Formation of milk protein–pectin conjugates with improved emulsifying properties by controlled dry heating

Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation

“…The results suggest that the open-chain, random-coil structure of sodium caseinate facilitates its Maillard modification with sugars of different molar mass and spatial structure. The formation of casein/glucose (Brands, Wedzicha, & van Boekel, 2002;Oliver et al, 2006a), casein/lactose (Scaloni et al, 2002), casein/pectin (Al-Hakkak & Kavale, 2002;Einhorn-Stoll et al, 2005) and casein/ dextran (Dickinson & Izgi, 1996;Fechner et al, 2007) Maillard products with molar masses of P 2 Â 10 5 g/mol was confirmed in literature. Varying amounts of saccharides of up to 4 mol lactose (Scaloni et al, 2002) or 0.1 mol dextran (Aminlari et al, 2005) were detected to be bound per mole of casein, yielding heterogeneous reaction products (Ajandouz, Desseaux, Tazi, & Puigserver, 2008;Oliver et al, 2006b).…”

Emulsifying properties of maillard conjugates produced from sodium caseinate and locust bean gum

“…The formation of conjugates was confirmed by the increase of the b*-value (Table 2), as observed by others authors (O'Regan and Mulvihill, 2009;Einhorn-Stoll et al, 2005). The b*-values of these materials are an indicator of the yellow color resulting from the Maillard-reaction (Einhorn-Stoll et al, 2005).…”

“…The b*-values of these materials are an indicator of the yellow color resulting from the Maillard-reaction (Einhorn-Stoll et al, 2005). The increase of the b*-values was verified mainly after 24 hours of incubation ( Table 2).…”

Improved heat stability of protein solutions and O/W emulsions upon dry heat treatment of whey protein isolate in the presence of low-methoxyl pectin

“…The functional properties and structure of proteins can change due to heat treatment. Loss of solubility, structural unfolding, and heat induced aggregation, are some of the consequences from the changed structure of proteins due to heat (Einhorn-Stoll, Ulbrich, Sever, & Kunzek, 2005). Thus, the loss of solubility can be used as an indicator of protein stability against heat.…”