RU2402763C1 - Method for assessment of slaughter products quality - Google Patents

Abstract

FIELD: veterinary science.

SUBSTANCE: method includes placement of biological test in solution of phenyl isothiocyanate in isopropyl alcohol, its exposure to capillary zone electrophoresis, using reaction buffer on the basis of β-cyclodextrin, detection of amino acids and their qualitative and quantitative analysis. At the same time biological test is represented by extract of animal organs and tissues, to make which, shot in amount of 0.1-0.2 g is poured up to 10 cm³ with 20% hydrochloric acid, closed and placed in thermostat for 14 hours at the temperature of 105°C. Then it is cooled, not more than 0.05 cm³ of hydrolysate is extracted and dried. Up to 0.1 cm³, 0.1 M solution of sodium carbonate is added, mixed, and not more than 0.3 cm³ of phenyl isothiocyanate solution in isopropyl alcohol is added. It is left to react for 40 minutes. Afterwards, as the mixture produced dries naturally, not more than 0.5 cm³ of distilled water is added, mixed and centrifuged. Then using method of capillary zone electrophoresis through reaction buffer on the basis of β-cyclodextrin, concentration of bound amino acids is detected and compared to reference result of bound amino acids concentration in clinically healthy animals. In case the concentration of bound amino acids compared to the reference value reduces, then products of slaughter are considered to be infected with helminths.

EFFECT: method makes it possible to provide for safety of slaughter products for consumer.

3 dwg, 14 tbl, 1 ex

Description

The invention relates to the field of veterinary medicine, in particular to veterinary and sanitary examination.

The definition of serum protein is known by electrophoresis [see Laboratory research in veterinary medicine, ed. V.Ya. Antonova and P.N. Blinova. M .: "Kolos", 1971, P.423-427], where by electrophoresis the protein is divided into four groups: albumin, alpha, beta and gammaglobulins. At pH 8.6, proteins in an electric field move toward the anode, because they are negatively charged under these conditions. Albumin, then alpha-globulins, beta-globulins, and finally gammaglobulins move most rapidly. Use a device for electrophoresis on paper; photoelectrocolorimeter for determining the amount of dye eluted from electrophoregrams, densitometer, chromatographic filter paper. Electrophoresis is carried out on strips of paper, then a colorimetric determination of the ratio of individual protein fractions is carried out by extracting ink from paper. After staining, four spots corresponding to albumin, alpha, beta and gammaglobulins are detected on the electrophoregram.

With electrophoresis on paper, only the ratio between the individual fractions of whey proteins is determined. Therefore, it is necessary to determine the total amount of protein and calculate the absolute number of individual protein fractions.

The closest in technical essence is the method for determining amino acids in the blood serum of animals through the system of capillary electrophoresis "Drops" (see. Practical guidance on the use of systems of capillary electrophoresis "Drops", N.V. Komarova, Ya.S. Kamentsev, S-P, 2008, p. 102), including derivatization of a bioassay based on a solution of phenylisothiocyanate in isopril alcohol, exposure to it by capillary zone electrophoresis using a working buffer based on β-cyclodystrin, detection of amino acids and their quality qualitative and quantitative analysis.

The disadvantages of the known methods are the limited capabilities, the complexity of the study, the lengthy determination process, the inability to determine the quantitative composition of bound amino acids in the extract of organs and tissues (the longest muscle of the back, heart muscle, liver, lungs, spleen and kidneys) with metastrongylosis (Metastrongylus elongates) on quality products of slaughter of pigs, in cattle with dicroceliosis (Dicrocoelium lanceatum) and echinococcosis (Echinococcus granulosus) on the quality of products of slaughter of cattle.

The technical solution to the problem is to expand the functional and technological capabilities, shorten the lead time and increase the accuracy of determination of bound amino acids in establishing the quality and safety of animal slaughter products in metastrongylosis of pigs (Metastrongylus elongates); with dicroceliosis (Dicrocoelium lanceatum) in cattle; echinococcosis (Echinococcus granulosus) in cattle.

The problem is achieved in that in a method for determining the nutritional value of products of slaughter of animals infected with helminths, for example pigs infected with metastrongylosis (Metastrongylus elongates); cattle infected with dicroceliosis (Dicrocoelium lanceatum) and echinococcosis (Echinococcus granulosus), including derivatization of a bioassay based on a solution of phenylisothiocyanate in isopropyl alcohol, exposure to it by capillary zone electrophoresis using a working buffer and their amino acid based on quantitative analysis, according to the invention, as a bioassay, an aqueous extract of organs and tissues of animals infected with helminths is used, preliminary hydrolysis of the bioassay is carried out, for To do this, take a sample of muscle tissue from 0.1-0.2 g of the sample and pour up to 10 cm ^{3 with} 20% hydrochloric acid into the vessels for hydrolysis, then they are closed with stoppers and placed in a thermostat for 14 hours at a temperature of no more than 105 ° C , then cooled, not more than 0.05 cm ^{3 of} hydrolyzate is taken with a pipette into a micro vessel and dried to dryness, up to 0.1 cm ^{3 of a} 0.1 M sodium carbonate solution is added, stirred, then no more than 0.3 cm ³ of a phenylisothiocyanate solution in isopropyl is added alcohol and left to undergo a reaction for 40 minutes, after drying the contents in natural conditions ditions are added by not more than 0.5 cm ³ distilled water, was stirred, transferred to an Eppendorf tube and centrifuged to remove suspended solids and gases, and then the data obtained as a result of qualitative and quantitative analysis result is compared with the reference concentration of amino acids related clinically healthy animals and determine the quality of the products, if the concentration of bound amino acids in infected animals is reduced compared with the control, then the products of slaughter of animals are considered poor quality.

The advantage of this method is as follows: high separation efficiency of components, not available with other research methods; low consumption of reagents and solvents; simplicity of equipment; high speed analysis and high reproducibility of reaction conditions; good solubility of derivatives in an aqueous medium; commercial availability; the wide possibilities of capillary electrophoresis in the analysis of bound amino acids. In addition, the proposed proposal is economical, because does not require the use of expensive chemicals.

The novelty of the proposed proposal is due to the fact that the method of capillary electrophoresis is used in the method for determining the concentration of bound amino acids in the aqueous extract of organs and tissues (the longest muscle of the back, heart muscle, liver, lungs, spleen and kidneys) in metastrongylesis of pigs, dicroceliosis and echinococcosis of cattle determination of the mass concentration of bound amino acids based on the separation of anionic forms of N-phenylthiocarbamyl derivatives of amino acids under the influence of an electric field due to and x various electrophoretic mobility. For identification and quantitative determination of the analyzed components, ultraviolet absorption is recorded at a wavelength of 254 nm in organs and tissues during pig metastrongyles, dicroceliosis and echinococcosis of cattle in order to determine the effect of their metabolic products Metastrongylus elongates on the quality of pig slaughter products, Dicrocoelium linococumum and on the quality of cattle slaughter products.

In addition, the novelty of the proposed proposal is due to the fact that the rapid analysis established the parameters for changing the concentration of bound amino acids in organs and tissues (the longest muscle of the back, heart muscle, liver, lungs, spleen and kidneys) during invasion of pigs by the pathogen Metastrongylus elongates, cattle - Dicrocoelium lanceatum, cattle - Echinococcus granulosus.

The invention is illustrated by drawings, where figure 1 presents a graph of the concentration of bound amino acids in the pulmonary tissue extract in pigs with metastrongylosis; figure 2 is a graph of the concentration of bound amino acids in the extract of liver tissue in cattle with dicroceliosis; figure 3 is a graph of the concentration of bound amino acids in the extraction of liver tissue in cattle with echinococcosis.

An example of a specific implementation of the method for determining the nutritional value of products of slaughter of animals infected with helminths, for example pigs infected with metastrongyles (Metastrongylus elongates); cattle infected with dicroceliosis (Dicrocoelium lanceatum) and echinococcosis (Echinococcus granulosus)

In the process of post-slaughter diagnostics of pigs in the amount of 500 animals, among them we diagnosed 100 animals in 100 animals based on the detection of a large number of helminths of metastrongilus in the lumen of the bronchi. In the process of post-mortem diagnosis in cattle in the amount of 2500 animals, among them 557 animals in the liver showed dicrocelia, 350 animals had echinococci in the liver and 150 animals in the lungs.

To determine the concentration of bound amino acids in metastrongylesis of pigs, dicroceliosis and echinococcosis of cattle, an extract of organs and tissues (the longest muscle of the back, heart muscle, liver, lungs, spleen and kidneys) is used. For this, for each disease of the animals, average samples are taken from 10 animals. In this case, the studied animals were divided into 2 groups of 10 average samples in each. The control group consisted of clinically healthy animals (pigs and cattle), and the experimental groups were affected by metastrongilus, dicrocelia, and echinococcus.

To determine the concentration of bound amino acids, hydrolysis is preliminarily carried out; for this, a sample of muscle tissue of 0.1-0.2 g of sample is taken and up to 10 cm ^{3 of} 20% hydrochloric acid is poured in special vessels for hydrolysis. The vessels are closed with stoppers and placed in a thermostat for 14 hours at a temperature of 105 ° C. Then it is cooled, taken with a pipette into a microvessel (glass or bottle) of 0.05 cm ^{3 of} hydrolyzate and dried to dryness. Then add up to 0.1 cm ³ 0.1 M sodium carbonate solution, mix, then add 0.3 cm ³ solution of phenylisothiocyanate (FITC) in isopropyl alcohol (0.2 cm ³ FITC in 12 cm isopropyl alcohol) and leave to pass reaction for 40 minutes. After the contents have dried under natural conditions, 0.5 cm ^{3 of} distilled water is added, mixed, transferred to an Eppendorf tube and centrifuged to remove gases and suspensions.

Conditions for the analysis of capillary electrophoresis: quartz capillary 0.5 m long to the detector, inner diameter 75 × 10 ^-6 m; adjustable high voltage source of positive polarity 3-25 kV; hydrostatic injection of a sample at a pressure of 30 mbar for 5 s; β-cyclodextrin-based buffer working solution (54 mg in 12.5 cm ^{3 of a} buffer solution of dihydrogen phosphate and sodium hydrogen phosphate); voltage "plus 10 kV"; analysis time passes within 40 minutes; forced air cooling of the capillary to room temperature; output and processing of results on a computer.

The method of capillary electrophoresis to determine the mass concentration of amino acids is based on the separation of anionic forms of N-phenylthiocarbamyl derivatives of amino acids under the influence of an electric field due to their different electrophoretic mobility. To identify and quantify the analyzed components, ultraviolet absorption is recorded at a wavelength of 254 nm.

Alpha amino acids, when reacted with phenylisothiocyanate in an alkaline medium, produce N-phenylthiocarbamyl (FTK) derivatives, which are acids that exist under basic conditions in the form of anions. Due to the presence in the structure of the obtained compounds of the benzene ring, phenylcarbamyl derivatives have an absorption band at 254 nm. The content of bound amino acids is determined through derivatives with phenylisothiocyanate by capillary electrophoresis.

In the process of analysis, the order and time of release of bound amino acids in organs and tissues in clinically healthy animals and for helminthiases was established (Table 1, Table 2, Table 3, Table 4 and Table 5).

As a result of the studies, it was found that during the invasion of pigs by metastrongilus in the longest muscle of the back, the concentration of bound amino acids was 3.6 times lower than lysine, 1.9 times lower than tryptophan, 1.6 times lower than methionine, 1.5 times lower than phenylalanine , 1.4 times - serine, 1.3 times - valine, leucine, proline and α-alanine, 1.2 times - arginine, histidine, glycine and threonine relative to clinically healthy animals (Table 6).

During pig invasion by metastrongylyus, the concentration of bound amino acids in the extract of the heart muscle was 2.9 times lower than arginine, 2.8 times lower than histidine and valine, 2.7 times lower than α-alanine, 2.5 times lower than glycine, leucine and serine, 2.4 times - threonine, 2 times - proline, and, conversely, higher than tyrosine 8.7 times, 1.1 times - tryptophan relative to clinically healthy animals (Table 6).

The concentration of bound amino acids in pigs invaded by metastrongilus in the liver extract was 1.6 times lower than arginine, 1.5 times lower than threonine and serine, 1.4 times lower than valine and glycine, 1.3 times lower than leucine and α- alanine, 1.2 times higher than proline and, conversely, 44 times higher than tyrosine, 1.8 times higher than phenylalanine, 1.6 times higher than histidine and 1.4 times higher than tryptophan relative to clinically healthy animals. At the same time, the concentration of the bound amino acid methionine was almost at the level of clinically healthy animals (Table 7).

During the invasion of pigs by metastrongylyus, the concentration of bound amino acids in the lung tissue extract was 3 times lower than glycine, 2.6 times lower than valine, 2.5 times lower than proline, 2 times lower than arginine, α-alanine, threonine, serine, 1 , 8 times histidine and methionine, 1.7 times leucine, 1.5 times tryptophan, 1.3 times phenylalanine and, conversely, 3 times higher than tyrosine relative to clinically healthy animals (Table 7).

The concentration of bound amino acids in pigs invaded by metastrongilus in the spleen extract was 60 times higher than leucine, 34 times higher than methionine, 32 times higher than histidine, 20 times higher than arginine, 2.4 times higher than lysine and tyrosine, 2 times higher than proline and valine, 1.5 times - serine, threonine, 1.3 times - α-alanine, glycine and phenylalanine relative to clinically healthy animals. It should be noted that the bound amino acid tryptophan was not detected in pigs with metastrongilosis (Table 8).

During pig invasion by metastrongylyus, the concentration of bound amino acids in the kidney tissue extract was 2.4 times lower than phenylalanine, 1.9 times lower than histidine, 1.8 times lower than methionine and glycine, 1.7 times lower than arginine, α-alanine and serine times, lysine - 1.6 times, valine, proline and threonine - 1.5 times, leucine and tyrosine - 1.4 times, relative to clinically healthy animals. At the same time, the concentration of the bound amino acid tryptophan was almost at the level of clinically healthy animals (Table 8).

Thus, during invasion by the helminths of Metastrongylus elongatus, there was a decrease in bound amino acids and their decomposition into free amino acids, as well as a change in their concentration depending on both the functional characteristics of the organ and the location (lungs) of the mature larvae of Metastrongylus elongatus. During the invasion of pigs by mature larvae of Metastrongylus elongatus, it was found that in the lung tissue there was a 2-fold decrease in the total concentration of bound amino acids relative to clinically healthy animals. In the longest muscle of the back and in the tissues of the liver, a 1.3-fold decrease in the total concentration of bound amino acids occurred, in the heart muscle - by 2.6 times, in the tissues of the spleen - by 2.8 times, in the renal tissue - by 1.7 times relative clinically healthy animals.

It should be noted that in pigs metastrongilosis, tyrosine was not detected in the longest muscle of the back, lysine and tyrosine in the heart muscle, lysine in the tissues of the liver and lung, and tryptophan in the tissues of the spleen. In the longest muscle of the back, cardiac muscle, in the tissues of the liver, pulmonary and renal, the maximum concentration was in histidine, and in the tissues of the spleen - on α-alanine in both the control and experimental groups.

As a result of the studies, it was found that in cattle echinococcosis, the concentration of bound amino acids in the extract of the longest muscle of the back was 2 times lower than glycine, methionine, proline, threonine, tryptophan and serine, 1.6 times - arginine, valine and leucine, 5 times - lysine, 1.3 times - α-alanine, 1.2 times - tyrosine and, conversely, 1.2 times higher than histidine and phenylalanine relative to clinically healthy animals (Table 9).

In cattle echinococcosis, the concentration of bound amino acids in the extract of the heart muscle was 3 times lower than tyrosine, 2.4 times lower than phenylalanine, 1.4 times lower than methionine, 1.1 times lower than glycine, serine, proline, threonine, and on the contrary, tryptophan is 1.3 times higher, and α-alanine, arginine, valine, histidine is 1.1 times higher in relation to clinically healthy animals. The concentration of the bound amino acid leucine was almost at the level of clinically healthy animals. The bound amino acid lysine was not detected in echinococcosis (Table 9).

The concentration of bound amino acids in cattle invaded by echinococcus in the liver tissue extract was 3 times lower than tryptophan and phenylalanine, 2 times lower than α-alanine, arginine, valine, glycine, proline, serine, threonine, 1.5 times lower than leucine, 1.1 times - methionine and, conversely, higher than 1.4 times histidine relative to clinically healthy animals. Bound amino acids lysine and tyrosine were not detected (Table 10).

During cattle echinococcus invasion, the concentration of bound amino acids in the pulmonary tissue extract was 1.4 times lower than valine, 1.3 times lower than histidine 1.2 times higher than glycine, leucine, threonine, serine, 1.1 times lower than arginine , methionine, proline, tryptophan and phenylalanine relative to clinically healthy animals. The bound amino acid α-alanine was almost on par with clinically healthy animals. Bound amino acids lysine and tyrosine were not detected (Table 10).

The concentration of bound amino acids in cattle echinococcosis in the spleen hood decreased: 10 times tyrosine, 2 times tryptophan, 1.6 times histidine, lysine and proline, 1.5 times leucine, methionine and serine, and vice versa 2-fold increase in phenylalanine, 1.6-fold increase in arginine, 1.5-fold increase in threonine, 1.4-fold increase in α-alanine, 1.3-fold increase in glycine, and 1.2-fold increase in clinical value of valine healthy animals (table 11).

During cattle echinococcus invasion, the concentration of bound amino acids in the kidney tissue extract was 17 times lower than tyrosine, 5 times lower than lysine, 2 times lower than tryptophan and phenylalanine, 1.3 times lower than arginine 1.1 times higher than histidine, valine , leucine and proline, and, conversely, a 1.2-fold increase in serine and threonine, 1.1-fold increase in α-alanine, the linked amino acid glycine was almost on par with clinically healthy animals (Table 11).

The total concentration of bound amino acids in clinically healthy cattle in the extraction of the longest back muscle was 155454.74 mg / kg of meat, in the heart muscle - 138380.29 mg / kg of meat, in the liver - 161367.88 mg / kg of meat, in the lungs 72,837.32 mg / kg of ground beef, 124095.40 mg / kg of ground beef in the spleen, 115,536.74 mg / kg of ground beef in the kidneys. The highest content of bound amino acids was noted in the liver tissues and was 2.2 times higher than in the lung tissues, 1.4 times higher than the kidneys, 1.3 times higher than the spleen; 1.2 times - the longest muscle of the back and heart muscle.

The total concentration of bound amino acids in the extraction of the longest back muscle in echinococcosis of cattle was 109453.32 mg / kg of meat, in the heart muscle - 132490.23 mg / kg of meat, in the liver - 109013.30 mg / kg of meat, in the lungs - 627006 , 90 mg / kg of minced meat, in the spleen - 115,536.74 mg / kg of minced meat, in the kidneys - 109,247.03 mg / kg of minced meat. The highest content of bound amino acids was noted in the lungs and was 6 times higher than in the stretching of the longest muscle of the back, liver and kidneys, 5 times - of the heart muscle and spleen.

Thus, with echinococcosis (Echinococcus granulosus) in cattle, it was found that a 1.5-fold decrease in the total concentration of bound amino acids relative to clinically healthy animals occurred in the liver tissues. In the longest muscle of the back, a 1.4-fold decrease in the total concentration of bound amino acids occurred, a 1.1-fold decrease in the cardiac muscle, renal, and spleen relative to clinically healthy animals. In the lung tissue, the total concentration of bound amino acids was almost on par with clinically healthy animals.

It should be noted that in echinococcosis in cattle the following linked amino acids were not registered: lysine in the heart muscle, lysine and tyrosine in the tissues of the liver and lungs. In clinically healthy animals, the associated amino acid lysine was not detected in the liver tissues, lysine and tyrosine in the lung tissue.

In the longest muscle of the back and in the liver tissue among the bound amino acids, the maximum concentration was attributable to α-alanine in clinically healthy animals, and for echinococcosis, to histidine. In clinically healthy animals, the maximum concentration in the lung tissue and spleen was in histidine, and in echinococcosis, in α-alanine. In both clinically healthy and echinococcal animals invaded by cardiac muscle and renal tissue, the maximum concentration was observed in histidine.

As a result of the studies, it was found that with cattle dicroceliosis, the concentration of bound amino acids in the longest muscle of the back was 3 times lower than tryptophan, 2 times glycine, valine, proline and serine, 1.6 times threonine, 1.5 times - α-alanine and leucine, 1.4 times - arginine and methionine, 1.3 times - phenylalanine, 1.1 times - histidine relative to clinically healthy animals. Bound amino acids lysine and tyrosine were not detected with dicroceliosis (Table 12).

In bovine dicrocele, the concentration of bound amino acids in the extract of the heart muscle was 2 times lower than lysine, glycine and phenylalanine, 1.5 times lower than leucine, methionine, serine and threonine, 1.4 times lower than valine and proline, 1 3 times - α-alanine and histidine, 1.2 times - arginine and, conversely, 3 times higher than tyrosine relative to clinically healthy animals. The bound amino acid tryptophan was practically on par with clinically healthy animals (Table 12).

The concentration of bound amino acids in cattle invaded by dicroceli in the liver hood was 4 times lower than tryptophan, 3 times lower than glycine, valine, proline and phenylalanine, 2 times lower than α-alanine, arginine, leucine, serine and tyrosine, 1 6 times - threonine, 1.2 times - methionine relative to clinically healthy animals. The linked amino acid histidine was almost on par with clinically healthy animals. With dicroceliosis, a linked amino acid lysine was detected in the liver tissues, the concentration of which was 52.96 ± 1.94 mg / kg (Table 13).

In cattle dicroceliosis, the concentration of bound amino acids in the pulmonary tissue extract was 3 times lower than tyrosine, 1.6 times lower than phenylalanine, 1.3 times lower than glycine and valine, 1.2 times lower than histidine, 1.1 times lower - α-alanine and proline, and, conversely, higher than 1.4 times tryptophan, 1.2 times higher than methionine, 1.1 times higher than threonine relative to clinically healthy animals. The concentrations of bound amino acids of arginine, leucine and serine were almost on par with clinically healthy animals. When dicroceliosis in the lung tissue was detected, the bound amino acid lysine, the concentration of which was 355.85 ± 5.33 mg / kg (Table 13).

The concentration of bound amino acids in cattle invaded by dicrocelia in the spleen hood decreased: 18 times tyrosine, 4 times lysine, 3 times histidine, leucine, proline, serine and tryptophan, 2 times α-alanine, valine, glycine , methionine and threonine, 1.6 times - arginine, 1.4 times - phenylalanine relative to clinically healthy animals (table 14).

When bovine dicrocelia was invaded, the concentration of bound amino acids in the kidney tissue extract was 23 times lower than histidine, 14 times lower than threonine, 12 times lower than leucine, 10 times lower than methionine, 7 times lower than valine, 6 times lower than lysine, 4 times - serine and tyrosine, 2 times - α-alanine, tryptophan and phenylalanine, 1.5 times - arginine and, conversely, 4 times higher proline relative to clinically healthy animals. The bound amino acid glycine was almost on a par with clinically healthy animals (Table 14).

The total concentration of bound amino acids in the stretching of the longest muscle of the back with cattle dicroceliosis was 106525.94 mg / kg of minced meat, in the heart muscle - 100518.56 mg / kg of minced meat, in the liver - 92036.26 mg / kg of minced meat, 68754 in the lungs , 07 mg / kg of meat, in the spleen - 51873.04 mg / kg of meat, in the kidneys - 32327.40 mg / kg of meat. The highest content of bound amino acids was noted in the stretching of the longest back muscle and was 3.3 times higher than in the stretching of the kidney tissue, 2 times - the spleen, 1.5 times - the lung tissue, 1.2 times - the liver and 1 , 1 time - of the heart muscle.

Thus, during the invasion of cattle by helminths of Dicrocoelium lanceatum, it was found that liver tissues decrease by 1.8 times the total concentration of bound amino acids relative to clinically healthy animals. In the longest back muscle, a 1.5-fold decrease in the total concentration of bound amino acids is noted, in the heart muscle - by 1.4 times, in lung tissue - by 1.1 times, in spleen tissues - by 2.4 times, in renal tissue - by 3.5 times relatively clinically healthy animals. It should be noted that with dicroceliosis in cattle in the longest muscle of the back, in the heart muscle, in the tissues of the liver, lung and spleen, the maximum concentration was in histidine, and in renal tissue - in glycine.

By the concentration, order and time of release of bound amino acids, it is possible to establish the quality of animal slaughter products during helminthiases.

The determination of the concentration of bound amino acids in the stretching of muscle tissue and organs is important for establishing the quality and safety of the products of slaughter of clinically healthy pigs and for metastrongylosis, dicroceliosis, and echinococcosis of cattle. A high concentration of bound amino acids in clinically healthy animals indicates the absence of protein breakdown processes in tissues and organs. With helminthiases, a decrease in bound amino acids occurs and their decomposition into free amino acids, and also a change in their concentration is noted depending on the functional characteristics of the organ and on the location of the helminths.

Therefore, according to the concentration of bound amino acids, it can be established that for metastrongyilism of pigs, dicroceliosis and echinococcosis of cattle, internal organs should be sent for technical utilization, carcasses for industrial processing (production of cooked and cooked smoked sausages) due to the low nutritional value of slaughter products animals.

In order to ensure the quality and safety of animal slaughter products during metastrongylosis, dicroceliosis, and echinococcosis during primary processing in production and sales, it is necessary to: increase control of technological production, the level of laboratory analysis of animal slaughter products, including determination of the concentration of bound amino acids using capillary electrophoresis “Drops 103- P "to establish the degree of tissue destruction caused by the waste products of helminths.

Claims (1)

A method for assessing the quality of animal slaughter products, including placing a bioassay in a solution of phenylisothiocyanate in isopropyl alcohol, exposing it to capillary zone electrophoresis using a working buffer based on β-cyclodextrin, detecting amino acids and their qualitative and quantitative analysis, characterized in that they use bioassays an extract from the organs and tissues of animals, to obtain which a sample in an amount of 0.1-0.2 g is poured into 10 cm ^{3 with} 20% hydrochloric acid, closed and placed in a thermostat for 14 hours at at a temperature of 105 ° C, after which it is cooled, no more than 0.05 cm ^{3 of} hydrolyzate is taken and dried, then up to 0.1 cm ^{3 of a} 0.1 M sodium carbonate solution is added, stirred and no more than 0.3 cm ³ of a phenylisothiocyanate solution is added to isopropyl alcohol is allowed to react for 40 minutes, and after the resulting mixture has dried under natural conditions, not more than 0.5 cm ^{3 of} distilled water is added, mixed and centrifuged, then by capillary zone electrophoresis using a working buffer based on β -cyclodextrin ODA eating the concentration of bound amino acids and comparing it with the control result of the concentration of bound amino acids in clinically healthy animals, and if the concentration of bound amino acids is reduced compared with the control, the products of slaughter of animals are considered infected helminths.

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