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Title of article REDUCING ALLERGENICITY BY BIOCATALYTIC CONVERSION OF WHEY PROTEIN USING ASPERGILLUS ORYX SEASON
Authors

Podlegaeva T., Cand.Sci.(Eng.), Associate Professor of the Department of Сatering Тechnology and Оrganization, Kemerovo State University, tpodlegaeva@yandex.ru

Kozlova O., Cand.Sci.(Eng.), Associate Professor of the Department of Bionanotechnology, Kemerovo State University, ms.okvk@mail.ru

Kriger O., Dr.Sci.(Eng.), Professor of the Institute of Living Systems, Immanuel Kant Baltic Federal University, olgakriger58@mail.ru

Poturaeva N., Kemerovo State University, 020678@mail.ru

Section
Year 2020 Issue 3 UDC 637:344
DOI 10.21603/2074-9414-2020-3-415-424
Abstract Introduction. More than 170 foods can cause allergic reactions in humans. The list of potential allergens includes a lot of dairy products. To reduce the antigenic properties, dairy raw materials can be subjected to thermal treatment. However, prolonged heating reduces the nutritional value, solubility, and digestibility of the final product. Biocatalytic conversion is considered a more effective way to reduce the allergenicity of milk proteins and dairy products.
Study objects and methods. The research featured the bioconversion process of milk whey using an enzyme complex of fungal protease and exo-peptidase produced by Aspergillus oryx season. The research provided an optimal concentration of the enzyme preparation, as well as temperature parameters, reaction time, and the effect of pH on the intensity of the process. The experiment involved standard research methods. The mass fraction of free amino acids was determined by distribution chromatography after protein hydrolysis.
Results and discussion. The research helped to define the effect of enzymatic treatment time and the pH on the hydrolysis of serum proteins after bioconversion. The indicator of the degree of hydrolysis and its time was affected by the concentration of the introduced enzyme preparation. The maximum degree of hydrolysis was observed at pH = 4.0 ± 0.1 with an enzyme-substrate ratio of 1:700. The degree of hydrolysis in samples with an enzyme-substrate ratio of 1:1,000 and 1:700 was almost the same. Therefore, the enzymesubstrate ratio of 1:1,000 proved more effective. The concentration of many important amino acids increased, which indicated the hydrolytic cleavage of the protein. The research made it possible to determine the most effective parameters of the process of biocatalytic conversion of whey enzyme by the protease complex Aspergillus oryx season: the ratio of enzyme-substrate – 1:1,000, time – 60–90 min, pH – 4.0 ± 0.1, temperature – 35–45°C.
Conclusion. The whey samples subjected to biocatalytic conversion by an enzyme complex of the genus Aspergillus oryx season showed the presence of low-molecular peptides in its composition, which indicated the effectiveness of the process and reducing the allergenicity of the whey protein.
Keywords Bioconversion, dairy products, antigens, exopeptidase, protease, chromatogram, demineralization, proteolysis, amino acids, protein
Artice information Received March 25, 2020
Accepted July 24, 2020
Available online October 8, 2020
For citation Podlegaeva TV, Kozlova OV, Kriger OV, Poturaeva NL. Reducing Allergenicity by Biocatalytic Conversion of Whey Protein Using Aspergillus oryx season. Food Processing: Techniques and Technology. 2020;50(3):415–424. (In Russ.). DOI: https://doi.org/10.21603/2074-9414-2020-3-415-424.
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References
  1. Luss LV. Food allergens and food additives: the role in the development of food allergy and food intolerance. Effective Pharmacotherapy. 2014;(33):12–19. (In Russ.).
  2. Muraro A, Werfel T, Hoffmann-Sommergruber K, Roberts G, Beyer K, Bindslev-Jensen C, et al. EAACI food allergy and anaphylaxis guidelines: diagnosis and management of food allergy. Allergy: European Journal of Allergy and Clinical Immunology. 2014;69(8):1008–1025. DOI: https://doi.org/10.1111/all.12429.
  3. Kharitonov VD, Budrik VG, Agarkova EJ, Botina SG, Berezkina KA, Kruchinin AG, et al. Perspective directions of struggle with allergy. Food Processing: Techniques and Technology. 2012;27(4):3–6. (In Russ.).
  4. Huang S-M, Chen K-N, Chen Y-P, Hong W-S, Chen M-J. Immunomodulatory properties of the milk whey products obtained by enzymatic and microbial hydrolysis. International Journal of Food Science and Technology. 2010;45(5):1061–1067. DOI: https://doi.org/10.1111/j.1365-2621.2010.02239.x.
  5. Gauthier SF, Pouliot Y, Saint-Sauveur D. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. International Dairy Journal. 2006;16(11):1315–1323. DOI: https://doi.org/10.1016/j.idairyj.2006.06.014.
  6. Ajonu R, Doran G, Torley P, Agboola S. Screening of whey protein isolate hydrolysates for their dual functionality: Influence of pre-treatment and enzyme specificity. Food Chemistry. 2013;136(3–4):1435–1443. DOI: https://doi.org/10.1016/j. foodchem.2012.09.053.
  7. Prosekov A, Babich O, Dyshlyuk L, Noskova S, Suhih S. A study of polyfunctional properties of biologically active peptides. Research Journal of Pharmaceutical, Biological and Chemical Sciences. 2016;7(4):2391–2400.
  8. Osmolovskiy AA, Popova EA, Kreyer VG, Baranova NA, Egorov NS. Fibrinolytic and collagenolytic activity of extracellular proteinases of the strains of micromycetes Aspergillus ochraceus L-1 and Aspergillus ustus 1. Moscow University Biological Sciences Bulletin. 2016;71(1):62–66. DOI: https://doi.org/10.3103/S0096392516010053.
  9. Milenteva IS, Dyshlyuk LS, Prosekov AYu, Babich OO, Shishin MV. Deriving biologically active peptides and study of their qualities. Science Evolution. 2016;1(2):20–33. DOI: https://doi.org/10.21603/2500-1418-2016-1-2-20-33.
  10. Prosekov A, Babich O, Asukhikh S, Noskova S, Dushlyuk L. The proteolytic activity research of the lactic acid microorganisms of different taxonomic groups. World Applied Sciences Journal. 2013;23(10):1284–1290.
  11. Prosekov A, Babich O, Kriger O, Ivanova S, Pavsky V, Sukhikh S, et al. Functional properties of the enzyme-modified protein from oat bran. Food Bioscience. 2018;24:46–49. DOI: https://doi.org/10.1016/j.fbio.2018.05.003.
  12. Kunda PB, Benavente F, Catala-Clariana S, Giménez E, Barbosa J, Sanz-Nebot V. Identification of bioactive peptides in a functional yoghurt by micro liquid chromatography time-of-flight mass spectrometry assisted by retention time prediction. Journal of Chromatography A. 2012;1229:121–128. DOI: https://doi.org/10.1016/j.chroma.2011.12.093.
  13. Baldasso C, Marczak LDF, Tessaro IC. A comparison of different electrodes solutions on demineralization of permeate whey. Separation Science and Technology. 2014;49(2):179–185.
  14. Poturaeva NL, Kriger OV, Podlegaeva TV, Drozdova TM. Demineralization of whey for the production of pro-ducts with low allergenicity. Storage and Processing of Farm Products. 2013;(8):24–26. (In Russ.).
  15. Villeneuve W, Perreault V, Chevallier P, Mikhaylin S, Bazinet L. Use of cation-coated filtration membranes for demineralization by electrodialysis. Separation and Purification Technology. 2019;218:70–80. DOI: https://doi.org/10.1016/j. seppur.2019.02.032.
  16. Estévez N, Fuciños P, Sobrosa AC, Pastrana L, Pérez N, Luisa Rúa M. Modeling the angiotensin-converting enzyme inhibitory activity of peptide mixtures obtained from cheese whey hydrolysates using concentration-response curves. Biotechnology Progress. 2012;28(5):1197–1206. DOI: https://doi.org/10.1002/btpr.1587.
  17. Biscola V, Tulini FL, Choiset Y, Rabesona H, Ivanova I, Chobert J-M, et al. Proteolytic activity of Enterococcus faecalis VB63F for reduction of allergenicity of bovine milk proteins. Journal of Dairy Science. 2016;99(7):5144–5154. DOI: https://doi. org/10.3168/jds.2016-11036.
  18. Prosekov AYu, Kiseleva TF. Foresight of food industry development up to 2030: challenges and solutions. Smart Innovation, Systems and Technologies. 2019;139:349–356. DOI: https://doi.org/10.1007/978-3-030-18553-4_44.
  19. Prosekov AYu, Babich OO, Bespomestnykh KV. Identification of industrially important lactic acid bacteria in foodstuffs. Foods and Raw Materials. 2013;1(2):42–45. DOI: https://doi.org/10.12737/2053.