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The PROViDE project is one of the 13 projects selected as part of the "Défi Mutations alimentaires" call for projects launched by INRA and CNRS to support new collaborations between their teams on emerging and interdisciplinary issues on food mutations.

The PROViDE project responds to a dual challenge, both food and environmental, in the area of research on food security and the demographic challenge. Indeed, a transition to a diet richer in vegetable proteins is currently recommended on a nutritional level. In addition, the extraction of proteins from by-products that are not directly consumable by humans makes it possible to better develop and preserve resources, with a beneficial impact on the environment.

The proteins that interest us in this project, rapeseed, peas, wheat, have one thing in common: they are plant storage proteins. They are accumulated during the development of the seed in order to store the amino acids necessary to restart the plant during germination. They are stored in the form of concentrated and dehydrated phases in the seeds. These plant proteins are then transformed into ingredients by washing the raw materials, isoelectric precipitation and/or ultrafiltration-diafiltration of the protein extract before drying. The proteins thus undergo a complex thermodynamic path that passes several times through highly concentrated and dehydrated phases: during the maturation of the seed, during the precipitation and membrane filtration stages and finally during the drying process. However, the concentration/dehydration stages are favourable to structural changes that have consequences on the techno-functional properties of proteins. Through the PROViDE project, we propose to study the role of dehydration on the assembly state, solubility and interfacial properties of plant storage proteins.

In the PROViDE project, we will focus on the effect of dehydration on the structure and solubility of plant proteins using a thermodynamic approach based on osmotic dehydration. The objective is to evaluate the effect of the thermodynamic dehydration path on the reversibility of observed structural changes. This fundamental thermodynamic approach will make it possible to better understand the mechanisms of assembling plant proteins under the effect of increasing concentration and, in the long term, to better reason the manufacturing processes of plant protein ingredients in order to obtain better functionalities and to better exploit these resources.

This exploratory project emerges from the complementarities of the INRA Biopolymers Interactions Assemblages (BIA) unit in Nantes and the Chemical Engineering Laboratory (LGC - CNRS UMR 5503) in Toulouse. It combines scientific skills in biochemistry and physicochemistry of plant proteins from the BIA Unit and thermodynamics of phase transitions, physicochemistry of interfaces and dynamics of material transfers from the LGC.

• Beginning of the project: April 2019
• Duration of the project : 1 year (renewable 1 time)

• Academic partners:
  • INRA – BIA
  • Laboratoire de Génie Chimique (LGC – CNRS UMR 5503, Toulouse)
• Budget: 30 k€/year
• Coordination : Adeline Boire (BIA Unit -  ISD team)
• Persons involved:
  • BIA : Denis Renard, Véronique Solé-Jamault, Joëlle Davy
  • LGC : Isaac Rodriguez Ruis, Pierre Roblin, Sébastien Teychené