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For more information about the cookies we use, you can contact INRAE's Data Protection Officer by email at cil-dpo@inrae.fr or by post at :

INRAE

24, chemin de Borde Rouge -Auzeville - CS52627 31326 Castanet Tolosan cedex - France

Last update: May 2021

Protein Purification Platform (3P)

Purification and characterization of plant, animal, and recombinant proteins

This technical platform brings together expertise in the purification of proteins and antibodies directed against the components of food products and their raw materials (proteins, polysaccharides, phenolic compounds).

Thanks to its equipment and expertise, the platform offers the possibility of purifying and characterizing proteins of plant, animal, and recombinant origin within the framework of collaborations or in autonomous use for academic laboratories and private structures.

These purified proteins are used for the study of structure-function relationships, whether it be techno-functional properties or enzymatic or biological activities.

The platform also uses the Transform department's collection of antibodies dedicated to foods and their raw materials.

Different substrates are processed:

Cereal, legume, and oilseed proteins
Food proteins of animal origin (milk, egg)
Proteins with biological activities (enzymes and enzyme inhibitors).
Recombinant proteins (antibodies, allergens...)

The aim of the platform is to purify proteins from natural or heterologously expressed raw materials.

The platform develops and implements extraction and separation methods for the preparation of protein-enriched fractions up to the preparative scale (10 mg-10 g): centrifugation, ultrafiltration, low-pressure chromatography.
The platform participates in the characterization of enriched extracts and purified proteins: protein content, composition, yield, purity, conformational state, activities...
The platform has flow-force fractionation (FFF) equipment coupled to a light scattering detector that allows the characterization in size and size distribution of polymers or nano-objects (1 nm to 1 μm).