Abstract
The protein aggregation mechanism in UHT milk samples stored at ambient temperature for 1, 3 and 5 months was assessed in this study. Three phases of the UHT milks were studied: supernatants, dispersed phase and sediments. The supernatants showed a great variability, suggesting the presence of a dynamic arrangement within the protein system of UHT milk, which moves towards the formation of the sediment. The application of 2D-electrophoresis (AU-PAGENR-SDS-PAGER) and mass spectrometry analyses were carried out to study the main heat-induced supramolecular protein aggregates. These aggregates were found mainly in the supernatant and their composition changed along the storage, as a consequence of the medium chemical changes, which are temperature- and pH-depended, whereas the composition of the dispersed phase and sediment denoted a hierarchical mechanism of assembling.
Similar content being viewed by others
References
Holland JW, Gupta R, Deeth HC, Alewood PF (2011) Proteomic analysis of temperature-dependent changes in stored UHT milk. J Agric Food Chem 59:1837–1846
Grewal MK, Chandrapala J, Donkor O, Apostolopoulos V, Vasiljevic T (2017) Electrophoretic characterization of protein interactions suggesting limited feasibility of accelerated shelf-life testing of ultra-high temperature milk. J Dairy Sci 100:76–88
Sakkas L, Moutafi A, Moschopoulou E, Moatsou G (2014) Assessment of heat treatment of various types of milk. Food Chem 159:293–301
Lopez C (2005) Focus on the supramolecular structure of milk fat in dairy products. Reprod Nutr Dev 45:497–511
McMahon DJ, Oommen BS (2008) Supramolecular structure of the casein micelle. J Dairy Sci 91(5):1709–1721
Bouhallab S, Croguennec T (2013) In: Martin M (ed) Advances in polymer science, 1st edn. Springer, Berlin
Deeth H, Lewis MJ (2016) In: Bond M, Singh H (eds) Milk proteins from expression to food, 3rd edn. Academic Press, London
Gaur V, Schalk J, Anema SG (2018) Sedimentation in UHT milk. I Dairy J 78:92–102
Patel A, Singh H, Anema SG, Creamer LK (2006) Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk. J Agric Food Chem 54(9):3409–3420
Chevalier F, Kelly AL (2010) Proteomic quantification of disulphide linked polymers in raw and heated bovine milk. J Agric Food Chem 58:7437–7444
Anema SG (2017) Storage stability and age gelation of reconstituted ultra-high temperature skim milk. Int Dairy J 75:56–67
Friedman M (1999) Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. J Agric Food Chem 47:1295–1319
Guyomarc'h F, Law AJR, Dalgleish DG (2003) Formation of soluble and micelle-bound protein aggregates in heated milk. J Agric Food Chem 51:4652–4660
Li Y, Dalgleish D, Corredig M (2015) Influence of heating treatment and membrane concentration on the formation of soluble aggregates. Food Res Int 76:309–316
Donato L, Guyomarc’h F (2009) Formation and properties of the whey protein/κ-casein complexes in heated skim milk—a review. Dairy Sci Technol 89:3–29
Corredig M, Dalgleish DG (1999) The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk. Int Dairy J 9:233–236
Oldfield DJ, Singh H, Taylor MW (1998) Association of β-lactoglobulin and α-lactalbumin with the casein micelles in skim milk heated in an ultra-high temperature plant. Int Dairy J 8:765–770
Donato L, Dalgleish DG (2006) Effect of the pH of heating on the qualitative and quantitative compositions of the sera of reconstituted skim milks and on the mechanisms of formation of soluble aggregates. J Agric Food Chem 54(20):7804–7811
Petrella G, Pati S, Gagliardi R, Rizzuti A, Mastrorilli P, la Gatta B, Di Luccia A (2015) Study of proteolysis in river buffalo mozzarella cheese using a proteomics approach. J Dairy Sci 98:7560–7572
Caira S, Iannelli A, Sciarrillo R, Picariello G, Renzone G, Scaloni A, Addeo P (2017) Differential representation of liver proteins in obese human subjects suggests novel biomarkers and promising targets for drug development in obesity. J Enzyme Inhib Med Chem 32(1):672–682
Lewis M, Grandison A, Lin MJ, Tsioulpas A (2011) Ionic calcium and pH as predictors of stability of milk to UHT processing. Milchwissenschaft 66(2):197–200
Anema SG (2019) Age gelation, sedimentation, and creaming in UHT milk: a review. Comp Rev Food Sci Food 18:140–166
Anema SG (2009) In: Thompson A, Boland M, Singh H (eds) Milk proteins: from expression to food, 2nd edn. Academic Press, London
Wang L, Lin J, Zhang X (2013) Hierarchical microstructures self-assembled from polymer systems. Polymer 54:3427–3442
Walstra P, Wouster JTM, Geurts TJ (2006) Dairy science and technology, 2nd edn. Taylor & Francis, Boca Raton, US
Karlsson MA, Langton M, Innings F, Malmgren B, Höjer A, Wikström M, Lundh Å (2019) Changes in stability and shelf-life of ultra-high temperature treated milk during long term storage at different temperatures. Heliyon 5(9):e02431
Faccia M, Trani A, Loizzo P, Gagliardi R, la Gatta B, Di Luccia A (2014) Detection of αs1-I casein in mozzarella fiordilatte: a possible tool to reveal the use of stored curd in cheesemaking. Food Control 42:101–108
Venkatachalam N, McMahon DJ, Savello PA (1993) Role of protein and lactose interactions in the age gelation of ultra-high temperature processed concentrated skim milk. J Dairy Sci 76(7):1882–1894
Datta N, Deeth HC (2003) Diagnosing the cause of proteolysis in UHT milk. LWT-Food Sci Technol 36(2):173–182
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Compliance with ethics requirements
This article does not contain any studies with human or animals subjects.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Rutigliano, M., Rusco, G., Picariello, G. et al. Protein aggregation mechanism in UHT milk: supramolecular evidences. Eur Food Res Technol 246, 1081–1094 (2020). https://doi.org/10.1007/s00217-020-03474-3
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00217-020-03474-3