The effect of the state of aggregation of casein (micellar or non-micellar, as milk protein concentrate [MPC] or sodium caseinate [Na-caseinate], respectively) on water sorption, plasticization, and crystallization of freeze-dried matrices containing sucrose, lactose or their blends were studied. The Guggenheim-Anderson-de Boer (GAB) equation satisfactorily fitted to the water sorption data. In most cases, sugar crystallization-studied by water sorption behavior, x-ray diffraction, and non-isothermal calorimetry-occurred significantly slower in systems containing Na-caseinate compared to MPC. The type of casein did not affect the temperature range where the glass transition (T g ) was observed. Sugar/Nacaseinate mixtures showed higher instant crystallization temperatures (up to 20°C) than sugar/MPC mixtures. X-ray diffraction showed that: (a) crystallinity increased with increasing relative vapor pressure (RVP)>44%; (b) lactose crystallized mainly as α-lactose monohydrate regardless of casein type; and (c) that sucrose crystals predominated the patterns of the sucrose/ lactose mixtures. Results suggested that the way proteins organize in space (i.e., aggregation state) affected their interactions with neighboring sugar and water molecules, which led to differences in sugar crystallization behavior.