CN114539360B - Polypeptide with characteristics of elk source and application thereof - Google Patents
Polypeptide with characteristics of elk source and application thereof Download PDFInfo
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- C—CHEMISTRY; METALLURGY
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Abstract
The invention belongs to the technical field of biology, and particularly relates to a characteristic polypeptide for identifying a moose and application thereof. The characteristic polypeptide provided by the invention specifically comprises the following components: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK. The characteristic polypeptide provided by the invention has excellent specificity and stability for the elk, has strong specificity, can be used for identifying the blended elk or the pseudo-product of the elk and the derived products of the elk, deer antler, deer skin, deer blood, deer penis and deer tendon, and has good application prospect.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a characteristic polypeptide for identifying a moose and application thereof.
Background
Moose (moose) is the largest deer in the world. The deer has high economic value, and the derived products are deer antler, deer skin, deer penis, deer meat, deer blood, deer tendon and the like. However, the fish and dragon products in the market are mixed, so that the people who sell dog meat by hanging sheep heads often forge sika deer or red deer to sell the product by using a camel product. Especially, as the elk is the deer with the largest body shape in the world, the yield is large and easy to obtain, and compared with the spotted deer antler and the hairy deer antler with tense resources, the cost is low. The deer skin, deer penis, deer meat, deer blood, deer tendons and the like have similar appearance, so that the main components are almost the same, and the existing identification method cannot distinguish species.
Disclosure of Invention
Aiming at the technical blank existing in the prior art, the invention provides a characteristic polypeptide for identifying a elk source.
The invention also provides application of the characteristic polypeptide in identifying the species of the elk.
The technical scheme adopted by the invention for achieving the purpose is as follows:
the invention provides a characteristic polypeptide for identifying a source of a moose, which specifically comprises the following components: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK.
The characteristic polypeptide discovered by the invention exists in the cervus elaphus blood beta globin.
Further, the mass to charge ratio of the peptide fragment 1 of SEQ ID No.1 is 734.85 (z=2).
The invention also provides a kit for identifying a source of elk, which comprises the characteristic polypeptide of claim 1.
The invention also provides a method for identifying the source of the moose by utilizing the characteristic polypeptide, which comprises the following steps:
(1) Pretreating a sample to be detected to obtain a solution to be detected;
(2) And detecting the solution to be detected by a liquid phase-triple quadrupole mass spectrometry, analyzing and comparing the mass spectrum result in the solution to be detected with the mass spectrum of the peptide 1, and judging that the sample to be detected is a camel or a doped camel when the mass spectrum of the peptide 1 appears in the mass spectrum.
Further, the pretreatment specific process of the sample to be tested is as follows: crushing a sample, weighing 50mg of the sample, adding 10ml of denaturation buffer solution and 1ml of DTT solution, shaking uniformly, standing at 80 ℃ for overnight, taking out, cooling to room temperature, centrifuging, taking 500 mu L of supernatant, adding 100 mu L of IAA solution, carrying out light-proof reaction for 30min, mixing uniformly, and centrifuging; desalting the sample solution, measuring 100 μl of supernatant, adding 900 μl ammonium bicarbonate solution (1%) and 10 μl bovine trypsin solution, performing enzymolysis at 37deg.C for 4 hr, taking out, cooling to room temperature, centrifuging, and collecting supernatant.
The preparation process of the denaturation buffer solution specifically comprises the following steps: weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane and 0.734g of ethylenediamine tetraacetic acid, adding water for dissolving, adding concentrated hydrochloric acid for regulating the pH to 8.0, adding water for diluting to 1L, and shaking uniformly to obtain the finished product; the concentration of the DTT solution is 2.5M; the IAA solution was at a concentration of 2M.
Further, the specific preparation process of the bovine trypsin solution comprises the following steps: weighing a proper amount of bovine trypsin, dissolving with acetic acid solution to prepare a solution with the concentration of 10mg/ml, and preparing the solution immediately after use; the concentration of the acetic acid solution was 2%.
In the liquid phase-triple quadrupole mass spectrometry used in the invention, the liquid phase conditions are as follows: the chromatographic column is ACQUITY UPLC [ beta ] BEH C18 (2.1X10 mm,1.7 μm), the column temperature is 43 ℃, the flow rate is 0.3mL/min, the mobile phase A is 0.1% formic acid solution, and the mobile phase B is 0.1% formic acid acetonitrile solution, and gradient elution is carried out.
The conditions of the gradient elution are as follows: 0-9 min,3% B to 7.5% B; 9-13 min, 7.5% B to 25% B; 13-14 min,25% B to 90% B; 14-17 min, 90% B; 17-17.5 min, 10-97% B; 17.5-21 min,97% B, and sample injection amount of 5 μl.
In the liquid phase-triple quadrupole mass spectrometry used in the invention, mass spectrometry conditions are as follows: adopting a mass spectrum detector, electrospray ionization (ESI), and carrying out multi-reaction monitoring in a positive ion mode; sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; spray voltage 3.5KV; the temperature of the ion source is 150 ℃; the temperature of the auxiliary gas is 400 ℃; cone hole voltage 30V, collision voltage 35V); the solvent delay (solvent delay) is 0-8 min and 14-20 min; m/z (two charges) 734.85 → 249.10, 734.85 → 360.20 were chosen as detection ion pairs.
The beneficial effects of the invention are as follows:
(1) The characteristic polypeptide and the detection method provided by the invention provide a solution for checking the product of the sika deer doped with or replaced by the sika deer.
(2) The characteristic polypeptide provided by the invention has excellent specificity and stability aiming at deer antler, deer skin, deer penis, deer meat, deer blood, deer tendon and the like, has strong specificity and has good application prospect.
Drawings
FIG. 1 shows a secondary mass spectrum of m/z (two-charge) 734.85 and the assignment of y ions and b ions.
FIG. 2 shows the results of a specific experiment of m/z (two charges) 734.85.
Fig. 3 shows BLAST (Basic Local Alignment Search Tool) results of EFTPELQADYQK.
Detailed Description
The technical scheme of the invention is further explained and illustrated by the specific embodiments.
Instrument and reagent (one): thermo EASY-nLC 1000 nanoliter liquid phase, thermo Scientific Orbitrap-Fusion high resolution mass spectrum, AB Triple Quad6500+ high performance liquid chromatography mass spectrometer, sidoris XSE205 electronic balance, trypsin (manufactured by Sigma Co., ltd., batch number: SLBG 6452V) guanidine hydrochloride, tris, ethylenediamine tetraacetic acid (EDTA), dithiothreitol (DTT), iodoacetamide (IAA), ammonium bicarbonate, acetic acid are all analytically pure. Formic acid and acetonitrile are both chromatographically pure.
The deer source is tested by PCR experiments of Shandong national academy of agricultural sciences through deer antler and deer antler samples provided by enterprises.
Example 1
1. Measurement conditions
1.1 Liquid phase-triple quadrupole mass spectrometry measurement conditions
Liquid phase conditions: the chromatographic column is ACQUITY UPLC [ beta ] BEH C18 (2.1X10 mm,1.7 μm), the column temperature is 43 ℃, the flow rate is 0.3mL/min, the mobile phase A is 0.1% formic acid solution, and the mobile phase B is 0.1% formic acid acetonitrile solution, and gradient elution is carried out. The sample injection amount is 5, wherein the sample injection amount is (0-9 min,3% B-7.5% B, 9-13 min, 7.5% B-25% B, 13-14 min,25% B-90% B, 14-17 min, 90% B, 17-17.5 min, 10% B-97% B, 17.5-21 min and 97% B). Mass spectrometry conditions: adopting a mass spectrum detector, electrospray ionization (ESI), and carrying out multi-reaction monitoring in a positive ion mode; sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; spray voltage 3.5KV; the temperature of the ion source is 150 ℃; the temperature of the auxiliary gas is 400 ℃. Cone voltage 30V, collision voltage 35V). The solvent delay (solvent delay) is 0 to 8min and 14 to 20min. M/z (two charges) 734.85 → 249.10, 734.85 → 360.20 were chosen as detection ion pairs.
Preparation of sample solution
Sample: the determination was performed using a velvet antler sample. Firstly, crushing a sample, weighing 50mg of the sample, adding 10ml of denaturation buffer solution (weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane, 0.734g of ethylenediamine tetraacetic acid, adding water for dissolving, adding concentrated hydrochloric acid for regulating the pH to 8.0, adding water for diluting to 1L, and shaking uniformly to obtain the finished product. And 1ml of DTT solution, shaking, standing at 80deg.C overnight, taking out, cooling to room temperature, and centrifuging (12000 rpm,10 min). Weighing 500 mu L of supernatant, adding 100 mu L of IAA solution, performing light-proof reaction for 30min, uniformly mixing, and centrifuging (12000 rpm,10 min); after desalting the sample solution, taking 100 mu L of supernatant, adding 900 mu L of ammonium bicarbonate solution (1%) and 10 mu L of bovine trypsin solution (proper amount of bovine trypsin is weighed by the solution, dissolved by acetic acid solution to prepare solution with the concentration of 10mg/ml, prepared immediately before use), performing enzymolysis for 4 hours at 37 ℃, taking out, cooling to room temperature, centrifuging (12000 rpm,10 min), and taking the supernatant to obtain the product. The experimental results are shown in Table 1, and the result pictures are shown in FIG. 1.
TABLE 1 results of specific experiments
The found characteristic peptide belongs to beta globin in deer blood, so the characteristic peptide can be applied to identifying deer products with rich blood content, such as camel horn, deer skin, deer penis, deer meat, deer blood, deer tendon and the like.
Comparative example 1
The measurement of the deer sample was performed using the ion pair (m/z) 553.29 (two charges) → 285.16, (m/z) 553.29 (two charges) → 329.19 previously searched for in the subject group, and it was found that the absorption peak was also present in sika deer in addition to that of elk.
<110> Shandong province food and drug inspection institute
<120> a characteristic polypeptide of a source of a moose and application thereof
<160> 1
<210> 1
<211>15
<212>PRT
<222>（1）…（12）
<400>1
Glu Phe Thr Pro Glu Leu Gln Ala Asp Tyr Gln Lys
1 5 10
Claims (10)
1. A characteristic polypeptide for identifying a elk, which is characterized by comprising the following specific components: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK.
2. The polypeptide of claim 1, wherein the mass to charge ratio of SEQ ID No.1 peptide fragment 1 is 734.85 (z=2).
3. A kit for identifying a moose, comprising the polypeptide of claim 1.
4. A method for identifying a moose using the characteristic polypeptide of claim 1 or 2, comprising the steps of:
(1) Pretreating a sample to be detected to obtain a solution to be detected;
(2) And detecting the solution to be detected by a liquid phase-triple quadrupole mass spectrometry, analyzing and comparing the mass spectrum result in the solution to be detected with the mass spectrum of the peptide 1, and judging that the sample to be detected contains the camel source component when the mass spectrum of the peptide 1 appears in the mass spectrum.
5. The method according to claim 4, wherein the specific process of pretreatment of the sample to be tested is as follows: crushing a sample, weighing 50mg of the sample, adding 10ml of denaturation buffer solution and 1ml of DTT solution, shaking uniformly, standing at 80 ℃ for overnight, taking out, cooling to room temperature, centrifuging, taking 500 mu L of supernatant, adding 100 mu L of IAA solution, carrying out light-proof reaction for 30min, mixing uniformly, and centrifuging; after desalting the sample solution, taking 100 mu L of supernatant, adding 900 mu L of ammonium bicarbonate solution with concentration of 1% and 10 mu L of bovine trypsin solution, carrying out enzymolysis for 4 hours at 37 ℃, taking out, cooling to room temperature, centrifuging, and taking the supernatant to obtain the final product.
6. The method of claim 5, wherein the denaturing buffer is prepared by: weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane and 0.734g of ethylenediamine tetraacetic acid, adding water for dissolving, adding concentrated hydrochloric acid for regulating the pH to 8.0, adding water for diluting to 1L, and shaking uniformly to obtain the finished product; the concentration of the DTT solution is 2.5M; the IAA solution was at a concentration of 2M.
7. The method according to claim 5 or 6, wherein the specific preparation process of the bovine trypsin solution is as follows: weighing a proper amount of bovine trypsin, dissolving with acetic acid solution to prepare a solution with the concentration of 10mg/ml, and preparing the solution immediately after use; the concentration of the acetic acid solution was 2%.
8. The method of claim 4, wherein in the liquid phase-triple quadrupole mass spectrometry, the liquid phase conditions are: the chromatographic column ACQUITY UPLC cube BEH C18 with the specification of 2.1×50mm and 1.7 μm has the column temperature of 43 ℃ and the flow rate of 0.3mL/min, the mobile phase A is 0.1% formic acid solution, and the mobile phase B is 0.1% formic acid acetonitrile solution, and gradient elution is carried out.
9. The method of claim 8, wherein the gradient elution conditions are: 0-9 min,3% B to 7.5% B; 9-13 min, 7.5% B to 25% B; 13-14 min,25% B to 90% B; 14-17 min, 90% B; 17-17.5 min, 10-97% B; 17.5-21 min,97% B, and sample injection amount of 5 μl.
10. The method according to claim 8 or 9, wherein in the liquid-phase-triple quadrupole mass spectrometry, mass spectrometry conditions: adopting a mass spectrum detector, electrospray ionization and multi-reaction monitoring in a positive ion mode; sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; spray voltage 3.5KV; the temperature of the ion source is 150 ℃; the temperature of the auxiliary gas is 400 ℃; cone hole voltage 30V, collision voltage 35V; the solvent delay is 0-8 min and 14-20 min; the m/z binary charges 734.85- > 249.10, 734.85- > 360.20 were chosen as detection ion pairs.
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| CN116143874B (en) * | 2022-06-01 | 2023-09-26 | 山东省食品药品检验研究院 | Polypeptide for identifying sika deer or red deer source characteristics and application thereof |
| CN114855285B (en) | 2022-06-02 | 2023-02-17 | 山东省食品药品检验研究院 | Characteristic polypeptide library for rapidly identifying species source of pilose antler and application thereof |
| CN115925789B (en) * | 2022-06-02 | 2023-06-23 | 山东省食品药品检验研究院 | Characteristic polypeptide library for identifying deer product mixture genus source and application thereof |
| CN116284247B (en) * | 2023-01-06 | 2023-10-03 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deerhorn glue confusion product, and combination method and application thereof |
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| CN112098579A (en) * | 2020-09-01 | 2020-12-18 | 南京中医药大学 | Deer-derived characteristic peptide fragment and detection method thereof |
| CN113307846A (en) * | 2021-06-23 | 2021-08-27 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antlers of sika deer or red deer and application thereof |
| CN113480599A (en) * | 2021-06-23 | 2021-10-08 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antler glue of sika deer or red deer and application thereof |
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| CN112898384B (en) * | 2021-01-23 | 2022-08-26 | 南京中医药大学 | Deer horn characteristic peptide segment and detection method thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN112098579A (en) * | 2020-09-01 | 2020-12-18 | 南京中医药大学 | Deer-derived characteristic peptide fragment and detection method thereof |
| CN113307846A (en) * | 2021-06-23 | 2021-08-27 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antlers of sika deer or red deer and application thereof |
| CN113480599A (en) * | 2021-06-23 | 2021-10-08 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antler glue of sika deer or red deer and application thereof |
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