypeptide FPKYPVEPF improves the experiment of drosophila survival ability
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；The milk-derived biologically active polypeptide FPKYPVEPF that embodiment 1 obtains.
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；G136T type Zealway intelligence
Energy high-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；BJ-CD SERIES bio-incubators, Shanghai, which is won, proves to be true after interrogation industry public affairs
Department；GRX-9073 type hot air sterilizers, the permanent Science and Technology Ltd. in Shanghai one.
2. experimental method：
Using drosophila as experimental model：Collect 8 it is small when the interior drosophila adult newly to sprout wings, male and female random transferring is divided after anesthesia to each
In experimental group, every group of each gender 100, every group of setting 3 is parallel, and control group gives conventional corn powder culture medium, experimental group
FPKYPVEPF biologically active peptides-corn culture medium respectively containing 0.05mg/ml, 0.5mg/ml, 1mg/ml.Replace within every 2 days
Fresh culture once, is observed and records the death toll of different sexes drosophila daily, untill drosophila is all dead.Draw fruit
Fly survivorship curve, and calculate the average life span of different sexes drosophila and maximum life span (takes 5 drosophilas of last death to unite
Meter).
3. experimental result and analysis：
This experiment is as follows to the result of study of the life span of drosophila melanogaster of feeding various concentrations biologically active peptide：Can be with from Fig. 4 (A)
It was found that for blank control group Male Drosophila, feeding concentration is that the FPKYPVEPF of 0.05mg/ml does not change significantly
Become the survival rate of Male Drosophila, and when peptide concentration reaches 0.5mg/ml and 1mg/ml, same time point, the survival of Male Drosophila
Rate is significantly improved.From Fig. 4 (B), relative to blank control group female Drosophila, feeding concentration is 0.5mg/ml and 1mg/ml
When, in same time point, the survival rate of female Drosophila increases, but result difference unobvious.
Influence situations of the table 3-1 FPKYPVEPF to the Male Drosophila service life
Note：* sign has significant difference (P compared with blank control group<0.05)；Similarly hereinafter.
Influence situations of the table 3-2 FPKYPVEPF to the female Drosophila service life
It was found from from table 3-1, relative to blank control group, low dose group Male Drosophila average life span does not have significant change,
It is respectively 17.09% and 10.52% but middle dose group and advanced amount group Male Drosophila average life span are improved, but only middle agent
Amount group generates significant difference (p<0.05), illustrate that the average life span conspicuousness of middle dose group Male Drosophila improves.In meanwhile
The half death time of dosage group and high dose group drosophila is improved, but does not have notable difference in terms of MaLS.By
Table 3-2 understands that female Drosophila low dose group, middle dose group and high dose group increase in terms of average life span, but not
Produce significant difference.But the MaLS of middle dose group and high dose group increases, extend 7 respectively compared with blank control group
It and 6 days, and generate significant difference (P<0.05).
This is the experiment results show that biologically active polypeptide FPKYPVEPF can improve the average longevity of drosophila under a certain concentration
Life and MaLS, but it is related with concentration and gender.It is this with tested material concentration, the relevant phenomenon of strain be probably because
FPKYPVEPF participates in the part biological metabolism of drosophila, or the antioxidant system organized by improving drosophila extends to reach
The effect of life span of drosophila melanogaster.Since the metabolism of different lines drosophila can have any different, so as to cause the difference of result.And the difference of gender
It is different, it may be possible to since female Drosophila inherently has certain conservative and the resistance to external environment, so FPKYPVEPF
Extend simultaneously unobvious to the female Drosophila service life.
2nd, biologically active polypeptide FPKYPVEPF improves the experiment of drosophila fertility
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；The milk-derived biologically active polypeptide FPKYPVEPF that embodiment 1 obtains.
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；G136T type Zealway intelligence
Energy high-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；BJ-CD SERIES bio-incubators, Shanghai, which is won, proves to be true after interrogation industry public affairs
Department；GRX-9073 type hot air sterilizers, the permanent Science and Technology Ltd. in Shanghai one.
2. experimental method：
Collect 8 it is small when the interior drosophila adult newly to sprout wings, its male and female is separately fed, concentration is separately added into culture medium is
The FPKYPVEPF solution of 0mg/ml, 0.05mg/ml, 0.5mg/ml, 1mg/ml, continuous culture 12 days.Collect within 13rd day identical dense
The adult drosophila of the lower culture of degree is simultaneously transferred in new Nostoc commune Vanch bottle, and each blake bottle ensures that 1 female and 2 males are (every
Group 5 bottles), every bottle give accurate 24 it is small when lay eggs.Parent drosophila is transferred in new Nostoc commune Vanch bottle after oviposition, it is old
Blake bottle continues breeding culture, counts progeny size, METHOD FOR CONTINUOUS DETERMINATION 7 days after larva sprouts wings, and be repeated 3 times.
3. experimental result and analysis：
4 reproductive capacity measurement result of table
From table 4, it can be seen that low concentration experimental group reproductive capacity does not produce conspicuousness change, but middle dosage compared with control group
Experimental group and the reproductive capacity of high dose experimental group drosophila are significantly increased (P compared with blank control group<0.05).Illustrate certain dense
The FPKYPVEPF of degree can promote the reproductive capacity of drosophila.Originally test result indicates that, the extension of life span of drosophila melanogaster is FPKYPVEPF straight
Connect effect as a result, rather than FPKYPVEPF by reducing two level physiological effect caused by reproductive capacity.Also illustrate at the same time
FPKYPVEPF is safe to drosophila, without toxic hazard.
3rd, biologically active polypeptide FPKYPVEPF hydrogen peroxide Acute oxidative is tested
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；Hydrogen peroxide, Shanghai Ling Feng chemical reagent Co., Ltd；The milk-derived that embodiment 1 obtains
Biologically active polypeptide FPKYPVEPF.
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；Mi Libo Millipore
MILLEX GP0.22 μm filter membranes, Millipore Corp. of the U.S.；GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument centrifuge instruments
Co., Ltd.
2. experimental method：
Collect 8 it is small when the interior drosophila adult newly to sprout wings, male and female random transferring is divided after anesthesia into each experimental group, takes the service life real
The preferable peptide concentration culture medium of middle result is tested, sets blank control group and experimental group, control group to give conventional corn powder culture medium.
Every group of male and female gender drosophila is 50, and drosophila is cultivated three weeks.Then 5 males and 5 female Drosophilas are taken to be transferred to every time
Contain a papery disk in one new container, in new container, disk contain 300 μ L concentration for 5% sucrose solution with
And concentration is 30% hydrogen peroxide 1ml, blank group and experimental group are exposed to the toxicity peroxide of this hydrogen peroxide generation
In environment, 10 Duplicate Samples of every group of setting, observe its oxidation resistance.Every 4 hour record drosophila The dead quantity and gender, until
Drosophila is all dead.
3. experimental result and analysis：
From Fig. 5 (A) as can be seen that for Male Drosophila, after FPKYPVEPF feedings, in Each point in time, male
The survival rate of drosophila is above the drosophila without FPKYPVEPF feedings, and the time-to-live increases compared with blank control group, explanation
After feeding FPKYPVEPF, Male Drosophila oxidation resistance increases.In Fig. 5 (B), the female Drosophila of feeding FPKYPVEPF,
Survival rate is obvious high in 15h in the hydrogen peroxide environment of high concentration and control group, illustrates that this period female Drosophila is anti-oxidant
Ability increases.But later experiments group and control group survival curve essentially coincide, and illustrate the female Drosophila of feeding FPKYPVEPF
Oxidation resistance gradually weaken, by there is no difference with control group after a certain period of time.This test result indicates that, FPKYPVEPF
The oxidation resistance of drosophila can be improved.According to H2O2Acute toxicity testing is as a result, can speculate that FPKYPVEPF may pass through tune
Cat catalase activity is saved to improve drosophila to H2O2The resistivity of damage.
Drawn by above example, the biologically active polypeptide FPKYPVEPF of the application has immunoloregulation function and resists
Aging function.
The above-mentioned description to embodiment is understood that for ease of those skilled in the art and using invention.
Person skilled in the art obviously easily can make these embodiments various modifications, and described herein general
Principle is applied in other embodiment without by performing creative labour.Therefore, the invention is not restricted to above-described embodiment, ability
Field technique personnel disclose according to the present invention, do not depart from improvement that scope made and modification all should be the present invention's
Within protection domain.
Sequence table
<110>Shanghai Communications University；Zhejiang Hui Tai life and healths Science and Technology Ltd.
<120>A kind of biologically active polypeptide FPKYPVEPF and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 9
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Phe Pro Lys Tyr Pro Val Glu Pro Phe
1 5
<210> 2
<211> 27
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
tttcctaaat atccagttga gcccttt 27
<210> 3
<211> 209
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 3
Arg Glu Leu Glu Glu Leu Asn Val Pro Gly Glu Ile Val Glu Ser Leu
1 5 10 15
Ser Ser Ser Glu Glu Ser Ile Thr Arg Ile Asn Lys Lys Ile Glu Lys
20 25 30
Phe Gln Ser Glu Glu Gln Gln Gln Thr Glu Asp Glu Leu Gln Asp Lys
35 40 45
Ile His Pro Phe Ala Gln Thr Gln Ser Leu Val Tyr Pro Phe Pro Gly
50 55 60
Pro Ile Pro Asn Ser Leu Pro Gln Asn Ile Pro Pro Leu Thr Gln Thr
65 70 75 80
Pro Val Val Val Pro Pro Phe Leu Gln Pro Glu Val Met Gly Val Ser
85 90 95
Lys Val Lys Glu Ala Met Ala Pro Lys His Lys Glu Met Pro Phe Pro
100 105 110
Lys Tyr Pro Val Glu Pro Phe Thr Glu Arg Gln Ser Leu Thr Leu Thr
115 120 125
Asp Val Glu Asn Leu His Leu Pro Leu Pro Leu Leu Gln Ser Trp Met
130 135 140
His Gln Pro His Gln Pro Leu Pro Pro Thr Val Met Phe Pro Pro Gln
145 150 155 160
Ser Val Leu Ser Leu Ser Gln Ser Lys Val Leu Pro Val Pro Gln Lys
165 170 175
Ala Val Pro Tyr Pro Gln Arg Asp Met Pro Ile Gln Ala Phe Leu Leu
180 185 190
Tyr Gln Glu Pro Val Leu Gly Pro Val Arg Gly Pro Phe Pro Ile Ile
195 200 205
Val
Claims (10)
1. a kind of biologically active polypeptide FPKYPVEPF, it is characterised in that its amino acid sequence is Phe-Pro-Lys-Tyr-Pro-
Val-Glu-Pro-Phe。
2. a kind of biologically active polypeptide FPKYPVEPF according to claim 1, it is characterised in that the bioactivity is more
Peptide is milk-derived.
3. encode the nucleotide fragments of biologically active polypeptide FPKYPVEPF described in claim 1, it is characterised in that the nucleosides
The sequence of acid fragment such as SEQ ID NO：Shown in 2.
4. the preparation method of biologically active polypeptide FPKYPVEPF as claimed in claim 1, it is characterised in that pass through genetic engineering
Method it is artificial synthesized, or directly obtained from dairy products by the method isolated and purified, or directly prepared by chemical synthesis.
5. the application of biologically active polypeptide FPKYPVEPF as claimed in claim 1, it is characterised in that the biologically active polypeptide
Applications of the FPKYPVEPF in the food with immunoloregulation function, health products, medicine or cosmetics are prepared.
6. the application of biologically active polypeptide FPKYPVEPF as claimed in claim 1, it is characterised in that the biologically active polypeptide
Applications of the FPKYPVEPF in the food with anti-senescence function, health products or medicine is prepared.
7. the application of biologically active polypeptide FPKYPVEPF as claimed in claim 1, it is characterised in that the biologically active polypeptide
Applications of the FPKYPVEPF in the food with immunoloregulation function and anti-senescence function, health products or medicine is prepared.
A kind of 8. immunological regulation product, it is characterised in that including biologically active polypeptide FPKYPVEPF as claimed in claim 1 or
The derivative of the biologically active polypeptide FPKYPVEPF；The immunological regulation product includes immunological regulation food, immunological regulation
Health products, immunoregulation medicament or immunological regulation cosmetics；The derivative of the biologically active polypeptide FPKYPVEPF, refers to
On the amino acid side groups of biologically active polypeptide FPKYPVEPF, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
9. a kind of anti-aging product, it is characterised in that including biologically active polypeptide FPKYPVEPF as claimed in claim 1 or institute
State the derivative of biologically active polypeptide FPKYPVEPF；The anti-aging product include antisenility cistanche food, antisenescence health product or
Antiaging agent；The derivative of the biologically active polypeptide FPKYPVEPF, refers to the ammonia in biologically active polypeptide FPKYPVEPF
On base acid side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, ester
Change or glycosylation modified, obtained polypeptide derivative.
10. a kind of product with immunoloregulation function and anti-senescence function, it is characterised in that including as claimed in claim 1
The derivative of biologically active polypeptide FPKYPVEPF or described biologically active polypeptides FPKYPVEPF；With immunoloregulation function and resist
The product of aging function includes food, health products or medicine；The derivative of the biologically active polypeptide FPKYPVEPF, refers to
On the amino acid side groups of biologically active polypeptide FPKYPVEPF, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
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| CN201711125053.6A CN108017701A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide FPKYPVEPF and its preparation method and application |
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| CN201711125053.6A CN108017701A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide FPKYPVEPF and its preparation method and application |
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Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112646023A (en) * | 2021-01-21 | 2021-04-13 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure VNVVPTFGKKKGP, and preparation method and application thereof |
| CN112679598A (en) * | 2021-01-19 | 2021-04-20 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide SGVSLAALKKALAAAGYDVEK, and preparation method and application thereof |
| CN112724239A (en) * | 2021-01-22 | 2021-04-30 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure NKELDPVQKLFVDKIREYK and application thereof |
| CN112745379A (en) * | 2021-01-22 | 2021-05-04 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure RDNKKTRIIPR, and preparation method and application thereof |
| CN116444611A (en) * | 2022-11-30 | 2023-07-18 | 内蒙古伊利实业集团股份有限公司 | Milk active peptide TDPLFKG, preparation method and application thereof |
| CN116444609A (en) * | 2022-11-30 | 2023-07-18 | 内蒙古伊利实业集团股份有限公司 | Milk active peptide LPPPLPSRWPL and preparation method and application thereof |
| CN116444619A (en) * | 2022-11-30 | 2023-07-18 | 内蒙古伊利实业集团股份有限公司 | Milk active peptide YPFPGPIHNSLP and preparation method and application thereof |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104479002A (en) * | 2014-12-19 | 2015-04-01 | 上海交通大学 | Preparation and applications of biological active peptides derived from beta-casein of cow milk |
| CN107163136A (en) * | 2017-07-06 | 2017-09-15 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide WNIPMGLIVNQ and its preparation method and application |
| CN107188949A (en) * | 2017-07-06 | 2017-09-22 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide EINTVQVTST and its preparation method and application |
| CN107200780A (en) * | 2017-07-06 | 2017-09-26 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide LVYPFPG and its preparation method and application |
-
2017
- 2017-11-14 CN CN201711125053.6A patent/CN108017701A/en not_active Withdrawn
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104479002A (en) * | 2014-12-19 | 2015-04-01 | 上海交通大学 | Preparation and applications of biological active peptides derived from beta-casein of cow milk |
| CN107163136A (en) * | 2017-07-06 | 2017-09-15 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide WNIPMGLIVNQ and its preparation method and application |
| CN107188949A (en) * | 2017-07-06 | 2017-09-22 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide EINTVQVTST and its preparation method and application |
| CN107200780A (en) * | 2017-07-06 | 2017-09-26 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide LVYPFPG and its preparation method and application |
Non-Patent Citations (4)
| Title |
|---|
| FLORIAN BAUM等: "Analysis of the Endogenous Peptide Profile of Milk: Identification of 248 Mainly Casein-Derived Peptides", 《JOURNAL OF PROTEOME》 * |
| 于洋等: "乳源生物活性肽研究进展", 《食品与发酵工艺》 * |
| 张宇琪等: "羊乳清蛋白ＡＣＥ及DPP-IV抑制肽的分离纯化与鉴定", 《中国农业大学学报》 * |
| 高扬等: "乳源性小肽QEPV的抗衰老功能研究", 《中国乳品工业》 * |
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| CN112646023A (en) * | 2021-01-21 | 2021-04-13 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure VNVVPTFGKKKGP, and preparation method and application thereof |
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| CN112745379A (en) * | 2021-01-22 | 2021-05-04 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure RDNKKTRIIPR, and preparation method and application thereof |
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| CN116444619B (en) * | 2022-11-30 | 2024-07-16 | 内蒙古伊利实业集团股份有限公司 | Milk active peptide YPFPGPIHNSLP and preparation method and application thereof |
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