Heteroprotein complex coacervation: mechanisms & potential applications
2017
Chapeau, Anne Laure | Hamon, Pascaline | Croguennec, Thomas | Bouhallab, Said
The application of fundamental physicochemical concepts for rational design of functional assemblies from food proteins constitutes a response to the growing trend toward the development of new and innovative food products and also an opportunity to generate new protein-based supramolecular structures with new applications. Given their omnipresence in food systems, proteins are the focus of many attempts for their use as building blocks forsuch supramolecular structures. Controlled self- co-assembly of proteins can generate a variety of supramolecular structures that vary in shape, size and density (fibrils, spherulites,nanotubes, etc). For instance, well-defined microspheres called coacervates can be formed by control mixing of oppositely charged proteins. The aim of our research is i- to understand the mechanisms behind such spontaneous complex coacervation process from molecular interaction to micro-scale organization, ii- to test the efficiency of formed heteroproteincomplex coacervates (HPCC) for encapsulation of nutrients and bioactives. In this presentation, we will summarize the results obtained on several binary protein systems and will show that co-assembly of proteins into coacervates is a generic process with however several specificities [1]. The ability of HPCC to encapsulate small molecules such as Vitamin B9 and ANS was also demonstrated [2]. Hence, HPCC constitute new structured biopolymerbased delivery systems for the elaboration of natural and functional foods.
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