CN105911127A - Rapid detection method of fish parvalbumin by capillary electrophoresis - Google Patents

Rapid detection method of fish parvalbumin by capillary electrophoresis Download PDF

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Publication number
CN105911127A
CN105911127A CN201610236444.4A CN201610236444A CN105911127A CN 105911127 A CN105911127 A CN 105911127A CN 201610236444 A CN201610236444 A CN 201610236444A CN 105911127 A CN105911127 A CN 105911127A
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fish
parvalbumin
sample
concentration
capillary
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王彦波
傅玲琳
周瑾茹
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Zhejiang Gongshang University
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Zhejiang Gongshang University
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    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N27/00Investigating or analysing materials by the use of electric, electrochemical, or magnetic means
    • G01N27/26Investigating or analysing materials by the use of electric, electrochemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
    • G01N27/416Systems
    • G01N27/447Systems using electrophoresis
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2550/00Electrophoretic profiling, e.g. for proteome analysis

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  • Life Sciences & Earth Sciences (AREA)
  • Molecular Biology (AREA)
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  • Physics & Mathematics (AREA)
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  • Peptides Or Proteins (AREA)

Abstract

The invention discloses a method for detecting fish parvalbumin by capillary electrophoresis. The method comprises the following steps: (1) extracting holoprotein from fish-muscle and dissolving in an equilibrium buffer with pH being 7-8, loading into an anion exchange chromatographic column, eluting with an eluant and collecting a solution corresponding to a flow-through peak so as to obtain a sample; and (2) carrying out capillary zone electrophoresis on the sample to obtain substituting peak area obtained in electrophoretogram into a standard curve regression equation of fish parvalbumin and calculating to obtain concentration of fish parvalbumin in the sample solution. The method of the invention is a method for rapid, qualitative and quantitative detection of aquatic product allergen fish parvalbumin by capillary electrophoresis. The method for qualitative and quantitative analysis of fish parvalbumin has been reported in the literature, and provides new basis for rapid and accurate detection of fish parvalbumin.

Description

A kind of Capillary Electrophoresis quickly detects the method for fish parvalbumin
Technical field
The present invention relates to Allergic skin test technical field, specifically, relate to one capillary electricity Swim quick, qualitative and quantitative detection fish collagen method.
Background technology
Aquatic products move due to its delicious flavour, rich in nutritive value, extremely people's eating, its Mesichthyes Thing is the big class in eight big class allergenic foods, causes allergic reaction due to edible fishes animal every year Example is not within minority, severe patient even threat to life.Parvalbumin (Parvalbumin, Pav) is low Exist in a large number etc. in vertebrate white muscle, be the main allergen of fish species.
Determine that the detection method of fish anaphylactogen mainly has following several at present:
(1) Histamine release experiments
Histamine release experiments is to use anaphylactogen to stimulate mast cell, causes it to discharge histamine isoreactivity Medium, then by measuring the burst size of histamine, allergen activity is identified.In experiment, logical Often using anti-IgE antibodies as positive control, and select sample media as negative reference, to get rid of group The amine non-specific release interference to experimental result.But this experiment affects the factor of histamine release relatively Many, measure difficulty bigger.
(2) immunoblot experiment
Immunoblot assay is on the basis of electrophoretic separation technique and antibody are to antigen specific detection, by A kind of food allergen Testing and appraisal technology that step grows up.Immunoblot experiment generally comprises following Three steps: the electrophoretic separation of holoprotein;The transfer of protein band (is transferred to celluloid (NC) On the solid phase carriers such as film, polyvinylidene fluoride (PVDF) film);The solid phase being printed on protein band is carried Body successively with IgE antibody and ELIAS secondary antibody effect after, add substance that show color, make anaphylactogen band show Look.
(3) anaphylactogen finger-print detection method
Finger-print is a kind of comprehensive, quantifiable discriminating means, main in order to Chinese medicine Discern the false from the genuine, be widely recognized as by WHO and U.S. FDA..Peptide mass fingerprinting analysis is front Phase electrophoresis (SDS-PAGE, 2-DE), on the basis of target protein is carried out separating qualification by chromatogram (LC), The peptide mass fingerprinting being obtained target protein by MALDI-TOF-MS mass spectrum is composed, and combines data Library searching analysing protein sequence and the method that realizes qualification further to protein.
Summary of the invention
For the problems referred to above, it is an object of the invention to provide one Capillary Electrophoresis quick, qualitative And the method quantitatively detecting fish Pav.
A kind of Capillary Electrophoresis quickly detects the method for fish parvalbumin, comprises the steps:
(1) extract the holoprotein in fish tissue and be dissolved in the level pad that pH is 7~8, then Adding in anion-exchange chromatography post, elution, collection penetrates the solution corresponding to peak and is sample Product liquid;
(2) gained sample liquid is carried out CZE, obtain electrophoresis pattern, by electrophoresis pattern Peak area corresponding to Mesichthyes parvalbumin substitutes into the calibration curve regression equation of fish parvalbumin In be calculated the concentration of sample liquid Mesichthyes parvalbumin.
Present invention Capillary Electrophoresis quick, the qualitative and quantitative detection little clear egg of aquatic products anaphylactogen fish In vain, the present invention method of the method qualitative and quantitative analysis fish parvalbumin set up, have no literary composition Offer report, for detecting the foundation that fish parvalbumin provides new fast and accurately.Extract in fish tissue Holoprotein, join in anion-exchange chromatography post, with elution, collect that to penetrate peak corresponding Solution, add in HPCE, by CZE, little clearly in sample liquid Albumen carries out qualitative and quantitative detection.It is higher that capillary electrophoresis of the present invention analyzes speed, Separating degree is more preferable, and the degree of accuracy and sensitivity are higher, can the most qualitative and quantitative detection fish Parvalbumin.
In the step (1) of the present invention:
Holoprotein in fish tissue uses kit to extract.
Described kit is that triumphant base holoprotein extracts kit (the Nanjing triumphant base limited public affairs of biotech development Department).
Preferably, described level pad be pH be the tris-HCl solution of 7.3~7.6, described tris-HCl The concentration of solution is 5~10mmol/L.It is further preferred that described level pad is pH is 7.5 Tris-HCl solution, the concentration of described tris-HCl solution is 10mmol/L.
Preferably, in anion-exchange chromatography post, filler used is DEAE-Sepharose Fast Flow.
Preferably, described eluent is the NaCl solution of 0-0.5mol/L, and NaCl solution is the most excellent Elect 0.04~0.14mol/L as.
Preferably, dissolved with holoprotein level pad with the flow velocity of 0.3~0.6ml/min add cloudy from In sub-displacement chromatography post, eluent with 0.8~1.2ml/min speed elution chromatography post, the most excellent Selection of land, the level pad dissolved with holoprotein adds anion-exchange chromatography with the flow velocity of 0.5ml/min In post, eluent is with the speed elution chromatography post of 1.0ml/min.
Add the level pad of 3~5 times of column volumes with the flow velocity of 1.5ml/min before carrying out Protein Separation To balance chromatographic column.
In the step (2) of the present invention:
Deposition condition is: capillary selects non-coating quartz capillary column, detects wavelength and is 210~220nm, input mode is hydrodynamic injection, and separation voltage is 15 ± 1kv, and capillary column temperature is 25 ± 1 DEG C, running buffer is the borax buffer solution of pH9.2.
Preferably, deposition condition is: capillary selects non-coating quartz capillary column, detects wavelength and is 214nm, input mode is hydrodynamic injection, and pressure is 0.5psi, and sample injection time is 5s, separation voltage For 15kv, capillary column temperature is 25 DEG C, and running buffer is pH9.2 and concentration is 20mmol/L's Borax buffer solution.
The preparation method of calibration curve equation of linear regression is as follows: accurate preparation fish parvalbumin standard Solution 5 μ g/mL, 10 μ g/mL, 25 μ g/mL, 50 μ g/mL, 100 μ g/mL, by step (2) Deposition condition sample introduction, each sample is repeated 3 times, and with peak area, concentration is carried out linear regression, obtains mark Directrix curve equation of linear regression.
The pretreatment of capillary: select non-coating quartz capillary column (45cm × 75 μm, P/ACETM MDQ System, Beckman company), new capillaries post rinses 10~12min with methyl alcohol the most successively, Distilled water flushing 5~6min, 0.1M Na0H solution flushing 30~35min, distilled water flushing 5~6min, Last again with running buffer flushing 10~12min;Successively with distilled water and running buffer before sample introduction Each punching 2~3min.
Further, new capillaries post first rinses 10min, distilled water flushing 5min with methyl alcohol successively, 0.1M Na0H solution rinses 30min, distilled water flushing 5min, rinses with running buffer the most again 10min;2min is respectively rushed with distilled water and running buffer successively before sample introduction.
Fish is grass carp.
Capillary Electrophoresis is not extensive, especially in aquatic products mistake in the application of food allergen context of detection In quick former detection, there is presently no feasible method.This is owing in aquatic products, protein ingredient compares Complexity, thus the detection to anaphylactogen a certain in aquatic products produces interference, and Capillary Electrophoresis detection is wanted Ask the composition in sample the simplest.Accordingly, it would be desirable to development simply, sample fast and effectively Pre-treating method so that it is be suitable for the Capillary Electrophoresis requirement to sample.
The present invention provides a kind of sample-pretreating method simple, quick.First it is to utilize kit to incite somebody to action Holoprotein in aquatic products extracts, then uses DEAE-Sepharose anion-exchange chromatography Method, by purpose anaphylactogen and other Protein Separation, makes sample composition single, is suitable for Capillary Electrophoresis pair The requirement of sample;Meanwhile, the condition of Capillary Electrophoresis is optimized by the present invention, it is achieved that to sample The mensuration of medium and small albumin content.
Under the optimal conditions of pre-treatment and the combination of Capillary Electrophoresis optimal conditions, detect more rapid, Sensitivity and accuracy are higher.
Beneficial effects of the present invention: the present invention is little clearly with the method qualitative and quantitative analysis fish set up The method of albumen, has no that document is reported, provides new for detecting fish parvalbumin fast and accurately Foundation.It is higher that capillary electrophoresis of the present invention analyzes speed, and separating degree is more preferable, the degree of accuracy Higher with sensitivity, can the most qualitative and quantitative detection fish parvalbumin.
Detailed description of the invention
Embodiment 1
1. the preparation of sample
The preparation of sample: use kit to extract the holoprotein in fish tissue, fish holoprotein is dissolved in The level pad of pH7.5 obtains sample liquid.3~5 times of cylinders are added with the flow velocity of 1.5ml/min Long-pending equilibrium liquid, to balance chromatographic column, then adds anion by sample liquid with the speed of 0.5ml/min In displacement chromatography post, then with 0.04~0.14mol/L elution chromatographic column, collect penetrate peak Corresponding solution, is sample.
2. capillary electrophoresis analysis condition optimizing
(1) capillary select and pretreatment: select non-coating quartz capillary column (45cm × 75 μm, P/ACETMMDQ System, Beckman company), new capillaries post first rinses with methyl alcohol successively 10min, distilled water flushing 5min, 0.1M Na0H solution rinses 30min, distilled water flushing 5min, Finally rinse 10min with running buffer again;Respectively rush with distilled water and running buffer successively before sample introduction 2min;
(2) capillary electrophoresis analysis condition: detection wavelength is 214nm, and input mode is that pressure enters Sample (0.5psi, 5s), separation voltage 15kv, capillary column temperature 25 DEG C;Running buffer is 20mmol/L Borax buffer solution (pH=9.2).
3. the foundation of calibration curve: accurate preparation fish parvalbumin standard liquid 5,10,25,50, 100 μ g/mL sample introductions, each sample is repeated 3 times, and with peak area, concentration is carried out linear regression.Knot Fruit linear relationship in the range of 5-100 μ g/mL is good, and regression equation is Y=1.51+0.027x, Coefficient R2=0.995, in good linear relationship in 5-100 μ g/mL concentration range.Minimum Concentrations is 0.1 μ g/mL (S/N > 3).
4. determination of recovery rates and precision measure: by the processing method (being not added with substrate) of sample, take 5,10, 25,50,100 μ g/mL concentration carry out recovery testu, 6 Duplicate Samples of each concentration, calculate The rate of recovery and precision (being shown in Table 1).
Table 1 parvalbumin TIANZHU XINGNAO Capsul and precision measure (n=6)
Add concentration (μ g/mL) Rate of recovery % RSD%
5 99.5 4.8
10 98.8 5.5
25 98.2 5.8
50 97.4 4.6
100 97.6 4.3
As shown in Table 1, in the range of 5-100 μ g/mL concentration is added, the rate of recovery > 95%, RSD < 6%, in the detection of protein macromolecule, is can be received.
Embodiment 2
1. the preparation of sample
The preparation of sample: use kit to extract the holoprotein in fish tissue, fish holoprotein is dissolved in The level pad of pH7.5 obtains sample liquid.3~5 times of cylinders are added with the flow velocity of 1.5ml/min Long-pending equilibrium liquid, to balance chromatographic column, then adds anion by sample liquid with the speed of 0.5ml/min In displacement chromatography post, then with 0.04~0.14mol/L elution chromatographic column, collect penetrate peak Corresponding solution, is sample.
2. capillary electrophoresis analysis condition optimizing
(1) capillary select and pretreatment: select non-coating quartz capillary column (45cm × 75 μm, P/ACETMMDQ System, Beckman company), new capillaries post first rinses with methyl alcohol successively 10min, distilled water flushing 5min, 0.1M Na0H solution rinses 30min, distilled water flushing 5min, Finally rinse 10min with running buffer again;Respectively rush with distilled water and running buffer successively before sample introduction 2min;
(2) capillary electrophoresis analysis condition: detection wavelength is 214nm, and input mode is that pressure enters Sample (0.5psi, 5s), separation voltage 15kv, capillary column temperature 25 DEG C;Running buffer is 30mmol/L Borax buffer solution (pH=9.4).
3. the foundation of calibration curve: accurate preparation fish parvalbumin standard liquid 5,10,25,50, 100 μ g/mL sample introductions, each sample is repeated 3 times, and with peak area, concentration is carried out linear regression.Knot Fruit linear relationship in the range of 5-100 μ g/mL is good, and regression equation is Y=3.47+277.5x, Coefficient R2=0.993, in good linear relationship in 5-100 μ g/mL concentration range.Minimum Concentrations is 0.1 μ g/mL (S/N > 3).
4. determination of recovery rates and precision measure: by the processing method (being not added with substrate) of sample, take 5,10, 25,50,100 μ g/mL concentration carry out recovery testu, 6 Duplicate Samples of each concentration, calculate The rate of recovery and precision (being shown in Table 2).Table 2 parvalbumin TIANZHU XINGNAO Capsul and precision measure (n=6)
Add concentration (μ g/mL) Rate of recovery % RSD%
5 99.8 5.0
10 99.5 5.7
25 98.7 4.7
50 98.5 4.4
100 96.6 4.9
As shown in Table 2, in the range of 5-100 μ g/mL concentration is added, the rate of recovery > 95%, RSD < 6%, in the detection of protein macromolecule, is can be received.
The foregoing is only the case that is embodied as of patent of the present invention, but the technical characteristic of patent of the present invention Be not limited thereto, any those skilled in the relevant art in the field of the invention, the change made Or modify all contain among the scope of the claims of the present invention.

Claims (10)

1. the method quickly detecting fish parvalbumin with Capillary Electrophoresis, it is characterised in that comprise the steps:
(1) extracting the holoprotein in fish tissue and be dissolved in the level pad that pH is 7~8, being subsequently adding in anion-exchange chromatography post, NaCl solution elutes, and collection penetrates the solution corresponding to peak and is sample liquid;
(2) gained sample liquid is carried out CZE, obtain electrophoresis pattern, the peak area corresponding to electrophoresis pattern Mesichthyes parvalbumin is substituted into the concentration being calculated sample liquid Mesichthyes parvalbumin in the calibration curve regression equation of fish parvalbumin.
Method the most according to claim 1, it is characterized in that, in step (2), deposition condition is: capillary selects non-coating quartz capillary column, detection wavelength is 210~220nm, input mode is hydrodynamic injection, separation voltage is 15 ± 1kv, and capillary column temperature is 25 ± 1 DEG C, and running buffer is the borax buffer solution of pH9.0~9.2.
Method the most according to claim 1, it is characterized in that, in step (2), deposition condition is: capillary selects non-coating quartz capillary column, detection wavelength is 214nm, and input mode is hydrodynamic injection, and pressure is 0.5psi, sample injection time is 5s, separation voltage is 15kv, and capillary column temperature is 25 DEG C, and running buffer is pH9.2 and concentration is the borax buffer solution of 20mmol/L.
Method the most according to claim 1, it is characterized in that, the preparation method of calibration curve equation of linear regression is as follows: accurate preparation fish parvalbumin standard liquid 5 μ g/mL, 10 μ g/mL, 25 μ g/mL, 50 μ g/mL, 100 μ g/mL, by deposition condition sample introduction in step (2), each sample is repeated 3 times, with peak area, concentration is carried out linear regression, obtain calibration curve equation of linear regression.
Method the most according to claim 1, it is characterised in that concentration 0-0.5mol/L of described NaCl solution.
Method the most according to claim 1, it is characterised in that described level pad be pH be the tris-HCl solution of 7.3~7.6, the concentration of described tris-HCl solution is 5~10mmol/L.
Method the most according to claim 1, it is characterised in that described level pad be pH be the tris-HCl solution of 7.5, the concentration of described tris-HCl solution is 10mmol/L.
Method the most according to claim 1, it is characterised in that the holoprotein in fish tissue uses kit to extract.
Method the most according to claim 1, it is characterised in that in anion-exchange chromatography post, filler used is DEAE-Sepharose Fast Flow.
Method the most according to claim 1, it is characterised in that fish is grass carp.
CN201610236444.4A 2016-04-14 2016-04-14 Rapid detection method of fish parvalbumin by capillary electrophoresis Pending CN105911127A (en)

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Cited By (5)

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CN108918885A (en) * 2018-06-12 2018-11-30 浙江工商大学 A kind of aptamer, kit and detection method specifically binding fish parvalbumin
CN109253983A (en) * 2018-11-30 2019-01-22 上海海洋大学 The method of Rapid identification and detection parvalbumin based on middle infrared spectrum and nerual network technique
CN109991303A (en) * 2019-02-27 2019-07-09 北京工商大学 Quickly identify the method for unifloal honey using capillary electrophoresis technique
CN110286098A (en) * 2019-05-07 2019-09-27 浙江工商大学 A kind of method of food-borne nano particle separation and quantitative analysis
WO2022237800A1 (en) * 2021-05-12 2022-11-17 浙江吉量科技有限公司 Method for determining average molecular weight of mrna, as well as cap0/1, modified nucleotides and oxides

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN108918885A (en) * 2018-06-12 2018-11-30 浙江工商大学 A kind of aptamer, kit and detection method specifically binding fish parvalbumin
CN108918885B (en) * 2018-06-12 2021-04-20 浙江工商大学 Aptamer specifically binding to fish parvalbumin, kit and detection method
CN109253983A (en) * 2018-11-30 2019-01-22 上海海洋大学 The method of Rapid identification and detection parvalbumin based on middle infrared spectrum and nerual network technique
CN109253983B (en) * 2018-11-30 2021-07-27 上海海洋大学 Method for rapidly identifying and detecting parvalbumin based on mid-infrared spectrum and neural network technology
CN109991303A (en) * 2019-02-27 2019-07-09 北京工商大学 Quickly identify the method for unifloal honey using capillary electrophoresis technique
CN109991303B (en) * 2019-02-27 2023-10-03 北京工商大学 Method for rapidly identifying single flower honey by capillary electrophoresis technology
CN110286098A (en) * 2019-05-07 2019-09-27 浙江工商大学 A kind of method of food-borne nano particle separation and quantitative analysis
WO2022237800A1 (en) * 2021-05-12 2022-11-17 浙江吉量科技有限公司 Method for determining average molecular weight of mrna, as well as cap0/1, modified nucleotides and oxides

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Application publication date: 20160831