Food Science and Technology

ISSN-print: 2073-8684
ISSN-online: 2409-7004
ISO: 26324:2012
Архiви

ELECTROPHORETIC SYSTEMS FOR PREPARATIVE FRACTIONATION OF PROTEIN PRECURSORS OF BIOACTIVE PEPTIDES FROM COW’S MILK

##plugins.themes.bootstrap3.article.main##

V. Yukalo
L. Storozh
K. Datsyshyn
O. Krupa

Анотація

The article considers the possibility of obtaining purified fractions-precursors of bioactive peptides from milk proteins by the method of preparative electrophoresis. To choose an electrophoretic system, a comparative study has been carried out of four methods of electrophoresis in polyacrylamide gel that are used to analyse milk proteins (disc-electrophoresis without disaggregating agents, and disc-electrophoresis in the presence of sodium dodecylsulfate in homogeneous and gradient gel, and electrophoresis in homogeneous gel with urea). Electrophoresis of the total milk protein has shown that none of these systems allows separating effectively all protein precursors of bioactive peptides. The next stage was obtaining two main groups of milk proteins – caseins and serum proteins for electrophoretic fractionation. With the help of analytical electrophoresis, it has been established that each of the obtained groups had a typical proteins composition. Then, the proteins groups obtained were fractionated by preparative electrophoresis using the four electrophoretic systems listed above. In this case, the casein proteins that differ in the primary structure (αS1-, αS2-, β-, and ϰ-caseins) can be effectively separated by preparative electrophoresis on the basis of a homogeneous gel system in the presence of urea. The composition of this electrophoretic system was simplified. Unlike the analytical variant of a homogeneous polyacrylamide gel system, the toxic 2-mercaptoethanol was excluded, and the urea concentration was reduced. For the fractionation of serum proteins, a disc-electrophoresis without disaggregating agents can be used as a basis. It allows obtaining the main precursors of bioactive peptides from milk serum proteins: β-lactoglobulin, α-lactalbumin, serum albumin, and immunoglobulins. The protein precursors obtained by preparative electrophoresis were used to develop the biotechnology of obtaining bioactive phosphopeptides and inhibitors of the angiotensin-converting enzyme.

Ключові слова:
Для цієї мови відсутні ключові слова

##plugins.themes.bootstrap3.article.details##

Як цитувати
Yukalo, V., Storozh, L., Datsyshyn, K., & Krupa, O. (2018). ELECTROPHORETIC SYSTEMS FOR PREPARATIVE FRACTIONATION OF PROTEIN PRECURSORS OF BIOACTIVE PEPTIDES FROM COW’S MILK. Food Science and Technology, 12(2). https://doi.org/10.15673/fst.v12i2.932
Розділ
Біопроцеси, біотехнологія харчових продуктів, БАР
Біографія автора

V. Yukalo, Одеська національна академія харчових технологій

Кафедра харчової хімії, доцент

Посилання

1. Szwajkowska M, Wolanciuk A, Barłowska J, et al. Bovine milk proteins as the source of bioactive peptides influence the consumers’ immune system – a review . Animal Science Papers and Reports. 2011; 29(4):269-280.

2. Fox PF,Uniacke T, Mc Sweeney PLH, O'Mahony JA. Dairy chemistry and Biochemistry . Second Edition. New York: Springer; 2015. DOI: 10.1007/978-3-319-14892-2.

3. Iukalo AV, Datsyshyn KYe., Yukalo VG. Bioaktyvni peptydy proteiniv syrovatky moloka koriv (Bos Taurus). Biotechnologia Acta. 2013; 6: 49-61.http://dx.doi.org/10.3168/jds.S0022-0302(04)73319-6.

4. Altamann K., Wutlkowski A, Klempt M, et al. Generation and identification of anti-inflammatory peptides from bovine β-casein using enzyme preparations from cod and hog. Journal of the Science of Food and Agriculture. 2016; 96(3): 868-877.DOI: 10.1002/jsfa.7159

5. Myronovskij S, Negrych N, Nehrych T, et al.Isolation and characterization of peptides from blood serum of patients with multiple sclerosis. Studia Biologica.2015; 9(2):51-58.

6. Holt C, Carver J.A, Ecroyd H, Thorn DC, Caseins and the casein micelle : Their biological functions, structures and behavior in foods. J. Dairy Sci. 2013; 96(10): 6127-6146.http://dx.doi.org/ 10.3168/jds.2013-6831

7. Park YW. Bioactive components in milk and dairy products. Boston: Wiley-Blackwell; 2009.

8. Corredig M. Dairy-derived ingredients. Food and nutraceutical uses. USA: CRC Press; 2009.

9. Iukalo AV, Storozh LA, Yukalo VG. Proteiny kazeinovoho kompleksu moloka koriv (Bos Taurus) yak poperednyky biolohichno aktyvnykh peptydiv . Biotekhnolohiia. 2012; 5(4): 21-33.

10. McSweeney PLH, O’Mahony JA. Advanced Dairy Chemistry. Proteins: Applied Aspects. Fouth Edition. New York: Springer; 2016. DOI: 10.1007/978-1-4939-2800-2.

11. Chandan RC, Kilara A. Dairy Ingredients for Food Processing . USA: Wiley-Blackwell; 2011.

12. Holland B, Rahimi Yazdi S, Ion Titapiccolo G, Corredig M. Separation and quantification of caseins and casein macropeptide using ion-exchange chromatography. J. Dairy Sci. 2010; 93(3): 893-900 doi: 10.3168/jds.2009-2820.

13. Yukalo V. Obtaining of casein protein complex from cow milk. NutraCos. 2005; 5: 17-19.

14. Bonnaillie L, Tomasula P. Fractionation of Whey Protein Isolate with Supercritical Carbon Dioxide to Produce Enriched α-lactalbumin and β-lactoglobulin.Food Ingredients.Journal of Agricultural and Food Chemistry. 2012; 60: 5257-5266.DOI: 10.1021/jf3011036.

15. Konrad G, Klenschmidt T. A new method for isolation of native α-lactalbumin from sweet whey. International Dairy Journal. 2008;18(1): 47-54.

16. Lozano J, Giraldo G, Romero C. An improved method for isolation of β-lactoglobulin. International Dairy Journal. 2008; 18(1): 55-63. DOI: 10.1016/j.idairyj.2007.05.003

17. Farrell H.M, Jimenez-Flores R, Bleck GT, et al.Nomenclature of the proteins of cows’ milk—sixth revision. Journal of Dairy Science. 2004; 87(6): 1641-1674.DOI:10.3168/jds.S0022-0302(04)73319-6.

18. Yukalo VG, Datsyshyn KYe. Dekstranovi heli dlia ekskliuzyvnoi khromatohrafii proteiniv syrovatky moloka. Naukovyi visnyk LNUVMB imeni S.Z. Gzhytskoho. 2018; 20(85): 3-8. doi: 10.15421/nvlvet8501.

19. Yukalo A, Yukalo V, Shynkaryk M. Electrophoresis separation of the Milk Protein. Proceedings of the International Conference on Bio and Food Electrotechnologies 22-23 October 2009. Compiegne: France; 2009: 227–231.

20. Osterman LA. Metody issledovaniya belkov i nukleinovykh kislot: Elektroforez i ultratsentrifugirovaniye (prakticheskoye posobiye). M.: Nauka; 1981.

21. Hasimoto K, Sato K, Nakamura Y, Ohtsuki K. Development of a Large-Scale (50 L) Apparatus for Ampholyte-free Isoelectric Focusing (Autofocusing) of Peptides in Enzymatic Hydrolysates of Food Proteins. Journal of Agricultural and Food Chemistry. 2005; 53(10): 3801-3806. DOI:10.1021/jf047967x

Найчастіше прочитані статті того самого автора (ів)