CN119039381A - Antibacterial pig spleen peptide and preparation method and application thereof - Google Patents
Antibacterial pig spleen peptide and preparation method and application thereof Download PDFInfo
- Publication number
- CN119039381A CN119039381A CN202411516038.4A CN202411516038A CN119039381A CN 119039381 A CN119039381 A CN 119039381A CN 202411516038 A CN202411516038 A CN 202411516038A CN 119039381 A CN119039381 A CN 119039381A
- Authority
- CN
- China
- Prior art keywords
- peptide
- antibacterial
- porcine spleen
- active peptide
- mlw
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/081—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/0808—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
本申请涉及活性肽的技术领域，具体公开了一种抗菌猪脾肽及其制备方法与应用。本申请公开的抗菌猪脾肽选自MLW活性肽、LGF活性肽中的一种或多种；所述MLW活性肽的氨基酸序列为：甲硫氨酸‑亮氨酸‑色氨酸；所述LGF活性肽的氨基酸序列为：亮氨酸‑甘氨酸‑苯丙氨酸。本申请还提供了上述抗菌猪脾肽的制备方法以及在抗菌领域中的应用。利用本申请的技术方案制备的猪脾肽对革兰氏阴性菌、革兰氏阳性菌均具有优异的抗菌性，在抗菌领域具有广阔的应用前景。The present application relates to the technical field of active peptides, and specifically discloses an antibacterial porcine spleen peptide and its preparation method and application. The antibacterial porcine spleen peptide disclosed in the present application is selected from one or more of MLW active peptide and LGF active peptide; the amino acid sequence of the MLW active peptide is: methionine-leucine-tryptophan; the amino acid sequence of the LGF active peptide is: leucine-glycine-phenylalanine. The present application also provides a preparation method of the above-mentioned antibacterial porcine spleen peptide and its application in the antibacterial field. The porcine spleen peptide prepared using the technical solution of the present application has excellent antibacterial properties against both Gram-negative bacteria and Gram-positive bacteria, and has broad application prospects in the antibacterial field.
Description
Technical Field
The application relates to the technical field of active peptides, in particular to an antibacterial pig spleen peptide and a preparation method and application thereof.
Background
Bioactive peptides are derived from proteins, which are fragments having biological activity therein, with an excess over basic nutritional requirements
The unique biological activity is receiving increasing attention due to its contribution to human health. Since peptides are complex structures hidden in parent proteins, their biological activity is difficult to exert effectively. Can produce various physiological functions after being subjected to biochemical reactions such as enzymolysis and fermentation of external protease or gastrointestinal tract digestion, and has positive influence on human health.
In recent years, many studies have been directed to the identification of novel egg white protein peptides, and the release of chicken genomes has greatly improved the ability to identify proteins and polypeptides in complex samples. Studies show that the egg white proteins are identified after enzymolysis by specific proteases to obtain bioactive peptides with different types.
Currently, bioactive peptides have been applied to prevention and treatment, and pig spleen contains abundant proteins and a large amount of bioactive substances, and has physiological functions of disease prevention, immune regulation and the like. At present, the deep development and the utilization of the pig spleen are less, so that a great amount of high-quality protein resources are wasted. Therefore, the development of the high-quality pig spleen polypeptide product by taking the pig spleen as the raw material has good prospect and significance.
Disclosure of Invention
In order to solve the technical problems, the application provides an antibacterial pig spleen peptide and a preparation method and application thereof.
In a first aspect, the application provides an antibacterial pig spleen peptide, which is one or more selected from MLW (MLW) active peptide and LGF (LGF) active peptide, wherein the amino acid sequence of the MLW active peptide is methionine-leucine-tryptophan, and the amino acid sequence of the LGF active peptide is leucine-glycine-phenylalanine.
Preferably, the antibiotic pig spleen peptide is composed of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 1-10:1-10.
Preferably, the antibiotic pig spleen peptide is composed of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 1-5:6-10.
In a specific embodiment, the weight ratio of the MLW active peptide to the LGF active peptide may be 1-3：1、1-5：3、1-8：5、1-8：6、1-10：8、1：1-10、3-5：1、3-5：5、3-8：6、3-10：8、3：3-10、5-8：1、5-10：3、5：3-6、5：5-8、5：5-10、6-8：1、6-8：3、6-10：5、6-10：8、6：3-10、8：1-5、8：3-6、8：5-10、8：5-6、8：8-10、10：1-6、10：3-8、8-10：5、10：6-10、10：6-8.
In some specific embodiments, the weight ratio of the MLW active peptide to the LGF active peptide may also be 1：1、1：3、1：5、1：6、1：8、1：10、3：1、3：5、3：6、3：8、3：10、5：1、5：3、5：6、5：8、5：10、6：1、6：3、6：5、6：8、6：10、8：1、8：3、8：5、8：6、8：10、10：1、10：3、10：5、10：6、10：8.
Experimental analysis shows that the pig spleen peptide is formed by mixing the MLW active peptide and the LGF active peptide in the weight ratio, so that the antibacterial performance of the pig spleen peptide can be further improved.
The second aspect of the application provides a preparation method of the antibacterial pig spleen peptide, which specifically comprises the steps of taking pig spleen for enzymolysis, and then filtering, ultrafiltering, concentrating, vacuum drying, screening and separating.
Preferably, the specific steps of the pig spleen enzymolysis comprise taking fresh pig spleen, adding physiological saline, adjusting pH to 7.5-9.0, adding a mixture of pancreatin and alkaline protease in a weight ratio of 5:1-5, carrying out enzymolysis for 2-4h at 45-65 ℃, then adjusting pH to 6.5-7.5, adding flavourzyme, carrying out enzymolysis for 2-4h at 45-65 ℃, and boiling to inactivate enzyme.
Through experimental analysis, the applicant finds that in the process of pig spleen enzymolysis, the yield of MLW active peptide and LGF active peptide can be effectively improved by reasonably selecting a proper pH value environment and reasonably matching and selecting the types and the amounts of protease for two-stage enzymolysis.
Preferably, the weight ratio of the mixture of pancreatin and alkaline protease to the pig spleen is 0.0005-0.0015:1.
Preferably, the weight ratio of the mixture of pancreatin and alkaline protease to the pig spleen is 0.0008-0.0012:1.
Preferably, the weight ratio of the flavourzyme to the pig spleen is 0.0002-0.001:1.
Preferably, the weight ratio of the flavourzyme to the pig spleen is 0.0004-0.008:1.
In a third aspect, the application provides application of the antibacterial pig spleen peptide in preparation of antibacterial drugs.
In summary, the technical scheme of the application has the following effects:
One or more of the antibacterial pig spleen peptide MLW active peptide and the LGF active peptide prepared by the technical scheme of the application has excellent antibacterial property on gram-negative bacteria and gram-positive bacteria, and has wide application prospect in the antibacterial field.
The preparation method of the antibacterial pig spleen peptide is optimized, so that the MLW active peptide and the LGF active peptide with higher yield are obtained.
Detailed Description
The present application is described in further detail below in conjunction with examples, comparative examples and performance test experiments, which should not be construed as limiting the scope of the application as claimed.
Examples
Example 1
Example 1 provides an antimicrobial porcine spleen peptide.
The preparation method of the antibacterial pig spleen peptide in the embodiment comprises the following steps:
The pig spleen enzymolysis comprises the steps of taking 10kg of fresh pig spleen, washing the fresh pig spleen with drinking water until no blood water exists, crushing the fresh pig spleen with a colloid mill, adding 50kg of physiological saline, adjusting the pH value to 8.0, adding 0.01kg of mixture of pancreatin and alkaline protease with the weight ratio of 5:2, carrying out enzymolysis for 3 hours at 55 ℃, then adjusting the pH value to 7.0, adding 0.006kg of flavourzyme, carrying out enzymolysis for 3 hours at 50 ℃, boiling, inactivating enzyme, and obtaining enzymolysis liquid.
Centrifuging, ultrafiltering, concentrating, vacuum drying, centrifuging at 6000r/min for 20min to obtain supernatant, filtering with 0.45 μm filter membrane, and collecting filtrate for the next step. The filtrate was separated with an ultrafiltration membrane of 10kDa, 5kDa, 3kDa, and polypeptides of different molecular weights (> 10kDa, 5-10kDa, 3-5kDa, and <3 kDa) were collected, and the 4 polypeptide solutions of different molecular weights were lyophilized in vacuo and stored at-80 ℃.
Screening and separating, namely performing LC-MS/MS liquid chromatography of polypeptide components with molecular weight less than 3kDa, and performing LC-MS/MS analysis and database search comparison to obtain 958 mug MLW active peptide and 1547 mug LGF active peptide.
Examples 2 to 8
Examples 2-8 provide an antimicrobial porcine spleen peptide, respectively.
The difference between the above examples and example 1 is that the method for enzymolysis of pig spleen is different, and the method is specifically shown as follows.
In the example 2, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed to be free of blood by using drinking water, crushed by using a colloid mill, 10kg of physiological saline is added, the pH is regulated to 8.0, 0.016kg of mixture of pancreatin, alkaline protease and flavourzyme in a weight ratio of 5:2:1 is added, enzymolysis is carried out for 3 hours at 55 ℃, and enzyme activity is boiled and inactivated, so that enzymolysis liquid is obtained. 737. Mu.g of MLW active peptide and 1056. Mu.g of LGF active peptide were obtained in this example.
In example 3, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed to be free of blood by using drinking water, crushed by using a colloid mill, 10kg of physiological saline is added, the pH is adjusted to 8.0, 0.01kg of pancreatin and flavourzyme mixture with the weight ratio of 5:2 is added, the enzymolysis is carried out for 3 hours at 55 ℃, then the pH is adjusted to 7.0, 0.006kg of alkaline protease is added, the enzymolysis is carried out for 3 hours at 50 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. This example gives 925. Mu.g of MLW active peptide, 874. Mu.g of LGF active peptide.
In example 4, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed by drinking water until no blood exists, crushed by a colloid mill, 10kg of physiological saline is added, the pH value is regulated to 7.0, 0.006kg of flavourzyme is added, the enzymolysis is carried out for 3 hours at 50 ℃, then the pH value is regulated to 8.0, 0.01kg of a mixture of pancreatin and alkaline protease with the weight ratio of 5:2 is added, the enzymolysis is carried out for 3 hours at 55 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. This example gives 623. Mu.g of MLW active peptide and 1076. Mu.g of LGF active peptide.
In example 5, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed by drinking water until no blood exists, crushed by a colloid mill, 10kg of physiological saline is added, the pH is adjusted to 8.0, 0.01kg of mixture of pancreatin and alkaline protease with the weight ratio of 5:0.5 is added, the enzymolysis is carried out for 3 hours at 55 ℃, then the pH is adjusted to 7.0, 0.006kg of flavourzyme is added, the enzymolysis is carried out for 3 hours at 50 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. In this example 527. Mu.g of MLW active peptide and 1078. Mu.g of LGF active peptide were obtained.
In example 6, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed to be free of blood by using drinking water, crushed by using a colloid mill, 10kg of physiological saline is added, the pH is adjusted to 8.0, 0.01kg of pancreatin and alkaline protease mixture with the weight ratio of 5:6 is added, the enzymolysis is carried out for 3 hours at 55 ℃, then the pH is adjusted to 7.0, 0.006kg of flavourzyme is added, the enzymolysis is carried out for 3 hours at 50 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. 908. Mu.g of MLW active peptide, 779. Mu.g of LGF active peptide was obtained in this example.
In example 7, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed to be free of blood by using drinking water, crushed by using a colloid mill, 10kg of physiological saline is added, the pH is adjusted to 8.0, 0.01kg of mixture of pancreatin and alkaline protease with the weight ratio of 5:1 is added, the enzymolysis is carried out for 3 hours at 55 ℃, then the pH is adjusted to 7.0, 0.006kg of flavourzyme is added, the enzymolysis is carried out for 3 hours at 50 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. This example yielded 938 μg of MLW active peptide and 1378 μg of LGF active peptide.
In example 8, pig spleen is subjected to enzymolysis, namely 10kg of fresh pig spleen is washed by drinking water until no blood exists, crushed by a colloid mill, 10kg of physiological saline is added, the pH is adjusted to 8.0, 0.01kg of mixture of pancreatin and alkaline protease with the weight ratio of 5:5 (1:1) is added, enzymolysis is carried out for 3 hours at 55 ℃, then the pH is adjusted to 7.0, 0.006kg of flavourzyme is added, enzymolysis is carried out for 3 hours at 50 ℃, and the enzymolysis liquid is obtained after boiling and enzyme deactivation. This example yielded 1027 μg of MLW active peptide, 1239 μg of LGF active peptide.
Other process parameters in the above examples are the same as in example 1.
The preparation method of the embodiment 1-8 is used for preparing the antibacterial pig spleen peptide and experimental results, and the specific step of pig spleen enzymolysis is that the enzymolysis process is controlled by adjusting the pH value to 7.5-9.0, adding a mixture of pancreatin and alkaline protease with the weight ratio of 5:1-5, carrying out enzymolysis for 2-4 hours at 45-65 ℃, then adjusting the pH value to 6.5-7.5, adding flavourzyme, carrying out enzymolysis for 2-4 hours at 45-65 ℃, and obtaining the MLW active peptide and the LGF active peptide with higher yield.
Examples 9 to 17
Examples 9-17 provide an antimicrobial porcine spleen peptide, respectively.
The difference in the above examples is the weight ratio between the MLW active peptide and the LGF active peptide, as shown in detail below. The MLW and LGF active peptides in the above examples were derived from example 1.
In example 9, the antibiotic porcine spleen peptide was an MLW active peptide.
In example 10, the antibiotic porcine spleen peptide was LGF active peptide.
In example 11, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 1:10.
In example 12, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 3:8.
In example 13, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 5:6.
In example 14, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 10:1.
In example 15, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 6:5.
In example 16, the antibiotic porcine spleen peptide consisted of a mixture of MLW active peptide and LGF active peptide in a weight ratio of 1:15.
In example 17, the antibiotic porcine spleen peptide consisted of a 15:1 mixture of MLW active peptide and LGF active peptide.
Performance test
Antibacterial property evaluation of antibacterial pig spleen peptide the antibacterial pig spleen peptide powder was dissolved in sterile water to prepare 20mg/mL of an antibacterial pig spleen peptide sample solution, 100. Mu.L of Mueller Hinton Broth medium containing 5X 10 5 CFU/mL of bacteria was added to each well of a 96-well plate, and the last well was an empty medium control containing no bacteria. 10 mu L of an antibacterial pig spleen peptide sample solution is added into the first hole, and the sample solution is diluted downwards in sequence according to a double dilution method, wherein each concentration is three compound holes. The 96-well plates were sealed with sealing film and incubated at 37℃for 20 hours, and the absorbance at 600nm was measured with an ELISA reader to determine the Minimum Inhibitory Concentration (MIC).
The total number of bacteria used for the test is 4, wherein 2 gram-negative bacteria are respectively escherichia coli and klebsiella pneumoniae, and 2 gram-positive bacteria are respectively staphylococcus aureus and methicillin-resistant staphylococcus aureus.
The results are shown in Table 1.
Table 1 results of Performance test of the antibacterial porcine spleen peptides in examples 9-17
The detection results of the table 1 show that the pig spleen peptide prepared by the technical scheme of the application has excellent antibacterial property on 2 gram-negative bacteria such as escherichia coli and klebsiella pneumoniae, and 2 gram-positive bacteria such as staphylococcus aureus and methicillin-resistant staphylococcus aureus.
As is clear from the detection results of comparative examples 9-17, the application selects the pig spleen peptide formed by mixing the MLW active peptide and the LGF active peptide in a weight ratio of 1-10:1-10, thereby effectively improving the antibacterial performance of the pig spleen peptide, and further selects the pig spleen peptide formed by mixing the MLW active peptide and the LGF active peptide in a weight ratio of 1-5:6-10.
While the invention has been described in detail in the foregoing general description and with reference to specific embodiments thereof, it will be apparent to one skilled in the art that modifications and improvements can be made thereto. Accordingly, such modifications or improvements may be made without departing from the spirit of the invention and are intended to be within the scope of the invention as claimed.
Claims (10)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202411516038.4A CN119039381B (en) | 2024-10-29 | 2024-10-29 | Antibacterial pig spleen peptide and preparation method and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202411516038.4A CN119039381B (en) | 2024-10-29 | 2024-10-29 | Antibacterial pig spleen peptide and preparation method and application thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN119039381A true CN119039381A (en) | 2024-11-29 |
| CN119039381B CN119039381B (en) | 2025-02-11 |
Family
ID=93586039
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202411516038.4A Active CN119039381B (en) | 2024-10-29 | 2024-10-29 | Antibacterial pig spleen peptide and preparation method and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN119039381B (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101296942A (en) * | 2005-08-11 | 2008-10-29 | 安米林药品公司 | Hybrid polypeptides with selectable properties |
| US20120322745A1 (en) * | 2011-06-15 | 2012-12-20 | Queizuar ,S.L. | Optimized method for obtaining ace activity inhibitory peptides from whey, ace inhibitory peptides and food comprising them |
| US20150197546A1 (en) * | 2012-08-08 | 2015-07-16 | Daiichi Sankyo Company, Limited | Peptide library and use thereof |
| CN113861272A (en) * | 2021-11-08 | 2021-12-31 | 时代生物科技（深圳）有限公司 | Sea cucumber active peptide and preparation method thereof |
| CN115029406A (en) * | 2022-06-10 | 2022-09-09 | 浙江丰安生物制药有限公司 | Preparation method of spleen aminopeptide powder |
-
2024
- 2024-10-29 CN CN202411516038.4A patent/CN119039381B/en active Active
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101296942A (en) * | 2005-08-11 | 2008-10-29 | 安米林药品公司 | Hybrid polypeptides with selectable properties |
| US20120322745A1 (en) * | 2011-06-15 | 2012-12-20 | Queizuar ,S.L. | Optimized method for obtaining ace activity inhibitory peptides from whey, ace inhibitory peptides and food comprising them |
| US20150197546A1 (en) * | 2012-08-08 | 2015-07-16 | Daiichi Sankyo Company, Limited | Peptide library and use thereof |
| CN113861272A (en) * | 2021-11-08 | 2021-12-31 | 时代生物科技（深圳）有限公司 | Sea cucumber active peptide and preparation method thereof |
| CN115029406A (en) * | 2022-06-10 | 2022-09-09 | 浙江丰安生物制药有限公司 | Preparation method of spleen aminopeptide powder |
Non-Patent Citations (2)
| Title |
|---|
| LARISSA K. MARTIN等: "Specific CD8+ T cells recognize human herpesvirus 6B", 《EUR. J. IMMUNOL.》, vol. 42, 31 December 2012 (2012-12-31), pages 2904 * |
| RUI MA等: "Identification of novel antioxidant peptides from sea squirt (Halocynthia roretzi) and its neuroprotective effect in 6-OHDA-induced neurotoxicity", 《FOOD FUNCT.》, vol. 13, 31 December 2022 (2022-12-31) * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN119039381B (en) | 2025-02-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN111454334B (en) | A kind of anti-enzymatic antibacterial peptide II4II and preparation method and application | |
| CN109232717B (en) | A kind of antibacterial peptide targeting gram-negative bacteria and preparation method and application | |
| CN111533786B (en) | Beta-hairpin antibacterial peptide with tryptophan and arginine cross-chain interaction and preparation method thereof | |
| CN116874614B (en) | Antibacterial polypeptide APH171 with high activity and low cracking effect, and preparation method and application thereof | |
| CN111423501B (en) | Antibacterial peptide derived from scorpion venom as well as preparation method and application thereof | |
| CN109810178B (en) | A kind of anti-enzymolysis antibacterial peptide I9H12 and its preparation method and application | |
| CN109627299B (en) | Bacteriocin Gr17 with broad-spectrum antibacterial activity and application thereof | |
| CN109705195B (en) | A kind of Escherichia coli targeting antimicrobial peptide KI-QK and preparation method and application | |
| CN119039381B (en) | Antibacterial pig spleen peptide and preparation method and application thereof | |
| CN111253474B (en) | Antibacterial peptide RG-27 and application thereof | |
| CN101948896B (en) | Integrated preparation method of multifunctional cheese protein active peptide | |
| CN111647044B (en) | Antibacterial peptide rich in phenylalanine as well as preparation method and application thereof | |
| CN107022593B (en) | Colostrum peptide rich in proline polypeptide and preparation method thereof | |
| CN116375877B (en) | A cell-penetrating antibacterial peptide PW2 and its preparation method and application | |
| CN110294809B (en) | Targeting Staphylococcus aureus antimicrobial peptide S2 and its preparation method and application | |
| CN115057916B (en) | A kind of antioxidative polypeptide of Pinctada martensii meat and its preparation method and application | |
| CN106473023A (en) | A kind of preparation method of the Stichopus japonicus ovum tunning with blood pressure lowering anticoagulant functions | |
| CN114349825B (en) | A scorpion venom-derived peptide and its application in the preparation of antibacterial or anti-inflammatory drugs | |
| CN107058433B (en) | Preparation method of tartary buckwheat active peptide with antibacterial and antioxidant activities | |
| CN116804046A (en) | Cyclic cation antibacterial peptide and application thereof | |
| CN116376124A (en) | Method for rapidly separating and enriching exosomes based on chitosan with specific molecular weight | |
| CN113603748A (en) | Beta-folded antibacterial peptide HINGE-RV and preparation method and application thereof | |
| CN115925814B (en) | Antibacterial peptide RMR26 and preparation method and application thereof | |
| US4513083A (en) | Preparation of an antibiotic selectively effective against staphylococcus infections | |
| CN118852349B (en) | An α-helical antimicrobial peptide W37 and its preparation method and application |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |