CN104928337B - Navodon septentrionalis fish skin zinc chelating peptide - Google Patents
Navodon septentrionalis fish skin zinc chelating peptide Download PDFInfo
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- CN104928337B CN104928337B CN201510177228.2A CN201510177228A CN104928337B CN 104928337 B CN104928337 B CN 104928337B CN 201510177228 A CN201510177228 A CN 201510177228A CN 104928337 B CN104928337 B CN 104928337B
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 34
- 239000011701 zinc Substances 0.000 title claims abstract description 30
- 229910052725 zinc Inorganic materials 0.000 title claims abstract description 26
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 title claims abstract description 25
- 241000075387 Thamnaconus septentrionalis Species 0.000 title description 5
- 241001676702 Thamnaconus modestus Species 0.000 claims abstract description 28
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 12
- 229920001184 polypeptide Polymers 0.000 claims abstract description 11
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 claims abstract description 4
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 3
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- 238000010521 absorption reaction Methods 0.000 abstract description 4
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- 238000004007 reversed phase HPLC Methods 0.000 abstract description 4
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- 238000002360 preparation method Methods 0.000 description 7
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- 230000010736 Chelating Activity Effects 0.000 description 5
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- FTOAOBMCPZCFFF-UHFFFAOYSA-N 5,5-diethylbarbituric acid Chemical compound CCC1(CC)C(=O)NC(=O)NC1=O FTOAOBMCPZCFFF-UHFFFAOYSA-N 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
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- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
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- OTNVGWMVOULBFZ-UHFFFAOYSA-N sodium;hydrochloride Chemical compound [Na].Cl OTNVGWMVOULBFZ-UHFFFAOYSA-N 0.000 description 2
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- 102000004190 Enzymes Human genes 0.000 description 1
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- IXHQLZIWBCQBLQ-STQMWFEESA-N Gly-Pro-Phe Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 IXHQLZIWBCQBLQ-STQMWFEESA-N 0.000 description 1
- ISSDODCYBOWWIP-GJZGRUSLSA-N Gly-Pro-Trp Chemical compound [H]NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O ISSDODCYBOWWIP-GJZGRUSLSA-N 0.000 description 1
- JNGHLWWFPGIJER-STQMWFEESA-N Gly-Pro-Tyr Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 JNGHLWWFPGIJER-STQMWFEESA-N 0.000 description 1
- 206010067868 Skin mass Diseases 0.000 description 1
- 241001627955 Tetraodon lineatus Species 0.000 description 1
- 206010048259 Zinc deficiency Diseases 0.000 description 1
- WHMDKBIGKVEYHS-IYEMJOQQSA-L Zinc gluconate Chemical compound [Zn+2].OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O.OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O WHMDKBIGKVEYHS-IYEMJOQQSA-L 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
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- AMMWFYKTZVIRFN-UHFFFAOYSA-N sodium 3-hydroxy-4-[(1-hydroxynaphthalen-2-yl)diazenyl]-7-nitronaphthalene-1-sulfonic acid Chemical compound [Na+].C1=CC=CC2=C(O)C(N=NC3=C4C=CC(=CC4=C(C=C3O)S(O)(=O)=O)[N+]([O-])=O)=CC=C21 AMMWFYKTZVIRFN-UHFFFAOYSA-N 0.000 description 1
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- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
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Abstract
The invention relates to a thamnaconus modestus fish skin zinc chelating peptide, which is prepared by taking thamnaconus modestus fish skin as a raw material, removing non-collagen and mineral substances from the fish skin by using acid and alkali, extracting fish skin gelatin, performing enzymolysis on the fish skin gelatin by using neutral protease and trypsin, and performing ultrafiltration, immobilized zinc ion affinity chromatography and reversed-phase high performance liquid chromatography for separation and purification to obtain the zinc chelating peptide Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly (GPYGPFGPWG) and ESI-MS for determining the molecular weight of 1034.09 Da. The zinc chelating peptide can obviously improve the absorption utilization rate of zinc due to the unique chelating and transporting mechanism, can also supplement polypeptide/amino acid required by a human body, is an ideal zinc supplement substance, and can be used for developing zinc supplement medicines or functional products.
Description
Technical Field
The invention relates to aquatic product polypeptide, in particular to thamnaconus modestus fish skin zinc chelating peptide.
Background
The common names of the Navodon modestus, namely rubber fishes and skinned fishes, belong to the Tavodon order and Tavodon Thodoptera, and are common fishes in China. The skin of the Navodon septentrionalis is thick and hard, has no edible value, and is mostly thrown away, thereby causing resource waste and environmental pollution. Zinc is a necessary trace element for human body, and zinc deficiency of children can cause diseases such as growth and development badness, behind intelligence development, immunity reduction and the like; the pregnant woman is lack of zinc and the fetal abnormality rate is increased. The traditional zinc supplement such as zinc sulfate and zinc gluconate has low absorption and utilization rate and large intestine and stomach irritation, and is not beneficial to long-term administration. The zinc chelating peptide can promote the absorption and utilization of zinc, can meet the requirements of organisms on active peptides, amino acids and the like, has no side effect, and is widely concerned.
However, the applicant finds that the preparation of the zinc chelating peptide from the thamnaconus modestus skin as a raw material and the process research thereof are blank.
Disclosure of Invention
The invention aims to solve the technical problem of providing the thamnaconus modestus skin zinc chelating peptide aiming at the technical current situation, and the peptide has strong zinc chelating capacity.
The technical scheme adopted by the invention for solving the technical problems is as follows: the thamnaconus modestus fish skin zinc chelating peptide is characterized in that the amino acid sequence of the polypeptide is Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly (GPYGPFGPWG), and the molecular weight is 1034.09Da when ESI-MS is used for determination.
The preparation method of the thamnaconus modestus skin zinc chelating peptide is characterized by comprising the following steps:
1) the preparation method of the thamnaconus modestus fish skin gelatin comprises the steps of mincing thamnaconus modestus fish skin, adding the minced thamnaconus modestus fish skin into 0.3-0.5% NaOH solution according to the feed-liquid ratio of 1g: 15-20 m L, stirring for 5-8H, washing with double-distilled water until the solution is neutral, adding the solution into 0.3-0.5% H L according to the feed-liquid ratio of 1g: 10-15 m2SO4Soaking at room temperature for 2 days, changing water every 8 hours, homogenizing the treated fish skin, adding the homogenized fish skin into double-distilled water according to the material-liquid ratio of 1g: 8-10 m L, dynamically extracting at 70 ℃ for 12-15 hours, centrifuging at 6000 g for 25-30 min, taking supernatant, and freeze-drying to obtain the thamnaconus modestus fish skin gelatin.
) Enzymolysis of thamnaconus modestus fish skin gelatin, namely adding the thamnaconus modestus fish skin gelatin into barbital sodium-hydrochloric acid according to the feed-liquid ratio of 1g to 8-12 m L, adjusting the pH value to 7.0, preserving the heat at 45-50 ℃ for 5-10 min, and adding neutral protease (1.0 × 10) according to 2-3% of the mass of the fish skin5U/g), performing enzymolysis at 45-50 ℃ for 3-5 h, heating the solution to 90-95 ℃, keeping the temperature for 5-10 min, cooling to 35-40 ℃, adjusting the pH value of the solution to 8.0, and adding trypsin (1.9 × 10) into the solution according to 1.5-2.0% of the mass of gelatin4U/g), performing enzymolysis for 3-4 h at the temperature of 35-40 ℃, heating the solution to 90-95 ℃, keeping the temperature for 10-15 min,centrifuging at 10000 g for 15-20 min, and taking supernatant fluid to obtain an enzymolysis product;
3) the preparation method of the thamnaconus modestus skin zinc chelating peptide comprises the steps of carrying out ultrafiltration treatment on a prepared enzymolysis product by using a 3kDa ultrafiltration membrane, collecting a part with the molecular weight less than 3kDa to obtain an ultrafiltration enzymolysis liquid, and purifying the ultrafiltration enzymolysis liquid by immobilized zinc ion affinity chromatography and reversed-phase high performance liquid chromatography (RP-HP L C) in sequence to obtain the thamnaconus modestus skin zinc chelating peptide.
Preferably, the thamnaconus modestus in the step 1) is Navodon globefish (Navodon septentrionalis).
As an improvement, the specific processes of the immobilized zinc ion affinity chromatography and the reversed-phase high performance liquid chromatography (RP-HP L C) purification in the step 3) are as follows:
dissolving the ultrafiltration enzymolysis liquid in double distilled water to prepare a solution with the concentration of 8-10 mg/m L, adsorbing by an immobilized zinc ion Sepharose 6B affinity chromatography column, eluting by using double distilled water with the column volume of 3-5 times to remove unadsorbed polypeptide, eluting the chromatography column by using double distilled water with the column volume of 5-8 times and the pH value of 3.0, collecting eluent, and freeze-drying to obtain an affinity chromatography enzymolysis product;
and (3) RP-HP L C purification, namely preparing the affinity chromatography zymolyte into a solution of 100-120 mu g/m L by using double distilled water, purifying by using RP-HP L C, and obtaining 1 polypeptide Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly (GPYGPFGPWG) with high Zn chelating activity according to the chelating activity to zinc ions.
Preferably, the RP-HP L C conditions include a sample injection amount of 10-15 mu L and a Gemini C chromatographic column18(250 × 4.6.6 mm, 5 μm), column temperature of 25-30 deg.C, mobile phase of 30% acetonitrile (containing 0.1% trifluoroacetic acid), elution speed of 0.5-0.8 m L/min, and ultraviolet detection wavelength of 220 nm.
Compared with the prior art, the invention has the advantages that: the invention selects neutral protease and trypsinase as enzymes for enzymolysis, and combines ultrafiltration fractionation and chromatographic refining at the same time by a biological enzymolysis method, so that the prepared polypeptide has strong zinc chelating capacity, has the advantages of easy digestion and absorption, safety, no toxic or side effect and the like, and can be used as a zinc supplement medicine or a functional product.
Drawings
FIG. 1 is a chromatogram of RP-HP L C of an immobilized zinc ion affinity chromatography substrate of the invention.
Detailed Description
The present invention will be described in further detail with reference to examples.
The preparation process flow of the thamnaconus modestus skin zinc chelating peptide is as follows: thamnaconus modestus fish skin-non-collagen removal, decalcification and gelatin extraction-enzymolysis-ultrafiltration-immobilized zinc ion affinity chromatography-high performance liquid chromatography purification-zinc chelating peptide-structure identification and activity evaluation.
Example (b):
1) a preparation method of thamnaconus modestus fish skin gelatin comprises mincing thamnaconus modestus (Navodon septentrionalis) fish skin, adding into 0.3% NaOH solution according to a feed-liquid ratio of 1g:15m L, stirring for 5H, washing with double-distilled water to neutrality, adding into 0.4% H according to a ratio of 1g:10m L2SO4Soaking at room temperature for 2d, and changing water every 8 h; and finally, homogenizing the treated fish skin, adding the homogenized fish skin into double distilled water according to the material-liquid ratio of 1:10, dynamically extracting for 15h at 70 ℃, centrifuging for 30min at 6000 g, taking supernatant, and freeze-drying to obtain the thamnaconus modestus fish skin gelatin.
) Enzymolysis of thamnaconus modestus skin gelatin, adding thamnaconus modestus skin gelatin into barbital sodium-hydrochloric acid buffer solution according to the feed-liquid ratio of 1g:12m L, adjusting pH to 7.0, keeping the temperature at 50 deg.C for 10min, adding neutral protease (1.0 × 10) according to 2% of the fish skin mass5U/g), performing enzymolysis at 50 deg.C for 3 hr, heating the solution to 90 deg.C, maintaining the temperature for 15min, cooling to 37 deg.C, adjusting pH to 8.0, and adding trypsin (1.9 × 10) to the solution according to 1.5% of gelatin mass4U/g), performing enzymolysis at 37 ℃ for 4h, heating the solution to 95 ℃, keeping the temperature for 10min, centrifuging at 10000 g for 15min, and taking supernatant, namely an enzymolysis product;
3) the preparation method of the thamnaconus modestus skin zinc chelating peptide comprises the steps of carrying out ultrafiltration treatment on a prepared enzymolysis product by using a 3kDa ultrafiltration membrane, collecting a part with the molecular weight less than 3kDa to obtain an ultrafiltration enzymolysis liquid, and purifying the ultrafiltration enzymolysis liquid by immobilized zinc ion affinity chromatography and reversed-phase high performance liquid chromatography (RP-HP L C) in sequence to obtain the thamnaconus modestus skin zinc chelating peptide.
①, performing immobilized zinc ion affinity chromatography, namely dissolving the ultrafiltration enzymolysis solution in double distilled water to prepare a solution with the concentration of 8-10 mg/m L, adsorbing by an immobilized zinc ion Sepharose 6B affinity chromatography column, eluting by using double distilled water with the column volume of 3-5 times to remove unadsorbed polypeptide, eluting the chromatography column by using double distilled water with the column volume of 5-8 times and the pH of 3.0, collecting eluent, and freeze-drying to obtain an affinity chromatography zymolyte;
② RP-HP L C purification, preparing the above affinity chromatography zymolyte into 120 μ g/m L solution with double distilled water, and purifying with RP-HP L C (conditions: sample amount 15 μ L; chromatographic column is Gemini C18(250 × 4.6.6 mm, 5 μm), a column temperature of 30 ℃, a mobile phase of 30% acetonitrile (containing 0.1% trifluoroacetic acid), an elution speed of 0.8m L/min, an ultraviolet detection wavelength of 220nm), and 1 polypeptide with high Zn chelating activity according to the chelating activity to zinc ions (figure 1).
③ structure detection, collecting polypeptide with highest Zn chelating activity, detecting to single peak, determining amino acid sequence as Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly (GPYGPFGPWG) by protein/polypeptide sequence analyzer, and determining molecular weight as 1034.09Da by ESI-MS.
The chelation of Zn-chelating peptide on zinc ion is determined by EDTA titration method, 100mg of sample to be tested is put into a 100m L beaker, a plurality of drops of water 50m L and HCl (6 mol/L) are added, the sample is completely dissolved by heating in water bath, the volume is determined to l00 m L after cooling, l 0m L is sucked from the beaker and is put into a triangular flask, 3 parts are paralleled, NH of l 0m L is added3-NH4Cl buffer (pH 10), chrome black T as indicator, then Na2The EDTA solution (0.01 mol/L) was titrated to blue, and the zinc content of the chelate was calculated by recording the amount of mL EDTA consumed.
The measurement result shows that: the Zn-chelated collagen peptide Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly (GPYGPFGPWG) obtained by purification has the chelating capacity of 56.74 mu g/mg for zinc ions, and compared with the thamnaconus modestus fish skin gelatin zymolyte (23.97 mu g/mg), the Zn-chelated collagen peptide has the remarkably improved chelating capacity for Zn.
Finally, it should be noted that the above-mentioned list is only one specific embodiment of the present invention. It is obvious that the invention is not limited to the above embodiments, but that many variations are possible. All modifications which can be derived or suggested by a person skilled in the art from the disclosure of the present invention are to be considered within the scope of the invention.
SEQUENCE LISTING
<110> Zhejiang ocean academy
<120> thamnaconus modestus fish skin zinc chelating peptide
<130>zjou-wb-201504-3
<160>1
<170>PatentIn version 3.5
<210>1
<211>10
<212>PRT
<213> Artificial Synthesis
<400>1
Gly Pro Tyr Gly Pro Phe Gly Pro Trp Gly
1 5 10
Claims (1)
1. The thamnaconus modestus fish skin zinc chelating peptide is characterized in that the amino acid sequence of the polypeptide is Gly-Pro-Tyr-Gly-Pro-Phe-Gly-Pro-Trp-Gly, and the molecular weight is 1034.09Da when ESI-MS is used for determination.
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| CN106084000B (en) * | 2016-04-18 | 2019-06-28 | 浙江省海洋水产研究所 | A kind of Urechis uniconctus visceral protein source zinc chelating peptide |
| CN111909238B (en) * | 2017-06-29 | 2022-04-08 | 安徽省农业科学院农产品加工研究所 | High-zinc-chelation-activity zinc chelating peptide containing Ser-Cys and application thereof |
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