Electrophoretic system for express analysis of whey protein fractions

Yukalo, V.; Datsyshyn, Kateryna

doi:10.15587/1729-4061.2019.160186

Cited by 9 publications

(14 citation statements)

References 15 publications

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“…However, electrophoresis can be used to establish proteins fractions that are not cleaved during proteolysis. It is known that the method of express electrophoresis in the anode system of homogeneous PAG allows to reliably identify the major whey proteins that are precursors of BAP [20]. Using this electrophoretic system allowed to obtain appropriate densitograms (Fig.…”

Section: Discussion Of the Results Of Whey Protein Concentrates Protementioning

confidence: 99%

“…The fractional composition of WPC and proteolysis products was analyzed by the method of express electrophoresis in the anode system of homogeneous PAG [20]. Quantitative processing of electrophoregrams was performed by using the image reading function imread [21].…”

Section: Spectrophotometric Chromatographic and Electrophoretic Mmentioning

confidence: 99%

“…For this purpose, samples taken at different stages of proteolysis (0 min, 60 min, 120 min and 180 min) were analyzed by electrophoresis. The express method previously proposed for the analysis of a large number of milk whey protein samples was used for analysis [20]. Densitometric analysis of the electrophoregram of the sample taken at the 120-th minute of proteolysis was also performed in all cases.…”

Section: Electrophoresis Of Whey Protein Concentrates Protein Fracmentioning

confidence: 99%

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Comparison of products of whey proteins concentrate proteolysis, obtained by different proteolytic preparations

Yukalo

Datsyshyn

2019

EEJET

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Proteolysis is one of the important ways of milk whey processing [4]. In particular, athletes' food products, infant formula, hypoallergenic products, and enteral nutrition products are produced with the help of proteolysis [5]. Different enzyme proteolytic preparations of animal, plant and microbiological origin are used in the technologies of these products [6]. Proteolysis is performed in optimal conditions for each of these preparations. The conditions and specificity of proteolytic action on whey proteins may significantly differ. In this context, the following questions arise: whether the positive potential laid by nature in the form of bioactive peptides is lost, and whether bioactive peptides can be formed in case of using different proteolytic preparations? Therefore, it is actual to compare the character of whey pro

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Section: Discussion Of the Results Of Whey Protein Concentrates Protementioning

confidence: 99%

Section: Spectrophotometric Chromatographic and Electrophoretic Mmentioning

confidence: 99%

Section: Electrophoresis Of Whey Protein Concentrates Protein Fracmentioning

confidence: 99%

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Comparison of products of whey proteins concentrate proteolysis, obtained by different proteolytic preparations

Yukalo

Datsyshyn

2019

EEJET

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“…The homogeneity of the received β-LG preparation was analyzed by expressing electroGphoresis in the polyacrylamide gel (PAG) plates. Gel's composition and conditions of electrophoresis are described in [13]. Gels were stained with 0.5 % solution of amido black 10 B and were kept in 7 % acetic acid.…”

Section: Methodsmentioning

confidence: 99%

Improvement of the Method of Comparative Study of Milk Whey Proteins Enzymatic Hydrolysis

Yukalo

Datsyshyn

2019

EUREKA: Life Sciences

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Milk whey proteins are valueble nutritional ingredients with a number of health-beneficial properties. Whey proteins are also a source of bioactive peptides that can be released in the process of proteins enzymatic hydrolysis. In this connection, there often is a need to compare their proteolytic action on milk whey proteins. It is important to take into account the specificities of the composition and properties of milk whey proteins. The aim of the research was to improve the method of comparative study of milk whey proteins enzymatic hydrolysis. Casein and whey were obtained from fresh cow skimmed milk. The whey was separated by centrifugation after casein precipitation at the isoelectric point. The following enzyme preparations were used in the research: neutral protease, papain, trypsin, chymotrypsin and pancreatin. To select β-LG, gel filtration of the milk whey on the chromatographic column with Sephadex G-150 (Pharmacia) was used. The homogeneity of the received β-LG preparation was analyzed by express electrophoresis in the polyacrylamide gel plates (PAG). The preparation of general casein was isolated by repeated precipitation at the isoelectric point. The fractional composition of the casein substrate was analyzed by electrophoresis in the anode system of homogeneous PAG in the presence of urea. Quantitative treatment of electrophoregrams of the β-LG preparation was performed using the imread reading function. Determination of proteolytic activity of enzyme preparations was carried out according to the method of V. F. Selemenev [6]. In the course of the research, it was determined, that for the research of proteolysis under conditions of identical total proteolytic activity, the concentration of neutral protease should be increased by 1.02 times, papain – by 4.2 times, trypsin – by 2.8 times, pancreatin – by 2.12 times as compared to chymotrypsin. As a result, it has been shown that the use of β-lactoglobulininstead of serum albumin in spectrophotometric determinations allows obtaining more accurate values of the concentrations of whey protein and proteolytic products. In determining the ratio of enzyme : substrate it is advisable to take into account the general proteolytic activity of various enzyme preparations in comparative studies of whey proteins proteolysis with various enzyme preparations. These will simplify the methodology and reduce the time for objective evaluation of enzymatic preparations for proteolysis of milk whey proteins. In some cases, considering the specificity of proteases it could increase the yield of biologically active peptides.

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“…Для аналізу гідролізатів концентрату КСБ використовували розроблений нами метод експрес-електрофорезу на пластинках однорідного ПАГ. Експрес-електрофорез проводили на апараті типу Стадієра (Yukalo et al, 2019). Аналіз складу білків казеїнового комплексу проводили в вертикальних пластинках однорідного ПАГ за наявності сечо-вини (Yukalo et al, 2018).…”

Section: матеріал і методи дослідженьunclassified

Technology of low allergenic milk with whey proteins hydrolysate

Yukalo¹,

Datsyshyn²

2019

SMLNUVMBF

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In recent years, there has been a steady increase in the number of various allergic diseases in children and adults. Clinical manifestations of allergic reactions can be observed almost from infancy, which is often associated with nutrition specificity. It is proved that one of the strongest milk allergens are the main whey fractions β-lactoglobulin and α-lactalbumin. One way to reduce allergies is to remove or completely replace whey proteins. Another way to reduce allergenicity is to use whey protein hydrolysates. In most cases, hydrolysates are obtained using cheap active proteolytic preparations. They usually have wide specificity, and the hydrolysates formed by them include short peptides with low allergenicity. Numerous biologically active peptides which have a positive effect on the organism are either lost or the possibility of their formation is reduced in such cases. A valuable source of such biologically active peptides is whey protein-precursors. Therefore, the purpose of the research is to develop a technology of low-allergenic milk with the preservation of natural biologically active peptides from whey proteins. The concentrate of natural casein was obtained in the result of the «milk-pectin-water» system dividing for creating a low-allergenic product. The fractional composition of the casein complex and milk whey proteins was analyzed by polyacrylamide gel electrophoresis. Whey protein concentrate was used as the substrate to obtain the hydrolysate. Proteolysis was performed with pancreatin at 37 °C and pH 7.9. The composition of the obtained hydrolysate was analyzed by gel filtration on Sephadex G-25. The peptides and polypeptides composition of hydrolysate was characterizated with the help of express electrophoresis. The technology of the proposed dairy product includes addition to a liquid concentrate of natural casein the whey protein hydrolysate obtained in physiological conditions. The results of electrophoretic and chromatographic researches indicate about the absence of main proteins allergens from milk whey in the product. This allows recommending it for the nutrition of people allergic to whey proteins.

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Electrophoretic system for express analysis of whey protein fractions

Cited by 9 publications

References 15 publications

Comparison of products of whey proteins concentrate proteolysis, obtained by different proteolytic preparations

Comparison of products of whey proteins concentrate proteolysis, obtained by different proteolytic preparations

Improvement of the Method of Comparative Study of Milk Whey Proteins Enzymatic Hydrolysis

Technology of low allergenic milk with whey proteins hydrolysate

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