CN111060622B - Labeled peptide of tuna-derived component and application of labeled peptide in detection of collagen degradation product and product thereof - Google Patents
Labeled peptide of tuna-derived component and application of labeled peptide in detection of collagen degradation product and product thereof Download PDFInfo
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Abstract
The invention discloses a labeled peptide of tuna-derived components and application thereof in detection of collagen degradation products and products thereof, belonging to the technical field of detection. The invention relates to a labeled peptide Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg of tuna-derived components, and whether tuna-derived components are contained can be determined by detecting the labeled peptide. Specifically, the protein components in the sample are subjected to pancreatin digestion to enable the labeled peptide to be dissociated, and then whether the labeled peptide is contained or not is detected by a liquid chromatograph-mass spectrometer, so that whether the tuna-derived component is contained or not is judged. The method has the advantages of strong characteristics, high sensitivity and simple operation, and can be used for measuring the collagen degradation product and the tuna-derived components in the product thereof.
Description
Technical Field
The invention relates to a labeled peptide of tuna-derived components and application thereof in detection of collagen degradation products and products thereof, belonging to the field of medicine and food detection.
Background
Collagen is present in animal bodies in very high amounts, mainly in the connective tissues of the animal, such as bones, skins, tendons and scales. Gelatin is a degradation product of collagen, is prepared by properly hydrolyzing animal bones, skins, tendons, scales and the like serving as raw materials, has excellent physicochemical properties, and is widely applied to the fields of food, medicine and the like. The gelatin is mostly made of skins or bones of pigs and cattle, but has important significance for tracing animal-derived components of the gelatin due to different safety risks, trueness and religious beliefs possibly brought by diseases of poultry and livestock.
With the improvement of living standard of people, the fish gelatin is considered to be safer and healthier compared with gelatin prepared by taking poultry, livestock and the like as raw materials, wherein the gelatin prepared by taking tuna as the raw material is the most precious. The main component of the gelatin is collagen polypeptide, and the animal source component can be traced by detecting the polypeptide by using a liquid chromatograph-mass spectrometer, however, whether the selected polypeptide can be used as a tracing marker or not is related to the success of tracing because the polypeptide has the phenomena of mutation and the like in the same species. The selection of the labeled peptide for tracing the source components of the tuna not only needs to overcome the influence caused by gene mutation, but also needs to be contained in the tuna, and other animals do not contain the labeled peptide. The selection of the marker peptide which is not mutated in the tuna becomes the key of the source tracing of the source ingredients of the tuna. The above difficulties cannot be overcome by directly adopting a liquid chromatograph-mass spectrometer to detect and analyze the sample. Starting from genes, analyzing and searching for marker peptides is a feasible path.
Disclosure of Invention
Aiming at the problems, the invention provides a labeled peptide of tuna-derived components and a method for detecting the tuna-derived components in collagen degradation products and products thereof, wherein the method is simple to operate, strong in characteristics and high in sensitivity, and can be used for source tracing and content determination of the tuna-derived components in the collagen degradation products and the products thereof.
The technical scheme of the invention is as follows:
a tuna-based labeled peptide comprises a labeled peptide in a collagen sequence based on tuna, wherein the amino acid sequence of the labeled peptide is Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg, and Hyp is 4 hydroxyproline or 3 hydroxyproline. The method is characterized in that a characteristic mRNA sequence of stably existing tuna is found out from mRNA of COL1A1 protein in cattle, pigs, horses and tunas, the mRNA sequence is translated into a protein sequence, and then the protein sequence is detected by using a liquid chromatography-mass spectrometry technology, and finally selected marker peptide.
The application of the labeled peptide in the detection of collagen degradation products and products thereof comprises the following steps:
(1) performing enzyme digestion on a sample to be detected by using trypsin, or extracting protein components in the sample to be detected and performing enzyme digestion by using trypsin;
(2) putting into a liquid chromatograph-mass spectrometer, and selecting parent ions m/z469 and daughter ions thereof for monitoring by using gelatin for marking peptides or tuna source components as reference; if the retention time of the ion is consistent with that of the reference substance and the daughter ion of the ion is consistent with that of the reference substance, the glue traditional Chinese medicine or the glue traditional Chinese medicine product contains tuna-derived components, and the content of the tuna-derived components can be calculated by peak areas in the reference substance and the detection sample; if there is no such ion with a retention time consistent with the control, no tuna derived ingredient is contained.
The collagen degradation product is gelatin prepared by hydrolyzing animal bone, skin and scale, and is food, health product or medicine containing gelatin.
By adopting the method, whether the collagen degradation product and the product thereof contain tuna-derived components can be rapidly detected. Although the protein sequence difference is caused by the gene mutation in animals, the gene of the labeled peptide has strong conservation in the tuna and is peculiar to the tuna, and the labeled peptide can be used for tracing and detecting the tuna-derived components in collagen degradation products and products thereof.
Drawings
FIG. 1 is a scanning mass spectrum of a daughter ion of a labeled peptide in tuna gelatin (parent ion m/z469, scanning range of daughter ion m/z 200-1200);
FIG. 2 is a mass spectrum of selected ion pairs m/z469 → 669.1, 556.4 monitoring in various animal gelatin SRM scan modes;
FIG. 3 is a graph relating the mass spectrometric peak detection areas (m/z469 → 669.1) of labeled peptides corresponding to different contents of tuna gelatin;
FIG. 4 is a mass spectrum of a tuna gelatin and gelatin preparation (in the case of QQ sugar) monitored in the SRM scan mode for the selected ion pair m/z469 → 669.1, 556.4.
Detailed Description
The invention will be further described with reference to specific embodiments, and the advantages and features of the invention will become apparent as the description proceeds. The examples are illustrative only and do not limit the scope of the present invention in any way. It will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention, and that such changes and modifications may be made without departing from the spirit and scope of the invention.
Example 1
1 materials and reagents
Materials: gelatin from different animal sources is respectively extracted from tuna, cattle, pig, and horse, and is obtained from tuna bone, cattle hide, pigskin, and horse skin.
Reagent: ammonium bicarbonate (analytically pure), trypsin (sequence pure, purchased from the chinese institute for drug and biological product assay).
2 detection method
(1) Preliminary screening of labeled peptides
Through a plurality of batches of mRNA comparison tests of various animal COL1A1 proteins, the first base A and T and the second base C and T in three bases corresponding to each amino acid are basically not mutated in the same species, and mutation among species is frequently occurred. The mRNA of the COL1A1 protein of tuna contains CTT GGA CCT CCA GGC CCC GTT GGA GCC AGA; in the corresponding positions, cattle are "CCT GGG CCC ATT GGC CCA GCG GGA GCA AGA", pigs are "CCT GGA CCA ATT GGC CCA GCT GGA GCA AGA" and horses are "CCT GGA CCA ATT GGC CCA GCT GGA GCA AGA". After translation, the corresponding polypeptide, tuna, is "Leu-Gly-Pro-Pro-Gly-Pro-Val-Gly-Ala-Arg", and all bovine, porcine and equine are "Pro-Gly-Pro-Ile-Gly-Pro-Ala-Gly-Ala-Arg". The polypeptide Leu-Gly-Pro-Pro-Gly-Pro-Val-Gly-Ala-Arg in the tuna is not contained in other animals, so that the polypeptide Leu-Gly-Pro-Pro-Gly-Pro-Val-Gly-Ala-Arg can be preliminarily determined to be the marker peptide of the tuna. It can be further determined whether there is a post-translational modification (i.e., whether there is hydroxylation of proline), and if so, the post-translationally modified polypeptide sequence is a tuna marker peptide. Therefore, a next mass spectrometric detection test was performed to determine whether there was a post-translational modification.
(2) Determination of labeled peptides
a) Taking 0.05g gelatin sample in a 25ml measuring flask, adding a small amount of 1% NH4HCO3Soaking in the solution for 10min, heating at 60 deg.C to dissolve, and dissolving with 1% NH4HCO3Diluting the solution to scale, shaking, filtering with microporous membrane, precisely taking 0.2ml of the subsequent filtrate, adding 20 μ l of 2mg/ml trypsin solution, and performing enzymolysis at 37 deg.C for 12 hr.
b) And (3) putting 5 mu l of enzymolysis solution of tuna gelatin into a liquid chromatography-mass spectrometer to detect whether the polypeptide is subjected to hydroxylation modification. Liquid phase conditions: c18Reversed phase chromatographic column (2.1mm × 100mm, 1.8 μm), mobile phase A is 0.1% formic acid solution, mobile phase B is acetonitrile, flow rate is 0.3 ml/min; gradient elution: 0-25 min, 98% → 80% mobile phase a, 2% → 20% mobile phase B. Mass spectrum conditions: electrospray positive ion mode (ESI)+) And selecting m/z461 and m/z469 as parent ions respectively to carry out full scanning of the child ions. As a result: (1) the mass spectrogram of the full scanning of the daughter ions by taking m/z461 as the parent ions does not accord with the polypeptide Leu-Gly-Pro-Pro-Gly-Pro-Val-Gly-Ala-Arg; (2) a mass spectrogram of a full scanning of a daughter ion taking m/z469 as a parent ion, wherein the ion is polypeptide Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg, and is shown in figure 1. The result shows that one amino acid in the peptide translated by the mRNA sequence 'CTT GGA CCT CCA GGC CCC GTT GGA GCC AGA' of the tuna is modified, namely one proline in the polypeptide is hydroxylated, and the hydroxylated polypeptide sequence is Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg.
c) And (3) putting 5 mu l of enzymolysis solution into a liquid chromatograph-mass spectrometer for detection. Liquid phase conditions: c18Reversed phase chromatographic column (2.1mm × 100mm, 1.8 μm), mobile phase A is 0.1% formic acid solution, mobile phase B is acetonitrile, flow rate is 0.3 ml/min; gradient elution: 0-25 min, 98% → 80% mobile phase a, 2% → 20% mobile phase B. Mass spectrum conditions: electrospray positive ion mode (ESI)+) Selecting for SRM detection, selecting m/z469 →669.1, 556.4 as detecting ion pairs. The results are shown in FIG. 2, with only the corresponding ion peak detected in tuna gelatin at 6.8min, and none others.
In conclusion, the polypeptide Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg can be used as a marking peptide of the tuna-derived component.
Example 2
1 materials and reagents
Materials: mixed gelatin samples (including 5% tuna gelatin in pig gelatin, 10% tuna gelatin in pig gelatin, 20% tuna gelatin in pig gelatin, 40% tuna gelatin in pig gelatin, pure tuna gelatin) were prepared by precision mixing of the gelatins of example 1.
Reagent: ammonium bicarbonate (analytically pure), trypsin (sequence pure, purchased from the chinese institute for drug and biological product assay).
2 detection method
(1) Taking 0.05g gelatin sample in a 25ml measuring flask, adding a small amount of 1% NH4HCO3Soaking in the solution for 10min, heating at 60 deg.C to dissolve, and dissolving with 1% NH4HCO3Diluting the solution to scale, shaking, filtering with microporous membrane, precisely taking 0.2ml of the subsequent filtrate, adding 20 μ l of 2mg/ml trypsin solution, and performing enzymolysis at 37 deg.C for 12 hr.
(2) And (3) putting 5 mu l of enzymolysis solution into a liquid chromatograph-mass spectrometer for detection. Liquid phase conditions: c18Reversed phase chromatographic column (2.1mm × 100mm, 1.8 μm), mobile phase A is 0.1% formic acid solution, mobile phase B is acetonitrile, flow rate is 0.3 ml/min; gradient elution: 0-25 min, 98% → 80% mobile phase a, 2% → 20% mobile phase B. Mass spectrum conditions: electrospray positive ion mode (ESI)+) SRM detection is selected, and m/z469 → 669.1, 556.4 is selected as a detection ion pair.
The curve was plotted with the percentage tuna gelatin as abscissa (X) and peak area (m/z469 → 669.1) as ordinate (Y). The result is shown in FIG. 3, where the standard curve Y is 99285X-4837.9 and the linear correlation coefficient R is2The linearity is good at 0.9986. Therefore, the method can be used for detecting the content of the tuna-derived components.
Example 3
1 materials and reagents
Materials: tuna gelatin, QQ sugar added with bovine gelatin (self-made), QQ sugar added with tuna gelatin (self-made);
reagent: ammonium bicarbonate (analytically pure), trypsin (sequence pure, purchased from the chinese institute for drug and biological product assay).
2 detection method
(1) Respectively placing 0.05-0.25 g of tuna gelatin, QQ sugar added with bovine gelatin and QQ sugar added with tuna gelatin in 25ml measuring bottles, and adding a small amount of 1% NH4HCO3Soaking in the solution for 10min, heating at 60 deg.C to dissolve, and dissolving with 1% NH4HCO3Diluting the solution to scale, shaking, filtering with microporous membrane, precisely taking 0.2ml of the subsequent filtrate, adding 20 μ l of 2mg/ml trypsin solution, and performing enzymolysis at 37 deg.C for 12 hr.
(2) And (3) putting 5 mu l of enzymolysis solution into a liquid chromatograph-mass spectrometer for detection. Liquid phase conditions: c18Reversed phase chromatographic column (2.1mm × 100mm, 1.8 μm), mobile phase A is 0.1% formic acid solution, mobile phase B is acetonitrile, flow rate is 0.3 ml/min; gradient elution: 0-25 min, 98% → 80% mobile phase a, 2% → 20% mobile phase B. Mass spectrum conditions: electrospray positive ion mode (ESI)+) SRM detection is selected, and m/z469 → 669.1, 556.4 is selected as a detection ion pair.
The results are shown in FIG. 4, corresponding ion peaks were detected at 6.8min for tuna gelatin and QQ sugar added to tuna gelatin, and no QQ sugar added to bovine gelatin was detected, indicating that this method can specifically detect tuna-derived components in gelatin products.
Claims (5)
1. A tuna-derived component labeled peptide has an amino acid sequence of Leu-Gly-Pro-Hyp-Gly-Pro-Val-Gly-Ala-Arg, wherein Hyp is 4 hydroxyproline or 3 hydroxyproline.
2. The use of the labeled peptide according to claim 1 in the detection of collagen degradation products and products thereof, comprising the steps of:
(1) performing enzyme digestion on a sample to be detected by using trypsin, or extracting protein components in the sample to be detected and performing enzyme digestion by using trypsin;
(2) putting into a liquid chromatograph-mass spectrometer, and selecting parent ions m/z469 and daughter ions thereof for monitoring by using marked peptide or gelatin of tuna as a reference; if the retention time of the ion is consistent with that of the reference substance, and the daughter ion is consistent with that of the reference substance, the collagen degradation product or the product thereof contains tuna-derived components, and if the ion with the retention time consistent with that of the reference substance is not present, the collagen degradation product or the product thereof does not contain the tuna-derived components.
3. Use according to claim 2, wherein the content of tuna derived components is calculated from the peak areas in the control and test samples.
4. The use according to claim 2, wherein the collagen degradation product is gelatin obtained by hydrolysis of animal bone, skin and scale.
5. The use according to claim 2, wherein the collagen degradation product is a food, health care product or pharmaceutical product comprising gelatin as a raw material.
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