Increasing the shelf-life of sensitive substances and targeting the release of nutritional/bioactive molecules are among the great challenges for the food industry. The development of food products with embedded encapsulation devices used to reach these objectives, constitutes a growing market. Milk proteins are biopolymers that are chemically and structurally versatile and are well adapted to several encapsulation purposes. Therefore, in this paper, the strategies, techniques, advantages and trends associated with the use of milk proteins as encapsulating device are reviewed. Special attention is given to the novel potential of reversibly co-assembled protein structures as encapsulating devices.

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Proteins exhibit a rich diversity of functional, physico-chemical and biodegradable properties which makes them appealing for various applications in the food and non-food sectors. Such properties are attributed to their ability to interact and assemble into a diversity of supramolecular structures. The present review addresses the updated research progress in the recent field of complex coacervation made from mixtures of oppositely charged proteins (i.e. heteroprotein systems). First, we describe briefly the main proteins used for heteroprotein coacervation. Then, through some selected examples, we illustrate the particularity and specificity of each heteroprotein system and the requirements that drive optimal assembly into coacervates. Finally, possible and promising applications of heteroprotein coacervates are mentioned.

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Few reports describe the effect of lactose hydrolysis on the properties of milk powder during production and storage. Hence, the aim of this study was to evaluate the effects of five different levels of enzymatic lactose hydrolysis during the production and storage of milk powder. As the lactose hydrolysis rate increased, adhesion to the drying chamber also increased, due to higher levels of particle agglomeration. Additionally, more brown powder was obtained when the lactose hydrolysis rate was increased, which in turn negatively affected rehydration ability. Using Raman spectroscopy, crystallization of the lactose residues in various samples was assessed over 6 weeks of accelerated aging at a room temperature environment with 75.5 % of air moisture.Products with 25% or greater lactose hydrolysis showed no signs of crystallization, in contrast to the non-hydrolyzed sample.