CN113896765A - Antioxidant peptide and preparation method and application thereof - Google Patents
Antioxidant peptide and preparation method and application thereof Download PDFInfo
- Publication number
- CN113896765A CN113896765A CN202111137452.0A CN202111137452A CN113896765A CN 113896765 A CN113896765 A CN 113896765A CN 202111137452 A CN202111137452 A CN 202111137452A CN 113896765 A CN113896765 A CN 113896765A
- Authority
- CN
- China
- Prior art keywords
- antioxidant
- peptide
- sequence
- polypeptide
- seq
- Prior art date
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- Granted
Links
- 101800000068 Antioxidant peptide Proteins 0.000 title claims abstract description 43
- 238000002360 preparation method Methods 0.000 title claims abstract description 12
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 44
- 230000003078 antioxidant effect Effects 0.000 claims abstract description 38
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 37
- 229920001184 polypeptide Polymers 0.000 claims abstract description 35
- 239000003963 antioxidant agent Substances 0.000 claims abstract description 26
- 108010053210 Phycocyanin Proteins 0.000 claims abstract description 23
- 235000016425 Arthrospira platensis Nutrition 0.000 claims abstract description 22
- 240000002900 Arthrospira platensis Species 0.000 claims abstract description 22
- 229940082787 spirulina Drugs 0.000 claims abstract description 22
- 150000001413 amino acids Chemical group 0.000 claims abstract description 15
- 238000012216 screening Methods 0.000 claims abstract description 4
- 230000002194 synthesizing effect Effects 0.000 claims abstract description 3
- 238000000034 method Methods 0.000 claims description 14
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- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 claims description 3
- 239000004480 active ingredient Substances 0.000 claims description 2
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
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Images
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
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Abstract
The invention provides an antioxidant peptide, which is characterized in that the amino acid sequence of the antioxidant peptide is SEQ ID NO. 1YLRTISYCC the invention also provides a preparation method of the antioxidant peptide derived from spirulina phycocyanin, which comprises the following steps: 1) analyzing a spirulina phycocyanin sequence by utilizing a bioinformatics program to obtain a polypeptide sequence group with potential antioxidant activity; 2) artificially synthesizing polypeptide sequences in a polypeptide sequence group; 3) and (3) verifying the antioxidant activity of the artificially synthesized polypeptide sequence, and screening to obtain the antioxidant peptide. The invention further provides application of the water-soluble antioxidant polypeptide. The antioxidant peptide provided by the invention is derived from a spirulina phycocyanin sequence, belongs to a natural antioxidant, has good safety, and has the total antioxidant capacity equivalent to that of glutathione through detection.
Description
Technical Field
The invention relates to the technical field of biomedicine, and particularly relates to an antioxidant peptide derived from spirulina phycocyanin.
Background
Reactive Oxygen Species (ROS) are normal metabolites of cells and are removed in time by cellular antioxidant systems. In some cases, the excessive accumulation in cells due to untimely clearance can cause oxidative damage to biological macromolecules in cells such as protein, lipid, DNA and the like, thereby accelerating the aging of the organism and causing various diseases such as neurodegenerative diseases, atherosclerosis, chronic inflammation, cancer and the like. Research shows that the in vitro intake of the antioxidant can eliminate excessive free radicals in vivo, reduce the oxidative stress level of the organism and play a role in preventing and even treating certain diseases. Oxidation is also one of the important causes of food deterioration, reduction of nutritional value and even generation of harmful substances, and thus antioxidants are in wide demand in the fields of health products, foods and cosmetics. Natural antioxidants are becoming increasingly popular because of the potential harm to human health from long-term intake of synthetic antioxidants. Among natural antioxidants, animal and plant-derived antioxidant peptides have attracted much attention because of their advantages of low molecular weight, high activity, easy absorption, no color or odor, no side effects, and the like. The antioxidant peptides have various types, different molecular sizes and different solubilities, and provide more choices for development and utilization of the antioxidant peptides.
The antioxidant capacity of antioxidant peptide is closely related to the composition of amino acid, and the action mechanism of amino acid depends on the functional group of the side chain. The most frequent components of the antioxidant peptide are aliphatic amino acid, polar uncharged amino acid, aromatic amino acid, positive charge amino acid and negative charge amino acid. The mechanism of aliphatic amino acids for scavenging free radicals is the addition of lipid free radicals, the mechanism of aromatic amino acids is similar to that of phenolic antioxidants, and through the transfer of hydrogen atoms, antioxidant free radicals are formed, positively charged amino acids can attract negative ion free radicals, and negatively charged amino acids can attract metal ions. The activity of antioxidant peptides is attributed to the complex interaction of their various functions including the inhibition of reactive oxygen species, scavenging free radicals, sequestering pro-oxidative metal ions, reducing hydroperoxide formation, scavenging specific oxidants, etc.
The antioxidant peptide is obtained mainly by the following ways: firstly, directly screening from animal and plant cell lysates; secondly, animal and plant proteins are used as raw materials, proper enzyme is selected for hydrolysis, polypeptide with certain molecular weight is separated and purified by methods such as ultrafiltration and chromatography, and the antioxidant activity of corresponding separated components is measured; after the sequence of the antioxidant peptide is determined, a large amount of antioxidant peptide can be obtained by separation and purification or synthesis technology; thirdly, protein with known sequence of animal and plant is analyzed by adopting a bioinformatics method, polypeptide fragments with high activity are predicted, and the polypeptide fragments are synthesized by a chemical synthesis method for activity verification.
Phycocyanin plays an important role in the photosynthesis of blue algae. Phycocyanin is widely used as a food colorant and a cosmetic additive because of its advantages of water solubility, non-toxicity, clearness, strong coloring power, etc.; in addition, researches show that phycocyanin has multiple physiological activities of resisting oxidation, mutation, tumor, radiation, aging, bacteria and immunity, and has potential application value in the field of biomedicine. However, these studies are mostly performed by using in vitro cell culture methods, phycocyanin is used as a biological macromolecule, has the characteristics of poor stability, easy inactivation and the like, and can stimulate an organism to generate antibodies and cause anaphylactic reaction when being directly applied in vivo. Although research shows that degradation products of phycocyanin still maintain biological activities such as antioxidation, the process for preparing active peptide by using an enzymolysis method is complex, the composition of the product is uneven, the quality of different batches is difficult to control, and the action mechanism of the active peptide is difficult to deeply research, so that the functional segment of phycocyanin generating antioxidation activity is not clear.
Disclosure of Invention
The invention identifies the polypeptide with biological activity such as oxidation resistance and the like in the spirulina phycocyanin by a bioinformatics method, then artificially synthesizes the polypeptide by a chemical method, and verifies the oxidation resistance activity by experiments, thereby determining a sequence section which generates the oxidation resistance function in the phycocyanin,
an antioxidant peptide, the amino acid sequence of which is SEQ ID NO. 1YLRTISYCC or SEQ ID NO. 2 AAANHVYHKF.
A method for preparing antioxidant peptide from spirulina phycocyanin comprises:
1) analyzing a spirulina phycocyanin sequence by utilizing a bioinformatics program to obtain a polypeptide sequence group with potential antioxidant activity;
2) artificially synthesizing polypeptide sequences in a polypeptide sequence group;
3) and (3) verifying the antioxidant activity of the artificially synthesized polypeptide sequence, and screening to obtain the antioxidant peptide.
In one embodiment according to the present invention, in step 1), the polypeptide length range is set to 8-15 amino acids when the phycocyanin sequence of spirulina is analyzed by bioinformatics program.
In one embodiment according to the present invention, the bioinformatics tool in step 1) is an AnOxPePred server.
In one embodiment according to the present invention, the amino acid sequence of phycocyanin of spirulina in step 1) is SEQ ID NO. 3.
GenBank:TVQ56796.1)SEQ ID NO:3
MKTPLTEAISAADSRGAYLSNTEMQAIFGRFNRASAGLDAAKAFNQNGQAWAEAAANHVYHKFPYTTQMEGSQYASTPEGKSKCVRDISHYLRTISYCCVVGGTGPLDEYVIAGVKEFNAALGLSPSWYVAALEFVRDNHGLSGDVGGEANIYLNYAINALS。
In one embodiment according to the present invention, the artificial synthesis method in step 2) is Fmoc solid phase synthesis.
In one embodiment according to the invention, the amino acid sequence of the antioxidant peptide is SEQ ID NO 1YLRTISYCC or SEQ ID NO 2 AAANHVYHKF.
The invention also provides the application of the antioxidant peptide or the antioxidant peptide obtained by the preparation method in preparing an antioxidant.
The invention further provides an antioxidant, wherein the antioxidant active ingredient at least comprises the antioxidant peptide or the antioxidant peptide obtained according to the preparation method.
Furthermore, the invention also provides application of the antioxidant in preparation of antioxidant functional food, health-care products and cosmetics.
The technical scheme of the invention has the following beneficial effects:
compared with the prior art, the invention has the advantages that:
1) the amino acid sequence of the antioxidant peptide is Tyr-Leu-Arg-Thr-Ile-Ser-Tyr-Cys-Cys (SEQ ID NO:1 YLRTISYCC), the antioxidant peptide is a novel antioxidant peptide, the antioxidant peptide has good antioxidant activity through detection, and the total antioxidant capacity of the antioxidant peptide is close to that of glutathione under the determination condition of the invention.
2) The antioxidant peptide is derived from a spirulina phycocyanin sequence, belongs to a natural antioxidant and has good safety.
3) The antioxidant peptide has good water solubility, is colorless and tasteless, and can be used as an additive of food, cosmetics or health products.
Drawings
FIG. 1 is a graph showing the results of the synthesis of antioxidant peptides measured by high performance liquid chromatography;
FIG. 2 is a graph showing the results of measuring the antioxidative activity of antioxidative peptides by an iron reduction method.
Detailed Description
In order to make the technical problems, technical solutions and advantages of the present invention more apparent, the following detailed description is given with reference to the accompanying drawings and specific embodiments.
Example 1 preparation of antioxidant peptides:
1. bioinformatics prediction of antioxidant activity sequence
The query of the alpha subunit sequence GenBank: TVQ56796.1(SEQ ID NO:3) of the phycocyanin of the spirulina:
MKTPLTEAISAADSRGAYLSNTEMQAIFGRFNRASAGLDAAKAFNQNGQAWAEAAANHVYHKFPYTTQMEGSQYASTPEGKSKCVRDISHYLRTISYCCVVGGTGPLDEYVIAGVKEFNAALGLSPSWYVAALEFVRDNHGLSGDVGGEANIYLNYAINALS。
the spirulina phycocyanin alpha subunit sequence SEQ ID NO:3 is submitted to an AnOxPered-1.0 server (AnOxPered-1.0-Services-DTU Health Tech), the polypeptide length range is set to be 8-15 amino acids, a protein mode is adopted to predict and obtain a series of polypeptide sequences with antioxidant activity, and the chemical synthesis and activity analysis are carried out on the polypeptide of which the sequence is SEQ ID NO:1(YLRTISYCC) and the sequence is SEQ ID NO:2 (AAANHVYHKF).
2. Solid phase synthesis of polypeptides
The Fmoc method is adopted, and the polypeptide is synthesized by a full-automatic polypeptide synthesizer. The cleaved polypeptide was precipitated with ether, centrifuged at 12000rpm for 10min, the precipitate was collected and lyophilized. After the freeze-dried crude peptide is dissolved, the crude peptide is centrifuged at 12000rpm for 10min to remove impurities, and then the crude peptide is put on a C18 reverse phase chromatographic column for High Performance Liquid Chromatography (HPLC) detection and purification and mass spectrometry detection and analysis.
Collecting target peak after HPLC purification, detecting to reach purity above 95%, lyophilizing into powder, and storing at-20 deg.C for use. The polypeptide sequence is synthesized by adopting a solid phase synthesis technology, the carboxyl terminal is aminated, the purity is over 95 percent through HPLC analysis, as shown in SEQ ID NO 1 shown in figure 1, and the structure of mass spectrometry shows that the polypeptide sequence is correct.
Example 2 determination of Total antioxidant Capacity of antioxidant peptides
Glutathione is used as a positive control, and the antioxidant activity of the two polypeptides is measured by using a total antioxidant capacity measuring kit (spectrophotometry), and the method comprises the following specific steps:
uniformly mixing reagents in the kit according to the specification, and preheating to 37 ℃ before use; the target peptide and the control peptide were prepared as 1mg/mL aqueous polypeptide solutions, respectively.
Adding 900 mu L of mixed solution, 30 mu L of polypeptide solution and 90 mu L of double distilled water into a test tube respectively, fully and uniformly mixing, reacting for 10 minutes, adding 120 mu L of double distilled water into a blank tube without adding polypeptide solution, adjusting zero by using the double distilled water, measuring the absorbance at 593nm by using the optical path of 1cm and 5 according to the formula: the antioxidant activity of the target and control peptides was calculated separately for total antioxidant capacity (U/mg prot) ═ 59.228X (Δ a + 0.0048)/Cpr.
As shown in FIG. 2, the polypeptide SEQ ID NO. 1 had an antioxidant activity of 35U/mg, the polypeptide SEQ ID NO. 2 had an antioxidant activity of 4U/mg, and glutathione was 40U/mg.
While the foregoing is directed to the preferred embodiment of the present invention, it will be understood by those skilled in the art that various changes and modifications may be made without departing from the spirit and scope of the invention as defined in the appended claims.
Sequence listing
<110> Qingdao university of science and technology
<120> antioxidant peptide, preparation method and application thereof
<141> 2021-09-27
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 9
<212> PRT
<213> Spirulina (Spirulina)
<400> 1
Tyr Leu Arg Thr Ile Ser Tyr Cys Cys
1 5
<210> 2
<211> 10
<212> PRT
<213> Spirulina (Spirulina)
<400> 2
Ala Ala Ala Asn His Val Tyr His Lys Phe
1 5 10
<210> 3
<211> 162
<212> PRT
<213> Spirulina (Spirulina)
<400> 3
Met Lys Thr Pro Leu Thr Glu Ala Ile Ser Ala Ala Asp Ser Arg Gly
1 5 10 15
Ala Tyr Leu Ser Asn Thr Glu Met Gln Ala Ile Phe Gly Arg Phe Asn
20 25 30
Arg Ala Ser Ala Gly Leu Asp Ala Ala Lys Ala Phe Asn Gln Asn Gly
35 40 45
Gln Ala Trp Ala Glu Ala Ala Ala Asn His Val Tyr His Lys Phe Pro
50 55 60
Tyr Thr Thr Gln Met Glu Gly Ser Gln Tyr Ala Ser Thr Pro Glu Gly
65 70 75 80
Lys Ser Lys Cys Val Arg Asp Ile Ser His Tyr Leu Arg Thr Ile Ser
85 90 95
Tyr Cys Cys Val Val Gly Gly Thr Gly Pro Leu Asp Glu Tyr Val Ile
100 105 110
Ala Gly Val Lys Glu Phe Asn Ala Ala Leu Gly Leu Ser Pro Ser Trp
115 120 125
Tyr Val Ala Ala Leu Glu Phe Val Arg Asp Asn His Gly Leu Ser Gly
130 135 140
Asp Val Gly Gly Glu Ala Asn Ile Tyr Leu Asn Tyr Ala Ile Asn Ala
145 150 155 160
Leu Ser
Claims (10)
1. An antioxidant peptide is characterized in that the amino acid sequence of the antioxidant peptide is SEQ ID NO. 1YLRTISYCC or SEQ ID NO. 2 AAANHVYHKF.
2. A preparation method of antioxidant peptide from spirulina phycocyanin is characterized by comprising the following steps:
1) analyzing a spirulina phycocyanin sequence by utilizing a bioinformatics program to obtain a polypeptide sequence group with potential antioxidant activity;
2) artificially synthesizing polypeptide sequences in a polypeptide sequence group;
3) and (3) verifying the antioxidant activity of the artificially synthesized polypeptide sequence, and screening to obtain the antioxidant peptide.
3. The method according to claim 2, wherein the polypeptide length is set to 8 to 15 amino acids in the step 1) when the phycocyanin sequence of spirulina is analyzed by bioinformatics program.
4. The method of claim 2, wherein the bioinformatics tool in step 1) is an AnOxPePred server.
5. The method according to claim 2, wherein the amino acid sequence of phycocyanin in Spirulina of step 1) is SEQ ID NO 3.
6. The method of claim 2, wherein the artificial synthesis in step 2) is Fmoc solid phase synthesis.
7. The method according to claim 2, wherein the amino acid sequence of the antioxidant peptide is SEQ ID NO. 1 or SEQ ID NO. 2.
8. Use of the antioxidant peptide according to claim 1 or obtained according to the preparation method of any one of claims 1 to 7 for the preparation of an antioxidant.
9. An antioxidant, characterized in that an antioxidant active ingredient comprises at least the antioxidant peptide as claimed in claim 1 or obtained by the production method according to any one of claims 1 to 7.
10. Use of the antioxidant according to claim 9 for the preparation of food, health care product and cosmetic with antioxidant function.
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Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2001299351A (en) * | 2000-04-20 | 2001-10-30 | Kyowa Hakko Kogyo Co Ltd | New polypeptide |
US20100281003A1 (en) * | 2009-04-02 | 2010-11-04 | New York University | System and uses for generating databases of protein secondary structures involved in inter-chain protein interactions |
CN101928743A (en) * | 2009-09-29 | 2010-12-29 | 香港中文大学 | Enzymolysis product of spirulina phycocyanin and application thereof |
CN104311629A (en) * | 2014-09-24 | 2015-01-28 | 四川大学 | Anti-oxidation peptide, and preparation method and application thereof |
CN106701874A (en) * | 2016-11-18 | 2017-05-24 | 中国科学院烟台海岸带研究所 | Preparation method for phycocyanin polypeptide |
CN107298710A (en) * | 2017-07-06 | 2017-10-27 | 浦江县欧立生物技术有限公司 | A kind of extracting method of spirulina phycocyanin |
CN108794587A (en) * | 2018-06-29 | 2018-11-13 | 上海铂辉生物科技有限公司 | A kind of biologically active polypeptide KVTPYQA and its preparation method and application |
WO2021015600A1 (en) * | 2019-07-25 | 2021-01-28 | 주식회사 네이처코아젠팜스 | Preparation method for spirulina hydrolysates prepared using enzyme and having improved thermostability and increased phycocyanin content |
-
2021
- 2021-09-27 CN CN202111137452.0A patent/CN113896765B/en active Active
Patent Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2001299351A (en) * | 2000-04-20 | 2001-10-30 | Kyowa Hakko Kogyo Co Ltd | New polypeptide |
US20100281003A1 (en) * | 2009-04-02 | 2010-11-04 | New York University | System and uses for generating databases of protein secondary structures involved in inter-chain protein interactions |
CN101928743A (en) * | 2009-09-29 | 2010-12-29 | 香港中文大学 | Enzymolysis product of spirulina phycocyanin and application thereof |
CN104311629A (en) * | 2014-09-24 | 2015-01-28 | 四川大学 | Anti-oxidation peptide, and preparation method and application thereof |
CN106701874A (en) * | 2016-11-18 | 2017-05-24 | 中国科学院烟台海岸带研究所 | Preparation method for phycocyanin polypeptide |
CN107298710A (en) * | 2017-07-06 | 2017-10-27 | 浦江县欧立生物技术有限公司 | A kind of extracting method of spirulina phycocyanin |
CN108794587A (en) * | 2018-06-29 | 2018-11-13 | 上海铂辉生物科技有限公司 | A kind of biologically active polypeptide KVTPYQA and its preparation method and application |
WO2021015600A1 (en) * | 2019-07-25 | 2021-01-28 | 주식회사 네이처코아젠팜스 | Preparation method for spirulina hydrolysates prepared using enzyme and having improved thermostability and increased phycocyanin content |
Non-Patent Citations (5)
Title |
---|
GENBANK: "MAG: phycocyanin subunit alpha [Spirulina sp. DLM2.Bin59]", 《GENBANK》, pages 56796 * |
JING ZHENG等: "Phycocyanin and phycocyanobilin from Spirulina platensis protect against diabetic nephropathy by inhibiting oxidative stress.", 《AMERICAN JOURNAL OF PHYSIOLOGY. REGULATORY, INTEGRATIVE AND COMPARATIVE PHYSIOLOGY》, no. 02, pages 110 * |
卓素珍;张虹;: "螺旋藻中藻蓝蛋白的生理功能及其提取纯化研究进展", 食品科技, no. 01 * |
宋春丽;: "抗氧化肽的研究进展", 农产品加工(学刊), no. 07 * |
陈洁;胡晓;: "蛋白水解物的抗氧化性研究与展望", 中国食品学报, no. 09 * |
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