CN117683085A - An ACE inhibitory peptide derived from cooking wine residue and its preparation method and application - Google Patents
An ACE inhibitory peptide derived from cooking wine residue and its preparation method and application Download PDFInfo
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- CN117683085A CN117683085A CN202311720042.8A CN202311720042A CN117683085A CN 117683085 A CN117683085 A CN 117683085A CN 202311720042 A CN202311720042 A CN 202311720042A CN 117683085 A CN117683085 A CN 117683085A
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- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
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Abstract
本发明属于料酒渣资源化利用技术领域，公开了一种来自料酒渣的ACE抑制肽。为提高料酒渣的经济利用价值，从中开发出具有降血压功效的寡肽，本发明以料酒渣为原料，通过水浸提法、膜过滤法、高效液相色谱法等多种分离纯化方法得到了一种降血压肽单体，氨基酸序列为WCYND，分子量为699.73Da，具有活性好，能人工合成，安全无毒的特点。经测定其ACE抑制活性，该降血压寡肽在体外对血管紧张素转化酶具有抑制作用，可以应用于降血压领域，且有利于料酒渣的高值化综合利用。
The invention belongs to the technical field of resource utilization of cooking wine residue and discloses an ACE inhibitory peptide derived from cooking wine residue. In order to improve the economic utilization value of cooking wine dregs and develop oligopeptides with blood pressure-lowering effects, the present invention uses cooking wine dregs as raw materials and obtains them through various separation and purification methods such as water extraction, membrane filtration, and high-performance liquid chromatography. A blood pressure-lowering peptide monomer has been developed. The amino acid sequence is WCYND and the molecular weight is 699.73Da. It has the characteristics of good activity, can be synthesized artificially, and is safe and non-toxic. After measuring its ACE inhibitory activity, the blood pressure-lowering oligopeptide has an inhibitory effect on angiotensin-converting enzyme in vitro, can be applied in the field of blood pressure lowering, and is conducive to the high-value comprehensive utilization of cooking wine residues.
Description
Technical Field
The invention relates to the technical field of cooking wine residue resource utilization, in particular to an ACE (angiotensin converting enzyme) inhibitory peptide from cooking wine residue sources, and a preparation method and application thereof.
Background
Hypertension is a disease characterized by elevated arterial pressure. The normal adult blood pressure standard is that the systolic pressure is less than or equal to 140mmHg and the diastolic pressure is less than or equal to 90mmHg. If the adult systolic pressure is more than or equal to 160mmHg and the diastolic pressure is more than or equal to 95mmHg, the hypertension can be judged. Hypertension is a serious chronic health disease which is most common in the world today, the early symptoms of the disease are not obvious, cerebral vascular rupture or sudden heart disease can occur in the later stage, and the disease seriously endangers the health condition of human bodies. According to research, many systems in human bodies are closely related to the regulation of blood pressure, and antihypertensive drugs can act on any link affecting the regulation of blood pressure so as to reduce the blood pressure. It has been demonstrated that the RAS system is a key target for the treatment of hypertension, ACE inhibitors can reduce mortality in patients with hypertension, and chemical synthetic drugs such as captopril and lisinopril are clinically used for the treatment of hypertension, but they may be accompanied by some side effects. In contrast, natural bioactive peptides are more environmentally friendly and safer, and thus have become a hot spot for research in recent years. Besides the daily healthy diet, the increase of the intake of fruits and vegetables and high-quality protein can reduce blood pressure, and the active peptide fragments contained in the protein also greatly help the human health.
Rice is one of the most important crops in the world, and the nutritional value of rice protein is comparable with animal proteins such as egg, fish, shrimp and beef protein. However, china has low level in the aspects of development and comprehensive utilization of rice resources, and the research level is behind developed countries, so that the economic value of rice is not fully reflected. Cooking wine is one of the ways to process and utilize rice, and a large amount of fermentation base material, also called distillers' grains, is produced in the production process. At present, most factories sell the dried materials as feeds at low price except a few factories, and other factories directly discharge the materials as wastes, so that the waste of protein resources is caused, and the environment is polluted. The cooking wine residue is rich in various amino acids, vitamins and various trace elements, and has rich nutrition, and various researches prove that polypeptide with antihypertensive activity can be extracted from the cooking wine residue at present, and the polypeptide has the advantage of no toxic or side effect, so that the polypeptide becomes the focus of attention in the field of antihypertensive research.
Disclosure of Invention
The technical problem to be solved by the invention is to overcome the problems in the prior art and provide the oligopeptide extracted from the cooking wine residues.
It is a second object of the present invention to provide the use of the above-described oligopeptides.
The aim of the invention is achieved by the following technical scheme:
an oligopeptide extracted from cooking wine residues, wherein the amino acid sequence of the oligopeptide is shown in SEQ ID NO: 1.
The invention takes cooking wine residues as raw materials, and obtains the antihypertensive oligopeptide by using various separation and purification means, wherein the oligopeptide has the amino acid sequence of WCYND and the molecular weight of 699.73Da, and has the characteristics of high purity, good activity, capability of being artificially synthesized, safety and innocuity.
The ACE inhibitory activity test result shows that the antihypertensive peptide has remarkable inhibitory effect on ACE in vitro, can be applied to the field of blood pressure reduction, and is beneficial to comprehensive utilization of cooking wine residues.
Therefore, the invention also provides application of the oligopeptide in preparing a functional product for inhibiting the activity of angiotensin converting enzyme ACE.
The invention also provides a preparation method of the oligopeptide, which is to carry out enzymolysis on cooking wine residues, and then aim to improve the inhibition activity of angiotensin converting enzyme, and obtain the oligopeptide through multiple separation and purification.
Preferably, the enzyme used for enzymolysis in the preparation method is neutral protease.
More preferably, the preparation method comprises the following steps:
s1, mixing the cooking wine residue raw material with water, adding neutral protease, performing enzymolysis reaction for 3 hours in a water bath at 46 ℃, stopping enzymolysis, cooling to room temperature, and centrifuging. The supernatant was retained and its ACE inhibition was measured;
s2, respectively passing the samples with high ACE inhibitory activity obtained in the step S1 through a microporous filter membrane with the size of 0.45 mu m and a microporous filter membrane with the size of 0.2 mu m, a coiled membrane with the size of 3000Da and an ultrafiltration cup membrane with the size of 1000Da, and respectively measuring ACE inhibitory activities of trapped fluid and permeate fluid;
s3, treating the high ACE inhibition active component obtained in the S2 by macroporous adsorption resin, eluting by using ethanol with different concentrations, and respectively measuring ACE inhibition rates. The high activity fraction was then separated by Sephadex G-25 column chromatography, absorbance was monitored, and the resultant fraction was subjected to ACE inhibition assay.
S4, subjecting the component with high ACE inhibitory activity obtained in the step S3 to high performance liquid chromatography separation by a C18 column (20 mm multiplied by 450mm,10 mu m), wherein the liquid chromatography elution conditions are as follows: 0-20min,10-30% B;20-50min,30-57% B;50-60min,57-90% B;60-62min,90-10% B;62-70min,10% B. Collecting the components according to the peak type of the chromatogram, taking the ACE inhibition rate as a judgment basis, and collecting and reserving the ACE inhibition active components with high activity for further subdivision;
s5, carrying out component analysis on the ACE high-activity component obtained in the S4 through an analytical high performance liquid chromatography, wherein the elution conditions of the liquid chromatography are as follows: 0-30min,5-35% B;30-50min,35-45% B;50-50.1min,45-70% B;50.1-60min,90% B. Collecting monomer peaks and measuring ACE inhibition rate to obtain high-activity ACE inhibition oligopeptide;
s6, identifying the high-activity monomer obtained in the S5 by using a UPLC-LTQ-Orbitrap-Velos Pro mass spectrum analyzer and a PPSQ amino acid sequencer. The EASY-nLC conditions were as follows: the elution condition is 0-60min,15-50% B;50-70min,50-100% B;70-75min,100% B; flow rate: 300nl/min; mobile phase: phase A is 0.1% (v/v) aqueous formic acid and phase B is pure acetonitrile. The mass spectrometry conditions were as follows: the sample injection flow rate is 20 mu l/min; sample volume 5. Mu.l; selecting a positive ion mode, and carrying out ESI electrospray ion source with a spray voltage of 2.0kV; collision mode: CID; scanning range: 350-2000m/z; the acquisition time was 75min. Analyzing the polypeptide structure by adopting Proteome Discoverer software.
The invention also provides application of the oligopeptide in preparation of functional products for reducing blood pressure.
The invention also provides an inhibitor of angiotensin converting enzyme ACE, the active ingredient of which is amino acid sequence shown in SEQ ID NO:1, and a polypeptide represented by formula 1.
The invention also provides a functional product for reducing blood pressure, the active ingredients of which are amino acid sequences shown in SEQ ID NO:1, and a polypeptide represented by formula 1.
Compared with the prior art, the invention has the following beneficial effects:
the invention provides ACE inhibitory peptide from cooking wine residues. In order to improve the economic utilization value of the cooking wine residue and develop the oligopeptide with the blood pressure reducing effect, the invention takes the cooking wine residue as a raw material, and obtains the antihypertensive peptide monomer through a plurality of separation and purification methods such as a water extraction method, a membrane filtration method, a high performance liquid chromatography method and the like, wherein the amino acid sequence is WCYND, the molecular weight is 699.73Da, and the oligopeptide has the characteristics of good activity, capability of being artificially synthesized, safety and innocuity. The ACE inhibitory activity of the antihypertensive oligopeptide is measured, so that the antihypertensive oligopeptide has an inhibitory effect on angiotensin converting enzyme in vitro, can be applied to the field of blood pressure reduction, and is beneficial to high-value comprehensive utilization of cooking wine residues.
Drawings
FIG. 1 shows an ACE inhibition ratio comparison of an enzymatic crude extract with commercially available antihypertensive peptides;
FIG. 2 is an ACE inhibitory activity of a membrane filtration component compared to commercially available antihypertensive peptides;
FIG. 3 is an illustration of the ACE inhibitory activity of ethanol eluted fractions of different concentrations compared to commercially available antihypertensive peptides;
FIG. 4 is an illustration of the ACE inhibitory activity of a macroporous adsorbent resin separation component in comparison to commercially available antihypertensive peptides;
FIG. 5 is an illustration of an ACE inhibitory activity of a prepared liquid phase separation fraction as compared to a commercially available antihypertensive peptide;
FIG. 6 is an analysis of ACE inhibitory activity of liquid phase separation monomers compared to commercially available antihypertensive peptides;
FIG. 7 is a primary mass spectrum of monomer F1 and a PPSQ sequencing result.
Detailed Description
The following describes the invention in more detail. The description of these embodiments is provided to assist understanding of the present invention, but is not intended to limit the present invention. In addition, the technical features of the embodiments of the present invention described below may be combined with each other as long as they do not collide with each other.
Example 1
The separation and purification of ACE inhibitory peptide comprises the following steps:
s1, mixing the cooking wine residue raw material with water, and adding 0.3% of neutral protease under the condition of pH of 7.2. The enzymatic hydrolysis was carried out in a water bath at 46℃for 3h, then the mixture was subjected to a high temperature of 90℃for 10min to stop the enzymatic hydrolysis, and after cooling the hydrolysate to room temperature, it was centrifuged at 4000rpm for 20 min. The supernatant was retained and its ACE inhibition was determined to be 40.33%. As shown in fig. 1.
S2, sequentially passing the enzymolysis crude extract through a 0.45 mu m microporous filter membrane and a 0.2 mu m microporous filter membrane, separating the 0.2 mu m permeate from a 1000Da ultrafiltration cup membrane (the whole ultrafiltration cup is used at normal temperature, and the pressure of a sealed space is kept at 0.1-0.22 MPa), and respectively measuring ACE inhibition activities of the trapped fluid and the permeate, wherein the highest inhibition activity of the 1000Da permeate is found, and the highest inhibition activity is up to 56.26 percent, as shown in figure 2.
S3, eluting the 1000Da ultrafiltration permeate with 10%, 20%, 35%, 50% and 70% ethanol through macroporous adsorption resin, respectively measuring ACE inhibition ratios, finding that the inhibition activity of a 10% ethanol elution sample is highest and reaches 58.85%, and then secondarily separating 10% ethanol elution components through a Sephadex G-25 chromatographic column, wherein the inhibition activity of M4 is found to be 63.29%, and the activity of all the components is highest, as shown in figures 3 and 4.
S4, separating the M4 component by means of preparative high performance liquid chromatography after passing the M4 component through a 0.45 mu M filter membrane. The preparation conditions are as follows: (1) chromatographic column: 20 mm. Times.450 mm, C18 filler (10 μm,MachereyNagel, france); (2) mobile phase: the pump A is ultrapure water, and the pump B is acetonitrile; (3) flow rate: 10ml/min; (4) sample injection amount: 5ml; (5) detection wavelength: 214nm. ACE inhibitory Activity determination the activity of the D3 fraction was up to 67.07% followed by sub-division of the D3 fraction. The results are shown in FIG. 5.
S5, carrying out component analysis on the D3 by using an analytical high performance liquid chromatography, wherein the separation conditions are as follows: (1) chromatographic column: ECOSIL C18 (260 mm. Times.4.6 mm,5 μm); (2) mobile phase: the pump A is ultrapure water, and the pump B is acetonitrile; (3) flow rate: 1ml/min; (4) sample injection amount: 20 μl; (5) detection wavelength: 214nm. ACE inhibitory Activity measurement the activity of the F1 monomer was up to 77.57% when ACE inhibitory activity was higher than that of commercially available antihypertensive peptides. The F1 monomer peak was then collected and structurally resolved. The results are shown in FIG. 6.
S6, collecting the peak tips of the D3 by using an analytical HPLC, finding that F1 is a target monomer with high ACE inhibition activity, and comparing by using a UPLC-LTQ-Orbitrap-Velos Pro mass spectrum analyzer and combining Proteome Discoverer (PD) software, and detecting by using a PPSQ amino acid sequencer. The molecular weight of the primary mass spectrogram corresponding to the main peak position of the ion flow graph can be deduced to be about 701.49Da [ M+H ], the result is imported into a Uniprot library in PD software, the searched matching sequence with possibility is compared with the result given by PPSQ, the amino acid sequence of F1 can be identified as Trp-Cys-Tyr-Asn-Asp (WCYND), the molecular weight of the F1 is 699.73Da, and the matching sequence is the oligopeptide with ACE inhibitory activity which is completely discovered by the patent. The results are shown in FIG. 7.
The ACE inhibition activity detection method is carried out according to the following method:
10. Mu.L of ACE solution (0.2U/mL) was added to the blank, control and sample groups, 10. Mu.L of ACEI was added to the sample group, 10. Mu.L of buffer was added to the blank and control groups, 30. Mu.L of HHT solution (6.5 mmol/mL, HHT was dissolved in 0.1mol/L boric acid buffer, pH8.3, containing 0.3 mol/LNaCl) was added to all groups after 5min at 37℃and after 1h reaction at 37℃the control and sample groups were quenched by adding 80. Mu.L of 1.0mol/L HCl, respectively.
TABLE 1
Liquid chromatography conditions: (1) chromatographic column: ECOSIL C18 (260 mm. Times.4.6 mm,5 μm); (2) mobile phase: acetonitrile: ultrapure water=25:75 (containing 0.1% (v/v) TFA); (3) flow rate: 1mL/min; (4) detection wavelength: 228nm; (5) column temperature: 30 ℃; (6) sample injection amount: 20. Mu.L.
And (3) calculating results:
principle of: HIL rapidly breaks down under the catalysis of ACE and produces hippuric acid (Hip) and dipeptides (His-Leu, HL), with a maximum absorption at 228 nm. When ACEI sample is added, ACE enzyme activity is inhibited, and the generation amount of hippuric acid is reduced, so that the inhibition rate of ACEI on ACE activity can be estimated by measuring the generation amount of hippuric acid through high performance liquid chromatography.
The calculation formula is as follows:
wherein: r: ACEI sample inhibition (%) of ACE;
a: peak area of hippuric acid in control group;
b: peak area of hippuric acid in ACEI group was added;
A 0 : peak area of hippuric acid in blank tube.
The embodiments of the present invention have been described in detail above, but the present invention is not limited to the described embodiments. It will be apparent to those skilled in the art that various changes, modifications, substitutions and alterations can be made to these embodiments without departing from the principles and spirit of the invention, and yet fall within the scope of the invention.
Claims (7)
1. An oligopeptide extracted from cooking wine residues, which is characterized in that the amino acid sequence of the oligopeptide is shown in SEQ ID NO: 1.
2. Use of the oligopeptide of claim 1 for the preparation of a functional product for inhibiting the activity of angiotensin converting enzyme ACE.
3. The method for producing an oligopeptide according to claim 1, wherein the cooking wine residue is subjected to enzymolysis to increase the inhibiting activity of angiotensin converting enzyme, and the cooking wine residue is obtained by multiple separation and purification.
4. The method according to claim 3, wherein the enzyme used for the enzymolysis is neutral protease.
5. Use of the oligopeptide according to claim 1 for the preparation of a functional product for reducing blood pressure.
6. An inhibitor of angiotensin converting enzyme ACE, characterized in that the active ingredient is an amino acid sequence as shown in SEQ ID NO:1, and a polypeptide represented by formula 1.
7. A functional product for reducing blood pressure is characterized in that the active ingredient is a polypeptide with an amino acid sequence shown as SEQ ID NO:1, and a polypeptide represented by formula 1.
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1907412A2 (en) * | 2005-06-30 | 2008-04-09 | Campina Nederland Holding B.V. | Peptides inhibiting angiotensin-converting enzyme |
| CN111484545A (en) * | 2020-03-31 | 2020-08-04 | 华南农业大学 | Blood pressure-lowering oligopeptide derived from rice distiller's grains and its preparation method and application |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1907412A2 (en) * | 2005-06-30 | 2008-04-09 | Campina Nederland Holding B.V. | Peptides inhibiting angiotensin-converting enzyme |
| CN111484545A (en) * | 2020-03-31 | 2020-08-04 | 华南农业大学 | Blood pressure-lowering oligopeptide derived from rice distiller's grains and its preparation method and application |
Non-Patent Citations (2)
| Title |
|---|
| WENJUAN QU, ET AL.: "Preparation of corn ACE inhibitory peptide-ferrous chelate by dual-frequency ultrasound and its structure and stability analyses", 《ULTRASON S ONOCHEM.》, vol. 83, 30 January 2022 (2022-01-30), pages 1 - 10 * |
| 王琳琳 等: "食源血管紧张素转化酶抑制肽研究进展", 《中国果菜》, no. 6, 15 June 2020 (2020-06-15), pages 77 - 82 * |
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