General background and objectives
Increasing plant protein content in human diet constitutes a world challenge to meet protein needs of the growing world population. However, the assembly properties of such proteins are poorly understood as compared to their dietary animal counterparts. This limits their use as ingredients in food matrices.
The PlAnt Protein Physics (PAPP) group will investigate the mechanisms of plant protein aggregation as well as the structure and dynamics of these aggregates. These studies will show how far the self-assembly of plant proteins can be controlled and tuned, and should help designing new functional assemblies for food applications.
Three protein models will be studied: rapeseed, pea and wheat proteins. The experimental approach will be developed in three steps: (i) purifying proteins to work on well-characterized simple systems, (ii) developing mid-throughput screening tools for phase behavior studies through the establishment of phase diagrams and (iii) coupling in situ or ex situ structural characterization tools to obtain “Structural phase diagrams”. Experimental phase diagrams will be compared to theory providing quantitative description of the protein interaction properties. These phase diagrams will also be used to generate new functional assemblies such as clusters, fibers, coacervates, gels and will provide guidelines for creating tailored food structures.
- Purification & Biochemistry of plant and recombinant proteins: BIA, Protein purification facility (V. Solé, C. Blassel)
- Micro-/Millifluidics development applied to biopolymers: BIA, Nano Team (D. Renard, M. Marquis, J. Davy)
- Biochemistry of wheat proteins & Physical-chemistry of biopolymers: IATE, Montpellier (M-H Morel, C. Sanchez)
- Soft Matter Physics applied on biopolymers: GENIAL, Paris (P. Menut)
- Biophysics: Institute, Amsterdam, Netherlands (G. Koenderink AMOL)
- Amine, C., A. Boire, A., J. Davy, M. Marquis, D. Renard. 2017. Droplets-based millifluidic for the rapid determination of biopolymers phase diagram. Food hydrocolloids, 70: 134.
- Boire, A., C. Sanchez, P.M. Lettinga, M.-H. Morel, and P. Menut. Unravelling the contrasting phase behavior of wheat gliadins: how to store storage proteins. Under review.
- Boire, A., P. Menut, M.-H. Morel, and C. Sanchez. 2015. Osmotic compression of anisotropic proteins: interaction properties and associated structures in wheat gliadin dispersions. J. Phys. Chem. B. 119: 5412–21. DOI:10.1021/acs.jpcb.5b01673
- Boire, A., P. Menut, M.-H. Morel, and C. Sanchez. 2013. Phase behaviour of a wheat protein isolate. Soft Matter. 9: 11417. DOI:10.1039/c3sm51489g