CN106701877A - Method for preparing ACE inhibitory peptide derived from oysters - Google Patents
Method for preparing ACE inhibitory peptide derived from oysters Download PDFInfo
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- CN106701877A CN106701877A CN201710037653.0A CN201710037653A CN106701877A CN 106701877 A CN106701877 A CN 106701877A CN 201710037653 A CN201710037653 A CN 201710037653A CN 106701877 A CN106701877 A CN 106701877A
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- Prior art keywords
- oyster
- ace inhibitory
- protein
- inhibitory peptide
- enzymolysis
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- 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
- C07K1/145—Extraction; Separation; Purification by extraction or solubilisation
-
- 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
- C07K1/30—Extraction; Separation; Purification by precipitation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
Abstract
The invention provides a method for preparing an ACE inhibitory peptide derived from oysters. The method comprises the step of performing enzymolysis on oyster protein with pepsin, wherein a compound microbial agent prepared from bacillus subtilis and lactobacillus in an arbitrary proportion is added into the system. The method can be used for effectively improving the yield of the ACE inhibitory peptide derived from oysters, is simple and feasible, and is easy for popularization to realize industrial application.
Description
Technical field
Extraction the invention belongs to the preparation of biogenetic derivation active material, more particularly to the active material of biogenetic derivation is separated
Method.
Background technology
The advance in theory of digesting and assimilating of peptide confirms that body can directly absorb small-molecule peptide material, and peptide matters are not only
Can be as the useful supplement of nutrition, there is the peptide of certain sequence also to have special physiologically active-- i.e. bioactivity for some
Peptide.Small molecule bioactive peptide in food protein has following advantage：Molecular mass is small, it is easy to digest and assimilate,
It is difficult to cause immunogenicity；Space structure-activity relationship is simple, it is easy to carry out the research of activity mechanism；From food protein, no
Easily cause toxic and side effect.
At present with food protein as raw material, the method for preparing small-molecular peptides mainly has：The acid and alkali hydrolysis method of protein, egg
The microbe fermentation method of white matter, the enzyme edman degradation Edman of protein.The acid and alkali hydrolysis method method of protein is simple, and speed is fast, is produced into
This is cheap, however, its protein degree is difficult to control, some amino acid are readily broken, while production process is easily caused
Environmental pollution.The microbe fermentation method of protein is with low cost, but its production time is long, and separation process is complicated, due to needing
Growth of microorganism, therefore its protein utilization degree is maintained to be greatly reduced.The enzyme edman degradation Edman of protein, its hydrolysis degree is easy to the palm
Control, enzymolysis time is short, and protein utilization degree is high, and enzymolysis product is easily isolated, with low cost；But pure peptide yield is relatively low so that big
The industrialized production of scale is subject to certain restrictions.And pass through the method that microbial fermentation associated proteins are digested, can be certain
Degree improves proterties, the yield of enzymolysis product, beneficial to large-scale production.
Over nearly 20 years, existing many researchers digest to Oyster Protein, obtain oyster oligopeptides, and such as anti-HIV-1 is few
Peptide, anti-oxidant oligopeptides and ACE suppress oligopeptides.ACE is a kind of Zn- dependent forms, the dipeptidyl carboxypeptidase of exocytosis, and it can be by Ang
I is converted into Ang II, Ang II and G- G-protein linked receptor ATR combinations to target cell, causes a series of liters of blood pressures
Process.Meanwhile, ACE can also inactivate a series of bradykinins with hypotensive activity, cause the further of body blood pressure
Raise.Therefore, the suppression of ACE activity can effectively alleviate hypertension and its relevant disease.In the present inventor's previous work, from male
(amino acid sequence is for isolated ace inhibitory peptide in oyster soluble protein：VVYPWTORF), IC50It is 0.079mg/mL (66 μ to be worth
Mol/L), after testing with excellent ACE inhibitory activity, but extraction efficiency is very low from oyster, has had a strong impact on its application and has set
Meter and the development of follow-up work.All the time, we are devoted to obtaining the small peptide product of more natural origins.
The content of the invention
Oyster is improved it is an object of the invention to provide one kind to carry out source ACE inhibitor peptides (amino acid sequence is：VVYPWTORF)
The method of yield, the preparation method of the ace inhibitory peptide for coming from oyster of the invention, including Oyster Protein is carried out with pepsin
The step of enzymolysis, wherein adding bacillus subtilis during described enzymolysis, in system and lactic acid bacteria constitutes according to arbitrary proportion
Composite bacteria agent.Under equal working condition, the ace inhibitory peptide that oyster is originated can be effectively greatly improved using the method for this law
Yield, method is simple and easy to apply, it is easy to promote and realize commercial application.
Brief description of the drawings
The separating resulting collection of illustrative plates of the width of accompanying drawing of the present invention 1, i.e. LH-20 gel chromatographies to oyster hydrolysates.
Specific embodiment
It is the system of VVYPWTORF bioactive peptides the present invention relates to a kind of ace inhibitory peptide for coming from oyster, i.e. amino acid sequence
Preparation Method.The small peptide with ACE inhibitory activity is prepared from oyster, it is necessary to be digested to Oyster Protein.The present invention also includes
The step of being digested to Oyster Protein using pepsin, characteristically, the present invention adds withered grass gemma in enzymatic hydrolysis system
The composite bacteria agent that bacillus and lactic acid bacteria constitute according to arbitrary proportion.
In specific embodiment, in terms of the addition of composite bacteria agent, the result of investigation shows, preferred composite bacteria agent
Consumption is the 0.4~0.6% of Oyster Protein quality.More preferably 0.5%.From the point of view of the composition of composite bacteria agent, by bacillus subtilis
Bacterium and lactic acid bacteria are according to mass ratio 1:The composite bacteria agent of 1 composition is optimal to effect of the invention.
In another specific embodiment, the enzymolysis process parameter to the addition of composite bacteria agent is investigated, and is found：Simple
Enzymolysis process is not high to the design requirement of procedure parameter, i.e., the various enzymolysis results implemented under Parameter Conditions are poor without conspicuousness
It is different.And the enzymolysis process of composite bacteria agent is with the addition of, just it is not merely enzymolysis process, wherein further comprises microbial fermentation and effect
Process, the change to parameter is more sensitive.Investigate result to find, using following enzymolysis process/parameters, preferred knot can be obtained
Really：8~10h of stirring reaction under the conditions of 37 ± 2 DEG C, system is then anti-then at 37 DEG C of stirrings in 4 ± 2 DEG C of 8~10h of standing afterwards
Answer 6~8h.Wherein described whipping process can use conventional method, such as but not limited to low speed magnetic agitation.
More specifically, the preparation method of bioactive peptide of the present invention comprises the following steps：
(1) Oyster Protein is prepared by raw material of fresh oyster；
(2) Oyster Protein prepared by step (1) is delayed according to the phosphoric acid that the concentration of 2g/100ml is added to 0.05mol/L
In fliud flushing, and pepsin and composite bacteria agent are added, be well mixed 8~10h of stirring reaction under the conditions of 37 ± 2 DEG C, afterwards
System stands 8~10h in 4 ± 2 DEG C, then then at 37 DEG C of 6~8h of stirring reaction；
The addition of described pepsin is the 1.5% of Oyster Protein quality；
The addition of described composite bacteria agent is the 0.5% of Oyster Protein quality；
Wherein described phosphate buffer：The NaH of 0.05mol/L2PO4The aqueous solution adjusts pH value to 2.0 with the HCl of 1mol/L.
(3) oyster ace inhibitory peptide is isolated and purified in the system completed from the reaction of step (2).
Wherein, the method that Oyster Protein can be using having recorded in the prior art is prepared by raw material of fresh oyster.This
Invention provides following specific step：Glandula digestive is removed after fresh oyster is shelled, (with homogenate under remainder low-temperature condition
Machine) rub after, be added in isometric PBS, be sufficiently stirred for；After mixture stands 6 hours in 4 DEG C, in centrifuging and taking
Clear liquid, ammonium sulfate is added according to 75wt%, stands 6 hours under the conditions of 4 DEG C again, centrifugation；Then by sediment with it is isometric
Moisture is dissipated, and loads bag filter, and flowing water is dialysed 24 hours, then is dialysed 24 hours with deionized water, then by content low-pressure refrigeration
Dry, obtain Oyster Protein.
Wherein described PBS：The NaH of 0.2mol/L2PO4The Na of solution and 0.2mol/L2HPO4Solution is by volume
39:61 mixing, pH 7.0.Without specified otherwise, the centrifugally operated in the step uses following condition：5000 × g, 4 DEG C,
25min。
Oyster Protein is resulting after being digested under protease and mix bacterium agent existence condition by foregoing invention step (2)
Product need to enter the bioactive peptide for isolating and purifying and being only target of the present invention.It is of the invention specifically to use what is isolated and purified as follows
Step：The product of step (2) first use Sephadex LH-20 gel chromatography post separations, mobile phase be 30% methyl alcohol it is molten
Liquid, flow velocity is 0.5mL/min, and loading volume is 10mL, and sample concentration is 0.2g/mL, and Detection wavelength is 280nm；Desk-top record
Instrument writing speed is 0.2mm/min, voltage 10mv, 2 amperes of electric current；25~30 pipe components are collected with the speed of 20min/ pipes；
Using RP-HPLC Hypersil BDS C18To the further separation of product, the μ l of loading volume 20, sample concentration
10mg/mL, flow velocity 1mL/min；
Gradient elution：Mobile phase A liquid：The 0.1% TFA aqueous solution；Mobile phase B liquid：Acetonitrile；
0min：A, 100%；B 0%；
40min：A, 0%；B, 100%；
50min：A, 0%；B, 100%；
Detection wavelength is 215nm；Signal component is collected, ACE inhibitory activity component is monitored and gather.
Unless specifically indicated, in the present invention, protein hydrolysis degree is detected using ninhydrin method method, uses liquid phase measurement hippuric acid
The method detection ACE inhibitory activity of content.
Following non-limiting examples are understood not to appoint present invention for the present invention will be further described
The restriction of meaning form.
Embodiment 1
The feed postition of compound bacteria influences on oyster enzymolysis liquid ACE inhibitory activity
The test method and conditional parameter of the present embodiment are male in pH2.0,37 DEG C of enzymolysis for the pepsin that E/S is 1.5%
Oyster protein 24 h is used as control；Experimental group for added in pepsin that E/S is 1.5% 0.5% composite bacteria agent (withered grass gemma
Bacillus and lactic acid bacteria, ratio are 1:1), be well mixed 8~10h of stirring reaction under the conditions of 37 ± 2 DEG C, afterwards system in 4 ±
2 DEG C of 8~10h of standing, then then at 37 DEG C of 6~8h of stirring reaction.
The degree of hydrolysis and ACE inhibitory activity of the Oyster Protein matter of table 1
As shown in Table 1, when pepsin digests Oyster Protein, its degree of hydrolysis is 17.8%, and ACE inhibitory activity is
62%；And after adding 0.5% compound bacteria, the degree of hydrolysis of enzymolysis liquid rises to 23%, and ACE inhibitory activity rises to 80%.
Embodiment 2
With isolating and purifying for ACE inhibitory activity peptide
According to the isolation and purification method of oyster ace inhibitory peptide, oyster enzymolysis liquid is separated as shown in figure 1, oyster enzyme
Solution product passes through isolated three main peaks of LH-20 chromatographic columns：Component I, component II, component III.It is freeze-dried to weigh
It is respectively 6.8%, 40%, 20.3% relative to the yield of the protein of enzymolysis, wherein VVYPWTORF activity can be isolated
The component III of peptide is higher than component III13.5% when not adding Escherichia coli.
Embodiment 3
Ace inhibitory peptide yield and proterties
By way of protease hydrolytic combination compound bacteria is digested, the preparation for obtaining ace inhibitory peptide (VVYPWTORF) is newly square
Method, 1.5% is brought up to by its yield by original 0.43%, and product is presented white powder, without fishy smell, without bitter taste, mouthfeel compared with
It is good.
Embodiment 4
Influence experiment of the species of compound bacteria to ace inhibitory peptide yield
The test method and conditional parameter of the present embodiment are male in pH2.0,37 DEG C of enzymolysis for the pepsin that E/S is 1.5%
Oyster protein 24 h is used as control；Experimental group in pepsin hydrolysis system, adds 0.5% different microorganisms respectively, wherein compound
Microorganism adding proportion is 1:1.Well mixed 8~10h of stirring reaction under the conditions of 37 ± 2 DEG C, system is in 4 ± 2 DEG C afterwards
8~10h is stood, then then at 37 DEG C of 6~8h of stirring reaction.
Influence of the table 2 using different composite bacterium to ace inhibitory peptide yield
From the results shown in Table 2, by protease combination bacillus subtilis and the condition of lactic acid bacteria complex enzyme hydrolysis
Under, the yield for obtaining ace inhibitory peptide (VVYPWTORF) brings up to 1.5% by original 0.43%；Significantly larger than other tests
Group.
Embodiment 5
Influence experiment of the mode of action to ace inhibitory peptide yield
In the present embodiment, the mode that pepsin and compound bacteria are digested jointly is compared：E/S is 1.5% stomach egg
(bacillus subtilis and lactic acid bacteria, ratio are 1 to the composite bacteria agent of addition 0.5% in white enzyme:1), enzymolysis program and result such as table 3
It is shown.
Table 3：The yield of ace inhibitory peptide under difference enzymolysis procedure condition
From the results shown in Table 3,37 DEG C of continuous enzymolysis, degree of hydrolysis is slightly higher, especially continuous 37 DEG C of enzymolysis 24h, water
Solution degree highest, is 28.6%.But the yield of the ace inhibitory peptide for being obtained is generally less than the result of subsection enzymolysis.From ace inhibitory peptide
The angle of yield optimization, 37 DEG C of enzymolysis 8h, 4 DEG C of standing 10h, 37 DEG C of procedure conditions for digesting 6h again are most suitable.
Claims (7)
1. the step of coming from the preparation method of the ace inhibitory peptide of oyster, including digested to Oyster Protein with pepsin, its
It is characterised by, the compound bacteria that bacillus subtilis and lactic acid bacteria constitute according to arbitrary proportion is added during described enzymolysis, in system
Agent.
2. method according to claim 1, it is characterised in that the addition of described composite bacteria agent is Oyster Protein quality
0.4~0.6%.
3. method according to claim 1, it is characterised in that described enzymolysis process is：Stirred under the conditions of 37 ± 2 DEG C anti-
8~10h is answered, system stands 8~10h in 4 ± 2 DEG C afterwards, then then at 37 DEG C of 6~8h of stirring reaction.
4. method according to claim 1, it is characterised in that described composite bacteria agent is bacillus subtilis and lactic acid bacteria
According to mass ratio 1:The composite bacteria agent of 1 composition.
5. method according to claim 1, comprises the following steps：
(1) Oyster Protein is prepared by raw material of fresh oyster；
(2) Oyster Protein prepared by step (1) is added to the phosphate buffer of 0.05mol/L according to the concentration of 2g/100ml
In, and pepsin and composite bacteria agent are added, 8~10h of stirring reaction under the conditions of 37 ± 2 DEG C is well mixed, afterwards system
8~10h is stood in 4 ± 2 DEG C, then then at 37 DEG C of 6~8h of stirring reaction；
(3) oyster ace inhibitory peptide is isolated and purified in the system completed from the reaction of step (2).
6. method according to claim 5, it is characterised in that described step (1) is：Removed after fresh oyster is shelled
Glandula digestive, after being rubbed under remainder low-temperature condition, is added in isometric PBS, is sufficiently stirred for；Mixture is in 4
DEG C stand 6 hours after, centrifuging and taking supernatant, according to 75wt% add ammonium sulfate, again under the conditions of 4 DEG C stand 6 hours, from
The heart；Then sediment is dissipated with isometric moisture, loads bag filter, flowing water is dialysed 24 hours, then it is small with deionized water dialysis 24
When, then content low-pressure refrigeration is dried, obtain Oyster Protein.
7. method according to claim 5, it is characterised in that described step (3) is：The product of step (2) is first
Sephadex LH-20 gel chromatography post separations are first used, mobile phase is 30% methanol solution, and flow velocity is 0.5mL/min, loading
Volume is 10mL, and sample concentration is 0.2g/mL, and Detection wavelength is 280nm；Desk-top record instrument writing speed is 0.2mm/min, electricity
Pressure 10mv, 2 amperes of electric current；25~30 pipe components are collected with the speed of 20min/ pipes；
Using RP-HPLC Hypersil BDS C18To the further separation of product, loading volume 20 μ l, sample concentration 10mg/mL,
Flow velocity 1mL/min；
Gradient elution：Mobile phase A liquid：The 0.1% TFA aqueous solution；Mobile phase B liquid：Acetonitrile；
0min：A, 100%；B 0%；
40min：A, 0%；B, 100%；
50min：A, 0%；B, 100%；
Detection wavelength is 215nm；Signal component is collected, ACE inhibitory activity component is monitored and gather.
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109180779A (en) * | 2018-10-30 | 2019-01-11 | 成都诺和晟泰生物科技有限公司 | A kind of method that purifying prepares antibacterial peptide |
| CN109517869A (en) * | 2018-12-22 | 2019-03-26 | 大连海洋大学 | A method of oyster ace inhibitory peptide is produced with immobilised enzymes |
| CN113151390A (en) * | 2021-04-27 | 2021-07-23 | 大连海洋大学 | Preparation method of oyster active peptide capable of improving ACE inhibitory activity |
| CN114032271A (en) * | 2021-11-02 | 2022-02-11 | 浙江工业大学 | Oyster polypeptide and polypeptide powder with uric acid reducing effect as well as preparation method and application of oyster polypeptide and polypeptide powder |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1557474A (en) * | 2004-02-04 | 2004-12-29 | 高春平 | Blood pressure reducing natural polypeptide nutrient |
| CN101210047A (en) * | 2006-12-29 | 2008-07-02 | 中国科学院大连化学物理研究所 | Active peptide and application thereof |
| CN102093471A (en) * | 2009-12-15 | 2011-06-15 | 大连水产学院 | Angiotensin I transferase inhibitor and preparation method and application thereof |
| CN104736552A (en) * | 2012-08-24 | 2015-06-24 | 庆熙大学校产学协力团 | Pharmaceutical composition comprising, as active ingredients, peptides which exhibit inhibitory activity against angiotensin-I converting enzyme for preventing or treating cardiovascular diseases |
| CN104878062A (en) * | 2015-05-18 | 2015-09-02 | 华南理工大学 | Microbiological method for preparing sea-fish protein antihypertensive peptides |
-
2017
- 2017-01-18 CN CN201710037653.0A patent/CN106701877A/en active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1557474A (en) * | 2004-02-04 | 2004-12-29 | 高春平 | Blood pressure reducing natural polypeptide nutrient |
| CN101210047A (en) * | 2006-12-29 | 2008-07-02 | 中国科学院大连化学物理研究所 | Active peptide and application thereof |
| CN102093471A (en) * | 2009-12-15 | 2011-06-15 | 大连水产学院 | Angiotensin I transferase inhibitor and preparation method and application thereof |
| CN104736552A (en) * | 2012-08-24 | 2015-06-24 | 庆熙大学校产学协力团 | Pharmaceutical composition comprising, as active ingredients, peptides which exhibit inhibitory activity against angiotensin-I converting enzyme for preventing or treating cardiovascular diseases |
| CN104878062A (en) * | 2015-05-18 | 2015-09-02 | 华南理工大学 | Microbiological method for preparing sea-fish protein antihypertensive peptides |
Non-Patent Citations (2)
| Title |
|---|
| JIAPEI WANG 等: ""Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats"", 《FOOD CHEMISTRY》 * |
| 余奕珂 等: ""源于食品蛋白质的血管紧张素I转换酶抑制肽"", 《FOOD AND DRUG》 * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109180779A (en) * | 2018-10-30 | 2019-01-11 | 成都诺和晟泰生物科技有限公司 | A kind of method that purifying prepares antibacterial peptide |
| CN109517869A (en) * | 2018-12-22 | 2019-03-26 | 大连海洋大学 | A method of oyster ace inhibitory peptide is produced with immobilised enzymes |
| CN113151390A (en) * | 2021-04-27 | 2021-07-23 | 大连海洋大学 | Preparation method of oyster active peptide capable of improving ACE inhibitory activity |
| CN114032271A (en) * | 2021-11-02 | 2022-02-11 | 浙江工业大学 | Oyster polypeptide and polypeptide powder with uric acid reducing effect as well as preparation method and application of oyster polypeptide and polypeptide powder |
| CN114032271B (en) * | 2021-11-02 | 2024-03-26 | 浙江工业大学 | Oyster polypeptide and polypeptide powder with uric acid reducing effect, and preparation method and application thereof |
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