A pulsed low-resolution NMR study of water binding to milk proteins

Pulsed low-resolution NMR was used to study water binding to the milk proteins: casein, albumin and y-globulin. The non-exponentiality of the spin-echo decay curves of water was exploited to determine the water mobility as well as the abundance of bound and free water in different samples, obtained by adding progressive amounts of water to 1 g of dry protein. The results obtained are discussed in relation to those obtained for the hydration mechanism of powdered milk.