CN107892716A - A kind of biologically active polypeptide LPPLL and its preparation method and application - Google Patents
A kind of biologically active polypeptide LPPLL and its preparation method and application Download PDFInfo
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- CN107892716A CN107892716A CN201711319330.7A CN201711319330A CN107892716A CN 107892716 A CN107892716 A CN 107892716A CN 201711319330 A CN201711319330 A CN 201711319330A CN 107892716 A CN107892716 A CN 107892716A
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- Prior art keywords
- lppll
- biologically active
- active polypeptide
- polypeptide
- derivative
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- C—CHEMISTRY; METALLURGY
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- 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
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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
- 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
- A61Q19/08—Anti-ageing preparations
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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
- 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)
- Animal Behavior & Ethology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Birds (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Mycology (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Dermatology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
Abstract
The present invention relates to albumen field, and in particular to its amino acid sequence of a kind of biologically active polypeptide LPPLL and its preparation method and application, biologically active polypeptide LPPLL is Leu Pro Pro Leu Leu.Tested by antioxidation in vitro, internal Antisenility Experiment, demonstrating polypeptide LPPLL has preferable antioxidation biology activity and activity of fighting against senium, on the one hand, biologically active polypeptide LPPLL of the invention has preferable antioxidation activity, free radical that can be in removing machine body, improve the quality of life；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 anti-oxidation 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 LPPLL and its preparation method and application.
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 has special
Physiological function, it is referred to as " biologically active peptide ".
It is particularly important that safe biologically active peptide is found in natural food source.In the last few 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 the polypeptide with bioactivity 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.
Oxidation reaction and oxidative metabolism are all vital for food and human body, and free radical and active oxygen cause
A series of oxidation reaction.When the free radical of excess is formed, they can exceed protective enzyme such as superoxide dismutase, peroxide
Change the protective effect of hydrogen enzyme, so as to cause a series of side effect such as lipid oxidation, Apoptosis to produce.This kind of oxidation is anti-
Should, the shelf-life of the food containing fat is not only influenceed, certain harm also is caused to the health of human body, such as rheumatic arthritis, sugar
Urinate disease, artery sclerosis etc..In addition, Collins et al. researchs in 2005 find that oxidative damage of the generation of cancer also with DNA has
Close.
Some artificial synthesized antioxidant such as butylated hydroxy anisoles (BHA), 2,6- di-t-butyl -4- methylbenzenes in early days
Phenol (BHT) is applied in food, as the antioxidant of lipid, but these artificial synthesized additives have for human body it is latent
Risk.In the research process of natural, from the anti-oxidation peptide of food proteins become popular research it
One.It is not only safe, is easier to be absorbed and used than macro-nutrients such as protein, and such as calcium, iron can be promoted micro-
The absorption of nutrient is measured, also with preferable antioxidation activity, is had a extensive future.
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 life-spans of these organisms and reach
As many as 6 times.
Anti-aging peptide in terms of physiological function there is amino acid can not 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, with anti-aging.Therefore, the nutrition and health care of biologically active peptide
Effect has turned into 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 come
The milk-derived biologically active polypeptide DELQDKIH of beta-casein is come from, Chinese patent CN105254739A discloses one kind and derived 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 LPPLL 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 LPPLL, its amino acid sequence are Leu-Pro-Pro-
Leu-Leu, 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 variant
The amino acid residue that A1 is the 135th~139.The amino acid sequence of beta-casein modification A 1 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 modification A
The biologically active polypeptide LPPLL of the nucleotide fragments energy encoding mature of 135th~139 amino acids residue.
Preferably, the biologically active polypeptide has anti-oxidation function and anti-senescence function.
Second aspect of the present invention, there is provided encode the nucleotide fragments of the biologically active polypeptide LPPLL, its sequence is：
5 '-ttg cct cct ctc ttg-3 ', such as SEQ ID NO：Shown in 2.
Third aspect present invention, there is provided the preparation method of the biologically active polypeptide LPPLL, genetic engineering can be passed through
Method it is artificial synthesized, can be directly obtained from dairy products by the method isolated and purified, can directly pass through chemical synthesis
Prepare.
Fourth aspect present invention, there is provided the biologically active polypeptide LPPLL prepare with anti-oxidation function food,
Application in health products, medicine or cosmetics.
Fifth aspect present invention, there is provided the biologically active polypeptide LPPLL prepare with anti-senescence function food,
Application in health products or medicine.
Sixth aspect present invention, there is provided the biologically active polypeptide LPPLL prepare simultaneously have anti-oxidation function and
Application in the food of anti-senescence function, health products or medicine.
Specifically, biologically active polypeptide LPPLL of the invention, which can be used for preparing, reduces free radical to skin damage
Cosmetics, preparation have anti-oxidant and/or anti-aging medicine；And because the biologically active polypeptide LPPLL of the present invention passes through
Product after intestines and stomach degraded still has bioactivity, therefore can be also used for preparing the food such as Yoghourt, oxidation-resisting health-care
Product, and the oral preparation that is used for have anti-oxidant and/or anti-aging medicine.
Seventh aspect present invention, there is provided a kind of oxidation resistant product, including the biologically active polypeptide LPPLL or described lifes
Thing active peptides LPPLL derivative；Described oxidation resistant product includes antioxidant food, antioxidant health-care product, antioxidant drug
Thing or antioxidation cosmetic product；The derivative of the biologically active polypeptide LPPLL, refers to the amino in biologically active polypeptide LPPLL
On sour side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification
Or the modification such as glycosylation, obtained polypeptide derivative.
Eighth aspect present invention, there is provided a kind of anti-aging product, including the biologically active polypeptide LPPLL or described lifes
Thing active peptides LPPLL derivative；Described anti-aging product includes antisenility cistanche food, antisenescence health product or Kangshuaining mixture
Thing；The derivative of the biologically active polypeptide LPPLL, refers on biologically active polypeptide LPPLL amino acid side groups, ammonia
Cardinal extremity or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation,
Obtained polypeptide derivative.
Ninth aspect present invention, there is provided product a kind of while that there is anti-oxidation function and anti-senescence function, including institute
State biologically active polypeptide LPPLL or described biologically active polypeptides LPPLL derivative；With anti-oxidation function and anti-senescence function
Product include food, health products or medicine；The derivative of the biologically active polypeptide LPPLL, refers in biologically active polypeptide
On LPPLL amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation,
Phosphorylation, esterification or glycosylation etc. are modified, obtained polypeptide derivative.
Biologically active polypeptide LPPLL's of the present invention has the beneficial effect that：The milk-derived biologically active polypeptide LPPLL tools of the present invention
There are preferable antioxidation activity and activity of fighting against senium；On the one hand, biologically active polypeptide LPPLL of the invention has preferable antioxygen
Change activity, free radical that can be in removing machine body, improve the quality of life；On the other hand, it is possible to increase internal antiperoxidase
The vigor of system, the function of enhancing body resistance external source sexual stimulus are split so as to reduce organism aging process, aging and sick probability
Hair is of great significance with anti-oxidation function, the food of anti-senescence function, health products and medicine tool.
Brief description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=552.3776)；
Fig. 2：Mass-to-charge ratio is the second order mses figure of 552.3776 fragment；
Fig. 3：Mass-to-charge ratio is 552.3776 polypeptide az, by crack conditions；
Fig. 4：[DPPH] methanol standard curve；
Fig. 5：Tocopherol Trolox standard curves；
Fig. 6：Influences of the various concentrations LPPLL to C. Elegans Automatic Screening fecundity；
Fig. 7：Nematode growth conditions in the L4 phases under different condition of culture；
Fig. 8：The influence that biologically active polypeptide LPPLL grows to C. Elegans Automatic Screening body；
Fig. 9：Influences of the biologically active polypeptide LPPLL to the C. Elegans Automatic Screening life-span.
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 end points.Unless otherwise defined, in the present invention all technologies for using and
Scientific terminology is identical with the meaning that those skilled in the art of the present technique are generally understood that.Except used in embodiment specific method, equipment,
Outside material, according to grasp of the those skilled in the art to 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 indicated, disclosed in this invention experimental method, detection method, preparation method using this technology lead
Domain conventional molecular biology, biochemistry, chromatin Structure and analysis, 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, 1989 and Third edition, 2001；Ausubel etc., CURRENT PROTOCOLS IN
MOLECULAR BIOLOGY, John Wiley＆Sons, New York, 1987 and 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.
The active peptide LPPLL's of embodiment 1 is artificial synthesized
First, the synthesis of biologically active peptide
1. RINK resin 3g (substitution value 0.3mmol/g) are weighed in 150ml reactor, with 50ml dichloromethane
(DCM) soak.
After 2.2 hours, resin is washed with nitrogen-dimethylformamide (DMF) of 3 times of resin volumes, is then drained, so weight
It is multiple four times, 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 Leu in right amount and 1- hydroxyls-benzene a pair of horses going side by side triazole (HOBT) is in right amount in 50ml centrifuge tube, addition
20ml DMF is dissolved, and then adds 3ml N, and N DICs (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 reacted.
After 6.2 hours, 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 50ml centrifuge tube, 25ml DMF generals are added
It dissolves, 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.
After 10.1 hours, take a small amount of resin to detect, (each two drop of inspection A, inspection B, 100 DEG C of reactions are detected with ninhydrin method
1min), if resin is colourless, illustrate that reaction is complete；If resin has color, illustrate that condensation is incomplete, continue to react.
After 11. question response is complete, washs 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, Pro, Leu and Leu 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 LPPLL.
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 LPPLL carries out chromatography and mass spectral analysis, and its mass chromatography extraction figure is as shown in figure 1, extract the second order mses figure at this peak
With az, by crack conditions as shown in Figures 2 and 3, the polypeptide mass-to-charge ratio that can obtain this peak is 552.3776Da, and retention time is
75.1min。
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
552.3776Da fragment sequence is Leu-Pro-Pro-Leu-Leu (LPPLL), is designated as SEQ ID NO：1.The fragment and β-junket
The residue sequence that protein variant A1 is the 135th~139 is corresponding, and the GenBank numberings of beta-casein amino acid sequence are
AAA30431.1, sequence are shown in SEQ ID NO：3.
The antioxidation activity experiment of the biologically active peptide of embodiment 2
First, [DPPH] method measure biologically active peptide LPPLL antioxidation activity in vitro
1. experiment reagent and instrument：
Reagent：1,1- diphenyl -2- trinitrophenyl-hydrazines (1,1-Diphenyl-2-picrylhydrazyl [DPPH]),
Japanese Wako companies production；Methanol, Shanghai traditional Chinese medicines company provide；The milk-derived biologically active polypeptide LPPLL that embodiment 1 obtains.
Key instrument：Sunrise ELIASAs, Austrian Tecan Products；96 porocyte culture plates, the U.S.
Millipore companies manufacture；Assay balance, Meitelei-tolido Products.
2. experimental method：
(1) 1mmol/L [DPPH] methanol solution
0.349mg [DPPH] is weighed with assay balance to be dissolved in 1mL methanol solutions, prepares obtained 1mmol/L
[DPPH] methanol solution, tinfoil are kept in dark place, i.e., with i.e. use.
(2) measure of [DPPH] methanol standard curve
100 μ L [DPPH] methanol standard curve samples are separately added into by table 1 in 96 orifice plates, are stored at room temperature 90min, are used
ELIASA detects light absorption value at 517nm.
[DPPH] methanol of table 1 calibration curve solution is prepared
According to experimental result, using Excel matched curves and regression equation is calculated, as a result sees Fig. 4 (regression equations：Y=-
0.192x+0.2271, R2=0.9991).The linear relationship of [DPPH] methanol standard curve is good, coefficient correlation 0.999,
Show that [DPPH] methanol standard curve preci-sion and accuracy meets testing requirements.In terms of result, absorbance with
[DPPH] content is in inverse relation, and [DPPH] content is fewer, and light absorption value is higher, i.e. the ability of sample removing free radical is got over
By force.
(3) [DPPH] method measure biologically active peptide LPPLL antioxidation activity
1) sample sets：80 μ L concentration are added in 96 orifice plates for 1mmol/L [DPPH] methanol solution, by table 2 respectively to add
Enter the testing sample (LPPLL), positive control 1 (2.5mg/mL Trolox), positive control 2 of 20 μ L various concentrations
(0.025mg/mL Trolox), and negative control (phytic acid)；
2) blank group：On same 96 orifice plate, to add 80 μ L concentration as 1mmol/L [DPPH] methanol solutions and 20 μ L
The sample of deionized water does blank control.
After detected sample is loaded, 90min is stored at room temperature, light absorption value is detected at 517nm with ELIASA.Under
Formula calculates free radical scavenging activity, and experimental result is shown in Table 2.
Formula：
Table 2 [DPPH] method determines the antioxidation activity result of biologically active polypeptide
From table 2 it can be seen that the Trolox as the 2.5mg/mL of positive control have under the same conditions it is most strong clear
Except the ability of free radical, free radical all in solution can be almost removed, is secondly 0.025mg/mL Trolox, phytic acid, work
Property polypeptide.Polypeptide LPPLL removes [DPPH] free radical rate and is presented bell with change in concentration, is to be reached at 2.5mg/mL in concentration
It is 24.80% to peak.
2nd, ABTS methods measure biologically active peptide LPPLL antioxidant activity in vitro
1. experiment reagent and instrument：
TAC detection kit (Total Antioxidant Capacity Assay Kit with ABTS
Method), purchased from the green skies biotechnology company in Shanghai；ABTS solution, oxidizing agent solution, watermiscible vitamin E (Trolox solution)
(10mmol/L), the milk-derived biologically active polypeptide LPPLL that embodiment 1 obtains.
Key instrument：Sunrise ELIASAs, Austrian Tecan Products；96 porocyte culture plates, the U.S.
Millipore companies manufacture；Assay balance, Meitelei-tolido Products.
2. experimental method：
(1) preparation of ABTS working solutions
According to TAC detection kit specification, by ABTS solution and ABTS oxidizing agent solutions 1:1 mixing, keeps away
Used after light storage 12-16h.The ABTS mother liquors prepared at room temperature deposit by lucifuge, stable in 2-3 days.It is before use, dilute with PBS
Release 38-42 times of ABTS working stocks so that after the absorbance of ABTS working solutions subtracts corresponding PBS blank controls, A734 be 0.7 ±
0.05, ABTS working solution tinfoil is kept in dark place, now with the current.
(2) the making measure of tocopherol (Trolox) standard curve curve
200 μ L ABTS working solutions are added in each detection hole of 96 orifice plates, by the requirement of table 3 in standard curve detection hole
Tocopherol (Trolox) solution that 10 μ L are diluted with PBS is added, 10 μ L PBS is added in blank control wells, gently mixes.Room temperature
After being incubated 4min, light absorption value is detected at 734nm.
The solution of the tocopherol of table 3 (Trolox) standard curve determination is prepared
Experimental result, with Excel fit regression curves and regression equation is drawn, as a result as shown in Figure 5.Trolox
Standard curve linear relationship is good, and its coefficient correlation reaches 0.998, and the degree of accuracy and accuracy for showing the standard curve all meet
Testing requirements, calculated available for subsequent result.It can be seen that well anti-is presented with light absorption value in Trolox standard curves
Than relation, the concentration of Trolox solution is higher, and its light absorption value under 734nm is lower, i.e. the Scavenging ability of institute's test sample product
It is stronger.
(3) ABTS methods measure biologically active polypeptide LPPLL oxidation resistance
200 μ L ABTS working solutions are added in each detection hole of 96 orifice plates, adding 10 μ L in sample detection hole treats test sample
Product, 10 μ L PBS are added in blank control wells, are gently mixed.After being incubated at room temperature 4min, extinction is detected at 734nm with ELIASA
Value.The TAC of sample is calculated according to standard curve.TAC representation is with Trolox standard liquids
Concentration represent that calculate free radical scavenging activity according to the following formula, experimental result is shown in Table 4.
TAC (mmol/g)=CTrolox/CS
In formula：CTrolox--- with sample light absorption value identical Trolox concentration of standard solution (mmol/L)
CS--- the concentration (mg/mL) of synthesis polypeptide sample
The ABTS methods of table 4 measure biologically active polypeptide LPPLL TAC result
Pass through TAC method (Total Antioxidant Capacity Assay Kit with ABTS methods)
Polypeptide LPPLL external total antioxidant activity is determined, finds biologically active polypeptide LPPLL compared to its extinction of blank group
It is worth decrease to some degree, the ability with preferable reduction-oxidation material.As shown in Table 4, it is found that polypeptide LPPLL's is total anti-
Oxidability raises with the rise of peptide concentration, and in the case of concentration is 5mg/mL, polypeptide LPPLL total antioxidation is horizontal
Reach 0.1968mmol/g, i.e., under 5mg/mL concentration, the total antioxidation of its TAC and 1mmol/L Trolox
Ability mutually maintains an equal level.Therefore, can assert the biologically active polypeptide LPPLL of invention has significant oxidation resistance.
The activity of fighting against senium experiment of the biologically active peptide of embodiment 3
First, the experiment that biologically active polypeptide LPPLL influences on C. Elegans Automatic Screening fecundity
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；The milk-derived biologically active polypeptide LPPLL that embodiment 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in flat board,
Choose nematode in flat board, then the ovum in flat board is in same growth period.
(4) index determining
Using C. Elegans Automatic Screening as animal model, the L4 phase nematodes after the processing of picking synchronization arrive respective concentration for this experiment
In NGM plates.Each concentration at least 8 nematodes, each NGM plates are transferred to one, are designated as 0 day, move to daily later in new plate until
Nematode reproduction is no longer laid eggs substantially, and the total laying of nematode is counted before it enters the egg-laying season.
3. experimental result and analysis：
Experimental result as shown in fig. 6, compared with not feeding polypeptide LPPLL blank group, feeding different quality concentration
In experimental group, its eggs on average number has different degrees of increase.When the polypeptide LPPLL concentration of feeding is 300mg/L, nematode is put down
Equal laying has highly significant difference (P compared with blank group<0.01), and when its concentration is 400mg/L, 500mg/L,
Significant difference (P is but only presented compared with blank group<0.05), this has also further demonstrated that 300mg/L for mixing galanin peptide
LPPLL acts on optium concentration, and as the raising of peptide concentration can't suppress nematode reproduction, but its action effect weakens.To sum up
Described, polypeptide LPPLL can be obviously improved the fecundity of nematode under finite concentration.Meanwhile this test result indicates that, polypeptide
LPPLL 300mg/L are optimum concentration.But with the increase of concentration, the fecundity of nematode but no longer significantly improves.
2nd, biologically active polypeptide LPPLL grows the experiment influenceed to C. Elegans Automatic Screening body
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；The milk-derived biologically active polypeptide LPPLL that embodiment 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in flat board,
Choose nematode in flat board, then the ovum in flat board is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.Difference group nematode, the difference between in the same period lower body is grown, Ke Yi
Reflect the influence that the active material is developed for nematode growth to a certain extent.The nematode of each group synchronization culture is growing to
During L2 phases (culture 2 days or so), 40 nematodes of picking to respective NGM flat boards respectively, continuous 2 days, 3 days, 4 days, 5 days, 6 days, 8
My god, observe its growth conditions with inverted microscope within 10 days, determine and record its body length, every group takes its average value.
3. experimental result and analysis：
Under 20 DEG C of condition of culture, since the L2 phases (the 2nd day) of nematode growth from, L3 phases (the 3rd day), L4 phases
(the 4th day), the adult stage (the 6th day), Continuous Observation 8 days, until the 10th day of nematode growth, determine nematode under each time point
Body is grown.Can be seen that each group nematode its body length in the L4 phases with reference to Fig. 7 and Fig. 8 is 1000 μm or so, no significant difference.Together
When, from the long change curve of nematode body it can also be seen that, the long change curve of experimental group body also almost with the long change curve of blank group body
Coincide, at nematode L3 phases (the 3rd day), although slightly different for the average body length of nematode, do not present statistically aobvious
Write sex differernce.Experiment shows that polypeptide LPPLL concentration can't influence the growth of nematode.Meanwhile it is also seen that nematode in the L3 phases
(the 3rd day) to L4 phases (the 4th day), it is that it grows the stage the most quick.
3rd, experiments of the biologically active polypeptide LPPLL to C. Elegans Automatic Screening aging effects
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；5-fluor-uracil, Sigma Co., USA；The milk-derived life that embodiment 1 obtains
Thing active peptides LPPLL.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in flat board,
Choose nematode in flat board, then the ovum in flat board is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.Some of L4 phase nematodes are chosen, after synchronization processing, are respectively placed in corresponding
In NGM plates；Every group of nematode population is no less than 60, is now designated as 0 day, transfers them to daily in new plate, to the reproduction later stage
Do not retransfer.Record nematode is dead daily and eliminates the bar number of experiment.Wherein contain in each NGM plates of life experiment
12.5mg/L 5-fluor-uracils are to suppress nematode reproduction.Nematode death criterion：Without mobile and swallowing act, after touching still
Without any reaction.Rejecting standard：1. flee to flat board wall or cover and thirst；2. worm's ovum is hatched into bag sample worm in vivo：③
Pierce in agar.
3. experimental result and analysis：
Influences of the biologically active polypeptide LPPLL of table 5 to the nematode life-span
It can be seen from table 5 and Fig. 9 when feeding polypeptide LPPLL mass concentration is 300mg/L, nematode in experimental group
Average life span extend about 9.68% respectively, meanwhile, its half death time has even more obtained conspicuousness raising (P ＜
0.05), the MaLS time also extends 4 days respectively compared to blank group.It is even more to be intuitive to see in Fig. 9, same time
Point, nematode survival rate was extended apparently higher than blank group, nematode life-span in experimental group.It is demonstrated experimentally that the polypeptide that experiment uses
Mass concentration is suitable.It can effectively delay nematode aging, improve survival rate, and also further demonstrate that polypeptide simultaneously
The effect that LPPLL extends the life-span realizes not by nematode reproductive capacity is suppressed, because its have good anti-oxidation function and compared with
Strong Scavenging ability.
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 can easily make various modifications to these embodiments, 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 do not depart from improvement that scope made and modification all should be the present invention's according to the announcement of the present invention
Within protection domain.
Sequence table
<110>Zhejiang Hui Tai life and healths Science and Technology Ltd.；Shanghai Bo Hui bio tech ltd
<120>A kind of biologically active polypeptide LPPLL and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 5
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Leu Pro Pro Leu Leu
1 5
<210> 2
<211> 15
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
ttgcctcctc tcttg 15
<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 His 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 Gln Pro Phe Thr Glu Ser Gln Ser Leu Thr Leu Thr
115 120 125
Asp Val Glu Asn Leu His Leu Pro Pro Leu 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 Glu 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 Gln 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 LPPLL, it is characterised in that its amino acid sequence is Leu-Pro-Pro-Leu-Leu.
2. a kind of biologically active polypeptide LPPLL according to claim 1, it is characterised in that the biologically active polypeptide is
Milk-derived.
3. encode the nucleotide fragments of biologically active polypeptide LPPLL described in claim 1, it is characterised in that the nucleotides piece
The sequence such as SEQ ID NO of section：Shown in 2.
4. biologically active polypeptide LPPLL as claimed in claim 1 preparation method, it is characterised in that pass through the side of genetic engineering
Method is artificial synthesized, or is directly obtained from dairy products by the method isolated and purified, or is directly prepared by chemical synthesis.
5. biologically active polypeptide LPPLL as claimed in claim 1 application, it is characterised in that the biologically active polypeptide LPPLL
Application in the food with anti-oxidation function, health products, medicine or cosmetics are prepared.
6. biologically active polypeptide LPPLL as claimed in claim 1 application, it is characterised in that the biologically active polypeptide LPPLL
Application in the food with anti-senescence function, health products or medicine is prepared.
7. biologically active polypeptide LPPLL as claimed in claim 1 application, it is characterised in that the biologically active polypeptide LPPLL
Application in the food with anti-oxidation function and anti-senescence function, health products or medicine is prepared.
8. a kind of oxidation resistant product, it is characterised in that including biologically active polypeptide LPPLL or described lifes as claimed in claim 1
Thing active peptides LPPLL derivative；Described oxidation resistant product includes antioxidant food, antioxidant health-care product, antioxidant drug
Thing or antioxidation cosmetic product；The derivative of the biologically active polypeptide LPPLL, refers to the amino in biologically active polypeptide LPPLL
On sour side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, 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 LPPLL or described lifes as claimed in claim 1
Thing active peptides LPPLL derivative；Described anti-aging product includes antisenility cistanche food, antisenescence health product or Kangshuaining mixture
Thing；The derivative of the biologically active polypeptide LPPLL, refers on biologically active polypeptide LPPLL amino acid side groups, ammonia
Cardinal extremity or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtain
The polypeptide derivative arrived.
10. a kind of product with anti-oxidation function and anti-senescence function, it is characterised in that including raw as claimed in claim 1
Thing active peptides LPPLL or described biologically active polypeptides LPPLL derivative；Production with anti-oxidation function and anti-senescence function
Product include food, health products or medicine；The derivative of the biologically active polypeptide LPPLL, refers in biologically active polypeptide LPPLL
Amino acid side groups on, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphoric acid
Change, esterification or glycosylation modified, obtained polypeptide derivative.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002030958A2 (en) * | 2000-10-09 | 2002-04-18 | GESELLSCHAFT FüR BIOTECHNOLOGISCHE FORSCHUNG MBH (GBF) | Casein peptide fragments with growth-influencing activity on cell cultures |
| CN105254714A (en) * | 2015-10-16 | 2016-01-20 | 中国农业大学 | Casein-derived antioxidant peptide and preparation method thereof |
| 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
- 2017-12-12 CN CN201711319330.7A patent/CN107892716A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002030958A2 (en) * | 2000-10-09 | 2002-04-18 | GESELLSCHAFT FüR BIOTECHNOLOGISCHE FORSCHUNG MBH (GBF) | Casein peptide fragments with growth-influencing activity on cell cultures |
| CN105254714A (en) * | 2015-10-16 | 2016-01-20 | 中国农业大学 | Casein-derived antioxidant peptide and preparation method thereof |
| 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 (2)
| Title |
|---|
| M. ALEXANDRA MONROY等: "SNF2-Related CBP Activator Protein (SRCAP) Functions as a Coactivator of Steroid Receptor-Mediated Transcription through Synergistic Interactions with CARM-1 and GRIP-1", 《MOLECULAR ENDOCRINOLOGY》 * |
| YAN JIN等: "Peptide profiling and the bioactivity character of yogurt in the simulated gastrointestinal digestion", 《JOURNAL OF PROTEOMICS》 * |
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Application publication date: 20180410 |