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Thermal effects on IgM-milk fat globule-mediated agglutination

Published online by Cambridge University Press:  06 December 2018

Steffen F. Hansen ,
Lotte B. Larsen  and
Lars Wiking
Steffen F. Hansen
Affiliation:
Department of Food Science, Aarhus University, AU Foulum, Blichers Alle 20, DK-8830 Tjele, Denmark
Lotte B. Larsen
Affiliation:
Department of Food Science, Aarhus University, AU Foulum, Blichers Alle 20, DK-8830 Tjele, Denmark
Lars Wiking*
Affiliation:
Department of Food Science, Aarhus University, AU Foulum, Blichers Alle 20, DK-8830 Tjele, Denmark
*
Authors for correspondence: Lars Wiking, Email: lars.wiking@food.au.dk
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Abstract

The process of agglutination causes firm cream layers in bovine milk, and a functioning agglutination mechanism is paramount to the quality of non-homogenized milks. The phenomenon is not well-described, but it is believed to occur due to interactions between immunoglobulins (Ig) and milk fat globules. For the first time, this paper demonstrates how the process of agglutination can be visualized using confocal laser scanning microscopy, rhodamine red and a fluoresceinisothiocynat-conjugated immunoglobulin M antibody. The method was used to illustrate the effect on agglutination of storage temperature and pasteurization temperature. Storage at 5 °C resulted in clearly visible agglutination which, however, was markedly reduced at 15 °C. Increasing storage temperature to 20 or 37 °C cancelled any detectable interaction between IgM and milk fat globules, whereby the occurrence of cold agglutination was documented. Increasing 20 s pasteurization temperatures from 69 °C to 71 °C and further to 73 °C lead to progressively higher inactivation of IgM and, hence, reduction of agglutination. Furthermore, 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that changes in storage temperature caused a redistribution of Ig-related proteins in milk fat globule membrane isolates. Poly-immunoglobulin G receptor was present in milk fat globule preparations stored at cold (4 °C) conditions, but absent at storage at higher temperature (25 °C). The findings provide valuable knowledge to dairy producers of non-homogenized milk in deciding the right pasteurization temperature to retain the crucial agglutination mechanism.

Keywords

Agglutinincreamingmilk fat globule membraneimmunoglobulinpasteurization
Type
Research Article
Information
Journal of Dairy Research , Volume 86 , Issue 1 , February 2019 , pp. 108 - 113
Copyright
Copyright © Hannah Dairy Research Foundation 2018 

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References

Blans, K, Hansen, MS, Sørensen, LV, Hvam, ML, Howard, KA, Möller, A, Wiking, L, Larsen, LB and Rasmussen, JT (2017) Pellet-free isolation of human and bovine milk extracellular vesicles by size-exclusion chromatography. Journal of Extracellular Vesicles 6, 1–15.Google Scholar
Caplan, Z, Melilli, C and Barbano, D (2013) Gravity separation of fat, somatic cells, and bacteria in raw and pasteurized milks. Journal of Dairy Science 96, 2011–2019.Google Scholar
Dickow, JA, Larsen, LB, Hammershøj, M and Wiking, L (2011) Cooling causes changes in the distribution of lipoprotein lipase and milk fat globule membrane proteins between the skim milk and cream phase. Journal of Dairy Science 94, 646–656.Google Scholar
Euber, JR, Brunner, JR, Nilsson, S, Mattsson, N and Singher, HO (1984) Reexamination of fat globule clustering and creaming in cow milk. Journal of Dairy Science 67, 2821–2832.Google Scholar
Fredrick, E, Walstra, P and Dewettinck, K (2009) Factors governing partial coalescence in oil-in-water emulsions. Advances in Colloid and Interface Science 153, 30–42.Google Scholar
Frenyo, VL, Butler, JE and Guidry, AJ (1986) The association of extrinsic bovine IgG1, IgG2, SIgA and IgM with the major fractions and cells of milk. Veterinary Immunology and Immunopathology 13, 239–254.Google Scholar
Geer, SR and Barbano, DM (2014) The effect of immunoglobulins and somatic cells on the gravity separation of fat, bacteria, and spores in pasteurized whole milk. Journal of Dairy Science 97, 2027–2038.Google Scholar
Heid, HW and Keenan, TW (2005) Intracellular origin and secretion of milk fat globules. European Journal of Cell Biology 84, 245–258.Google Scholar
Honkanen-Buzalski, T and Sandholm, M (1981) Association of bovine secretory immunoglobulins with milk fat globule membranes. Comparative Immunology, Microbiology & Infectious Diseases 44, 329–342.Google Scholar
Hood, L, Kronenberg, M and Hunkapiller, T (1985) T cell antigen receptors and the immunoglobulin supergene family review. Cell 40, 225–229.Google Scholar
Huppertz, T and Kelly, AL (2006) Physical chemistry of milk fat globules. In Advanced Dairy Chemistry Volume 2, pp. 184–190 (Ed. Fox, PF & Sweeney, PLH) , Boston, MA, US: Springer.Google Scholar
Huppertz, T, Kelly, AL and Fox, PF (2009) Milk lipids – composition, origin and properties. In Dairy Fats and Related Products, p. 20 (Ed. Tamime, AY) Hoboken, NJ, US: Blackwell Publishing.Google Scholar
Larsen, LB, Wedholm-Pallas, A, Lindmark-Månsson, H and Andrén, A (2010) Different proteomic profiles of sweet whey and rennet casein obtained after preparation from raw vs. heat-treated skimmed milk. Dairy Science & Technology 90, 641–656.Google Scholar
Lombardi, R, Erne, B, Lauria, G, Pareyson, D, Borgna, M, Morbin, M, Arnold, A, Czaplinski, A, Fuhr, P and Schaeren-Wiemers, N et al. (2005) IgM deposits on skin nerves in anti-myelin-associated glycoprotein neuropathy. Annals of Neurology 57, 180–187.Google Scholar
Mainer, G, Sánchez, L, Ena, JM and Calvo, M (1997) Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM. Journal of Food Science 62, 1034–1038.Google Scholar
Miyazaki, Y, Nishimoto, S, Sasaki, T and Sugahara, T (1998) Spermine enhances IgM productivity of human-human hybridoma HB4C5 cells and human peripheral blood lymphocytes. Cytotechnology 26, 111–118.Google Scholar
Payens, TAJ, Koops, J and Kerkhof Mogot, MF (1965) Adsorption of euglobulin on agglutinating milk fat globules. Biochimica et Biophysica Acta 94, 576–578.Google Scholar
Stadtmueller, BM, Huey-Tubman, KE, López, CJ, Yang, Z, Hubbell, WL and Bjorkman, PJ (2016) The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins. eLife 5, e10640. DOI: 107.554/eLife.10640.Google Scholar
Ustonol, Z and Sypien, C (1997) Heat stability of bovine milk immunoglobulins and their ability to bind Lactococci as determined by an ELISA. Journal of Food Science 62, 1218–1222.Google Scholar
Ye, A, Singh, H, Taylor, MW and Anema, SG (2004) Interactions of fat globule surface proteins during concentration of whole milk in a pilot-scale multiple-effect evaporator. Journal of Dairy Science 71, 471–479.Google Scholar