In: Paraf A, Damodaran S (eds) Food proteins and their application. J Agric Food Chem 45:3459–3464ĭamodaran S (1997) Protein-stabilized foams and emulsions. Food Hydrocoll 20:415–422ĭalgleish DG, Senaratne V, Francois S (1997) Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. Marcel Dekker, New York, pp 1–44ĭalgleish DG (2006) Food emulsions-their structures and structure-forming properties. ![]() In: Friberg SE, Larsson K, Sjöblom J (eds) Food emulsions. Trends Food Sci Technol 8:1–6ĭalgleish DG (2004) Food emulsions: their structures and properties. Marcel Dekker, New York, pp 287–325ĭalgleish DG (1997) Adsorption of protein and the stability of emulsions. In: Sjöblom J (ed) Emulsions and emulsion stability. Food Res Int 29:541–547ĭalgleish DG (1996b) Food emulsions. ![]() Royal Society of Chemistry, Cambridge, pp 23–34ĭalgleish DG (1996a) Conformations and structures of milk proteins adsorbed to oil–water interfaces. ![]() In: Lorient D, Dickinson E (eds) Food macromolecules and colloids. Colloids Surf B 1:1–8ĭalgleish DG (1995) Structures and properties of adsorbed layers in emulsions containing milk proteins. Colloids Surf 46:141–155ĭalgleish DG (1993) The sizes and conformations of the proteins in adsorbed layers of individual caseins on latices and in oil-in-water interfaces. J Colloid Interface Sci 302:32–39ĭalgleish DG (1990) The conformations of proteins on solid/water interfaces-caseins and phosvitin on polystyrene latices. Innovat Food Sci Emerg Technol 8:1–23Ĭroguennec T, Renault A, Bouhallab S, Pezennec S (2006) Interfacial and foaming properties of sulfydryl-modified bovine β-lactoglobulin. J Colloid Interface Sci 161:38–42Ĭonsidine T, Patel HA, Anema SG, Singh H, Creamer LK (2007) Interactions of milk proteins during heat and high hydrostatic pressure treatments-a review. Springer, Berlinīrooksbank DV, Leaver J, Horne DS (1993) Adsorption of milk-proteins to phosphatidyl-glycerol and phosphatidyl choline liposomes. Asian Aust J Anim Sci 18:282–295īikerman JJ (1973) Foams. Curr Opin Colloid Interface Sci 11:164–170īauer E, Jakob S, Mosenthin R (2005) Principles of physiology of lipid digestion. Cell Mol Life Sci 62:2531–2539īansil R, Turner BS (2006) Mucin structure, aggregation, physiological functions and biomedical applications. Elsevier Applied Science, London, pp 221–255īaker EN, Baker HM (2005) Molecular structure, binding properties and dynamics of lactoferrin. In: Stainsby G, Dickinson E (eds) Advances in food emulsions and foams. J Agric Food Chem 46:84–90Īnderson M, Brooker BE (1988) Dairy foams. J Agric Food Chem 44:3631–3636Īgboola SO, Singh H, Munro PA, Dalgleish DG, Singh AM (1998) Destabilization of oil-in-water emulsions formed using highly hydrolyzed whey proteins. 1 Kinetics of protein breakdown and storage stability of the emulsions. KeywordsĪgnboola SO, Dalgleish DG (1996) Enzymatic hydrolysis of milk proteins used for emulsion formation. Highlights on the behaviour of milk-protein-stabilised emulsions after consumption that have recently attracted a great deal of research interest are discussed briefly. This chapter provides an overview of the emulsifying and foaming properties of milk proteins, focusing on the adsorption of milk proteins at oil–water and air–water interfaces with emphasis on the preferential adsorption among milk proteins and the stability of milk-protein-based emulsions and foams. These functional properties of milk proteins are exploited in the manufacture of dairy and other products, such as recombined milk, cream, butter, yoghurt, ice cream, cream liqueurs, dressings, mayonnaise, sauces and desserts. ![]() Milk proteins facilitate the formation and stabilisation of oil droplets in emulsions or of air bubbles in foams in formulated foods. Milk proteins are known to possess a wide range of functional properties, such as emulsification, thickening, gelling and foaming.
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