CN110144377A - A kind of preparation method of shellfish high F value oligopeptide - Google Patents
A kind of preparation method of shellfish high F value oligopeptide Download PDFInfo
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- CN110144377A CN110144377A CN201910634784.6A CN201910634784A CN110144377A CN 110144377 A CN110144377 A CN 110144377A CN 201910634784 A CN201910634784 A CN 201910634784A CN 110144377 A CN110144377 A CN 110144377A
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- 238000002360 preparation method Methods 0.000 title claims abstract description 53
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 43
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 43
- 235000015170 shellfish Nutrition 0.000 title claims abstract description 36
- -1 aromatic amino acid Chemical class 0.000 claims abstract description 30
- 239000007788 liquid Substances 0.000 claims abstract description 13
- 235000013372 meat Nutrition 0.000 claims abstract description 11
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 75
- 230000016507 interphase Effects 0.000 claims description 74
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 30
- 102000004190 Enzymes Human genes 0.000 claims description 20
- 108090000790 Enzymes Proteins 0.000 claims description 20
- 239000002002 slurry Substances 0.000 claims description 20
- 229920000344 molecularly imprinted polymer Polymers 0.000 claims description 16
- 238000003756 stirring Methods 0.000 claims description 16
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 15
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 claims description 15
- PIICEJLVQHRZGT-UHFFFAOYSA-N Ethylenediamine Chemical compound NCCN PIICEJLVQHRZGT-UHFFFAOYSA-N 0.000 claims description 15
- BAPJBEWLBFYGME-UHFFFAOYSA-N Methyl acrylate Chemical class COC(=O)C=C BAPJBEWLBFYGME-UHFFFAOYSA-N 0.000 claims description 15
- 238000006845 Michael addition reaction Methods 0.000 claims description 15
- 229910052757 nitrogen Inorganic materials 0.000 claims description 15
- 239000000047 product Substances 0.000 claims description 13
- 230000009435 amidation Effects 0.000 claims description 12
- 238000007112 amidation reaction Methods 0.000 claims description 12
- 230000017854 proteolysis Effects 0.000 claims description 12
- 238000006116 polymerization reaction Methods 0.000 claims description 11
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 10
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 10
- 239000000654 additive Substances 0.000 claims description 10
- 230000000996 additive effect Effects 0.000 claims description 10
- 230000009849 deactivation Effects 0.000 claims description 10
- 230000007062 hydrolysis Effects 0.000 claims description 10
- 238000006460 hydrolysis reaction Methods 0.000 claims description 10
- 239000005457 ice water Substances 0.000 claims description 10
- 239000000178 monomer Substances 0.000 claims description 10
- 239000002904 solvent Substances 0.000 claims description 10
- 239000006228 supernatant Substances 0.000 claims description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 10
- 239000003463 adsorbent Substances 0.000 claims description 9
- 150000002171 ethylene diamines Chemical class 0.000 claims description 9
- HFBMWMNUJJDEQZ-UHFFFAOYSA-N acryloyl chloride Chemical compound ClC(=O)C=C HFBMWMNUJJDEQZ-UHFFFAOYSA-N 0.000 claims description 8
- 239000003999 initiator Substances 0.000 claims description 8
- 238000006482 condensation reaction Methods 0.000 claims description 7
- 238000004090 dissolution Methods 0.000 claims description 7
- 230000007071 enzymatic hydrolysis Effects 0.000 claims description 7
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 7
- OZAIFHULBGXAKX-UHFFFAOYSA-N 2-(2-cyanopropan-2-yldiazenyl)-2-methylpropanenitrile Chemical group N#CC(C)(C)N=NC(C)(C)C#N OZAIFHULBGXAKX-UHFFFAOYSA-N 0.000 claims description 5
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 5
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 5
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 5
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 5
- 150000001413 amino acids Chemical class 0.000 claims description 5
- 238000007098 aminolysis reaction Methods 0.000 claims description 5
- 238000006243 chemical reaction Methods 0.000 claims description 5
- 238000009833 condensation Methods 0.000 claims description 5
- 230000005494 condensation Effects 0.000 claims description 5
- 238000006392 deoxygenation reaction Methods 0.000 claims description 5
- 235000019441 ethanol Nutrition 0.000 claims description 5
- 125000005395 methacrylic acid group Chemical group 0.000 claims description 5
- 229940087646 methanolamine Drugs 0.000 claims description 5
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 5
- 238000010992 reflux Methods 0.000 claims description 5
- 239000013049 sediment Substances 0.000 claims description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 5
- 238000001291 vacuum drying Methods 0.000 claims description 5
- 241001441955 Argopecten irradians Species 0.000 claims description 3
- 241000237516 Mizuhopecten yessoensis Species 0.000 claims description 3
- 101710118538 Protease Proteins 0.000 claims description 3
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 claims description 2
- 125000003647 acryloyl group Chemical group O=C([*])C([H])=C([H])[H] 0.000 claims description 2
- 239000000460 chlorine Substances 0.000 claims description 2
- 229910052801 chlorine Inorganic materials 0.000 claims description 2
- 238000002604 ultrasonography Methods 0.000 claims description 2
- 238000013019 agitation Methods 0.000 claims 1
- 125000003118 aryl group Chemical group 0.000 claims 1
- 208000019423 liver disease Diseases 0.000 abstract description 3
- 239000000843 powder Substances 0.000 abstract description 2
- 239000002994 raw material Substances 0.000 abstract description 2
- 238000004140 cleaning Methods 0.000 abstract 1
- 235000005911 diet Nutrition 0.000 abstract 1
- 230000000378 dietary effect Effects 0.000 abstract 1
- 238000004108 freeze drying Methods 0.000 abstract 1
- 239000004615 ingredient Substances 0.000 abstract 1
- 238000004519 manufacturing process Methods 0.000 abstract 1
- 239000000463 material Substances 0.000 abstract 1
- 108091005804 Peptidases Proteins 0.000 description 9
- 239000004365 Protease Substances 0.000 description 9
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 9
- 238000000034 method Methods 0.000 description 6
- 241000555268 Dendroides Species 0.000 description 4
- 238000010521 absorption reaction Methods 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000000796 flavoring agent Substances 0.000 description 4
- 235000019634 flavors Nutrition 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000004821 distillation Methods 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 238000001179 sorption measurement Methods 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 241001526627 Azumapecten farreri Species 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000000227 grinding Methods 0.000 description 2
- 208000007386 hepatic encephalopathy Diseases 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 201000011252 Phenylketonuria Diseases 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 241000219000 Populus Species 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002929 anti-fatigue Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 150000005693 branched-chain amino acids Chemical class 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 150000004985 diamines Chemical class 0.000 description 1
- 235000021245 dietary protein Nutrition 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/22—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising organic material
- B01J20/26—Synthetic macromolecular compounds
- B01J20/268—Polymers created by use of a template, e.g. molecularly imprinted polymers
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08F—MACROMOLECULAR COMPOUNDS OBTAINED BY REACTIONS ONLY INVOLVING CARBON-TO-CARBON UNSATURATED BONDS
- C08F2/00—Processes of polymerisation
- C08F2/46—Polymerisation initiated by wave energy or particle radiation
- C08F2/48—Polymerisation initiated by wave energy or particle radiation by ultraviolet or visible light
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08F—MACROMOLECULAR COMPOUNDS OBTAINED BY REACTIONS ONLY INVOLVING CARBON-TO-CARBON UNSATURATED BONDS
- C08F290/00—Macromolecular compounds obtained by polymerising monomers on to polymers modified by introduction of aliphatic unsaturated end or side groups
- C08F290/02—Macromolecular compounds obtained by polymerising monomers on to polymers modified by introduction of aliphatic unsaturated end or side groups on to polymers modified by introduction of unsaturated end groups
- C08F290/06—Polymers provided for in subclass C08G
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08G—MACROMOLECULAR COMPOUNDS OBTAINED OTHERWISE THAN BY REACTIONS ONLY INVOLVING UNSATURATED CARBON-TO-CARBON BONDS
- C08G73/00—Macromolecular compounds obtained by reactions forming a linkage containing nitrogen with or without oxygen or carbon in the main chain of the macromolecule, not provided for in groups C08G12/00 - C08G71/00
- C08G73/02—Polyamines
- C08G73/028—Polyamidoamines
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J9/00—Working-up of macromolecular substances to porous or cellular articles or materials; After-treatment thereof
- C08J9/26—Working-up of macromolecular substances to porous or cellular articles or materials; After-treatment thereof by elimination of a solid phase from a macromolecular composition or article, e.g. leaching out
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- 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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- C08J2201/00—Foams characterised by the foaming process
- C08J2201/04—Foams characterised by the foaming process characterised by the elimination of a liquid or solid component, e.g. precipitation, leaching out, evaporation
- C08J2201/042—Elimination of an organic solid phase
- C08J2201/0424—Elimination of an organic solid phase containing halogen, nitrogen, sulphur or phosphorus atoms
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- C08J2351/00—Characterised by the use of graft polymers in which the grafted component is obtained by reactions only involving carbon-to-carbon unsaturated bonds; Derivatives of such polymers
- C08J2351/08—Characterised by the use of graft polymers in which the grafted component is obtained by reactions only involving carbon-to-carbon unsaturated bonds; Derivatives of such polymers grafted on to macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
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Abstract
The invention discloses a kind of preparation methods of shellfish high F value oligopeptide, comprising the following steps: is homogenized after cleaning shellfish meat, is then digested, obtains upper layer enzymolysis liquid.Molecular engram material is prepared with dendritic, the aromatic amino acid in enzymolysis liquid is adsorbed, obtains high F value oligopeptide solution, high F value oligopeptide powder is prepared using freeze-drying.Product of the present invention raw material is easy to get and inexpensively, and preparation method is simple, is convenient for industrialized production, 75% or more product yield, and 50 or more F value can be used as the dietary source ingredient of hepatopathy patients.
Description
Technical field
The present invention relates to biological peptide preparation fields, and in particular to a kind of preparation method of shellfish high F value oligopeptide.
Background technique
High F value oligopeptides is that protease acts on a kind of low molecular weight physiologically active peptide formed after food protein, by propping up
Chain amino acid content height and aromatic amino acid content it is low special acid composition.F value (Fischer ratio), is branch
The molal quantity ratio of amino acid and aromatic amino acid content.It is generally believed that the high F value for clinical treatment hepatic encephalopathy is few
The F value of peptide should be greater than 20.
F value is 3.0-3.5 in the blood of normal person, and the F value with liver diseases patient only has 1.0 or lower.
For hepatopath, plasma F value can reflect out the severity of patient's hepatopathy.High F value oligopeptides can be used for preventing
The generation of hepatic encephalopathy slows down its symptom, while improving the nutrition condition of patient again.High F value oligopeptides also have provide energy,
It is antifatigue, improve after operation and the nutrient protein situation of bed patient, the effect for treating phenylketonuria, sought in medicine with clinical
Feeding aspect receives significant attention.
The high F value oligopeptide mixed liquor of enzymatic isolation method preparation contains largely free aromatic amino acid, carries out de- virtue to oligopeptides liquid
Processing, could improve the F value of oligopeptides.Currently used high F value method mainly has absorption method and is separated by filtration method.Domestic high F
Value processing mainly uses active carbon adsorption, and this method is at low cost, is very suitable to industrial applications, but active carbon is to fragrance
The absorption of race's amino acid does not have specificity, can not only remove aromatic amino acid, can adsorb yet and exist comprising branched-chain amino acid
Interior other amino acid, it is difficult to reach ideal adsorption effect, it is undesirable and unstable to the promotion effect of F value, to raw material and
Enzymolysis process is more demanding.
Summary of the invention
The present invention in view of the deficiencies of the prior art, improves the de- virtue processing of absorption method, it is poly- to be prepared for molecular engram
Object is closed as aromatic amino acid adsorbent, specific summary of the invention is as follows:
A kind of preparation method of shellfish high F value oligopeptide, step include proteolysis, the single-minded adsorbent system of aromatic amino acid
Standby, aromatic amino acid removing, the single-minded adsorbent of aromatic amino acid are molecularly imprinted polymer.
Preferably, the aromatic amino acid removing includes the following steps:
Add its 1-5wt% molecularly imprinted polymer into the product after the proteolysis, 10-20 DEG C of stirring 30-100min,
4000-10000r/min is centrifuged 5-30min, collects supernatant, obtains high F value oligopeptide solution.
Preferably, the molecularly imprinted polymer is prepared by poplar bundles polyamide-amide.
Further, the molecularly imprinted polymer, preparation method include the following steps:
The preparation of (1) 0.5 generation dendritic interphase: using ethylenediamine as core, Michael addition reaction is carried out, prepares 0.5 generation tree
Dendritic polyamide-amide；
The preparation of (2) 1 generation dendritic interphases: it is anti-that amidation condensation is carried out with 0.5 generation dendritic interphase and ethylenediamine
1 generation dendritic interphase should be prepared；
The preparation of (3) 2 generation dendritic interphases: the 1 generation dendritic interphase obtained to step (2) repeats step
(2) the amidation condensation reaction in Michael addition and step (2) in prepares 2 generation dendritic interphases；
(4) preparation of terminal double bond dendritic: carrying out aminolysis reaction by 2 generation dendritic interphases and acryloyl chloride is
Obtain terminal double bond dendritic interphase;
(5) molecularly imprinted polymer synthesizes: using aromatic amino acid as template, with the terminal double bond branch obtained in step (4)
Shape polyamide-amide synthesizes to get molecularly imprinted polymer.
Further, in the preparation method step (1) Michael addition reaction, operating condition are as follows: by 9 parts of second
Diamines and 32 parts of methanol are added in the three-necked flask with magnetic stir bar, reflux condensing tube and thermometer, and 15-30 DEG C logical
Nitrogen 5-20 min deoxygenation under stirring condition, is added dropwise 103.2 parts of methyl acrylates, reacts 10-30 h, at 20-35 DEG C,
It is evaporated under reduced pressure under the pressure of 100-200 Pa, removes solvent methanol and excessive methyl acrylate, obtain 0.5 generation dendroid polyamides
Amine-amine；
The amidation condensation reaction of step (1), operating condition in the preparation method are as follows: will be obtained in 20.2 parts of steps (1)
The 0.5 generation dendritic interphase and 64 parts of methanol obtained mixes, and under 15-30 DEG C of stirring condition, 72 parts of ethylenediamines is added dropwise, instead
10-30 h is answered, is evaporated under reduced pressure under 45-75 DEG C, the pressure of 100-300 Pa, solvent methanol and ethylenediamine is removed, obtains 1.0
For dendritic interphase；
The operating condition of step (4) in the preparation method are as follows: weigh 1 part of 2 generation dendritic interphase and 8-16 parts of acryloyls
Chlorine is dissolved with methylene chloride, is led to nitrogen protection, is protected from light 2-4 DEG C of reaction 1-3h, obtains the solution with sediment, filter at low temperature,
Obtain terminal double bond dendritic interphase product；
The operating condition of step (5) in the preparation method are as follows: weigh 1 part of aromatic amino acid as template molecule, be added 5-
10 parts of ethyl alcohol, the hydrochloric acid that 50-200 μ L 37wt% is added dropwise dissolve template molecule all；It is added in 3-8 mmo1 step (4) and obtains
Function monomer and initiator, ultrasound is added after acting on 5-10h in ice-water bath in the terminal double bond dendritic interphase obtained, dissolution
It is uniformly mixed, inflated with nitrogen 3-15min is subsequently placed in ice-water bath and carries out uv-light polymerization；Gained is produced after the completion of polymerization
Object is crushed, is ground, and removes template molecule with methanol and acetic acid, spare after vacuum drying；The function monomer is methacrylic acid,
The initiator is azodiisobutyronitrile.
Further, the aromatic amino acid is tyrosine, tryptophan or phenylalanine.
Preferably, the proteolysis includes the following steps:
(1) it takes fresh shellfish meat to clean, adds water to be homogenized according to the mass ratio 1:5-1:10 of shellfish meat and water, obtain slurry；
(2) endo protease, enzymatic hydrolysis condition is added in the slurry obtained to step (1) are as follows: enzyme additive amount is to account for slurry gross mass
1000-3000U/g, pH 5-8,30-50 DEG C of hydrolysis temperature, then enzymolysis time 5-10 h boils 5-15min enzyme deactivation, obtains
Enzymolysis liquid；
(3) in the enzymolysis liquid obtained to step (2), exoproteinase, enzymatic hydrolysis condition is added are as follows: enzyme additive amount is to account for the total matter of slurry
1000-2000U/g, 30-55 DEG C of pH 5-8, hydrolysis temperature are measured, then enzymolysis time 8-12 h boils 5-15min enzyme deactivation.
3000-8000r/min is centrifuged 5-30min, collects supernatant, obtains shellfish oligopeptide solution.
Preferably, the shellfish is Chlamys farreri, Patinopecten yessoensis or bay scallop.
Preferably, the F value of the high F value oligopeptide is 50 or more.
Part described above is mass fraction.
Beneficial effects of the present invention are as follows:
The present invention using aromatic amino acid as template prepares molecularly imprinted polymer, it can be achieved that specificity to aromatic amino acid
Precisely absorption, helps to improve the F value of oligopeptides, effectively overcomes existing adsorbent adsorption effect poor, big etc. scarce without specificity, loss
Point realizes the fast lifting of F value, increases the yield of high F value oligopeptide, is the beneficial improvement to high F value oligopeptide preparation process；
The F value of the high F value oligopeptide of acquisition is 50 or more, can be widely applied to medicine, field of food.
Specific embodiment
Principles and features of the present invention are described below in conjunction with example, the given examples are served only to explain the present invention, and
It is non-to be used to limit the scope of the invention.
Endo protease used in the embodiment of the present invention is compound protease Protemax, and purchase believes (China) in Novi
Bioisystech Co., Ltd, exoproteinase are flavor protease, are bought in Pangbo Bioengineering Co Ltd, Nanning.Embodiment
Described in part be mass fraction.
High F value oligopeptide F value calculation formula are as follows: F=QUOTE
High F value oligopeptide yield calculation formula are as follows: product yield=QUOTE
Embodiment 1
A kind of preparation method of shellfish high F value oligopeptide, its step are as follows:
1. proteolysis
(1) it takes the shellfish meat of fresh bay scallop to clean, adds water to be homogenized according to the mass ratio 1:5 of shellfish meat and water, obtain slurry；
(2) compound protease Protemax is added in the slurry obtained to step (1), enzyme additive amount is to account for slurry gross mass
1000U/g, pH5,30 DEG C of hydrolysis temperature, then 10 h of enzymolysis time boils 5min enzyme deactivation, obtains enzymolysis liquid；
(3) in the enzymolysis liquid obtained to step (2), flavor protease, enzymatic hydrolysis condition is added are as follows: enzyme additive amount is to account for the total matter of slurry
1000U/g, 55 DEG C of pH 5, hydrolysis temperature are measured, then enzymolysis time 8h boils 5min enzyme deactivation.3000r/min is centrifuged 30 min,
Supernatant is collected, shellfish oligopeptide solution is obtained.
2. prepared by aromatic amino acid adsorbent
The preparation of (1) 0.5 generation dendritic interphase: using ethylenediamine as core, Michael addition reaction is carried out, prepares 0.5 generation tree
Dendritic polyamide-amide；The operating condition of Michael addition reaction are as follows: 9 parts of ethylenediamines and 32 parts of methanol are added to magnetic
In the three-necked flask of power stirrer, reflux condensing tube and thermometer, 15 DEG C of logical 20 min deoxygenations of nitrogen under stirring condition, are added dropwise
103.2 parts of methyl acrylates react 10h, are evaporated under reduced pressure under 20 DEG C, the pressure of 200 Pa, remove solvent methanol and excess
Methyl acrylate, obtain 0.5 generation dendritic interphase；
The preparation of (2) 1 generation dendritic interphases: it is anti-that amidation condensation is carried out with 0.5 generation dendritic interphase and ethylenediamine
1 generation dendritic interphase should be prepared；By the 0.5 generation dendritic interphase obtained in 20.2 parts of steps (1) and 64 parts
Methanol mixes, and under 15 DEG C of stirring conditions, 72 parts of ethylenediamines are added dropwise, reacts 10h, depressurizes under 45 DEG C, the pressure of 300 Pa
Distillation removes solvent methanol and ethylenediamine, obtains 1.0 generation dendritic interphases；
The preparation of (3) 2 generation dendritic interphases: the 1 generation dendritic interphase obtained to step (2) repeats step
(1) the amidation condensation reaction in Michael addition and step (2) in prepares 2 generation dendritic interphases；
(4) preparation of terminal double bond dendritic: carrying out aminolysis reaction by 2 generation dendritic interphases and acryloyl chloride is
Obtain terminal double bond dendritic interphase;1 part of 2 generation dendritic interphase and 8 parts of acryloyl chlorides are weighed, it is molten with methylene chloride
Solution leads to nitrogen protection, is protected from light 2 DEG C of reaction 3h, obtains the solution with sediment, and it is poly- to obtain terminal double bond dendroid for filter at low temperature
Amide-amine product；
(5) molecularly imprinted polymer synthesizes: respectively using tyrosine, tryptophan, phenylalanine as obtaining in template, with step (4)
The terminal double bond dendritic interphase Synthesis of Molecular Imprinting Polymers obtained.1 part of aromatic amino acid is weighed as template molecule,
5 parts of ethyl alcohol are added, the hydrochloric acid that 50 μ L 37wt% are added dropwise dissolves template molecule all；Acquisition in 3 mmo1 steps (4) is added
Terminal double bond dendritic interphase, dissolution are added function monomer after acting on 5h in ice-water bath and initiator, ultrasonic mixing are equal
Even, inflated with nitrogen 3min is subsequently placed in ice-water bath and carries out uv-light polymerization；Products therefrom is crushed after the completion of polymerization, is ground
Mill removes template molecule with methanol and acetic acid, spare after vacuum drying；The function monomer is methacrylic acid, the initiation
Agent is azodiisobutyronitrile.
3. aromatic amino acid removes
Its 1wt% molecularly imprinted polymer, 20 DEG C of stirrings 100min, 4000r/ are added into the product after the proteolysis
Min is centrifuged 30min, collects supernatant, obtains high F value oligopeptide solution, and measuring F value at this time is 52, yield 68%.
Embodiment 2
A kind of preparation method of shellfish high F value oligopeptide, its step are as follows:
1. proteolysis
(1) it takes the shellfish meat of fresh Patinopecten yessoensis to clean, adds water to be homogenized according to the mass ratio 1:10 of shellfish meat and water, obtain slurry；
(2) compound protease Protemax is added in the slurry obtained to step (1), enzyme additive amount is to account for slurry gross mass
2000U/g, pH 6.5,45 DEG C of hydrolysis temperature, then 5 h of enzymolysis time boils 15min enzyme deactivation, obtains enzymolysis liquid；
(3) in the enzymolysis liquid obtained to step (2), flavor protease, enzymatic hydrolysis condition is added are as follows: enzyme additive amount is to account for the total matter of slurry
1200 U/g, 40 DEG C of pH 7, hydrolysis temperature are measured, then 9 h of enzymolysis time boils 15min enzyme deactivation.5000r/min centrifugation
20min collects supernatant, obtains shellfish oligopeptide solution.
2. prepared by aromatic amino acid adsorbent
The preparation of (1) 0.5 generation dendritic interphase: using ethylenediamine as core, Michael addition reaction is carried out, prepares 0.5 generation tree
Dendritic polyamide-amide；The operating condition of Michael addition reaction are as follows: 9 parts of ethylenediamines and 32 parts of methanol are added to magnetic
In the three-necked flask of power stirrer, reflux condensing tube and thermometer, 20 DEG C of logical 10 min deoxygenations of nitrogen under stirring condition, are added dropwise
103.2 parts of methyl acrylates react 20h, are evaporated under reduced pressure under 30 DEG C, the pressure of 140 Pa, remove solvent methanol and excess
Methyl acrylate, obtain 0.5 generation dendritic interphase；
The preparation of (2) 1 generation dendritic interphases: it is anti-that amidation condensation is carried out with 0.5 generation dendritic interphase and ethylenediamine
1 generation dendritic interphase should be prepared；By the 0.5 generation dendritic interphase obtained in 20.2 parts of steps (1) and 64 parts
Methanol mixes, and under 20 DEG C of stirring conditions, 72 parts of ethylenediamines are added dropwise, reacts 20 h, depressurizes under 65 DEG C, the pressure of 180 Pa
Distillation removes solvent methanol and ethylenediamine, obtains 1.0 generation dendritic interphases；
The preparation of (3) 2 generation dendritic interphases: the 1 generation dendritic interphase obtained to step (2) repeats step
(1) the amidation condensation reaction of Michael addition and step (2) in prepares 2 generation dendritic interphases；
(4) preparation of terminal double bond dendritic: carrying out aminolysis reaction by 2 generation dendritic interphases and acryloyl chloride is
Obtain terminal double bond dendritic interphase;1 part of 2 generation dendritic interphase and 10 parts of acryloyl chlorides are weighed, methylene chloride is used
Dissolution leads to nitrogen protection, is protected from light 3 DEG C of 2 h of reaction, obtains the solution with sediment, filter at low temperature obtains terminal double bond dendroid
Polyamide-amide product；
(5) molecularly imprinted polymer synthesizes: respectively using tyrosine, tryptophan, phenylalanine as obtaining in template, with step (4)
The terminal double bond dendritic interphase Synthesis of Molecular Imprinting Polymers obtained.1 part of aromatic amino acid is weighed as template molecule,
8 parts of ethyl alcohol are added, the hydrochloric acid that 120 μ L 37wt% are added dropwise dissolves template molecule all；It is added in 5 mmo1 steps (4) and obtains
Terminal double bond dendritic interphase, dissolution acts in ice-water bath and function monomer and initiator, ultrasonic mixing is added after 8 h
Uniformly, 10 min of inflated with nitrogen is subsequently placed in ice-water bath and carries out uv-light polymerization；By products therefrom powder after the completion of polymerization
Broken, grinding removes template molecule with methanol and acetic acid, spare after vacuum drying；The function monomer is methacrylic acid, described
Initiator is azodiisobutyronitrile.
3. aromatic amino acid removes
Its 3wt% molecularly imprinted polymer, 10 DEG C of stirrings 30min, 10000r/ are added into the product after the proteolysis
Min is centrifuged 5min, collects supernatant, obtains high F value oligopeptide solution, and measuring F value at this time is 54, yield 73%.
Embodiment 3
A kind of preparation method of shellfish high F value oligopeptide, its step are as follows:
1. proteolysis
(1) it takes the shellfish meat of fresh Chlamys farreri to clean, adds water to be homogenized according to the mass ratio 1:8 of shellfish meat and water, obtain slurry；
(2) compound protease Protemax is added in the slurry obtained to step (1), enzyme additive amount is to account for slurry gross mass
3000U/g, pH 8,50 DEG C of hydrolysis temperature, then 5 h of enzymolysis time boils 10min enzyme deactivation, obtains enzymolysis liquid；
(3) in the enzymolysis liquid obtained to step (2), flavor protease, enzymatic hydrolysis condition is added are as follows: enzyme additive amount is to account for the total matter of slurry
2000 U/g, 30 DEG C of pH 8, hydrolysis temperature are measured, then 12 h of enzymolysis time boils 10min enzyme deactivation.8000r/min centrifugation
5min collects supernatant, obtains shellfish oligopeptide solution.
2. prepared by aromatic amino acid adsorbent
The preparation of (1) 0.5 generation dendritic interphase: using ethylenediamine as core, Michael addition reaction is carried out, prepares 0.5 generation tree
Dendritic polyamide-amide；The operating condition of Michael addition reaction are as follows: 9 parts of ethylenediamines and 32 parts of methanol are added to magnetic
In the three-necked flask of power stirrer, reflux condensing tube and thermometer, 30 DEG C of logical 5 min deoxygenations of nitrogen under stirring condition, are added dropwise
103.2 parts of methyl acrylates react 30 h, are evaporated under reduced pressure under 35 DEG C, the pressure of 100 Pa, remove solvent methanol and mistake
The methyl acrylate of amount obtains 0.5 generation dendritic interphase；
The preparation of (2) 1 generation dendritic interphases: it is anti-that amidation condensation is carried out with 0.5 generation dendritic interphase and ethylenediamine
1 generation dendritic interphase should be prepared；By the 0.5 generation dendritic interphase obtained in 20.2 parts of steps (1) and 64 parts
Methanol mixes, and under 30 DEG C of stirring conditions, 72 parts of ethylenediamines are added dropwise, reacts 30 h, subtracts under 75 DEG C, the pressure of 100 Pa
Pressure distillation, removes solvent methanol and ethylenediamine, obtains 1.0 generation dendritic interphases；
The preparation of (3) 2 generation dendritic interphases: the 1 generation dendritic interphase obtained to step (2) repeats step
(1) the amidation condensation reaction in Michael addition and step (2) in prepares the dendritic interphase in 2 generations；
(4) preparation of terminal double bond dendritic: carrying out aminolysis reaction by 2 generation dendritic interphases and acryloyl chloride is
Obtain terminal double bond dendritic interphase;1 part of 2 generation dendritic interphase and 16 parts of acryloyl chlorides are weighed, methylene chloride is used
Dissolution leads to nitrogen protection, is protected from light 4 DEG C of reaction 1h, obtains the solution with sediment, filter at low temperature obtains terminal double bond dendroid
Polyamide-amide product；
(5) molecularly imprinted polymer synthesizes: respectively using tyrosine, tryptophan, phenylalanine as obtaining in template, with step (4)
The terminal double bond dendritic interphase Synthesis of Molecular Imprinting Polymers obtained.1 part of aromatic amino acid is weighed as template molecule,
10 parts of ethyl alcohol are added, the hydrochloric acid that 200 μ L 37wt% are added dropwise dissolves template molecule all；It is added in 8 mmo1 steps (4) and obtains
Terminal double bond dendritic interphase, function monomer and initiator, ultrasonic mixing is added after acting on 10h in ice-water bath in dissolution
Uniformly, inflated with nitrogen 15min is subsequently placed in ice-water bath and carries out uv-light polymerization；Crush products therefrom after the completion of polymerization,
Grinding removes template molecule with methanol and acetic acid, spare after vacuum drying；The function monomer is methacrylic acid, described to draw
Hair agent is azodiisobutyronitrile.
3. aromatic amino acid removes
Its 5wt% molecularly imprinted polymer, 15 DEG C of stirrings 60min, 6000r/min are added into the product after the proteolysis
It is centrifuged 20min, collects supernatant, obtains high F value oligopeptide solution, measuring F value at this time is 60, yield 76%.
The foregoing is merely presently preferred embodiments of the present invention, is not intended to limit the invention, it is all in spirit of the invention and
Within principle, any modification, equivalent replacement, improvement and so on be should all be included in the protection scope of the present invention.
Claims (9)
1. a kind of preparation method of shellfish high F value oligopeptide, which is characterized in that the preparation method includes proteolysis, aromatic series
The single-minded adsorbent preparation of amino acid, aromatic amino acid removing, the single-minded adsorbent of aromatic amino acid are poly- for molecular engram
Close object.
2. the preparation method of shellfish high F value oligopeptide according to claim 1, which is characterized in that the aromatic amino acid
Removing includes the following steps:
Add its 1-5wt% molecularly imprinted polymer into the product after the proteolysis, 10-20 DEG C of stirring 30-100min,
4000-10000r/min is centrifuged 5-30min, collects supernatant, obtains high F value oligopeptide solution.
3. the preparation method of shellfish high F value oligopeptide according to claim 1 or 2, which is characterized in that the molecular engram is poly-
Object is closed to be prepared by dendritic.
4. the preparation method of shellfish high F value oligopeptide according to claim 3, which is characterized in that the molecular engram polymerization
The preparation method of object includes the following steps:
The preparation of (1) 0.5 generation dendritic interphase: using ethylenediamine as core, Michael addition reaction is carried out, prepares 0.5 generation tree
Dendritic polyamide-amide；
The preparation of (2) 1 generation dendritic interphases: it is anti-that amidation condensation is carried out with 0.5 generation dendritic interphase and ethylenediamine
1 generation dendritic interphase should be prepared；
The preparation of (3) 2 generation dendritic interphases: the 1 generation dendritic interphase obtained to step (2) repeats step
(1) the amidation condensation reaction in Michael addition and step (2) in prepares 2 generation dendritic interphases；
(4) preparation of terminal double bond dendritic: carrying out aminolysis reaction by 2 generation dendritic interphases and acryloyl chloride is
Obtain terminal double bond dendritic interphase;
(5) molecularly imprinted polymer synthesizes: using aromatic amino acid as template, with the terminal double bond branch obtained in step (4)
Shape polyamide-amide synthesizes to get molecularly imprinted polymer.
5. the preparation method of shellfish high F value oligopeptide according to claim 4, which is characterized in that walked in the preparation method
Suddenly the Michael addition reaction of (1), operating condition are as follows: 9 parts of ethylenediamines and 32 parts of methanol are added to magnetic agitation
Son, reflux condensing tube and thermometer three-necked flask in, 15-30 DEG C of logical nitrogen 5-20 min deoxygenation under stirring condition, is added dropwise
103.2 parts of methyl acrylates react 10-30 h, are evaporated under reduced pressure under 20-35 DEG C, the pressure of 100-200 Pa, remove solvent
Methanol and excessive methyl acrylate obtain 0.5 generation dendritic interphase；
The amidation condensation reaction of step (2), operating condition in the preparation method are as follows: will be obtained in 20.2 parts of steps (1)
The 0.5 generation dendritic interphase and 64 parts of methanol obtained mixes, and under 15-30 DEG C of stirring condition, 72 parts of ethylenediamines is added dropwise, instead
10-30 h is answered, is evaporated under reduced pressure under 45-75 DEG C, the pressure of 100-300 Pa, solvent methanol and ethylenediamine is removed, obtains 1.0
For dendritic interphase；
The operating condition of step (4) in the preparation method are as follows: weigh 1 part of 2 generation dendritic interphase and 8-16 parts of acryloyls
Chlorine is dissolved with methylene chloride, is led to nitrogen protection, is protected from light 2-4 DEG C of reaction 1-3h, obtains the solution with sediment, filter at low temperature,
Obtain terminal double bond dendritic interphase product；
The operating condition of step (5) in the preparation method are as follows: weigh 1 part of aromatic amino acid as template molecule, 5- is added
10 parts of ethyl alcohol, the hydrochloric acid that 50-200 μ L 37wt% is added dropwise dissolve template molecule all；It is added in 3-8 mmo1 step (5) and obtains
Function monomer and initiator, ultrasound is added after acting on 5-10h in ice-water bath in the terminal double bond dendritic interphase obtained, dissolution
It is uniformly mixed, inflated with nitrogen 3-15min is subsequently placed in ice-water bath and carries out uv-light polymerization；Gained is produced after the completion of polymerization
Object is crushed, is ground, and removes template molecule with methanol and acetic acid, spare after vacuum drying；The function monomer is methacrylic acid,
The initiator is azodiisobutyronitrile.
6. the preparation method of shellfish high F value oligopeptide according to claim 4 or 5, which is characterized in that the aromatic series amino
Acid is tyrosine, tryptophan or phenylalanine.
7. the preparation method of shellfish high F value oligopeptide according to claim 1, which is characterized in that the proteolysis includes
Following steps:
(1) it takes fresh shellfish meat to clean, adds water to be homogenized according to the mass ratio 1:5-1:10 of shellfish meat and water, obtain slurry；
(2) endo protease, enzymatic hydrolysis condition is added in the slurry obtained to step (1) are as follows: enzyme additive amount is to account for slurry gross mass
1000-3000U/g, pH 5-8,30-50 DEG C of hydrolysis temperature, then enzymolysis time 5-10 h boils 5-15min enzyme deactivation, obtains
Enzymolysis liquid；
(3) in the enzymolysis liquid obtained to step (2), exoproteinase, enzymatic hydrolysis condition is added are as follows: enzyme additive amount is to account for the total matter of slurry
1000-2000U/g, 30-55 DEG C of pH 5-8, hydrolysis temperature are measured, then enzymolysis time 8-12 h boils 5-15min enzyme deactivation,
3000-8000r/min is centrifuged 5-30min, collects supernatant, obtains shellfish oligopeptide solution.
8. the preparation method of shellfish high F value oligopeptide according to claim 1, which is characterized in that the shellfish is comb hole fan
Shellfish, Patinopecten yessoensis or bay scallop.
9. the preparation method of shellfish high F value oligopeptide according to claim 1, which is characterized in that the F of the high F value oligopeptide
Value is 50 or more.
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111235206A (en) * | 2020-04-27 | 2020-06-05 | 鲁东大学 | Method for preparing shellfish high F value oligopeptide by subcritical water-assisted enzyme method |
| CN111979286A (en) * | 2020-08-31 | 2020-11-24 | 鲁东大学 | Method for preparing shellfish high F value oligopeptide by combining fermentation method and enzyme method |
| CN112250884A (en) * | 2020-08-21 | 2021-01-22 | 江苏省农业科学院 | Dendritic polymeric antibacterial peptide and preparation method and application thereof |
| CN112940247A (en) * | 2021-02-05 | 2021-06-11 | 浙江大学 | Production method and equipment of oil-soluble hyperbranched polyamidoamine |
| CN117165646A (en) * | 2023-08-25 | 2023-12-05 | 广州菲勒生物科技有限公司 | Collagen tripeptide composition and purification method thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102911374A (en) * | 2012-11-11 | 2013-02-06 | 安徽工业大学 | Preparation method for 2.0 generation of polyamidoamine PAMAM dendrimer |
| CN105087730A (en) * | 2015-08-14 | 2015-11-25 | 浙江省海洋开发研究院 | High-F (Fischer)-value tuna oligopeptide preparation method |
-
2019
- 2019-07-15 CN CN201910634784.6A patent/CN110144377B/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102911374A (en) * | 2012-11-11 | 2013-02-06 | 安徽工业大学 | Preparation method for 2.0 generation of polyamidoamine PAMAM dendrimer |
| CN105087730A (en) * | 2015-08-14 | 2015-11-25 | 浙江省海洋开发研究院 | High-F (Fischer)-value tuna oligopeptide preparation method |
Non-Patent Citations (1)
| Title |
|---|
| HUINA ZHENG ET AL.: "Preparation and characterisation of the pearl oyster(Pinctada martensii) meat protein hydrolysates with a high Fischer ratio", 《INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY》 * |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111235206A (en) * | 2020-04-27 | 2020-06-05 | 鲁东大学 | Method for preparing shellfish high F value oligopeptide by subcritical water-assisted enzyme method |
| CN112250884A (en) * | 2020-08-21 | 2021-01-22 | 江苏省农业科学院 | Dendritic polymeric antibacterial peptide and preparation method and application thereof |
| CN111979286A (en) * | 2020-08-31 | 2020-11-24 | 鲁东大学 | Method for preparing shellfish high F value oligopeptide by combining fermentation method and enzyme method |
| CN111979286B (en) * | 2020-08-31 | 2021-11-26 | 鲁东大学 | Method for preparing shellfish high F value oligopeptide by combining fermentation method and enzyme method |
| CN112940247A (en) * | 2021-02-05 | 2021-06-11 | 浙江大学 | Production method and equipment of oil-soluble hyperbranched polyamidoamine |
| CN117165646A (en) * | 2023-08-25 | 2023-12-05 | 广州菲勒生物科技有限公司 | Collagen tripeptide composition and purification method thereof |
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