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Resume - Grâce a une connaissance precise de leurs structures primaire et tridimensionnelle, on sait mieux comprendre les proprietes fonctionnelles des 5 proteines majeures du lait (caseines as1' ~ et K, ~-Iactoglobuline et a-lactalbumine) et mieux les utiliser dans des produits carnes, des pâtisseries, des sauces et cremes glacees. On a pu ainsi relier aux proprietes de surface, des proprietes dynamiques telles que la flexibilite, ou hydrodynamiques telles que la viscosite intrinseque. En melange, des interactions s'etablissent entre proteines et molecules proteiques ou non proteiques qui modifient le comportement fonctionnel des proteines du lait, ce qui permet d'expliquer: - l'amelioration des proprietes tensioactives par purification : caseine ~ > caseine as1 = caseine K > caseine entiere, ~-Iactoglobuline > a-lactalbumine> lactoserum; - l'amelioration du pouvoir gelifiant des carraghenanes par la caseine K (laits gelifies); - l'effet des surfactants sur les proprietes tensioactives des proteines dans les emulsions foisonnees (cremes, glaces). Les proprietes fonctionnelles du lactoserum peuvent etre ameliorees en modifiant le milieu (electredialyse, ultrafiltration, echange d'ions), en denaturant par voie thermique a pH neutre ou acide, en batch ou par des traitements en continu (echangeurs a surface raclee, cuisson-extrusion). Les traitements chimiques restent des methodes de laboratoire utilisees pour expliquer les relations structure-fonction. Quant a la proteolyse, elle ne peut s'appliquer que pour ameliorer la solubilite. propriete fonctionnelle / proteine / lait / lactoserum / gel/emulsion / mousse 5ummary - Recent knowledge on the functional properties of milk proteins and related products. A study of the physica-chemical and functianal properties of milk prateins in isolation is more straightfarward than in camplex food systems such as meat, baked praducts, sauces or lee cream. Caseinates are used for their binding and emulsifying properties, whilst whey pro teins are mastly used for their gelling and faaming praperties. A knawledge of the primary and 3-dimensianal structures of the 5 main milk proteins (asr, 13-, and x-ceseins, f3-lactaglabulin and a-Iactalbumin), enables a better understanding of the functianal behaviaur of pure campanents on their awn or in mixtures. Surface properties may be related ta dynamic or hydrodynamic behaviaur such as f1exibility or intrinsic viscasity. These in turn depend on the extent of unfalding. Surface-acting praperties are enhanced by f3-casein, an amphipathic malecule which is naturally unfalded at pH 7, while a rigid 3dimensianal structure is required for f3-lactaglabulin ta stabilise emulsians and faams. The behaviaur of milk pro teins is changed when they are mixed with ather protein or non-protein malecules (polysaccharides, lipids, surfactants). Different interactions accur, altering the behaviaur of milk pro teins by competition or synergistic effects. In the present study, the fallawing situations are cansidered: - the surface-active properties of pure proteins in the fallawing arder: f3-casein > as! casein = K: casein > whale caseinate, {3-lactaglabulin > a-Iactalbumin > whey; - the impravement in the gel/ing capacity of carrageenans and galactamannans by the presence of x-cesein;

Connaissances nouvelles sur les propriétés fonctionnelles des protéines du lait et des dérivés