CN106632642B - A kind of turtle proteins peptide suppressed with ACE with anti-oxidation function and preparation method thereof - Google Patents
A kind of turtle proteins peptide suppressed with ACE with anti-oxidation function and preparation method thereof Download PDFInfo
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- CN106632642B CN106632642B CN201610866528.6A CN201610866528A CN106632642B CN 106632642 B CN106632642 B CN 106632642B CN 201610866528 A CN201610866528 A CN 201610866528A CN 106632642 B CN106632642 B CN 106632642B
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- 241000270666 Testudines Species 0.000 title claims abstract description 78
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 65
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 57
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- 230000003064 anti-oxidating effect Effects 0.000 title claims abstract description 22
- 238000002360 preparation method Methods 0.000 title claims abstract description 19
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- 108091005804 Peptidases Proteins 0.000 claims abstract description 29
- 238000000034 method Methods 0.000 claims abstract description 29
- 239000002002 slurry Substances 0.000 claims abstract description 23
- 150000001875 compounds Chemical class 0.000 claims abstract description 21
- 238000005238 degreasing Methods 0.000 claims abstract description 13
- 239000003513 alkali Substances 0.000 claims abstract description 11
- 239000007788 liquid Substances 0.000 claims abstract description 11
- 239000000047 product Substances 0.000 claims abstract description 11
- 239000006228 supernatant Substances 0.000 claims abstract description 10
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 10
- 235000013305 food Nutrition 0.000 claims abstract description 9
- 230000008569 process Effects 0.000 claims abstract description 9
- 239000002253 acid Substances 0.000 claims abstract description 6
- 230000033228 biological regulation Effects 0.000 claims abstract description 5
- 238000012545 processing Methods 0.000 claims abstract description 4
- 239000000706 filtrate Substances 0.000 claims abstract description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 8
- 235000019419 proteases Nutrition 0.000 claims description 28
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 27
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 20
- 241001482311 Trionychidae Species 0.000 claims description 15
- 235000013372 meat Nutrition 0.000 claims description 9
- 239000000796 flavoring agent Substances 0.000 claims description 7
- 235000019634 flavors Nutrition 0.000 claims description 7
- 108010004032 Bromelains Proteins 0.000 claims description 6
- 108090000526 Papain Proteins 0.000 claims description 6
- 235000019835 bromelain Nutrition 0.000 claims description 6
- 239000000499 gel Substances 0.000 claims description 6
- 229920005654 Sephadex Polymers 0.000 claims description 5
- 239000012507 Sephadex™ Substances 0.000 claims description 5
- 239000003814 drug Substances 0.000 claims description 5
- 239000003480 eluent Substances 0.000 claims description 5
- 235000019834 papain Nutrition 0.000 claims description 5
- 229940055729 papain Drugs 0.000 claims description 5
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- 229910021641 deionized water Inorganic materials 0.000 claims description 4
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- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 4
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- 238000010009 beating Methods 0.000 claims 1
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- -1 DPPH free radical Chemical class 0.000 description 4
- QIAFMBKCNZACKA-UHFFFAOYSA-N N-benzoylglycine Chemical compound OC(=O)CNC(=O)C1=CC=CC=C1 QIAFMBKCNZACKA-UHFFFAOYSA-N 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
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- 239000003651 drinking water Substances 0.000 description 4
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- 206010020772 Hypertension Diseases 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- GLEVLJDDWXEYCO-UHFFFAOYSA-N Trolox Chemical compound O1C(C)(C(O)=O)CCC2=C1C(C)=C(C)C(O)=C2C GLEVLJDDWXEYCO-UHFFFAOYSA-N 0.000 description 3
- ORWYRWWVDCYOMK-HBZPZAIKSA-N angiotensin I Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 ORWYRWWVDCYOMK-HBZPZAIKSA-N 0.000 description 3
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- 230000002000 scavenging effect Effects 0.000 description 3
- 101800000734 Angiotensin-1 Proteins 0.000 description 2
- 102400000344 Angiotensin-1 Human genes 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
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- 230000036772 blood pressure Effects 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
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- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 229910021642 ultra pure water Inorganic materials 0.000 description 2
- 239000012498 ultrapure water Substances 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- OCZVHBZNPVABKX-UHFFFAOYSA-N 1,1-diphenyl-2-(2,4,6-trinitrophenyl)hydrazine;ethanol Chemical compound CCO.[O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1NN(C=1C=CC=CC=1)C1=CC=CC=C1 OCZVHBZNPVABKX-UHFFFAOYSA-N 0.000 description 1
- LXEKPEMOWBOYRF-QDBORUFSSA-N AAPH Chemical compound Cl.Cl.NC(=N)C(C)(C)\N=N\C(C)(C)C(N)=N LXEKPEMOWBOYRF-QDBORUFSSA-N 0.000 description 1
- 102000005862 Angiotensin II Human genes 0.000 description 1
- 101800000733 Angiotensin-2 Proteins 0.000 description 1
- 108090001067 Angiotensinogen Proteins 0.000 description 1
- 102000004881 Angiotensinogen Human genes 0.000 description 1
- CZGUSIXMZVURDU-JZXHSEFVSA-N Ile(5)-angiotensin II Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C([O-])=O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=[NH2+])NC(=O)[C@@H]([NH3+])CC([O-])=O)C(C)C)C1=CC=C(O)C=C1 CZGUSIXMZVURDU-JZXHSEFVSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
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- 108010046377 Whey Proteins Proteins 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 229950006323 angiotensin ii Drugs 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 150000007516 brønsted-lowry acids Chemical class 0.000 description 1
- 150000007528 brønsted-lowry bases Chemical class 0.000 description 1
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- 238000004440 column chromatography Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000001877 deodorizing effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- MGJZITXUQXWAKY-UHFFFAOYSA-N diphenyl-(2,4,6-trinitrophenyl)iminoazanium Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1N=[N+](C=1C=CC=CC=1)C1=CC=CC=C1 MGJZITXUQXWAKY-UHFFFAOYSA-N 0.000 description 1
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- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000001573 invertase Substances 0.000 description 1
- 235000011073 invertase Nutrition 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 231100000957 no side effect Toxicity 0.000 description 1
- 238000013546 non-drug therapy Methods 0.000 description 1
- 238000011017 operating method Methods 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
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- 239000011780 sodium chloride Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 108010021724 tonin Proteins 0.000 description 1
- 235000021119 whey protein Nutrition 0.000 description 1
Classifications
-
- 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
- C07K14/463—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from amphibians
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Toxicology (AREA)
- General Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention provides a kind of turtle proteins peptide with ACE suppression and anti-oxidation function and preparation method thereof, belong to aquatic products food processing technology field.The preparation method of the turtle proteins peptide of the present invention includes：(1) the turtle slurries of degreasing are ultrasonically treated；(2) add compound protease and carry out two step method enzymolysis, enzymolysis process is without adding acid or alkali regulation pH value；(3) enzymolysis liquid is centrifuged and takes supernatant to pass through two step Treatment with Ultrafiltration；(4) filtrate crosses post separation, collects eluting peak, produces.The inventive method is simple to operate, suitable for industrialization production, preparation process does not add any additive without adding acid or alkali regulation pH value, preferably keeps the functional characteristic of product, product yield is high, there is excellent ACE to suppress function for raciness, obtained turtle proteins peptide, and IC50 is less than 0.4mg/mL, and there is preferable anti-oxidation function, it is widely used in special procuring the manufacture of food and nutraceutical.
Description
Technical field
The present invention relates to aquatic food processing technique field, has ACE suppression and anti-oxidation function more particularly to one kind
Turtle proteins peptide and preparation method thereof.
Background technology
Hypertension is that greatly a kind of disease, incubation period are grown to human health risk.The early stage of hypertension, does not have typically
Have significant discomfort disease, until occur clinical indication heart attack, rupture of blood vessel in brain and cause death.
Angiotensin converting enzyme (Angiotensin I converting enzyme, ACE) is renin-angiotensin
The key enzyme of prime system system.Proangiotensin is converted into angiotensin I in the presence of feritin, and angiotensin I is ACE's
Angiotensin II is converted under effect, vessel retraction is stimulated, causes blood pressure to rise.The activity for suppressing ACE has to reducing blood pressure
Positive effect, thus develops the very big concern that effective Vel-Tyr-Pro-Trp-Thr-Gln-Arg-Phe causes people.Although food-based ACE suppressions
Peptide processed is weaker than artificial synthesized Vel-Tyr-Pro-Trp-Thr-Gln-Arg-Phe effect, but it has the advantages of its is unique, will not produce the problem of decompression is excessive,
It is safe, have no side effect, in addition to buck functionality, often there is the functions such as Immune enhancement, absorption easy to digest simultaneously.Due to medicine
There is side effect in therapy, the utilization of the blood pressure-lowering functional factor in natural food will turn into hypertension non-drug therapy from now on
Pith.
Report on ace inhibitory peptide exploitation in the prior art, mainly by the method for enzymolysis from aquatic livestock body or
Milk whey protein source obtains ace inhibitory peptide, and enzymolysis process is generally required for by adding acid or alkali come the pH value of regulation system,
This undoubtedly have impact on the functional characteristic of the ace inhibitory peptide product of acquisition, and add the fussy degree of operation；ACE suppressions also
The preparation method of peptide processed also has de- bitter the step of deodorizing after enzymolysis, to improve the unpalatable taste such as the fishy smell of aquatic livestock,
These methods add operating procedure and production cost to some extent, constrain the life of industrialized scale ace inhibitory peptide
Production and the yield of protein peptides.On the other hand, what prior art obtained from aquatile there is ACE to suppress the peptide of function often only
Suppress function with ACE, find no other bioactive functions, i.e. properties of product are single.
Have no the patent text that inhibiting peptide of tonin is prepared using turtle resource in patent both at home and abroad at present
Offer report.The present invention is directed to the present situation of current turtle proteins product development, is raw material using turtle, by surpassing to turtle
Sound wave etc. pre-processes, and under the conditions of any bronsted lowry acids and bases bronsted lowry is not added, using multiple protein enzyme complex enzyme hydrolysis, passes through UF membrane and gel
Isolation technics, develop while there is the turtle proteins peptide of specific decompression and anti-oxidation function, establish a set of simple efficient more
The preparation method of the turtle proteins peptide of function.
The content of the invention
In view of the shortcomings of the prior art, the purpose of the present invention is to be that providing one kind has ACE suppression and anti-oxidation function
Turtle proteins peptide.
Another object of the present invention is to provide the preparation method of above-mentioned turtle proteins peptide.
It is yet a further object of the present invention to provide the application of above-mentioned turtle proteins peptide.
In order to realize above-mentioned technical purpose, the invention provides a kind of soft-shelled turtle egg with ACE suppression and anti-oxidation function
White peptide and preparation method thereof, comprises the following steps:
(1) the turtle slurries of degreasing are ultrasonically treated；
(2) add compound protease and carry out two step method enzymolysis, enzymolysis process is without adding acid or alkali regulation pH value；
(3) enzymolysis liquid is centrifuged and takes supernatant to pass through two step Treatment with Ultrafiltration；
(4) filtrate crosses column chromatography for separation, collects eluting peak, produces.
Turtle slurries described in step (1) obtain in the following manner：Fresh soft-shelled turtle bloodletting is slaughtered, and takes turtle, is used
Meet the clean water cleaning of sanitary standard for drinking water, 5-10 minutes are incubated in 95 DEG C of water after flesh of fish cleaning, then in turtle
The middle water for adding 2.0~4.0 times, slurry is broken into beater by turtle, is centrifuged 10~15min by 6000~8000g, is gone
Layer fat, obtains the soft-shelled turtle flesh of fish slurries of degreasing.
Wherein, step (1) ultrasonic processing method is that the turtle slurry temperature of degreasing is adjusted into 55-65 DEG C, 25-30kH's
Supersonic frequency handles 15-25min.
The present invention has found that turtle slurry temperature is adjusted to 55-65 DEG C and is ultrasonically treated, and effect is most by many experiments
It is good, it can preferably change the institutional framework of soft-shelled turtle meat albumen, following enzymolysis step is shortened enzymolysis time and less is used enzyme
Amount, it becomes possible to obtain high-quality protein peptides.
The above method the step of in (2) two step method enzymolysis, the compound protease that first step enzymolysis adds is basic protein
Enzyme and bromelain, the two mass ratio are 1-2:1, and the compound protease quality added is the 0.1%- of soft-shelled turtle meat quality
0.3%.
Preferably, first step enzymatic hydrolysis condition is 55-65 DEG C of enzymolysis 1-2h.
The above method the step of in (2) two step method enzymolysis, the compound protease that second step enzymolysis adds is Papain
Enzyme and flavor protease, the two mass ratio are 1:1-2, and the compound protease quality added is the 0.1%- of soft-shelled turtle meat quality
0.3%.
Preferably, second step enzymatic hydrolysis condition is 50-60 DEG C of enzymolysis 1-2h.
Second step enzymolysis end after being incubated 3-5min at 90-95 DEG C, be cooled to room temperature.
In the above method, two step ultrafiltrations of step (3) are to be first more than 5000D film ultrafiltration with aperture, then with aperture
3000D film ultrafiltration, obtain the protein peptides that molecular weight is less than 3000D.
In an embodiment of the present invention, two step ultrafiltrations are using the ceramic membrane ultrafitration that aperture is 10000 dalton, first will
Albumen of the molecular weight less than 10000 and peptide separation are come out, then molecular weight is less than into 3000 for the film of 3000 dalton with aperture
The protein peptides of dalton are separated.
The preparation method step (4) of turtle proteins peptide of the present invention, it is to take molecular weight as the protein peptides liquid less than 3000, then passes through
Gel separation is crossed, collects eluting peak；By concentrating, being freeze-dried, it is to have preferable blood vessel tight less than 3000D to obtain molecular weight
Open the turtle protein peptides of plain invertase (ACE) suppression and anti-oxidation function.
In an embodiment of the present invention, it is to take molecular weight to be coagulated for the protein peptides liquid less than 3000 by Sephadex G-25
Glue is separated, and eluent is deionized water, flow velocity 1.8-2.8mL/min, and eluting peak is detected under 280nm, collects the 2nd
Eluting peak；By concentrating, being freeze-dried, it is to have preferable angiotensin converting enzyme (ACE) suppression less than 3000 to obtain molecular weight
The turtle protein peptides of system and anti-oxidation function.
The turtle proteins peptide that above-mentioned preparation method is prepared belongs to protection scope of the present invention.The present invention is sent out by testing
Existing, the turtle proteins peptide that the above method of the present invention is prepared has excellent ACE suppression and anti-oxidation function.
And then the application the invention provides the turtle proteins peptide in hypotensive or anti-oxidation medicine is prepared.Contain this
The food of turtle proteins peptide, health products or medicine fall within protection scope of the present invention made from inventive method.
The advantage of the invention is that：
(1) the turtle protein peptides preparation method that the present invention develops is simple, without addition acid or alkali in whole process
PH adjustment is carried out, product keeps preferable functional characteristic, is easier to realize industrialization production.
(2) protein peptides of exploitation have the function of preferable angiotensin converting enzyme (ACE) activity suppression, its IC 50
It is worth and reaches more than 90% for the ACE inhibiting rates less than 0.4mg/mL, 1.2mg/mL sample concentrations, while has preferably anti-oxidant
Function.The manufacture of food and nutraceutical can be widely used in special procuring.
(3) present invention, can using the turtle protein milk of specific frequency ultrasonic technology processing certain temperature (55-65 DEG C)
To be obviously improved the structure of soft-shelled turtle meat albumen, shorten enzymolysis time, improve the function of turtle protein peptides and the yield of product.
(4) the turtle proteins peptide edible safety that the inventive method is prepared, the present invention use the compound egg of numerous food level
White enzyme (alkali protease, bromelain, papain and flavor protease), through in a mild condition, by appropriate enzyme
Solution obtains the turtle protein peptides of specified molecular weight, is not added with any additive, is 100% turtle protein peptides, product has good
Good flavor, higher yield.
(5) ratio of peptide of the present invention exploitation turtle proteins peptide middle-molecular-weihydroxyethyl less than 1000D is more than 90%, is easy to body
Digestion and absorption.
Embodiment
Unless otherwise defined, the implication that all technical terms used hereinafter are generally understood that with those skilled in the art
It is identical.Technical term used herein is intended merely to describe the purpose of specific embodiment, is not intended to the limitation present invention
Protection domain.
Except there is a special instruction, the various reagents used in the present invention, raw material be can be commercially commodity or
Person can pass through product made from known method.
There is embodiment 1 ACE to suppress the preparation method with the turtle protein peptides of anti-oxidation function
(1) 100 grams of turtle is taken, is cleaned with the clean water for meeting sanitary standard for drinking water, in 95 DEG C of water after flesh of fish cleaning
Middle insulation 10 minutes, 2.0 times of 200 grams of water is then added in turtle, turtle is broken into slurry with beater, passed through
6000g centrifuges 10min, goes upper-layer fat, obtains the soft-shelled turtle flesh of fish slurries of degreasing.
(2) temperature of degreasing turtle slurries is adjusted to 55 DEG C, is through ultrasonic frequency in supersonic generator
30kH is handled 15 minutes, changes the institutional framework of soft-shelled turtle meat albumen.
(3) according to the percentage by weight ratio of turtle weight 0.3% to the turtle slurries body being ultrasonically treated
It is middle addition compound protease carry out stepwise discretization, the first step add compound protease one (alkali protease and bromelain composition,
Mass ratio between them is 1：1) 0.2%, enzymolysis 2h is carried out under the conditions of 60 DEG C；Then carry out second step and utilize compound protein
(papain and flavor protease composition, the mass ratio between them are 1 to enzyme two：2) 0.1%, carried out under the conditions of 55 DEG C
Enzyme digestion reaction 1.5h；3 minutes are incubated at 95 DEG C, is cooled to room temperature, 15min is centrifuged under the conditions of 4000g, collects supernatant.
(4) supernatant obtained by step (3) is handled by two step hyperfiltration process, is 10000 dongles using aperture
Ceramic membrane ultrafitration, first take and come out albumen of the molecular weight less than 10000 and peptide separation, then with aperture be 3000 dalton
Film by molecular weight be less than 3000 dalton protein peptides separate.
(5) molecular weight is taken to be separated for the protein liquid less than 3000, then by Sephadex G-25 gels, eluent is to go
Ionized water, flow velocity 2.0mL/min, eluting peak are detected under 280nm, collect the 2nd eluting peak；By concentrating, freezing
Dry, obtain molecular weight as the turtle protein peptides less than 3000D.
There is embodiment 2 angiotensin converting enzyme to suppress the preparation method with the turtle protein peptides of anti-oxidation function
(1) 500 grams of turtle is taken, is cleaned with the clean water for meeting sanitary standard for drinking water, in 90 DEG C of water after flesh of fish cleaning
Middle insulation 8 minutes, 3.0 times of water is then added in turtle, turtle is broken into slurry with beater, centrifuged by 7000g
10min, upper-layer fat is gone, obtain the soft-shelled turtle flesh of fish slurries of degreasing.
(2) temperature of degreasing turtle slurries is adjusted to 60 DEG C, (frequency is through ultrasonic wave in supersonic generator
25kH) handle 25 minutes, change the institutional framework of soft-shelled turtle meat albumen.
(3) according to the percentage by weight ratio of turtle weight 0.2% to the turtle slurries body being ultrasonically treated
Middle addition compound protease progress stepwise discretization, first step addition protease one (alkali protease and bromelain composition, it
Between mass ratio be 1：1) 0.1%, enzyme digestion reaction 2h is carried out under the conditions of 65 DEG C；Then carry out second step and add compound egg
(papain and flavor protease composition, the mass ratio between them are 1 to white enzyme two：1) 0.1%, enter under the conditions of 60 DEG C
Row enzyme digestion reaction 2h；3~5 minutes are incubated at 90 DEG C, is cooled to room temperature, 15min is centrifuged under the conditions of 3500g, collects supernatant
Liquid.
(4) supernatant obtained by step (3) is handled by two step hyperfiltration process, is 10000 dongles using aperture
Ceramic membrane ultrafitration, first take and come out albumen of the molecular weight less than 10000 and peptide separation, then with aperture be 3000 dalton
Film by molecular weight be less than 3000 dalton protein peptides separate.
(5) molecular weight is taken to be separated for the protein liquid less than 3000, then by Sephadex G-25 gels, eluent is to go
Ionized water, flow velocity 2.0mL/min, eluting peak are detected under 280nm, collect the 2nd eluting peak；By concentrating, freezing
Dry, obtain molecular weight as the turtle protein peptides less than 3000D.
There is embodiment 3 angiotensin converting enzyme to suppress the preparation method with the turtle protein peptides of anti-oxidation function
(1) 1000 grams of turtle is taken, is cleaned with the clean water for meeting sanitary standard for drinking water, in 95 DEG C of water after flesh of fish cleaning
Middle insulation 10 minutes, 2.5 times of 2500 grams of water is then added in turtle, turtle is broken into slurry with beater, passed through
7000g centrifuges 12min, goes upper-layer fat, obtains the soft-shelled turtle flesh of fish slurries of degreasing.
(2) temperature of degreasing turtle slurries is adjusted to 65 DEG C, is through ultrasonic frequency in supersonic generator
30kH is handled 15 minutes, changes the institutional framework of soft-shelled turtle meat albumen.
(3) according to the percentage by weight ratio of turtle weight 0.4% to the turtle slurries body being ultrasonically treated
It is middle addition compound protease carry out stepwise discretization, the first step add compound protease one (alkali protease and bromelain composition,
Mass ratio between them is 2：1) 0.2%, enzymolysis 1.5h is carried out under the conditions of 60 DEG C；Then second step adds turtle weight
(papain and flavor protease composition, the mass ratio between them are 1 to 0.2% compound protease two：1), in 55 DEG C of bars
Enzyme digestion reaction 1.5h is carried out under part；3 minutes are incubated at 92 DEG C, room temperature is cooled to, 13min is centrifuged under the conditions of 4000g, is collected
Supernatant.
(4) supernatant obtained by step (3) is handled by two step hyperfiltration process, is 10000 dongles using aperture
Ceramic membrane ultrafitration, first take and come out albumen of the molecular weight less than 10000 and peptide separation, then with aperture be 3000 dalton
Film by molecular weight be less than 3000 dalton protein peptides separate.
(5) molecular weight is taken to be separated for the protein liquid less than 3000, then by Sephadex G-25 gels, eluent is to go
Ionized water, flow velocity 2.5mL/min, eluting peak are detected under 280nm, collect the 2nd eluting peak；By concentrating, freezing
Dry, obtain molecular weight as the turtle protein peptides less than 3000D.
The determination test of embodiment 4 turtle protein peptides angiotensin converting enzyme (ACE) rejection ability
Test specimen：Turtle protein peptides ACE rejection abilities prepared by embodiment 1, embodiment 2, embodiment 3 are according to as follows
Method is carried out：
The method of ACE inhibiting rates.The Hip amounts discharged can be quantitatively detected under 228nm with high performance liquid chromatography, so as to
Calculate the ACE inhibiting rates of polypeptide.
1) configuration of reagent
PH8.3 phosphate buffer solution：Prepared with ultra-pure water, wherein phosphate-containing 50mmol/L, NaCl 300mmol/
L, adjust pH to 8.3；
ACE enzyme liquids：2mL phosphate buffer is added in 1U ACE, its concentration is changed into 0.5U/mL.
HHL solution：HHL is dissolved using phosphate buffer, makes its final concentration of 5mmol/L.
Sample solution：Appropriate amount of sample is weighed, the solution of concentration needed for phosphate buffer.
2) chromatographic condition of ACE inhibiting rates measure
Detection wavelength：228nm；Flow velocity:1mL/min；Mobile phase A:Ultra-pure water (contains 0.1% trifluoroacetic acid), Mobile phase B:
Methanol (contains 0.1% trifluoroacetic acid)；Sample size:10 μ L, hand sampling；
3) method for determining ACE inhibitory activity
120 μ L HHL substrate solutions are taken, the sample for adding 20 μ L is well mixed, and 10min is incubated in 37 DEG C of waters bath with thermostatic control.
Then 10 μ L ACE enzyme liquids are added and react 30min in 37 DEG C of waters bath with thermostatic control, the HCl for adding 150 μ L 1mol/L is terminated instead
Should, obtain reaction solution.The reaction solution is analyzed using HPLC, while sets blank control group.ACE inhibitory activity calculation formula
It is as follows：
ACE inhibitory activity %=(M-N)/M × 100,
In formula, M is the peak area of hippuric acid in control group, and N is the peak area of hippuric acid in the sample sets added.
4) measure of 503nhibiting concentration
Its inhibitory activity is determined according to ace inhibitory peptide external detection method, using concentration as abscissa, ACE inhibiting rates are vertical
Coordinate plots round and smooth curve, and IC50 values are calculated from curve.It the results are shown in Table 1.
The determination test of the turtle protein antioxidant activity of the present invention of embodiment 5
Test specimen：Turtle protein antioxidation active peptide prepared by embodiment 1, embodiment 2, embodiment 3.
Carry out as follows：
(1) scavenging ability of DPPH free radical：1mg/mL antioxidation active peptides 1.5mL is taken, adds 99.5% ethanol 1.5mL
Mixed with 0.02%DPPH ethanol solutions 0.675mL, vibration is mixed, and lucifuge water-bath 30min, is then examined under 517nm at room temperature
Survey system light absorption value.Light absorption value is lower, and the scavenging ability of DPPH free radical of system is stronger.Blank control is by sample solution
1.5mL changes deionized water 1.5mL into.
DPPH radical scavenging activities %=((blank absorbency-sample light absorption value)/blank absorbency) × 100.As a result
It is shown in Table 1.
(2) reducing power determines：1mg/mL antioxidation active peptides 1mL is taken, adds 0.2M phosphate buffers (pH 6.6)
2.5mL and 1% (mass fraction) potassium ferricyanide solution 2.5mL, mix, then in 50 DEG C of heating water bath 20min.Take out rapid
Cooling, 10% (mass fraction) trichloroacetic acid (TCA) solution 2.5mL is added, be well mixed, then centrifuged under 3000g
10min.Supernatant 2.5mL is taken, adds deionized water 2.5mL and 1% (mass fraction) liquor ferri trichloridi 0.5mL, it is fully mixed
It is even, 10min is reacted at room temperature, and absorbance is determined with 700nm wavelength.Light absorption value represents at the i.e. available 700nm wavelength of reducing power.
It the results are shown in Table 1.
(3) oxyradical absorbability (ORAC)：The μ L of antioxidation activity peptide solution 20 of various concentrations and 75mM phosphoric acid
The μ L (pH 7.4) and 200nM of the salt buffer 80 μ L of fluorometric reagent 50 are sufficiently mixed, and are then incubated 15min at 37 DEG C, are added
The 80mM μ L of AAPH solution 50.100min is carried out altogether with the ELIASA fluorescent value per minute that reads.The excitation wavelength of fluorescence and transmitting
Wavelength is 485nm and 538nm respectively.By the use of phosphate buffer solution blank is used as instead of sample.Using Trolox as standard control, make
Concentration is 0,2,4,8,12,16 μM, draws fluorescent quenching curve, and calculate the integral area under fluorescent quenching curve
(AUC).AUC calculation formula is as follows：
Wherein：Fluorescent value when f0 is 0min, fluorescent value when fi is the i-th min.
The ratio between slope and Trolox slope of a curves of ORAC value sample curves, ORAC are worth unit to be expressed as μM
Trolox/mg peptides.
The molecular weight of turtle proteins peptide and angiotensin converting enzyme (ACE) suppression made from three embodiments of the invention of table 1
System and antioxidant activity tests result
As a result (being shown in Table 1), turtle proteins peptide of the present invention has good angiotensin converting enzyme (ACE) rejection ability ACE
Inhibitory activity (IC50Value) it is less than 0.35mg/mL, the IC of substantially less than similar compound protein peptide50Value, 1.2mg/mL samples ACE suppressions
Rate processed reaches more than 90%, has good angiotensin converting enzyme (ACE) rejection ability.Invention turtle proteins peptide tool simultaneously
Have with preferable oxidation resistance, under conditions of 1mgg/mL, its scavenging ability of DPPH free radical reaches more than 89%, also
Former power reaches more than 0.87, and its ORAC is more than 16, and a kind of preferable anti-oxidation peptide.
Embodiment above is only that the preferred embodiment of the present invention is described, and not the scope of the present invention is entered
Row limits, on the premise of design spirit of the present invention is not departed from, technical side of this area ordinary skill technical staff to the present invention
The all variations and modifications that case is made, it all should fall into the protection domain of claims of the present invention determination.
Claims (5)
1. a kind of preparation method suppressed with ACE with the turtle proteins peptide of anti-oxidation function, it is characterised in that including following step
Suddenly：
(1) the turtle slurries of degreasing are ultrasonically treated；Described be ultrasonically treated is that the turtle slurry temperature of degreasing is adjusted into 55-65
DEG C, 25-30kH supersonic frequency processing 15-25min；The turtle slurries of the degreasing are that water is added in turtle, with beating
Turtle is broken into slurry by pulp grinder, and centrifugation goes upper-layer fat to obtain；
(2) add compound protease and carry out two step method enzymolysis, enzymolysis process is without adding acid or alkali regulation pH value；The two step method
Enzymolysis, the compound protease that first step enzymolysis adds is alkali protease and bromelain, and the two mass ratio is 1-2:1, and
The compound protease quality of addition is the 0.1%-0.3% of soft-shelled turtle meat quality；First step enzymatic hydrolysis condition is 55-65 DEG C of enzymolysis 1-
2h；
The compound protease that second step enzymolysis adds is papain and flavor protease, and the two mass ratio is 1:1-2, and add
The compound protease quality entered is the 0.1%-0.3% of soft-shelled turtle meat quality；Second step enzymatic hydrolysis condition is 50-60 DEG C of enzymolysis 1-2h；
(3) enzymolysis liquid is centrifuged and takes supernatant to pass through two step Treatment with Ultrafiltration；The two steps ultrafiltration is first to be more than with aperture
5000D film ultrafiltration, then with the film ultrafiltration that aperture is 3000D, obtain the protein peptides that molecular weight is less than 3000D；
(4) filtrate separates by Sephadex G-25 gels, and eluent is deionized water, flow velocity 1.8-2.8mL/min, is washed
De- peak is detected under 280nm, is collected the 2nd eluting peak and is produced.
2. preparation method according to claim 1, it is characterised in that：Second step enzymolysis after being incubated 3- at 90-95 DEG C
5min, it is cooled to room temperature.
3. the turtle proteins peptide that the preparation method according to claim any one of 1-2 is prepared.
4. application of the turtle proteins peptide in hypotensive or anti-oxidation medicine is prepared described in claim 3.
5. contain the food of turtle proteins peptide, health products or medicine described in claim 3.
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| CN107245094B (en) * | 2017-06-23 | 2020-08-18 | 广东华肽生物科技有限公司 | Antioxidant peptide and separation preparation method and application thereof |
| CN108178785A (en) * | 2017-12-28 | 2018-06-19 | 澳优乳业（中国）有限公司 | A kind of sheep whey protein peptide with ACE inhibition and its application |
| CN108358994B (en) * | 2018-02-08 | 2021-09-28 | 广西大学 | Angiotensin converting enzyme inhibitory peptide extracted from carapax Trionycis and its preparation method |
| CN108251484B (en) * | 2018-03-21 | 2021-02-19 | 杭州早稻田生物技术有限公司 | Soft-shelled turtle active peptide protein powder and preparation method thereof |
| CN111777679A (en) * | 2019-04-04 | 2020-10-16 | 福建鼍龙实业有限责任公司 | Crocodile bone glue polypeptide and preparation method and application thereof |
| CN110122785A (en) * | 2019-05-17 | 2019-08-16 | 中国科学院理化技术研究所 | A kind of preparation method of soft-shelled turtle hydrolyzing composition |
| CN110577579A (en) * | 2019-07-31 | 2019-12-17 | 浙江树人学院（浙江树人大学） | turtle protein source with ACE (angiotensin converting enzyme) inhibitory active peptide AIMAG and application |
| CN110498837A (en) * | 2019-07-31 | 2019-11-26 | 浙江省农业科学院 | Turtle proteins source has ACE inhibitory activity peptide HQTWTKVHF and purposes |
| CN110540576B (en) * | 2019-09-04 | 2021-10-08 | 安徽国肽生物科技有限公司 | Algae protein peptide with ACE (angiotensin converting enzyme) inhibition and antioxidation functions and preparation method thereof |
| CN110467649A (en) * | 2019-09-12 | 2019-11-19 | 浙江省农业科学院 | A kind of active polypeptide QEIP of inhibition Angiotensin-Converting and its application |
| CN110467653B (en) * | 2019-09-12 | 2021-01-08 | 浙江省农业科学院 | Polypeptide for inhibiting angiotensin converting enzyme activity and application thereof |
| CN110607288A (en) * | 2019-09-30 | 2019-12-24 | 浙江省农业科学院 | Turtle protein source with ACE inhibitory active peptide AGMPRRYSDYP and application thereof |
| CN110845576A (en) * | 2019-09-30 | 2020-02-28 | 浙江树人学院（浙江树人大学） | Turtle protein source with ACE inhibitory active peptide HDTYYVVAH and application thereof |
| CN114711324A (en) * | 2021-02-04 | 2022-07-08 | 云南海王水产有限公司 | Fish scale collagen peptide with probiotic growth promoting and antioxidant effects and preparation method thereof |
| CN114468311B (en) * | 2022-03-24 | 2023-12-29 | 上海市农业科学院 | Stropharia rugoso-annulata flavor active peptide base material and preparation method and application thereof |
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| CN104558115A (en) * | 2014-12-29 | 2015-04-29 | 浙江海洋学院 | Antioxidant polypeptide with Raja porosa meat protein as well as preparation method and application of antioxidant polypeptide |
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| CN104558115A (en) * | 2014-12-29 | 2015-04-29 | 浙江海洋学院 | Antioxidant polypeptide with Raja porosa meat protein as well as preparation method and application of antioxidant polypeptide |
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