Method for determination of natural amino acids in food products protein composition

FIELD: food industry.

SUBSTANCE: method envisages the sample acid hydrolysis, the hydrolysate filtration and chromatographic separation with subsequent automatic identification and quantitative evaluation of amino acids content using an automatic analyser. The invention allows to determine amino acids in the food product proteins composition with amino acids content equal to nearly 0.1-3.5 g/100 g of the product (1.5-17 g/100 g of protein) with application of sequential elution of amino acids with a buffer solutions mixture and simultaneous detection of the components at two wave lengths being 440 and 570 nm.

EFFECT: acceleration of the process of amino acids isolation from the food product and determination accuracy enhancement due to losses decrease and highly sensitive material application.

2 tbl

 

The invention relates to the field of analysis of biological value of food and medical purposes, in particular of animal raw materials and products on its basis, and can be used in medicine, food and perfume industry, and agriculture.

Known various methods for determining the composition of amino acids in proteins. The most commonly used method is the classic high-performance liquid chromatography (HPLC), which allows the separation and identification of most of the amino acids in the mixture, but the lack of specificity of the method does not allow full differentiation of all 20 natural amino acids, in particular not there is a complete separation and proper identification from serine valine, phenylalanine from Proline and some other pairs of amino acids with similar chromatographic mobility in the conditions of HPLC [Neklyudov A.D., A. Ivankin. Collagen: synthesis, properties and application: monograph. - M.: GOU VPO at MSFU, 2007].

There is also known a method of increasing the accuracy of determining the sequence of amino acid residues of a biopolymer according to mass spectrometric analysis using computational system [Patent RU No. 2408011 C2]. The method is accurate, but is a complex technical implementation and requires dorogostojascego mass spectrometric detection.

The known method of identification 11-16 amino acids by capillary electrophoresis [Patent RU No. 2346931 C1], however this method does not allow to identify the full range of natural amino acids.

Closest to the claimed method is the separation of basic amino acids, which is that amino acids shared by two-dimensional thin-layer chromatography and sequential use of two new chromatographic systems solvents: isopropyl alcohol - acetone - 24-25% solution of ammonia - water in the ratio(19,0-27,0):(20,0-26,0):(3,0-6,5):(6,0-10,0) (by volume) and chloroform - ethanol - glacial acetic acid - water in the ratio(23,0-27,0):(13,5-16,0):(1,3-3,5) (by volume). For detection of amino acids using ninhydrin reagent and optionally reagents Ehrlich or Nessler [Application RU # 94028253 A1, CL G01N 30/02]. The method is time consuming and does not allow for quick identification in automatic mode.

The technical objective of the claimed invention is to accelerate the process of separating amino acids from food and increase detection accuracy by reducing losses and use of sensitive material.

The problem is solved in the method comprising the acidic hydrolysis of the sample filter and the chromatographic separation of the hydrolysate followed automatically the second identification and quantification of amino acids on the automated analyzer.

The technical result consists in the determination of amino acids in the proteins of the food product when their content is about 0.1-3.5 g/100 g of product (1.5 to 17 g/100 g protein) using sequential elution of amino acids with a mixture of buffer solutions and simultaneous detection of components at two wavelengths 440 and 570 nm.

The inventive method of determination carried out by the following method.

Analysis of the amino acids being performed on the amino acid analyzer, which is injected hydrolyzate food product. For the separation of amino acids using a buffer system components A-F, the composition of the buffer solutions is listed in table 1. pH buffer solutions pre-installed with the use of orthophosphoric acid and sodium hydroxide, the solution before introduction into the analyzer is filtered through a Teflon filter with a pore size of 0.22 μm.

Table 1
The composition of the buffer solutions
NameABCDF
pH3,33,6 4,511,011,0
Normality0,100,100,100,250,3
Sodium acetate, g8,28,28,28,20
Methanol ml750000
Formic acid, ml3,03,02,01,20
Acetic acid, ml15,020,01,55,00
Boric acid, g0002,00
Ethylenediaminetetraacetate disodium salt, g 0000,50
Sodium hydroxide, g0006,0to 12.0
Caprylic acid, ál100100100100100
Deionized water for HPLC, lto 1to 1to 1to 1to 1

The principle of determination of amino acids is as follows. 20 ál of the test sample is placed in a plastic vessel, which is mounted in rotating tripod automatic temperature-controlled injector. Sakol samples is carried out in accordance with the program after washing and regeneration of the chromatography column having a temperature of 47°C and filled with ion exchanger is a cation exchange resin with carboxylic ionic groups in the Na+-form. The flow of eluent is carried out by capillary high-pressure hoses with an inner diameter of 0.2 mm Separation AMI is ocelot is carried out automatically in accordance with a given program (table 2). After separation column, the solution comes in a temperature-controlled reactor for color reaction. The feed to the reactor ninhydrin solution containing 15 g/l of ninhydrin, 0.55 g/l hydrogentartrate, 1% methylcellosolve, 10% methanol in 0.1 M acetate buffer pH of 4.8, if the reactor temperature 125°C to implement a color reaction analyzed and last amino acids with ninhydrin. Next colored solution with a complex of amino acids with ninhydrin is pumped in the UV detector. Registration of amino acids that are related in complex with ninhydrin, carried out automatically at the same time at 570 nm, Proline assayed at 440 nm, as this is the maximum absorbance data of the designated amino acids.

Operation of the analyzer is performed according to the program, providing for a simultaneous step change of the type of buffer and temperature of the chromatographic column at each stage. Standard analysis time from the moment you enter the sample until the completion of the last peak, which corresponds to arginine, 50 minutes at a feed rate of the eluent 0.2 ml/min

Table 2
Program analysis of amino acids (P in column (50 ATM, flow 0.2 ml/min)
1245678910111213
Time minto 12.05,57,59,03,011,09,08,00,18,04,06,10,4
The input sampleX
Ninhydrin bufferXXX XXXXX
Buffer AXX
Buffer BX
Buffer CXX
Buffer DXXX
Buffer FXXXXX
The column temperature, °C4747484849525660607070 5555

The method used allows to determine with accuracy of ±(5-10)% availability of all natural amino acids with a minimum level of their content in the solution (0,500±0,006) µmol/ml Minimum interval reliable determination signal of amino acids constituting a >200 mV, to get a concentration of >0.3 ág/ml was taken for analysis of protein in the sample.

Example. 0.1 g of the sample (food or protein of unknown composition containing the protein component of more than 20%) treated with 6 M HCl solution (1 ml at a temperature of 120°C for 24 h in an atmosphere of Ar, the resulting hydrolysate is mixed with 5 ml of buffer with a pH of 2.2, contains: sodium citrate of 9.8 g of concentrated HCl to 8.3 ml, 1 ml thiodiglycol and Caprylic acid 50 ál per liter, filtered through a membrane filter with pores of 0.45 μm and injected into the amino acid analyzer.

Upon completion of the automatic analysis get the chromatogram, the content of amino acids (X) in μm/ml (or mg/ml, %, conventional machine units mm or the height or the peak areas in accordance with the preset automatic calibration processing of chromatograms) carried out automatically by the formula: X=S1/S2·C, where S1- the peak area defined by amino acids on the aminogram are determined; S2the peak area of the same amino acid standard mixture; C is the concentration of the situation amino acids in the standard mixture, μm/ml as a calibration using standard solution containing 2.5 μmol/ml of ASP, THR, GLU, PRO, GLY, ALA, CYS, VAL, MET, ILEY, LEY, TYR, PHE, HIS, LYS, TRP, and ARG. The results of determination calculated to the second decimal place and rounded to the first decimal place after the decimal point.

The method of determining the composition and content of amino acids in proteins food products that include acid hydrolysis of the sample, filtration, chromatographic separation and subsequent identification and quantification of amino acids, characterized in that the chromatographic separation and subsequent identification and quantification of amino acids in a concentration of 0.5 mmol/ml solution mixture initially carried out in the system buffer solutions of variable composition with increasing normality of from 0.1 to 0.3 on a chromatographic column with cation exchange resin with carboxylic ionic groups in the Na+form in the interval of rising temperatures ranging from 47 to 70°C, then in the buffer with a normality of 0.1 in the interval decreasing temperature 70-55°C with simultaneous detection of separated at the output of amino acids in the form of a colored complex with ninhydrin at two wavelengths 440 and 570 nm in an automatic mode.



 

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5 cl

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1 dwg

FIELD: mining.

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3 cl, 3 dwg

FIELD: physics.

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EFFECT: high rate and accuracy of detecting properties of a stream of a grinding product.

26 cl, 3 dwg

FIELD: veterinary.

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EFFECT: improving accuracy and reliability, diagnostics informativity as per a provisional dysbiosis index - the ratio of content of free water and amines; detection of different classes of organic substances and equilibrium gas phase above manure samples is simplified.

3 tbl

FIELD: medicine, pharmaceutics.

SUBSTANCE: invention relates to application of peptide, which has sequence originating from amino acid sequence of protein SNAP-25, for treatment of pain and/or inflammation.

EFFECT: obtaining novel composition.

9 cl, 1 dwg, 1 tbl, 2 ex

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