Abstract
Beyond their nutritional value, food proteins are a versatile group of biopolymers with a considerable number of functionalities throughout their extensive structures, conformations and interaction–aggregation behaviour in solution. In the present paper, we give an overview of the induced aggregation and spontaneous reversible assembly of food proteins that lead to a diversity of supramolecular structures. After a brief description of the properties of some food proteins, the first part summarises the aggregation processes that lead to supramolecular structures with a variety of morphologies and sizes. The second part reports on the requirements that drive spontaneous assembly of oppositely charged proteins into reversible supramolecular structures. The promising new applications of these structures in food and non-food sectors are also mentioned.
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Abbreviations
- α-La:
-
α-Lactalbumin
- β-Lg:
-
β-Lactoglobulin
- BSA:
-
Bovine serum albumin
- Lf:
-
Lactoferrin
- LYS:
-
Lysozyme
- Ova:
-
Ovalbumin
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Acknowledgements
Many thanks to our collaborators: M. Nigen, D. Salvatore, P. Hamon and M.N. Madec. Part of the work performed in our laboratory was supported by INRA and by the French National Research Agency (Agence Nationale de la Recherche, grant ANR-07-PNRA-010, project LACLYS).
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Bouhallab, S., Croguennec, T. (2013). Spontaneous Assembly and Induced Aggregation of Food Proteins. In: Müller, M. (eds) Polyelectrolyte Complexes in the Dispersed and Solid State II. Advances in Polymer Science, vol 256. Springer, Berlin, Heidelberg. https://doi.org/10.1007/12_2012_201
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