Effect of Fermentation on the Milk Allergen Proteins During Yogurt-making

Year 2021, , 94 - 103, 30.12.2021

Özgür Tarhan , Ahmet Kaya , Mustafa Gözler

https://doi.org/10.47137/uujes.1032643

Cited By: 2

Abstract

Cow milk and dairy products have a great significance in human nutrition but may lead to concerns due to milk protein allergy. Reduction or elimination of cow milk allergy is mainly achieved by the destruction of allergenic epitopes in the molecular structure of relevant proteins via various treatments during dairy processing. Yogurt is one of the most consumed fermented dairy foods. The purpose of this study was to investigate the effect of fermentation on the protein content and molecular structure of milk during yogurt production. Protein profiles and structural features of the dairy samples collected at various steps of yogurt manufacturing were analyzed using electrophoresis and spectroscopy. Fermentation after pasteurization treatment remarkably altered the content and structure of allergen proteins through unfolding, denaturation, and aggregation. This might suggest a correlation with the modified allergenicity of milk proteins in the end product. Immunological assays ongoing will help a better understanding of the allergenicity of yogurt products analyzed in this study.

Keywords

yogurt, fermentation, milk allergens, protein, electrophoresis, FTIR

Supporting Institution

Uşak Üniversitesi BAP Birimi

Project Number

UBAP06/TP044/2017

Thanks

This work has been financially supported by Uşak University Scientific Research Projects Department with the projects (UBAP06/TP044/2017). The authors would like to thank Dr. Senem Şanlı and Dr. Eyüp Yıldırır for their valuable helps in Capillary electrophoresis and FTIR studies, respectively.

References

• De Jong N, Visser S, Olieman C. Determination of milk proteins by capillary electrophoresis. Journal of Chromatography A. 1993;652(1):207-13.
• Caira S, Pizzano R, Picariello G, Pinto G, Cuollo M, Chianese L, et al. Allergenicity of milk proteins. Milk protein. 2012;4.
• El-Agamy E. The challenge of cow milk protein allergy. Small Ruminant Research. 2007;68(1-2):64-72.
• Bogahawaththa D, Chandrapala J, Vasiljevic T. Modulation of milk immunogenicity by thermal processing. International dairy journal. 2017;69:23-32.
• Wal J-M. Cow's milk proteins/allergens. Annals of Allergy, Asthma & Immunology. 2002;89(6):3-10.
• Kleber N, Krause I, Illgner S, Hinrichs J. The antigenic response of β-lactoglobulin is modulated by thermally induced aggregation. European Food Research and Technology. 2004;219(2):105-10.
• Konstantinou GN, Kim JS. Paradigm shift in the management of milk and egg allergy: baked milk and egg diet. Immunology and Allergy Clinics. 2012;32(1):151-64.
• Järvinen K-M, Chatchatee P, Bardina L, Beyer K, Sampson HA. IgE and IgG binding epitopes on α-lactalbumin and β-lactoglobulin in cow’s milk allergy. International archives of allergy and immunology. 2001;126(2):111-8.
• Villa C, Costa J, Oliveira MBP, Mafra I. Bovine milk allergens: A comprehensive review. Comprehensive Reviews in Food Science and Food Safety. 2018;17(1):137-64.
• Rahaman T, Vasiljevic T, Ramchandran L. Effect of processing on conformational changes of food proteins related to allergenicity. Trends in Food Science & Technology. 2016;49:24-34.
• Verhoeckx KC, Vissers YM, Baumert JL, Faludi R, Feys M, Flanagan S, et al. Food processing and allergenicity. Food and Chemical Toxicology. 2015;80:223-40.
• Spotti MJ, Tarhan Ö, Schaffter S, Corvalan C, Campanella OH. Whey protein gelation induced by enzymatic hydrolysis and heat treatment: Comparison of creep and recovery behavior. Food Hydrocolloids. 2017;63:696-704.
• Bu G, Luo Y, Zheng Z, Zheng H. Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate. Food and Agricultural Immunology. 2009;20(3):195-206.
• Rahaman T, Vasiljevic T, Ramchandran L. Conformational changes of β-lactoglobulin induced by shear, heat, and pH—Effects on antigenicity. Journal of dairy science. 2015;98(7):4255-65.
• Bhat MY, Dar TA, Singh LR. Casein proteins: structural and functional aspects. Milk proteins–from structure to biological properties and health aspects InTech, Rijeka. 2016:1-17.
• Xu Q, Shi J, Yao M, Jiang M, Luo Y. Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates. Food and agricultural immunology. 2016;27(3):401-13.
• Niggemann B, Von Berg A, Bollrath C, Berdel D, Schauer U, Rieger C, et al. Safety and efficacy of a new extensively hydrolyzed formula for infants with cow’s milk protein allergy. Pediatric allergy and immunology. 2008;19(4):348-54.
• Yao M, Xu Q, Luo Y, Shi J, Li Z. Study on reducing antigenic response and IgE‐binding inhibitions of four milk proteins of Lactobacillus casei 1134. Journal of the Science of Food and Agriculture. 2015;95(6):1303-12.
• Fotschki J, Szyc A, Wróblewska B. Immunoreactivity of lactic acid-treated mare's milk after simulated digestion. Journal of Dairy Research. 2015;82(1):78-85.
• Wróblewska B, Kaliszewska A. Cow’s milk proteins immunoreactivity and allergenicity in processed food. Czech Journal of Food Sciences. 2012;30(3):211-9.
• Omar A, Harbourne N, Oruna-Concha MJ. Quantification of major camel milk proteins by capillary electrophoresis. International Dairy Journal. 2016;58:31-5.
• Tarhan Ö, Kaya A. Investigation of the compositional and structural changes in the proteins of cow milk when processed to cheese. LWT. 2021;151:112102.
• Barth A. Infrared spectroscopy of proteins. Biochimica et Biophysica Acta (BBA)-Bioenergetics. 2007;1767(9):1073-101.
• Farrell Jr H, Wickham E, Unruh J, Qi P, Hoagland P. Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids. 2001;15(4-6):341-54.
• Gomaa A, Boye J. Impact of irradiation and thermal processing on the immunochemical detection of milk and egg allergens in foods. Food research international. 2015;74:275-83.
• Laemmli U. Glycine-SDS-PAGE for separation of proteins. Nature. 1970;227(5).
• Kumral A. Nutritional, chemical and microbiological changes during fermentation of tarhana formulated with different flours. Chemistry Central Journal. 2015;9(1):1-8.
• TOLU A, ALTUN I. Comparison of homemade and commercial yoghurt in Van province, Turkey. Food Science and Technology. 2021.
• Alessandri C, Sforza S, Palazzo P, Lambertini F, Paolella S, Zennaro D, et al. Tolerability of a fully maturated cheese in cow’s milk allergic children: biochemical, immunochemical, and clinical aspects. PloS one. 2012;7(7):e40945.
• Maier I, Okun VM, Pittner F, Lindner W. Changes in peptic digestibility of bovine β-lactoglobulin as a result of food processing studied by capillary electrophoresis and immunochemical methods. Journal of Chromatography B. 2006;841(1-2):160-7.
• Tarhan Ö, Tarhan E, Harsa Ş. Investigation of the structure of alpha-lactalbumin protein nanotubes using optical spectroscopy. Journal of Dairy Research. 2014;81(1):98-106.
• Niemi M, Jylhä S, Laukkanen M-L, Söderlund H, Mäkinen-Kiljunen S, Kallio JM, et al. Molecular interactions between a recombinant IgE antibody and the β-lactoglobulin allergen. Structure. 2007;15(11):1413-21.
• Matsuo H, Yokooji T, Taogoshi T. Common food allergens and their IgE-binding epitopes. Allergology International. 2015;64(4):332-43.
• Sletten GB, Holden L, Egaas E, Faeste CK. Differential influence of the degree of processing on immunogenicity following proteolysis of casein and β-lactoglobulin. Food and agricultural immunology. 2008;19(3):213-28.