CN105237625A - Angiotensin converting enzyme inhibitory polypeptide with silkworm pupa protein source, and preparation method and application thereof - Google Patents
Angiotensin converting enzyme inhibitory polypeptide with silkworm pupa protein source, and preparation method and application thereof Download PDFInfo
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- CN105237625A CN105237625A CN201510726848.7A CN201510726848A CN105237625A CN 105237625 A CN105237625 A CN 105237625A CN 201510726848 A CN201510726848 A CN 201510726848A CN 105237625 A CN105237625 A CN 105237625A
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Abstract
The invention belongs to the technical field of biological engineering, and specifically relates to an angiotensin converting enzyme inhibitory polypeptide with a silkworm pupa protein source, and a preparation method and application thereof. The angiotensin converting enzyme inhibitory polypeptide with the silkworm pupa protein source is the angiotensin converting enzyme inhibitory polypeptide obtained by separation from hydrolysis liquid, and has an amino acid sequence as shown in SEQ ID No.1. The angiotensin converting enzyme inhibitory polypeptide with the silkworm pupa protein source has the characteristics of novel structure, small molecular weight, high antihypertensive activity, etc., opens up a novel approach for development and utilization of food, medicines and health-care products for treatment of hypertension, and has extensive application prospects.
Description
Technical field
The invention belongs to technical field of bioengineering, be specifically related to a kind of pupa albumen source Zinc metallopeptidase Zace1 and suppress polypeptide and its preparation method and application.
Background technology
Zinc metallopeptidase Zace1 (AngotensinConvertingEnzyme, ACE) is that a kind of multi-functional born of the same parents be present in different tissues contain zinc two carboxypeptidase outward, can be activated by chlorion and have wider substrate specificity.It has important and crucial physiological function in renin-angiotensin system (RenialAngiotensinSystem, RAS) and kininase-kinin system (Kallikrein-Kinin, KKS).Its Main Function is that angiotensin I (AngiotensinIConvertingEnzyme) is changed into Angiotensin II (AngiotensinIIConvertingEnzyme), also can make bradykinin inactivation simultaneously, finally cause human blood-pressure to raise.
Zinc metallopeptidase Zace1 suppresses polypeptide to be made up of several amino acid and to have bioactive polypeptide, and ACE active region is had to the inhibitor of stronger avidity, their avidity with ACE than angiotensin I or bradykinin stronger, and be comparatively not easy to discharge from ACE land, reduce ACE activity or make it lose activity, thus hinder the angiotensin I converting one-tenth Angiotensin II of ACE catalysis, and hinder ACE hydrolysis bradykinin to become inactive fragments, thus reach the effect reduced blood pressure.
The information being disclosed in this background technology part is only intended to increase the understanding to general background of the present invention, and should not be regarded as admitting or imply in any form that this information structure has been prior art that persons skilled in the art are known.
Summary of the invention
The object of this invention is to provide a kind of pupa albumen source Zinc metallopeptidase Zace1 and suppress polypeptide, it extracts and obtains from the hydrolysate of pupa albumen, and it has obvious ACE inhibitory activity, provides theoretical direction for preparing Altace Ramipril.
The invention provides a kind of pupa albumen source Zinc metallopeptidase Zace1 and suppress polypeptide, its aminoacid sequence is as shown in SEQIDNO.1.
Present invention also offers the preparation method that described pupa albumen source Zinc metallopeptidase Zace1 suppresses polypeptide, comprise the steps:
(1) join in distilled water by freezing silkworm chrysalis according to the ratio of 1:3, homogenate is filtered after stirring 1h, repeats 3 times; Merging filtrate, filtrate heats 30min to protein denaturation under 100 DEG C of water bath condition, pH is regulated 3.0 to make protein deposition again, protein solution leaves standstill 12h under 4 DEG C of conditions, albumen is fully precipitated and solution layering, and high speed frozen centrifugation 4 DEG C, the centrifugal 45min of 8000r/min remove supernatant liquor, collecting precipitation subsequently, drying, namely obtains silkworm chrysalis crude protein powder;
(2) joining in distilled water by silkworm chrysalis crude protein powder according to mass ratio 1:50, dissolve completely, then add the neutral protease of 1.5%, is 7.0 at pH, and temperature is carry out enzymolysis under 50 DEG C of conditions, and enzymolysis time is 3h; At 90 DEG C of water-bath deactivation 10min after enzymolysis completes, after hydrolyzed solution is centrifugal, get supernatant liquor; Be 5KDa ultrafiltration membrance filter with molecular weight cut-off, by ultrafiltration permeate lyophilize, obtain lyophilized powder;
(3) lyophilized powder obtained in step (2) is dissolved in concentration is 0.01mol/L, pH is in the phosphate buffered saline buffer of 8.5; Be splined on the anionite-exchange resin chromatographic column balanced with the speed of 1.0mL/min, wash post to getting back to baseline at 220nm place absorption peak with phosphate buffered saline buffer, elution flow rate is 1.0mL/min; Carry out gradient elution by NaCl solution to sample, elution flow rate is 1.0mL/min, and gradient is 0-1.0mg/mL; Collect each component according to the time period and carry out lyophilize and detection of active, preserve under-20 DEG C of conditions;
(4) best lyophilized powder active in step (3) is splined on the SephadexG-15 gel chromatographic columns balanced, be that moving phase carries out wash-out with water, elution flow rate is 1.0mL/min; Determined wavelength is 280nm; Collect each component according to the time period and carry out lyophilize and detection of active, preserve under-20 DEG C of conditions;
(5) best lyophilized powder active in step (4) is dissolved in ultrapure water, carries out RPLC separation, moving phase, A phase: containing the pure water of 0.1% trifluoroacetic acid; B phase: acetonitrile; Determined wavelength is 220nm, and each component of Fractional Collections carries out lyophilize and detection of active, preserves under-20 DEG C of conditions;
(6) the best lyophilized powder of activity step (5) obtained is separated through RPLC again, moving phase, A phase: containing the pure water of 0.1% trifluoroacetic acid; B phase: acetonitrile; Determined wavelength is 220nm, and collection retention time is that the component of 17.5-20min carries out lyophilize, obtains Zinc metallopeptidase Zace1 and suppresses polypeptide.
As preferably, the acetonitrile described in step (5) carries out gradient elution, and its concentration rises to 30% from 5% within the 0-60min time.
As preferably, the acetonitrile described in step (6) carries out gradient elution, and its concentration rises to 9% from 7% within the 0-30min time.
Present invention also offers described pupa albumen source Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in Altace Ramipril.
Present invention also offers described pupa albumen source Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in food.
Present invention also offers described pupa albumen source Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in healthcare products.
Compared with prior art, the present invention has following beneficial effect:
(1) the present invention is separated and obtains a kind of Zinc metallopeptidase Zace1 suppression polypeptide with ACE inhibitory activity, for the exploitation for the treatment of hypertensive food, medicine or healthcare products provide a kind of brand-new approach from the hydrolysate of pupa albumen.
(2) raw material sources of the present invention are in the by product silkworm chrysalis of silk textile industry, its aboundresources, cheap, have application prospect widely.
Accompanying drawing explanation
Fig. 1 is that pupa albumen source of the present invention Zinc metallopeptidase Zace1 suppresses ion-exchange chromatography figure in the preparation method of polypeptide and each component inhibiting rate figure.
Fig. 2 is that pupa albumen source of the present invention Zinc metallopeptidase Zace1 suppresses gel chromatography figure in the preparation method of polypeptide and each component inhibiting rate figure.
Fig. 3 is the first time RPLC figure that pupa albumen source of the present invention Zinc metallopeptidase Zace1 suppresses in the preparation method of polypeptide.
Fig. 4 is the second time RPLC figure that pupa albumen source of the present invention Zinc metallopeptidase Zace1 suppresses in the preparation method of polypeptide.
Fig. 5 is that pupa albumen source Zinc metallopeptidase Zace1 prepared by the present invention suppresses polypeptide content figure under different reserve temperatures.
Fig. 6 is that pupa albumen source Zinc metallopeptidase Zace1 prepared by the present invention suppresses polypeptide under different reserve temperatures to the variation diagram of ACE inhibiting rate.
Fig. 7 is that pupa albumen source Zinc metallopeptidase Zace1 prepared by the present invention suppresses polypeptide content figure after manual simulation digests.
Fig. 8 is that pupa albumen source Zinc metallopeptidase Zace1 prepared by the present invention suppresses the variation diagram of polypeptide to ACE inhibiting rate after manual simulation's digestion.
Embodiment
Below in conjunction with specific embodiment, elaboration detailed is further done to the present invention, but embodiments of the present invention are not limited to the scope that embodiment represents.These embodiments only for illustration of the present invention, but not for limiting the scope of the invention.In addition, after reading content of the present invention, those skilled in the art can do various amendment to the present invention, and these equivalent variations fall within appended claims limited range of the present invention equally.
The experimental technique used in following embodiment if no special instructions, is ordinary method.
In following embodiment thus material, reagent etc., if no special instructions, all can obtain from commercial channels.
embodiment1: Zinc metallopeptidase Zace1 suppresses the preparation of polypeptide
(1) join in distilled water by freezing silkworm chrysalis according to the ratio of 1:3, homogenate is filtered after stirring 1h, repeats 3 times; Merging filtrate, filtrate heats 30min to protein denaturation under 100 DEG C of water bath condition, pH is regulated 3.0 to make protein deposition again, protein solution leaves standstill 12h under 4 DEG C of conditions, albumen is fully precipitated and solution layering, and high speed frozen centrifugation 4 DEG C, the centrifugal 45min of 8000r/min remove supernatant liquor, collecting precipitation subsequently, drying, namely obtains silkworm chrysalis crude protein powder;
(2) silkworm chrysalis crude protein powder is joined in distilled water according to mass ratio 1:50, in solution, then adds the neutral protease of 1.5%, pH be 7.0, temperature carries out enzymolysis under being 50 DEG C of conditions, enzymolysis time is 3h; At 90 DEG C of water-bath deactivation 10min after enzymolysis completes, after hydrolyzed solution is centrifugal, get supernatant liquor; Be 5kDa ultrafiltration membrance filter with molecular weight cut-off, by ultrafiltration permeate lyophilize, obtain lyophilized powder;
(3) be 0.01mol/L, pH by the powder dissolution obtained in step (2) in concentration be in the phosphate buffered saline buffer of 8.5; With the speed of 1.0mg/mL be splined on balanced D201 anionite-exchange resin chromatographic column (10 × 300mm), wash post to getting back to baseline at 220nm place absorption peak with phosphate buffered saline buffer, elution flow rate is 1.0mg/mL; Carry out gradient elution by NaCl solution to sample, elution flow rate is 1.0mg/mL, and gradient is 0-1.0mg/mL; Collect each component and carry out lyophilize and detection of active (see Fig. 1), preserve under-20 DEG C of conditions;
(4) the best lyophilized powder (i.e. component I E1) of activity step (3) obtained is splined on the SephadexG-15 gel chromatographic columns (20 × 500mm) balanced, be that moving phase carries out wash-out with water, elution flow rate is 1.0mg/mL; Determined wavelength is 280nm; Collect each component and carry out lyophilize and detection of active (see Fig. 2), preserve under-20 DEG C of conditions;
(5) the best lyophilized powder (i.e. component GF2) of activity step (4) obtained is dissolved in ultrapure water, carries out RPLC and is separated.Moving phase, A phase: pure water (containing 0.1% trifluoroacetic acid); B phase: acetonitrile, carries out gradient elution within the 0-60min time, and acetonitrile concentration is 5-30%; Determined wavelength is 220nm, collects each component (see Fig. 3, table 1) and carries out lyophilize and detection of active, preserve under-20 DEG C of conditions.
Table 1 first time, efficient reversed-phase liquid chromatography was separated each component inhibit activities (sample concentration 0.006mg/mL)
| 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 |
| HP 10 | 26.0-60.0 | 38.56 |
The efficient reversed-phase liquid chromatography of table 2 second time is separated each component inhibit activities (sample concentration 0.004mg/mL)
| Component | Retention time (min) | Inhibiting rate (%) |
| HP 61 | 2.5-4.5 | 41.52 |
| HP 62 | 15.5-16.5 | 51.46 |
| HP 63 | 16.5-17.5 | 67.30 |
| HP 64 | 17.5-20.0 | 77.60 |
(6) the best lyophilized powder (i.e. component HP6) of activity step (5) obtained is separated through Reversed phase high performance liquid chromatography again.Moving phase, A phase: containing the pure water of 0.1% trifluoroacetic acid; B phase: acetonitrile, carries out gradient elution within the 0-30min time, and acetonitrile concentration is 7-9%, and determined wavelength is 220nm, collects each component (see Fig. 4, table 2) and carries out lyophilize and detection of active, preserve under-20 DEG C of conditions.Collect the component (i.e. HP64) that retention time is 17.5-20min, Zinc metallopeptidase Zace1 can be obtained and suppress polypeptide.
Polypeptide A CE inhibit activities is suppressed to measure the above-mentioned Zinc metallopeptidase Zace1 prepared.
The measuring principle of ACE inhibitory activity is: the ACE inhibitory activity of polypeptide measures and adopts in-vitro simulated assay method, its principle is: substrate hippuryl histidyl leucine (HHL) is under the katalysis of ACE, the dipeptides generating urobenzoic acid (HA) and be combined with a Histidine and leucine can be hydrolyzed, detected the content of the urobenzoic acid generated by high performance liquid chromatography, ACE activity can be measured; And ACE suppresses the existence of polypeptide can suppress the activity of ACE, the growing amount of HA is caused to reduce, can the activity of indirect measurement ACE suppression polypeptide.
The method for measuring step of ACE inhibitory activity is as follows: choose eppendof (EP) pipe as reactor, numbering A, B, C, test by the reaction system of table 3, measures ACE and suppresses polypeptide to the inhibit activities of ACE.
Table 3ACE suppresses polypeptide external activity detection reaction system
Cross the filter membrane of 0.45 μm after reaction terminating, then utilize high performance liquid chromatography (HPLC) to measure the content of HA.
Liquid-phase condition is: 15% methyl alcohol: 85% ultrapure water (containing 0.1%TFA), determined wavelength 228nm, column temperature 25 DEG C, applied sample amount 20 μ L.
ACE inhibiting rate (IA) calculates according to the following formula:
In above formula: IA represents ACE inhibiting rate (%); A
arepresent because substrate self is hydrolyzed the chromatographic peak area (blank) of the urobenzoic acid generated; A
brepresent in reaction system there is not urobenzoic acid under the condition of ACE inhibitor by chromatographic peak area (contrast); A
crepresent the urobenzoic acid chromatographic peak area (sample) under ACE and the equal existent condition of ACE inhibitor.
After measured, the Zinc metallopeptidase Zace1 that prepared by the present invention suppresses the external ACE of polypeptide to suppress IC50 to be 12.61 μ g/mL.
embodiment 2: Zinc metallopeptidase Zace1 suppresses the sequential analysis of polypeptide
In Example 1, preparation-obtained Zinc metallopeptidase Zace1 suppresses polypeptide, measure through Matrix-assisted laser desorption ionization (MALDI-TOF/TOF-MS), its molecular weight is 603.7Da, and its aminoacid sequence is Gly-Asn-Pro-Trp-Met (as shown in SEQIDNO:1).
embodiment 3: reserve temperature suppresses content and the inhibiting rate impact of polypeptide to Zinc metallopeptidase Zace1
Polypeptide is suppressed to be dissolved in 0.1mol/L borate buffer (containing NaCl0.3mol/L, pH8.3) Zinc metallopeptidase Zace1 preparation-obtained in embodiment 1.Polypeptide solution is preserved 6h under 40 DEG C, 60 DEG C, 80 DEG C conditions.After end, measure the content (see Fig. 5) of polypeptide and the inhibiting rate (see Fig. 6) to ACE thereof in solution.Calculate content of peptides storage rate according to the following formula:
Result shows: preserve 6h under different reserve temperatures after, Zinc metallopeptidase Zace1 suppresses the content of polypeptide slightly to decline (Fig. 5), but still remaining with higher ACE inhibiting rate (Fig. 6), this illustrates that this angiotensin converting enzyme inhibitor has good thermostability.
embodiment 4: manual simulation's digestion suppresses the activity influence of polypeptide to Zinc metallopeptidase Zace1
The method configuration simulated gastric fluid provided according to " Chinese Pharmacopoeia 2010 editions " and simulated intestinal fluid, Zinc metallopeptidase Zace1 embodiment 1 prepared suppresses polypeptide to mix according to 1:1 with simulated gastric fluid, after digestion process 2h, adjust ph is 7.0, mixes, digestion process 4h with simulated intestinal fluid 1:1.The content (see Fig. 7) of polypeptide and the inhibiting rate (see Fig. 8) to ACE thereof in 0,2 (sampling 40 μ L) and 6h (sampling 80 μ L) difference sampling and measuring solution.
Result shows: after simulated gastric fluid process, and Zinc metallopeptidase Zace1 suppresses the content of polypeptide slightly to decline (Fig. 7), but ACE inhibiting rate change little (Fig. 8); Subsequently again through the process of simulated intestinal fluid, Zinc metallopeptidase Zace1 suppresses the content of polypeptide acutely to decline (Fig. 7), simultaneously, ACE inhibiting rate raises (Fig. 8), this explanation has better ACE inhibiting rate after simulated intestinal fluid process, can provide theoretical direction for the research of Altace Ramipril.
The aforementioned description to concrete exemplary of the present invention is to illustrate and the object of illustration.These descriptions not want the present invention to be defined as disclosed precise forms, and obviously, according to above-mentioned instruction, can much change and change.The object selected exemplary embodiment and describe is to explain certain principles of the present invention and practical application thereof, thus those skilled in the art can be realized and utilize various different exemplary of the present invention and various different selection and change.Scope of the present invention is intended to limited by claims and equivalents thereof.
Claims (7)
1. pupa albumen source Zinc metallopeptidase Zace1 suppresses a polypeptide, and it is characterized in that, the aminoacid sequence of described polypeptide is as shown in SEQIDNO.1.
2. pupa albumen source according to claim 1 Zinc metallopeptidase Zace1 suppresses the preparation method of polypeptide, it is characterized in that, comprises the steps:
(1) join in distilled water by freezing silkworm chrysalis according to the ratio of 1:3, homogenate is filtered after stirring 1h, repeats 3 times; Merging filtrate, filtrate heats 30min to protein denaturation under 100 DEG C of water bath condition, pH is regulated 3.0 to make protein deposition again, protein solution leaves standstill 12h under 4 DEG C of conditions, albumen is fully precipitated and solution layering, and high speed frozen centrifugation 4 DEG C, the centrifugal 45min of 8000r/min remove supernatant liquor, collecting precipitation subsequently, drying, namely obtains silkworm chrysalis crude protein powder;
(2) joining in distilled water by silkworm chrysalis crude protein powder according to mass ratio 1:50, dissolve completely, then add the neutral protease of 1.5%, is 7.0 at pH, and temperature is carry out enzymolysis under 50 DEG C of conditions, and enzymolysis time is 3h; At 90 DEG C of water-bath deactivation 10min after enzymolysis completes, after hydrolyzed solution is centrifugal, get supernatant liquor; Be 5KDa ultrafiltration membrance filter with molecular weight cut-off, by ultrafiltration permeate lyophilize, obtain lyophilized powder;
(3) lyophilized powder obtained in step (2) is dissolved in concentration is 0.01mol/L, pH is in the phosphate buffered saline buffer of 8.5; Be splined on the anionite-exchange resin chromatographic column balanced with the speed of 1.0mL/min, wash post to getting back to baseline at 220nm place absorption peak with phosphate buffered saline buffer, elution flow rate is 1.0mL/min; Carry out gradient elution by NaCl solution to sample, elution flow rate is 1.0mL/min, and gradient is 0-1.0mg/mL; Collect each component according to the time period and carry out lyophilize and detection of active, preserve under-20 DEG C of conditions;
(4) best lyophilized powder active in step (3) is splined on the SephadexG-15 gel chromatographic columns balanced, be that moving phase carries out wash-out with water, elution flow rate is 1.0mL/min; Determined wavelength is 280nm; Collect each component according to the time period and carry out lyophilize and detection of active, preserve under-20 DEG C of conditions;
(5) best lyophilized powder active in step (4) is dissolved in ultrapure water, carries out RPLC separation, moving phase, A phase: containing the pure water of 0.1% trifluoroacetic acid; B phase: acetonitrile; Determined wavelength is 220nm, and each component of Fractional Collections carries out lyophilize and detection of active, preserves under-20 DEG C of conditions;
(6) the best lyophilized powder of activity step (5) obtained is separated through RPLC again, moving phase, A phase: containing the pure water of 0.1% trifluoroacetic acid; B phase: acetonitrile; Determined wavelength is 220nm, and collection retention time is that the component of 17.5-20min carries out lyophilize, obtains Zinc metallopeptidase Zace1 and suppresses polypeptide.
3. the pupa albumen source Zinc metallopeptidase Zace1 as requested described in 2 suppresses the preparation method of polypeptide, it is characterized in that: the acetonitrile described in step (5) carries out gradient elution, and its concentration rises to 30% from 5% within the 0-60min time.
4. the pupa albumen source Zinc metallopeptidase Zace1 as requested described in 2 suppresses the preparation method of polypeptide, it is characterized in that: the acetonitrile described in step (6) carries out gradient elution, and its concentration rises to 9% from 7% within the 0-30min time.
5. pupa albumen source according to claim 1 Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in Altace Ramipril.
6. pupa albumen source according to claim 1 Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in food.
7. pupa albumen source according to claim 1 Zinc metallopeptidase Zace1 suppresses polypeptide preparing the application in healthcare products.
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| CN105859868A (en) * | 2016-06-08 | 2016-08-17 | 广西科技大学 | Angiotensin converting enzyme inhibition peptide and preparing method thereof |
| CN109055468A (en) * | 2018-08-21 | 2018-12-21 | 浙江大学 | Mulberry silkworm chrysalis anticancer active peptide BPP-1 and the preparation method and application thereof |
| CN109182428A (en) * | 2018-08-21 | 2019-01-11 | 浙江大学 | Mulberry silkworm chrysalis anticancer active peptide BPP-2 and the preparation method and application thereof |
| CN117229352A (en) * | 2023-09-08 | 2023-12-15 | 广州白云山维一实业股份有限公司 | Heptapeptide and application thereof |
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105859868A (en) * | 2016-06-08 | 2016-08-17 | 广西科技大学 | Angiotensin converting enzyme inhibition peptide and preparing method thereof |
| CN109055468A (en) * | 2018-08-21 | 2018-12-21 | 浙江大学 | Mulberry silkworm chrysalis anticancer active peptide BPP-1 and the preparation method and application thereof |
| CN109182428A (en) * | 2018-08-21 | 2019-01-11 | 浙江大学 | Mulberry silkworm chrysalis anticancer active peptide BPP-2 and the preparation method and application thereof |
| CN117229352A (en) * | 2023-09-08 | 2023-12-15 | 广州白云山维一实业股份有限公司 | Heptapeptide and application thereof |
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