CN111560051A - Shrimp-derived nonapeptide with iron absorption promoting activity and application thereof - Google Patents
Shrimp-derived nonapeptide with iron absorption promoting activity and application thereof Download PDFInfo
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- CN111560051A CN111560051A CN202010455581.3A CN202010455581A CN111560051A CN 111560051 A CN111560051 A CN 111560051A CN 202010455581 A CN202010455581 A CN 202010455581A CN 111560051 A CN111560051 A CN 111560051A
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- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 title claims abstract description 107
- 229910052742 iron Inorganic materials 0.000 title claims abstract description 54
- 238000010521 absorption reaction Methods 0.000 title description 29
- 230000001737 promoting effect Effects 0.000 title description 15
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- 230000036541 health Effects 0.000 claims abstract description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 5
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- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 7
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- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
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- IWLZBRTUIVXZJD-OLHMAJIHSA-N Asp-Thr-Asp Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(O)=O IWLZBRTUIVXZJD-OLHMAJIHSA-N 0.000 description 1
- QIQABBIDHGQXGA-ZPFDUUQYSA-N Glu-Ile-Arg Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O QIQABBIDHGQXGA-ZPFDUUQYSA-N 0.000 description 1
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- 229920002684 Sepharose Polymers 0.000 description 1
- UOLGINIHBRIECN-FXQIFTODSA-N Ser-Glu-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O UOLGINIHBRIECN-FXQIFTODSA-N 0.000 description 1
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- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- IEECXTSVVFWGSE-UHFFFAOYSA-M iron(3+);oxygen(2-);hydroxide Chemical compound [OH-].[O-2].[Fe+3] IEECXTSVVFWGSE-UHFFFAOYSA-M 0.000 description 1
- 210000001630 jejunum Anatomy 0.000 description 1
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- 230000008092 positive effect Effects 0.000 description 1
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- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
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Images
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- 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
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a shrimp-derived nonapeptide and application thereof, wherein the amino acid sequence of the shrimp-derived nonapeptide is as follows: Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg, molecular weight 1093.05 Da. The shrimp-derived nonapeptide is obtained by using a polypeptide synthesizer, synthesizing by a solid phase synthesis method, purifying by high-phase liquid chromatography and freeze-drying. The shrimp-derived nonapeptide can resist gastrointestinal tract digestion, and Fe is transported for 90min by a rat exocarpium-turning model2+The transport capacity is 65.6 +/-12.6 mu g/mL; can enhance the delivery capacity of iron, and can be used in the fields of functional health products, nutrition-enriched foods, etc.
Description
Technical Field
The invention relates to the fields of functional foods, nutrition-enriched foods and the like, in particular to a shrimp-derived nonapeptide and application thereof.
Background
The iron element is a trace element with the largest content in a human body, and is widely distributed in the human body, wherein the content in an adult male is 50mg, and the content in an adult female is 35 mg. The human body mainly realizes the regulation and control of iron through the absorption of iron by intestinal tracts, 1-2 mg of iron is lost by the human body every day and is usually obtained through dietary supplement, and the iron in the diet enters the human body and is mainly absorbed in the duodenum and the upper part of the jejunum. The iron in food is mainly classified into heme iron and non-heme iron. The heme iron exists in animal food, and has high absorption rate of 15-35%. However, the diet of residents in China is mainly based on plant food, and iron in the plant food is non-heme iron. After being ingested, the non-heme iron is influenced by pH to form insoluble ferric hydroxide precipitate under the human intestinal environment, so that the absorption rate is low, and various dietary factors such as polyphenol compounds and oxalic acid phytic acid in diet influence the absorption and utilization of the non-heme iron, so that the iron deficiency is caused. Therefore, how to improve the absorption utilization of non-heme iron has attracted extensive attention.
Some researches show that some 'meat factors' have positive effects on improving the absorption and utilization of iron. The food-derived active peptide for promoting iron absorption can promote the absorption of iron and enhance the bioavailability of the iron. The food-derived active peptide for promoting iron absorption has wide sources and generally has smaller molecular weight, and can improve the transport effect of iron in intestinal tracts.
Disclosure of Invention
The invention aims to provide a shrimp-derived nonapeptide which is obtained from a pancreatic protease hydrolysate of Antarctic krill by mass spectrometry and has the function of promoting iron ion absorption, and the shrimp-derived nonapeptide can be applied to the fields of functional health products, nutrition-enriched foods and the like. The invention uses a rat external intestine turning capsule model to evaluate the function of the shrimp-derived nonapeptide for delivering iron ions.
An amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1, and is Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg, which is abbreviated as DTDSEEEIR, and the molecular weight is 1093.05 Da; wherein the content of the first and second substances,
asp represents the corresponding residue of the amino acid designated England under the name Aspartic acid;
thr represents the corresponding residue of an amino acid having the English name Threonine and the Chinese name Threonine;
ser represents the corresponding residue of an amino acid with the English name of Serine and the Chinese name of Serine;
glu represents the corresponding residue of the amino acid known by the English name Glutamic acid and the Chinese name Glutamic acid;
ile represents the corresponding residue of amino acid with English name of Isoleucine and Chinese name of Isoleucine;
arg represents the corresponding residue of the amino acid known by the English name Arginine and the Chinese name Arginine.
The amino acid sequence of the invention adopts a standard Fmoc scheme, and a reasonable polypeptide synthesis method is realized by screening resin. Linking the C-terminal carboxyl of target polypeptide with insoluble high-molecular resin in the form of covalent bond, taking the amino group of said amino acid as starting point, reacting with the carboxyl of another amino acid to form peptide bond, repeating said process to form target polypeptide sequence, then separating the peptide bond from resin to obtain the target polypeptide product. Polypeptide synthesis is a process of repeated addition of amino acids, and the solid phase synthesis sequence is synthesized from the C-terminus to the N-terminus. After the synthesis is finished, purifying by adopting a high performance liquid chromatography, quickly freezing by using liquid nitrogen, and carrying out vacuum freeze drying to obtain a polypeptide finished product.
The shrimp-derived nonapeptide DTDSEEEIR prepared by the invention has certain capability of resisting digestion of gastrointestinal protease and has the capability of delivering iron ions through a rat abdominating intestinal tract model. In Fe2+60mg/mL of shrimp-derived nonapeptide Fe2+When the molar ratio is 1:2 and the transport time is 90min through a rat external intestine turning capsule model, Fe2+The transport capacity is 65.6 +/-12.6 mu g/mL; and same Fe2+FeSO of concentration4The solution is transported for 90min by rat intestinal tract turning model, and Fe2+The transport volume was only 44.7. + -. 6.0. mu.g/mL.
Delivery of Fe by shrimp-derived nonapeptide2+The amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
An application of shrimp-derived nonapeptide in preparing iron-supplementing medicine, food and/or health-care products, wherein the amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
An iron supplement is prepared by adding shrimp-derived nonapeptide and Fe2+Contains shrimp-derived nonapeptide and Fe2+The amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
Preferably, the iron supplement contains shrimp-derived nonapeptides and Fe2+The molar ratio is 1: 2.
Compared with the prior art, the invention has the following advantages and technical effects:
the invention synthesizes the shrimp-derived nonapeptide for the first time, the integrity of the shrimp-derived nonapeptide is better maintained after the shrimp-derived nonapeptide is digested by gastrointestinal tracts, iron ions can be delivered through a rat enteroclysis model, the shrimp-derived nonapeptide has the effect of promoting iron absorption, and can be applied to the fields of iron supplements, nutrition-enriched foods and the like.
Drawings
FIG. 1 is an HPLC chart of the synthetic shrimp-derived nonapeptide Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg (abbreviation DTDSEEEIR) of the present invention.
FIG. 2 is an ESI-MS spectrum of the synthetic shrimp-derived nonapeptide Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg (abbreviation DTDSEEEIR) of the present invention.
FIG. 3 is an HPLC chromatogram of the shrimp-derived nonapeptide DTDSEEEIR of the present invention after simulated digestion in the gastrointestinal tract.
FIG. 4 shows shrimp-derived nonapeptide DTDSEEEIR and Fe2+HPLC profile after simulated digestion of gastrointestinal tract at a molar ratio of 1: 2.
FIG. 5 shows shrimp-derived nonapeptide DTDSEEEIR and Fe2+HPLC profile after simulated digestion of gastrointestinal tract at a molar ratio of 1: 1.
FIG. 6 shows shrimp-derived nonapeptide DTDSEEEIR and Fe2+HPLC profile after simulated digestion of gastrointestinal tract at a molar ratio of 2: 1.
FIG. 7 shows Fe of the present invention2+Graph of iron transport results at a concentration of 60 mg/mL. Different letters indicate that there is a significant difference between groups (P)<0.05)。
FIG. 8 shows the shrimp-derived nonapeptide DTDSEEEIR and Fe2+In a molar ratio ofHPLC (high performance liquid chromatography) spectra after absorption by a rat intestinal tract externalization model at the ratio of 1: 2.
FIG. 9 shows shrimp-derived nonapeptide DTDSEEEIR and Fe2+HPLC (high performance liquid chromatography) spectra after absorption by a rat intestinal tract externalizing model when the molar ratio is 1: 1.
FIG. 10 shows shrimp-derived nonapeptide DTDSEEEIR and Fe2+HPLC (high performance liquid chromatography) after absorption by a rat intestinal tract externalizing model when the molar ratio is 2: 1.
FIG. 11 shows the transport amount of the shrimp-derived nonapeptide DTDSEEEIR of the present invention after absorption in the rat exocarpium capsulizing model. Different letters indicate significant differences between groups (P < 0.05).
Detailed Description
The present invention is further illustrated by the following specific examples, but the scope of the invention is not limited thereto. For process parameters not specifically noted, reference may be made to conventional techniques.
The shrimp-derived nonapeptide is abbreviated as DTDSEEEIR, and has a molecular weight of 1093.05 Da. The sequence is as follows: Asp-Thr-Asp-Ser-Glu-Glu-Ile-Arg; wherein the content of the first and second substances,
asp represents the corresponding residue of the amino acid designated England under the name Aspartic acid;
thr represents the corresponding residue of an amino acid having the English name Threonine and the Chinese name Threonine;
ser represents the corresponding residue of an amino acid with the English name of Serine and the Chinese name of Serine;
glu represents the corresponding residue of the amino acid known by the English name Glutamic acid and the Chinese name Glutamic acid;
ile represents the corresponding residue of amino acid with English name of Isoleucine and Chinese name of Isoleucine;
arg represents the corresponding residue of the amino acid known by the English name Arginine and the Chinese name Arginine.
The amino acid sequence of the invention adopts a standard Fmoc scheme, and a reasonable polypeptide synthesis method is realized by screening resin. The C-terminal carboxyl group of the target polypeptide is covalently linked to an insoluble polymer resin, and then the amino group of the amino acid is used as a starting point to react with the carboxyl group of another molecule of amino acid to form a peptide bond. The process is repeated continuously to obtain the target polypeptide sequence. And after the synthesis reaction is finished, removing the protecting group, and separating the peptide chain from the resin to obtain the target product. Polypeptide synthesis is a process of repeated addition of amino acids, and the solid phase synthesis sequence is synthesized from the C-terminus to the N-terminus. After the synthesis is finished, purifying by adopting a high performance liquid chromatography, quickly freezing by using liquid nitrogen, and carrying out vacuum freeze drying to obtain a polypeptide finished product.
The shrimp-derived nonapeptide DTDSEEEIR prepared by the invention can resist gastrointestinal tract digestion and has the capability of delivering iron ions through a rat outer turning intestinal capsule model.
In the invention, the iron content is 60mg/mL, and the shrimp-derived nonapeptide is Fe2+When the molar ratio is 1:2 and the transport time is 90min through a rat external intestine turning capsule model, Fe2+The transport capacity is 65.6 +/-12.6 mu g/mL; while FeSO of the same iron concentration4The solution is transported for 90min by rat intestinal tract turning model, and Fe2+The transport volume was only 44.7. + -. 6.0. mu.g/mL.
Example 1: obtaining of shrimp-derived nonapeptide DTDSEEEIR
S1, preparing the euphausia superba defatted powder: adding n-hexane/anhydrous ethanol mixture into Euphausia superba (Euphausia superba) powder, and stirring at 50 deg.C for 6 hr; then, filtering out an organic solvent by suction filtration, adding an equal volume of n-hexane/absolute ethyl alcohol mixed solution, stirring for 6 hours at 50 ℃, filtering out the organic solvent by suction filtration, naturally drying and crushing a filter cake to obtain euphausia superba defatted powder; wherein the feed-liquid ratio of the antarctic krill powder to the mixed solution of n-hexane/absolute ethyl alcohol is 1:10g/mL (w/v); the n-hexane/anhydrous ethanol mixed solution is prepared by mixing n-hexane and anhydrous ethanol according to the volume ratio of 3: 1;
s2, preparation of antarctic krill zymolyte: adding water into the degreased euphausia superba powder obtained in the step S1 until the concentration of substrate protein is 2g/100mL to prepare an enzymolysis reaction solution, adjusting the pH to 8.0, adding trypsin into the enzymolysis reaction solution according to the ratio of 3000U/g substrate protein, and reacting for 3 hours; adjusting the pH value to 7.0, carrying out water bath at 100 ℃ for 10min, centrifuging at 10000r/min for 20min, taking the supernatant, and carrying out freeze drying to obtain an antarctic krill zymolyte;
s3, separation and purification of active peptide for promoting iron absorption: loading of Sepharose 6Fastflow was packed into a chromatographic column and 0.2M FeCl was added3Loading onto a chromatographic column at a flow rate of 1 mL/min; after incubation for 30min, washing with ultrapure water to remove unbound iron ions; equilibrating the chromatographic column with equilibration buffer; then, the antarctic krill zymolyte obtained in the step S2 is dissolved in an equilibrium buffer solution with the concentration of 10mg/mL, and the sample is loaded and incubated for 30 min; washing away peptides which are not combined with iron by using an equilibrium buffer solution, eluting by using an eluent to obtain iron-combined peptides, collecting, freezing and drying to obtain the active peptide for promoting iron absorption; wherein the equilibration buffer is a solution containing 0.05M sodium acetate and 0.1M NaCl at pH 5.5; the eluent is pH5.5 and contains 0.02M Na2HPO40.1M NaCl, 0.01mg/mL ammonium acetate solution;
s4, and HPLC-MS/MS identification of the active peptide for promoting iron absorption: the peptide sequence of the iron absorption promoting active peptide of step S3 was identified by a NanoLC-MS/MS mass spectrometer, and a shrimp-derived nonapeptide was identified by searching the peptide sequence from the established database using Peaks Studio software.
The experimental results are as follows: a shrimp-derived nonapeptide with the molecular weight of 1093.05Da, which contains two Asp residues, three Glu residues and one Ser residue and one Thr residue, is identified, and the amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO:1, Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg (DTDSEEEIR) contains a potential iron ion binding site.
Example 2: solid phase synthesis of shrimp-derived nonapeptide DTDSEEEIR
Selecting high molecular resin (Hefei Semano Biotechnology Co., Ltd.), covalently connecting carboxyl of Arg with resin according to the characteristics of amino acid sequence Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg (SEQ ID NO:1), then carrying out condensation reaction on amino of Arg and carboxyl of Ile, then adding Glu, sequentially adding amino acids from right to left until the last amino acid Asp is connected, and cutting off the resin to obtain the target polypeptide. Purifying by high performance liquid chromatography, wherein the chromatography column is VYDAC-C18, the size is 4.6 x 250mm, and the mobile phase A is acetonitrile containing 0.1% (v/v) trifluoroacetic acid; mobile phase B was water containing 0.1% (v/v) trifluoroacetic acid; the elution conditions were: 0-20.0 min: the mobile phase A rises from 22.0% to 32.0%; 20.0-20.1 min: the mobile phase A rises from 32.0% to 100.0%; the flow rate was 1.0mL/min, and the detection wavelength was 220 nm. Quick freezing with liquid nitrogen, and freeze drying to obtain shrimp-derived nonapeptide with purity over 98% and actual purity of 98.49%, and identifying structure by ESI-MS. FIG. 1 is an HPLC chart of shrimp-derived nonapeptide Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg. FIG. 2 is an ESI-MS diagram of shrimp-derived nonapeptide Asp-Thr-Asp-Ser-Glu-Glu-Glu-Ile-Arg.
Example 3: digestion characteristics of shrimp-derived nonapeptides
S1, preparation methods of simulated stomach digestive juice and intestinal digestive juice: dissolving 40mg of pepsin in 1mL of 0.1N HCl to prepare simulated gastric digestive juice; 120mg sodium taurocholate and 20mg trypsin were dissolved in 10mL0.1M NaHCO3In the solution, preparing simulated intestinal digestive juice; the enzyme activity of the pepsin is 3000U/mg, and the enzyme activity of the trypsin is 2500U/mg;
s2, simulated gastric digestion: 30mL of 1mM FeSO was prepared4Solution, adding the shrimp-derived nonapeptide prepared in example 2 of the present invention, the concentration of the shrimp-derived nonapeptide and Fe2+The molar ratio of the concentration is 1:2, 1:1 and 2:1 respectively, and FeSO is not added4Taking 1mM shrimp-derived nonapeptide aqueous solution as a control, incubating at 37 ℃ for 30min, adjusting pH to 2.0 by using 1M HCl, adding simulated gastric digestion solution (pepsin: shrimp-derived nonapeptide is 1:100w/w), stirring at 140rpm for 90min, simulating gastric digestion process to obtain simulated gastric digestion product, taking 2mL simulated gastric digestion product, heating in 100 ℃ water bath for 5min, centrifuging at 10000r/min for 10min, and taking supernatant, namely gastric digestion product;
s3, simulated intestinal digestion: adjusting the pH of the simulated gastric digest in the step S3 to 6.5, adding simulated intestinal digest (trypsin: shrimp-derived nonapeptide is 1:80w/w), stirring at 140rpm, continuing intestinal digestion for 150min, heating in 100 ℃ water bath for 5min to inactivate enzyme, and centrifuging at 10000rpm for 10min to obtain intestinal digest;
s4, identifying retention rate of digestion products: after filtering the gastric and intestinal digests obtained in steps S2 and S3, the retention of the shrimp-derived nonapeptide was determined by HPLC under the following conditions: the mobile phase A is acetonitrile solution containing 0.1% (v/v) trifluoroacetic acid; the mobile phase B is an aqueous solution containing 0.1% (v/v) of trifluoroacetic acid; the elution conditions were: 0.0-20.0 min, 12-32% A, 20.0-20.1 min, 32-100% A, 20.1-25 min, 100-12% A, flow rate of 1.0mL/min, detection wavelength of 220nm, and sample injection amount of 10 muL.
The experimental results are as follows: HPLC of shrimp-derived nonapeptide after simulated digestion is shown in FIGS. 3 to 6, and a peak of about 6.5min is observed as shrimp-derived nonapeptide, and no significant degradation occurs. The pure shrimp-derived nonapeptide shows digestion resistance after simulating gastrointestinal tract digestion, as shown in Table 1, the retention rate of the shrimp-derived nonapeptide is 80%, and Fe with different molar ratios is added2+Then, the resistance of the shrimp-derived nonapeptide to digestion is improved, the retention rate after simulated gastric digestion is improved to more than 90 percent, and the shrimp-derived nonapeptide and Fe are continuously simulated after intestinal digestion is continued2+The retention was up to 93% at a 1:2 molar ratio. Thus, the shrimp-derived nonapeptide is bound to Fe2+When mixed in a molar ratio of 1:2, the shrimp-derived nonapeptide exhibits the highest digestion resistance and is more stable in gastrointestinal tract digestion.
Table 1: simulating peptide retention after gastrointestinal digestion
Note: different letters indicate significant differences between groups (P < 0.05).
Example 4: research on iron absorption promoting characteristics of shrimp-derived nonapeptide
S1, establishing a rat external turn intestinal sac model: before the experiment, 180-220 g of SD rats are fasted for 12-16 h. The fasted rats were anesthetized by intraperitoneal injection of 4% (w/v g/mL) chloral hydrate, and after the rats were unconscious, they were laparotomized and the small intestine of about 7cm was removed, the intestinal contents were rinsed clean and placed in an oxygen-filled (95% O) chamber2) Ligating one end of the intestinal section in a buffer solution at 4 ℃, then turning up carefully, filling the turned-up intestinal section with the buffer solution to obtain an intestinal sac, and placing the intestinal sac in the buffer solution at 37 ℃ for standby application, wherein oxygen is continuously introduced into the intestinal sac; wherein the buffer solution is: containing 136mM NaCl, 8.17mM KCl, 1.0mM MgCl211.1mM glucose and 20mM HEPES.
S2, shrimp-derived nonapeptide iron absorption promotion experiment: placing the intestinal segment in the step S1 in a sample buffer solution at 37 ℃ and FeSO4Continuously introducing oxygen into buffer solution, incubating for 90min, collecting intestinal solution, and performing atomic absorptionMeasuring the iron content of the intestinal solution by a spectrophotometer; wherein the sample buffer is configured to: the shrimp-derived nonapeptide prepared in example 2 and FeSO4Dissolving the shrimp-derived nonapeptide in the buffer solution of step S1 with Fe2+Dissolving the mixture into the buffer solution in the step S1 according to the molar ratio of 1:2, 1:1 and 2:1, wherein the concentration of iron ions is 60 mg/mL; FeSO4The buffer solution is FeSO4Dissolving in the buffer solution of step S1 to obtain Fe2+The final concentration was 60 mg/mL.
S3, analyzing the stability of the shrimp-derived nonapeptide: the enteral solution described in step S2 was filtered through a 0.22 μm filter and then the content of the shrimp-derived nonapeptide was measured by HPLC. The detection conditions were as follows: the mobile phase A is acetonitrile solution containing 0.1% (v/v) trifluoroacetic acid; the mobile phase B is an aqueous solution containing 0.1% (v/v) of trifluoroacetic acid; the elution conditions were: 0.0-20.0 min, 12-32% A, 20.0-20.1 min, 32-100% A, 20.1-25 min, 100-12% A, flow rate of 1.0mL/min, detection wavelength of 220nm, and sample injection amount of 10 muL.
The experimental results are as follows: the invention uses FeSO4For comparison, the iron absorption-promoting activity of the shrimp-derived nonapeptide via intestinal cells was analyzed using a rat intestinal turn-over model. As shown in FIG. 7, in Fe2+60mg/mL of shrimp-derived nonapeptide Fe2+When the molar ratio is 1:2, the shrimp-derived nonapeptide is Fe when being transported for 90min by a rat external intestine turning capsule model2+The transport capacity is 65.6 +/-12.6 mu g/mL and is obviously higher than that of FeSO4(44.7±6.0μg/mL)(P<0.05), indicating that the shrimp-derived nonapeptide has good function of promoting iron absorption. With Fe2+HPLC (high Performance liquid chromatography) spectra of the shrimp-derived nonapeptide with different molar ratios after transportation are shown in figures 8-10, and are shown in the specification2+The shrimp-derived nonapeptides with different molar ratios are degraded after being absorbed by a rat abdominopectinal capsule model. FIG. 11 is the results of the transport amount of the shrimp-derived nonapeptide after absorption by the rat exochelial vesicle model, which is expressed as the ratio of the shrimp-derived nonapeptide after transport to the total amount of the added shrimp-derived nonapeptide. As can be seen in FIG. 11, the shrimp-derived nonapeptide is bound to Fe2+The molar ratio of (1: 2) is 1:2, the transport amount of the shrimp-derived nonapeptide is the highest, and the transport amount is reduced along with the increase of the peptide ratio, which indicates that the shrimp-derived nonapeptide is likely to be degraded in the transport process, thereby causing the transport amount to be reduced, and the likeFe2+The transport amount is in the same trend, so the iron absorption promoting capacity of the shrimp-derived nonapeptide is related to the integrity of the shrimp-derived nonapeptide in the absorption process.
And (4) conclusion: the invention synthesizes the shrimp-derived nonapeptide for the first time, the shrimp-derived nonapeptide can resist simulated digestion of gastrointestinal tracts, can deliver iron ions through a rat abdominopectinal capsule model, and has the function of promoting iron absorption.
The above description is only for the preferred embodiment of the present invention, but the scope of the present invention is not limited thereto, and any person skilled in the art should be able to cover the technical solutions and the inventive concepts of the present invention within the technical scope of the present invention.
Sequence listing
<110> university of Dalian Industrial university
<120> shrimp-derived nonapeptide with iron absorption promoting activity and application thereof
<130>ZR201109LQ
<160>1
<170>SIPOSequenceListing 1.0
<210>1
<211>9
<212>PRT
<213> Artificial sequence (artificial sequence)
<400>1
Asp Thr Asp Ser Glu Glu Glu Ile Arg
1 5
Claims (7)
1. The shrimp-derived nonapeptide is characterized in that the amino acid sequence is shown as SEQ ID NO. 1.
2. The shrimp-derived nonapeptide of claim 1, wherein Fe is2+The content of the shrimp-derived nonapeptide is 60mg/mL and the content of the shrimp-derived nonapeptide is Fe2+In a molar ratio of1:2 hours, and Fe when the transfer time is 90min through a rat external turning intestinal capsule model2+The transport volume was 65.6. + -. 12.6. mu.g/mL.
3. The shrimp-derived nonapeptide of claim 1, having the ability to resist gastrointestinal digestion.
4. Delivery of Fe by shrimp-derived nonapeptide2+The application of (1), wherein the amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
5. An application of a shrimp-derived nonapeptide in preparing iron-supplementing medicines, foods and/or health care products is characterized in that the amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
6. An iron supplement comprising a shrimp-derived nonapeptide and Fe2+The amino acid sequence of the shrimp-derived nonapeptide is shown as SEQ ID NO. 1.
7. The iron supplement of claim 6, wherein the shrimp-derived nonapeptides and Fe2+The molar ratio is 1: 2.
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| JPH05229959A (en) * | 1992-02-25 | 1993-09-07 | Senmi Ekisu Kk | Iron absorption accelerating composition |
| US20110166208A1 (en) * | 2009-04-09 | 2011-07-07 | University Of Kentucky | Nucleotide and Amino Acid Sequences for Calmodulin Protein Methyltransferase |
| US20160222076A1 (en) * | 2013-03-15 | 2016-08-04 | Portagonist Therapeutics, Inc. | Hepcidin analogues and uses thereof |
| US20170313754A1 (en) * | 2014-06-27 | 2017-11-02 | Protagonist Therapeutics, Inc. | Hepcidin and mini-hepcidin analogues and uses thereof |
| CN110731512A (en) * | 2019-11-12 | 2020-01-31 | 大连工业大学 | Antarctic krill iron chelate peptide and preparation method and application of iron chelate peptide and iron chelate thereof |
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| JPH05229959A (en) * | 1992-02-25 | 1993-09-07 | Senmi Ekisu Kk | Iron absorption accelerating composition |
| US20110166208A1 (en) * | 2009-04-09 | 2011-07-07 | University Of Kentucky | Nucleotide and Amino Acid Sequences for Calmodulin Protein Methyltransferase |
| US20160222076A1 (en) * | 2013-03-15 | 2016-08-04 | Portagonist Therapeutics, Inc. | Hepcidin analogues and uses thereof |
| US20170313754A1 (en) * | 2014-06-27 | 2017-11-02 | Protagonist Therapeutics, Inc. | Hepcidin and mini-hepcidin analogues and uses thereof |
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