CN105601708B - A kind of pupa albumen source Angiotensin-Converting inhibits polypeptide and its preparation method and application - Google Patents
A kind of pupa albumen source Angiotensin-Converting inhibits polypeptide and its preparation method and application Download PDFInfo
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- CN105601708B CN105601708B CN201510718114.4A CN201510718114A CN105601708B CN 105601708 B CN105601708 B CN 105601708B CN 201510718114 A CN201510718114 A CN 201510718114A CN 105601708 B CN105601708 B CN 105601708B
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Abstract
The invention belongs to technical field of bioengineering, and in particular to a kind of pupa albumen source Angiotensin-Converting inhibits polypeptide and its preparation method and application.A kind of pupa albumen source Angiotensin-Converting inhibits polypeptide, is isolated angiotensin converting enzyme-inhibiting peptide from pupa albumen hydrolyzate, amino acid sequence is as shown in SEQ ID NO.1.Pupa albumen source angiotensin converting enzyme of the invention inhibits polypeptide to have structure novel, molecular weight is small, the features such as hypotensive activity is high opens a completely new approach for the food for the treatment of hypertension, drug and health care product, has very extensive application prospect.
Description
Technical field
The invention belongs to technical field of bioengineering, and in particular to a kind of pupa albumen source Angiotensin-Converting inhibits
Polypeptide and its preparation method and application.
Background technique
Angiotensin-Converting (Angotensin Converting Enzyme, ACE) is that one kind is present in different groups
Multi-functional extracellular two carboxypeptidase containing zinc in knitting, can be activated by chloride ion and have wider substrate specificity.It is in feritin-blood
Angiotensin system (Renial Angiotensin System, RAS) and kininase-kinin system (Kallikrein-
Kinin, KKS) there is important and crucial physiological function.Its main function is angiotensin I (Angiotensin I
Converting Enzyme) it is converted to Angiotensin II (Angiotensin II Converting Enzyme), simultaneously also
Bradykinin can be made to inactivate, eventually lead to human blood-pressure raising.
Angiotensin-Converting inhibits polypeptide to form biologically active polypeptide by several amino acid, and right
The active region ACE has an inhibitor compared with strong affinity, the affinity of they and ACE is more than angiotensin I or bradykinin
By force, and less easily it discharges, reduce ACE activity or causes it to lose its activity from the combined area ACE, so that ACE be hindered to be catalyzed blood
Angiotensin I is converted to Angiotensin II, and ACE hydrolysis bradykinin is hindered to become inactive fragments, to reach reduction
The effect of blood pressure.
The information disclosed in the background technology section is intended only to increase the understanding to general background of the invention, without answering
When being considered as recognizing or imply that the information constitutes the prior art already known to those of ordinary skill in the art in any form.
Summary of the invention
The object of the present invention is to provide a kind of pupa albumen source Angiotensin-Convertings to inhibit polypeptide, from pupa albumen
Hydrolysate in extract and obtain, with apparent ACE inhibitory activity, provide theoretical direction to prepare blood-pressure drug.
The present invention provides a kind of pupa albumen source Angiotensin-Convertings to inhibit polypeptide, amino acid sequence such as SEQ
Shown in ID NO.1.
The present invention also provides the preparation methods that the pupa albumen source Angiotensin-Converting inhibits polypeptide, including
Following steps:
(1) freezing silkworm chrysalis is added in distilled water according to the ratio of 1:3, filters, is repeated 3 times after homogenate stirring 1h；It closes
And filtrate, filtrate heat 30min to albuminous degeneration under 100 DEG C of water bath conditions, then adjusting pH is 3.0 to make protein deposition, albumen
Solution stands 12h under the conditions of 4 DEG C, precipitates albumen sufficiently and is layered with solution, 4 DEG C of subsequent high speed refrigerated centrifuge, 8000r/min
It is centrifuged 45min and removes supernatant, collect precipitating, it is dry to get arriving silkworm chrysalis crude protein powder；
(2) silkworm chrysalis crude protein powder is added in distilled water according to mass ratio 1:50, is completely dissolved, is then added 1.5%
Neutral proteinase, pH be 7.0, temperature be 50 DEG C under the conditions of digested, enzymolysis time 3h；At 90 DEG C after the completion of enzymatic hydrolysis
Water-bath inactivates 10min, takes supernatant after hydrolyzate centrifugation；It is 5KDa ultrafiltration membrance filter with molecular cut off, by ultrafiltration permeate
Freeze-drying, obtains freeze-dried powder；
(3) freeze-dried powder obtained in step (2) is dissolved in concentration is 0.01mol/L, the phosphate-buffered that pH is 8.5
In liquid；It is splined on the anion exchange resin chromatographic column balanced with the speed of 1.0mL/min, washes column extremely with phosphate buffer
Absorption peak returns to baseline, elution flow rate 1.0mL/min at 220nm；Gradient elution is carried out to sample with NaCl solution, is eluted
Flow velocity is 1.0mL/min, gradient 0-1.0mg/mL；It is freeze-dried and is detected according to each component of period collection
Activity saves under the conditions of -20 DEG C；
(4) the best freeze-dried powder of activity in step (3) is splined on the Sephadex G-15 gel chromatography balanced
Column is eluted by mobile phase of water, elution flow rate 1.0mL/min；Detection wavelength is 280nm；It is collected according to the period each
A component is freeze-dried and is detected activity, is saved under the conditions of -20 DEG C；
(5) the best freeze-dried powder of activity in step (4) is dissolved in ultrapure water, carries out reversed-phase high performance liquid chromatography point
From, mobile phase, A phase: the pure water containing 0.1% trifluoroacetic acid；B phase: acetonitrile；Detection wavelength is 220nm, each component of Fractional Collections
It is freeze-dried and is detected activity, is saved under the conditions of -20 DEG C；
(6) the best freeze-dried powder of the activity that step (5) obtains is again passed by into reversed-phase high performance liquid chromatography separation, flowing
Phase, A phase: the pure water containing 0.1% trifluoroacetic acid；B phase: acetonitrile；Detection wavelength is 220nm, and collection retention time is 19.0-
The component of 21.5min, which is freeze-dried, inhibits polypeptide to get Angiotensin-Converting.
Preferably, acetonitrile described in step (5) carries out gradient elution, concentration is within the 0-60min time from 5%
It is upgraded to 30%.
Preferably, the concentration of acetonitrile described in step (6) is 7%.
The present invention also provides the pupa albumen source Angiotensin-Convertings, and polypeptide to be inhibited to prepare hypotensor
Application in object.
The present invention also provides the pupa albumen source Angiotensin-Convertings to inhibit polypeptide in preparing food
Using.
The present invention also provides the pupa albumen source Angiotensin-Convertings to inhibit polypeptide in preparing health care product
Application.
Compared with prior art, the invention has the following beneficial effects:
(1) a kind of present invention isolated blood vessel with ACE inhibitory activity from the hydrolysate of pupa albumen is tight
Plain converting Enzyme inhibits polypeptide, for treat the development and utilization of the food of hypertension, drug or health care product provide it is a kind of completely newly
Approach.
(2) raw material sources of the invention are resourceful, cheap in the by-product silkworm chrysalis of silk textile industry, have non-
Normal broad application prospect.
Detailed description of the invention
Fig. 1 is the ion exchange in the preparation method of Angiotensin-Converting inhibition polypeptide in pupa albumen source of the invention
Chromatogram and each component inhibiting rate figure.
Fig. 2 is the gel chromatography in the preparation method of Angiotensin-Converting inhibition polypeptide in pupa albumen source of the invention
Figure and each component inhibiting rate figure.
Fig. 3 is that pupa albumen source Angiotensin-Converting of the invention inhibits the first time in the preparation method of polypeptide anti-
Phase high-efficient liquid phase chromatogram.
Fig. 4 is second of reverse phase in the preparation method of pupa albumen source of the present invention Angiotensin-Converting inhibition polypeptide
High-efficient liquid phase chromatogram.
Fig. 5 is that pupa albumen source prepared by the present invention Angiotensin-Converting inhibits polypeptide under different reserve temperatures
Content change diagram.
Fig. 6 is that pupa albumen source prepared by the present invention Angiotensin-Converting inhibits polypeptide under different reserve temperatures
To the variation diagram of ACE inhibiting rate.
Fig. 7 is that pupa albumen source prepared by the present invention Angiotensin-Converting inhibits polypeptide to contain after manual simulation's digestion
Measure variation diagram.
Fig. 8 is that pupa albumen source prepared by the present invention Angiotensin-Converting inhibits polypeptide right after manual simulation's digestion
The variation diagram of ACE inhibiting rate.
Specific embodiment
Combined with specific embodiments below, further details of elaboration is made to the present invention, but embodiments of the present invention are not
It is confined to the range of embodiment expression.These embodiments are merely to illustrate the present invention, range and is not intended to limit the present invention.This
Outside, after reading the contents of the present invention, those skilled in the art can various modifications may be made to the present invention, these equivalent variations are same
Sample falls within the appended claims limited range of the present invention.
Experimental method used in following embodiments is conventional method unless otherwise specified.
In following embodiments thus material, reagent etc., be commercially available unless otherwise specified.
Embodiment1: the preparation of Angiotensin-Converting inhibition polypeptide
(1) freezing silkworm chrysalis is added in distilled water according to the ratio of 1:3, filters, is repeated 3 times after homogenate stirring 1h；It closes
And filtrate, filtrate heat 30min to albuminous degeneration under 100 DEG C of water bath conditions, then adjusting pH is 3.0 to make protein deposition, albumen
Solution stands 12h under the conditions of 4 DEG C, precipitates albumen sufficiently and is layered with solution, 4 DEG C of subsequent high speed refrigerated centrifuge, 8000r/min
It is centrifuged 45min and removes supernatant, collect precipitating, it is dry to get arriving silkworm chrysalis crude protein powder；
(2) silkworm chrysalis crude protein powder is added in distilled water according to mass ratio 1:50,1.5% is then added into solution
Neutral proteinase is digested, enzymolysis time 3h under the conditions of pH is 7.0, temperature is 50 DEG C；In 90 DEG C of water after the completion of enzymatic hydrolysis
Bath inactivation 10min, takes supernatant after hydrolyzate centrifugation；It is 5kDa ultrafiltration membrance filter with molecular cut off, ultrafiltration is penetrated into liquid cooling
It is lyophilized dry, obtains freeze-dried powder；
(3) powder obtained in step (2) is dissolved in concentration is the phosphate buffer that 0.01mol/L, pH are 8.5
In；It is splined on the D201 anion exchange resin chromatographic column (10 × 300mm) balanced with the speed of 1.0mg/mL, uses phosphoric acid
Salt buffer washes the column extremely absorption peak at 220nm and returns to baseline, elution flow rate 1.0mg/mL；Sample is carried out with NaCl solution
Gradient elution, elution flow rate 1.0mg/mL, gradient 0-1.0mg/mL；Each component is collected to be freeze-dried and examined
Active (see Fig. 1) is surveyed, is saved under the conditions of -20 DEG C；
(4) the best freeze-dried powder (i.e. component IE1) of the activity that step (3) obtains is splined on the Sephadex balanced
G-15 gel chromatographic columns (20 × 500mm), are eluted by mobile phase of water, elution flow rate 1.0mg/mL；Detection wavelength is
280nm；It collects each component to be freeze-dried and detected active (see Fig. 2), be saved under the conditions of -20 DEG C；
(5) the best freeze-dried powder (i.e. component GF2) of the activity that step (4) obtains is dissolved in ultrapure water, is carried out anti-
Phase high performance liquid chromatography is separated.Mobile phase, A phase: pure water (contains 0.1% trifluoroacetic acid)；B phase: acetonitrile, in 0-60min
Interior carry out gradient elution, acetonitrile concentration 5-30%；Detection wavelength is 220nm, collects each component (see Fig. 3, table 1) progress
It is freeze-dried and is detected activity, is saved under the conditions of -20 DEG C.
Efficiently reversed-phase liquid chromatography separation each component inhibitory activity (sample concentration 0.006mg/mL) for the first time of table 1
| Component | Retention time (min) | Inhibiting rate (%) |
| HP 1 | 0.0-10.0 | 47.18 |
| HP 2 | 10.0-12.0 | 69.05 |
| HP 3 | 12.0-14.0 | 47.78 |
| HP 4 | 14.0-16.0 | 56.23 |
| HP 5 | 16.0-18.0 | 74.31 |
| HP 6 | 18.0-20.0 | 76.27 |
| HP 7 | 20.0-22.0 | 69.08 |
| HP 8 | 22.0-24.0 | 56.39 |
| HP 9 | 24.0-26.0 | 35.91 |
| HP10 | 26.0-60.0 | 38.56 |
Second of table 2 efficient reversed-phase liquid chromatography separation each component inhibitory activity (sample concentration 0.004mg/mL)
| Component | Retention time (min) | Inhibiting rate (%) |
| HP 61 | 2.5-4.5 | 41.52 |
| HP 62 | 16.5-17.9 | 58.46 |
| HP 63 | 17.9-19.0 | 64.30 |
| HP 64 | 19.0-21.5 | 73.54 |
(6) by the best freeze-dried powder (i.e. component HP6) of activity that step (5) obtains again pass by Reversed phase high performance liquid chromatography into
Row separation.Mobile phase, A phase: the pure water containing 0.1% trifluoroacetic acid；B phase: acetonitrile, acetonitrile concentration 7%, Detection wavelength are
220nm collects each component (see Fig. 4, table 2) and is freeze-dried and is detected activity, saves under the conditions of -20 DEG C.It collects and protects
Staying the time is the component (i.e. HP64) of 19.0-21.5min, and Angiotensin-Converting can be obtained and inhibit polypeptide.
Polypeptide A CE inhibitory activity is inhibited to be measured the above-mentioned Angiotensin-Converting being prepared.
The measuring principle of ACE inhibitory activity are as follows: the ACE inhibitory activity measurement of polypeptide uses in-vitro simulated measuring method, former
Reason are as follows: substrate hippuroyl histamine acyl leucine (HHL) can hydrolyze under the catalytic action of ACE and generate hippuric acid (HA) and one
The dipeptides that a histidine and leucine combine can be measured by the content for the hippuric acid that high performance liquid chromatography detection generates
ACE activity；And ACE inhibits the presence of polypeptide that can inhibit the activity of ACE, and the production quantity of HA is caused to reduce, it can be with indirect determination
The activity of ACE inhibition polypeptide.
Steps are as follows for the method for measuring of ACE inhibitory activity: choose eppendof (EP) pipe as reactor, number A, B,
C is tested by the reaction system of table 3, and measurement ACE inhibits polypeptide to the inhibitory activity of ACE.
3 ACE of table inhibits polypeptide external activity to detect reaction system
0.45 μm of filter membrane is crossed after reaction terminating, then utilizes the content of high performance liquid chromatography (HPLC) measurement HA.
Liquid-phase condition are as follows: 15% methanol: 85% ultrapure water (contains 0.1%TFA), Detection wavelength 228nm, and 25 DEG C of column temperature, on
20 μ L of sample amount.
ACE inhibiting rate (IA) calculates according to the following formula:
In above formula: IA indicates ACE inhibiting rate (%)；AaIt indicates to hydrolyze the chromatography of hippuric acid generated due to substrate itself
Peak area (blank)；AbIt is (right by chromatographic peak area that there is no the hippuric acids under conditions of Vel-Tyr-Pro-Trp-Thr-Gln-Arg-Phe in expression reaction system
According to)；AcHippuric acid chromatographic peak area (sample) under the conditions of existing for indicating ACE and Vel-Tyr-Pro-Trp-Thr-Gln-Arg-Phe.
After measured, it is 15.78 μ that Angiotensin-Converting prepared by the present invention, which inhibits the external ACE of polypeptide to inhibit IC50,
g/mL。
Embodiment 2: Angiotensin-Converting inhibits the sequence analysis of polypeptide
Preparation-obtained Angiotensin-Converting inhibits polypeptide in Example 1, through substance assistant laser desorpted electricity
It is measured from flight time mass spectrum (MALDI-TOF/TOF-MS), molecular weight 613.2Da, amino acid sequence are as follows: Gly-
Ala-Met-Val-Val-His (as shown in SEQ ID NO:1).
Embodiment 3: reserve temperature inhibits the content of polypeptide and inhibiting rate to influence Angiotensin-Converting
Angiotensin-Converting preparation-obtained in embodiment 1 inhibition polypeptide is dissolved in 0.1mol/L borate buffer
In liquid (0.3mol/L containing NaCl, pH 8.3).Polypeptide solution is stored into 6h under the conditions of 40 DEG C, 60 DEG C, 80 DEG C.After end,
Measure the content (see Fig. 5) of polypeptide and its inhibiting rate to ACE in solution (see Fig. 6).Content of peptides is calculated according to the following formula to save
Rate:
The result shows that: after saving 6h under different reserve temperatures, Angiotensin-Converting inhibits the content of polypeptide to omit
Micro- decline (Fig. 5), but still higher ACE inhibiting rate (Fig. 6) is remained with, this illustrates that the angiotensin converting enzyme inhibitor has
Preferable thermal stability.
Embodiment 4: manual simulation's digestion inhibits the activity influence of polypeptide to Angiotensin-Converting
The method configuration simulated gastric fluid and simulated intestinal fluid provided according to " Chinese Pharmacopoeia 2010 editions ", prepared by embodiment 1
Angiotensin-Converting inhibits polypeptide to mix with simulated gastric fluid according to 1:1, and it is 7.0 that pH value is adjusted after digestion process 2h, with people
Work intestinal juice 1:1 mixing, digestion process 4h.The polypeptide in 0,2 (40 μ L of sampling) and 6h (80 μ L of sampling) separately sampled measurement solution
Content (see Fig. 7) and its inhibiting rate to ACE (see Fig. 8).
The result shows that: by simulated gastric fluid processing after, Angiotensin-Converting inhibit polypeptide content slightly under
It drops (Fig. 7), but ACE inhibiting rate changes less (Fig. 8)；Then using the processing of simulated intestinal fluid, Angiotensin-Converting suppression
The content of polypeptide processed acutely declines (Fig. 7), meanwhile, ACE inhibiting rate increases (Fig. 8), this explanation is after simulated intestinal fluid processing
With better ACE inhibiting rate, theoretical direction can be provided for the research of blood-pressure drug.
The aforementioned description to specific exemplary embodiment of the invention is in order to illustrate and illustration purpose.These descriptions
It is not wishing to limit the invention to disclosed precise forms, and it will be apparent that according to the above instruction, can much be changed
And variation.The purpose of selecting and describing the exemplary embodiment is that explaining specific principle of the invention and its actually answering
With so that those skilled in the art can be realized and utilize a variety of different exemplary implementation schemes of the invention and
Various chooses and changes.The scope of the present invention is intended to be limited by claims and its equivalents.
SEQUENCE LISTING
<110>Guangxi University
<120>a kind of pupa albumen source Angiotensin-Converting inhibits polypeptide and its preparation method and application
<130> 2015
<160> 4
<170> PatentIn version 3.3
<210> 1
<211> 6
<212> PRT
<213> Bombyx mori L.
<400> 1
Gly Ala Met Val Val His
1 5
Claims (6)
1. a kind of pupa albumen source Angiotensin-Converting inhibits polypeptide, the amino acid sequence of the polypeptide such as SEQ ID
Shown in NO.1, which is characterized in that the pupa albumen source Angiotensin-Converting inhibits the preparation method of polypeptide, including such as
Lower step:
(1) freezing silkworm chrysalis is added in distilled water according to the ratio of 1:3, filters, is repeated 3 times after homogenate stirring 1h；Merge filter
Liquid, filtrate heat 30min to albuminous degeneration under 100 DEG C of water bath conditions, then adjusting pH is 3.0 to make protein deposition, protein solution
12h is stood under the conditions of 4 DEG C, albumen is precipitated sufficiently and is layered with solution, 4 DEG C of subsequent high speed refrigerated centrifuge, 8000r/min centrifugation
45min removes supernatant, collects precipitating, dry to get arriving silkworm chrysalis crude protein powder；
(2) silkworm chrysalis crude protein powder is added in distilled water according to mass ratio 1:50, is completely dissolved, is then added in 1.5%
Property protease, pH be 7.0, temperature be 50 DEG C under the conditions of digested, enzymolysis time 3h；In 90 DEG C of water-baths after the completion of enzymatic hydrolysis
10min is inactivated, takes supernatant after hydrolyzate centrifugation；It is 5KDa ultrafiltration membrance filter with molecular cut off, ultrafiltration permeate is freezed
It is dry, obtain freeze-dried powder；
(3) freeze-dried powder obtained in step (2) is dissolved in concentration is 0.01mol/L, the phosphate buffer that pH is 8.5
In；It is splined on the anion exchange resin chromatographic column balanced with the speed of 1.0mL/min, washes column with phosphate buffer and extremely exists
Absorption peak returns to baseline, elution flow rate 1.0mL/min at 220nm；Gradient elution, elution stream are carried out to sample with NaCl solution
Speed is 1.0mL/min, gradient 0-1.0mg/mL；It is freeze-dried according to each component of period collection and detects work
Property, it is saved under the conditions of -20 DEG C；
(4) the best freeze-dried powder of activity in step (3) is splined on the Sephadex G-15 gel chromatographic columns balanced, with
Water is that mobile phase is eluted, elution flow rate 1.0mL/min；Detection wavelength is 280nm；Each component is collected according to the period
It is freeze-dried and is detected activity, is saved under the conditions of -20 DEG C；
(5) the best freeze-dried powder of activity in step (4) is dissolved in ultrapure water, carries out reversed-phase high performance liquid chromatography separation,
Mobile phase, A phase: the pure water containing 0.1% trifluoroacetic acid；B phase: acetonitrile；Detection wavelength is 220nm, each component of Fractional Collections into
Row is freeze-dried and detects activity, saves under the conditions of -20 DEG C；
(6) the best freeze-dried powder of the activity that step (5) obtains is again passed by into reversed-phase high performance liquid chromatography separation, mobile phase, A
Phase: the pure water containing 0.1% trifluoroacetic acid；B phase: acetonitrile；Detection wavelength is 220nm, and collection retention time is 19.0-21.5min
Component be freeze-dried to get Angiotensin-Converting inhibit polypeptide.
2. the pupa albumen source Angiotensin-Converting according to requiring 1 inhibits polypeptide, it is characterised in that: in step (5)
The acetonitrile carries out gradient elution, and concentration rises to 30% from 5% within the 0-60min time.
3. the pupa albumen source Angiotensin-Converting according to requiring 1 inhibits polypeptide, it is characterised in that: in step (6)
The concentration of the acetonitrile is 7%.
4. pupa albumen source according to claim 1 Angiotensin-Converting inhibits polypeptide in preparing blood-pressure drug
Application.
5. pupa albumen source according to claim 1 Angiotensin-Converting inhibits polypeptide preparing answering in food
With.
6. pupa albumen source according to claim 1 Angiotensin-Converting inhibits polypeptide preparing answering in health care product
With.
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| CN108220375A (en) * | 2018-02-10 | 2018-06-29 | 海盐县凌特生物科技有限公司 | The hypolipemic function peptide prepared using silkworm chrysalis as raw material |
| CN108396049B (en) * | 2018-03-08 | 2021-06-15 | 浙江汇能生物股份有限公司 | Preparation method of silkworm pupa protein polypeptide |
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Non-Patent Citations (3)
| Title |
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| 蚕蛹蛋白活性多肽的;闵建华;《中国优秀硕士论文全文数据库 农业科技辑》;CNKI;20111215;D051-20 * |
| 蚕蛹蛋白源血管紧张素转换酶抑制多肽的分离纯化;王朝阳等;《2015年中国化工学会年会论文集》;CNKI;20151017;全文 * |
| 酶解蚕蛹蛋白制备血管紧张素转换酶抑;贾俊强等;《蚕业科学》;CNKI;20111231;第37卷(第5期);第872-877页 * |
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