a drop of coacervates
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Protein coacervates with extremely high viscosity!

Two or more proteins with opposite electric charges can co-assemble and form a separate dense phase called coacervates. Knowing the fundamental properties of this phase can help understanding the internal structure of coacervates and coacervation mechanisms and could also generate innovative applications

Part of Rima Soussi Hachfi’s PhD focused on in-depth characterization of the rheological properties of coacervates formed between two globular protein, β-Lactoglobulin (β-Lg) and Lactoferrin (Lf) at 20°C.

We demonstrated that:

  • β-lg/Lf coacervates exhibit viscoelastic properties, with essentially a liquid-like behavior,
  • β-lg/Lf coacervates showed an extremely high viscosity, 2500 times higher than that of individual proteins at the same concentration,
  • a thixotropic behavior is evidenced, proving a reversible de-structuring of the assembly between the 2 proteins.
viscosity curve

Structural reversibility: the dynamic viscosity of β-lg/Lf coacervates showed a high hysteresis. After shearing, the initial viscosity was fully recovered by the end of the downward step

 

 

 

 

These results open new perspectives for the use of coacervates as ingredients or texturing agents in food matrices at rather low concentrations. Before using functional properties of  coacervate in food, work is in progress to study how temperature and/or ionic strength could modulate these properties. 

Read more

Croguennec T., Miranda-Tavares G., Bouhallab S. (2017). Heteroprotein complex coacervation: A generic process. Advances in Colloid and Interface Science, 239, 115-126.

Soussi Hachfi R., Famelart M.H., Rousseau R., Hamon P., Bouhallab S. (2022).  Rheological characterization of β-lactoglobulin/lactoferrin complex coacervates. LWT - Food Science and Technology 163, 113577.

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Date de modification : 26 janvier 2023 | Date de création : 12 décembre 2022 | Rédaction : MH Famelart