Hostname: page-component-848d4c4894-wzw2p Total loading time: 0 Render date: 2024-05-05T07:41:31.058Z Has data issue: false hasContentIssue false

Denaturation of selected bioactive whey proteins during pasteurization and their ability to modulate milk immunogenicity

Published online by Cambridge University Press:  10 December 2020

Dimuthu Bogahawaththa*
Affiliation:
Advanced Food Systems Research Unit, Institute of Sustainable Industries & Liveable Cities and College of Health and Biomedicine, Victoria University, Werribee Campus, Victoria3030, Australia
Todor Vasiljevic
Affiliation:
Advanced Food Systems Research Unit, Institute of Sustainable Industries & Liveable Cities and College of Health and Biomedicine, Victoria University, Werribee Campus, Victoria3030, Australia
*
Author for correspondence: Dimuthu Bogahawaththa, Email: dimuthu.hewabogahawaththage@live.vu.edu.au

Abstract

This research communication relates to the hypothesis that the consumption of raw or unprocessed cow's milk contributes to lowered prevalence of allergies. Thermal pasteurization of bovine milk can result in denaturation of minor whey proteins and loss of their bioactivity. Denaturation of bovine serum albumin (BSA), immunoglobulin G (IgG) and lactoferrin (LF) in skim milk was studied under different temperature (72, 75 or 78°C) and time (0–300 s) combinations. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) results revealed that denaturation of all 3 proteins occurred at 72°C and progressed with increase in temperature and holding time. About 59% of LF and 12% of IgG denatured under high-temperature short-time (72°C/ 15 s) pasteurization, while BSA was least impacted. To assess modulation of milk immunogenicity, secretion of selected T helper (Th)-type cytokines by human peripheral blood mononuclear cells (PBMCs) was studied in vitro in response to different concentrations of BSA (0.4–1.0 mg/ml) and IgG (0.8–1.6 mg/ml) in unheated skim milk. Addition of IgG at 1.6 mg/ml induced a prominent Th1-skewed cytokine profile that may not trigger a Th2-skewed allergic reaction. BSA did not appear to modulate milk immunogenicity to any significant extent.

Type
Research Article
Copyright
Copyright © The Author(s), 2020. Published by Cambridge University Press on behalf of Hannah Dairy Research Foundation

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abbring, S, Hols, G, Garssen, J and Van Esch, BC (2019) Raw cow's milk consumption and allergic diseases – the potential role of bioactive whey proteins. European Journal of Pharmacology 843, 5565.CrossRefGoogle ScholarPubMed
Anema, SG (2017) A comparison of the kinetics of the thermal denaturation of the immunoglobulins in caprine and bovine skim milk samples. International Dairy Journal 65, 14.CrossRefGoogle Scholar
Bogahawaththa, D, Chandrapala, J and Vasiljevic, T (2017 a) Modulation of milk immunogenicity by thermal processing. International Dairy Journal 69, 2332.CrossRefGoogle Scholar
Bogahawaththa, D, Chandrapala, J and Vasiljevic, T (2017 b) Thermal denaturation of bovine immunoglobulin G and its association with other whey proteins. Food Hydrocolloids 72, 350357.CrossRefGoogle Scholar
Bogahawaththa, D, Ashraf, R, Chandrapala, J, Donkor, O and Vasiljevic, T (2018 a) In vitro immunogenicity of various native and thermally processed bovine milk proteins and their mixtures. Journal of Dairy Science 101, 87268736.CrossRefGoogle ScholarPubMed
Bogahawaththa, D, Buckow, R, Chandrapala, J and Vasiljevic, T (2018 b) Comparison between thermal pasteurization and high pressure processing of bovine skim milk in relation to denaturation and immunogenicity of native milk proteins. Innovative Food Science & Emerging Technologies 47, 301308.CrossRefGoogle Scholar
Brick, T, Ege, M, Boeren, S, Böck, A, Von Mutius, E, Vervoort, J and Hettinga, K (2017) Effect of processing intensity on immunologically active bovine milk serum proteins. Nutrients 9, 963.CrossRefGoogle ScholarPubMed
Lluis, A, Depner, M, Gaugler, B, Saas, P, Casaca, VI, Raedler, D, Michel, S, Tost, J, Liu, J and Genuneit, J (2014) Increased regulatory T-cell numbers are associated with farm milk exposure and lower atopic sensitization and asthma in childhood. Journal of Allergy and Clinical Immunology 133, 551559, e510.CrossRefGoogle ScholarPubMed
Patel, HA, Singh, H, Anema, SG and Creamer, LK (2006) Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk. Journal of Agricultural and Food Chemistry 54, 34093420.CrossRefGoogle ScholarPubMed
Sozańska, B (2019) Raw cow's milk and its protective effect on allergies and asthma. Nutrients 11, 469.CrossRefGoogle ScholarPubMed
van Neerven, R and Savelkoul, HF (2019) The two faces of cow's milk and allergy: induction of cow's milk allergy vs. prevention of asthma. Multidisciplinary Digital Publishing Institute.CrossRefGoogle Scholar
van Neerven, RJ, Knol, EF, Heck, JM and Savelkoul, HF (2012) Which factors in raw cow's milk contribute to protection against allergies? Journal of Allergy and Clinical Immunology 130, 853858.CrossRefGoogle ScholarPubMed
Vocca, I, Canani, RB, Camarca, A, Ruotolo, S, Nocerino, R, Radano, G, Del Mastro, A, Troncone, R and Gianfrani, C (2011) Peripheral blood immune response elicited by beta-lactoglobulin in childhood cow's milk allergy. Pediatric Research 70, 549554.CrossRefGoogle ScholarPubMed
Wijayanti, HB, Bansal, N and Deeth, HC (2014) Stability of whey proteins during thermal processing: a review. Comprehensive Reviews in Food Science and Food Safety 13, 12351251.CrossRefGoogle Scholar
Supplementary material: PDF

Bogahawaththa and Vasiljevic supplementary material

Figure S1

Download Bogahawaththa and Vasiljevic supplementary material(PDF)
PDF 146.6 KB