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INRA
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31326 Castanet Tolosan CEDEX - France

Dernière mise à jour : Mai 2018

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Internet de l'unité STLO Science et Technologie du Lait et de l'Oeuf

STLO Research Unit

Structuring egg white proteins to modulate in vitro digestibility

ovalbumin_gels
Faced with the development of food-related chronic diseases, the scientific community concentrates on understanding the digestion process, taking into account food in all its aspects and complexity. Especially, the issue of food structure influence on nutrient bioavailability is addressed.

Thanks to egg white, as a model enabling to create, at constant composition, protein aggregates and protein gels with variable structures, we confirmed the role of protein structuration on in vitro proteolysis by gastro-intestinal enzymes. Thus, ovalbumin aggregation systematically favors its hydrolysis compared to native ovalbumin, and the aggregation conditions that favor maximum protein unfolding always lead to maximum proteolysis. Over these quantitative aspects, the nature of released peptides also varied. The structure of the aggregates might then have an impact on the accessibility of digestive enzymes to their respective cleavage sites. Similarly for egg white gels: the higher the in vitro digestion degree of proteins, the looser the gel network; the nature of peptides also varied from one gel to another. Then, these in vitro results strengthen food structure, controllable through technological processing, as a key parameter for food disintegration during digestion, and consequently, potentially for food nutritional quality.

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FiletGris

Collaborations

  • Riddet Institute, Massey University, New Zealand
  • UMR6625 IRMAR CNRS

Read more

Nyemb K, Guérin-Dubiard C, Dupont D, Jardin J, Rutherfurd SM, Nau F (2014) The extent of ovalbumin in vitro digestion and the nature of generated peptides are modulated by the morphology of protein aggregates. Food Chemistry 157:429–438. http://dx.doi.org/10.1016/j.foodchem.2014.02.048

Nyemb K, Jardin J, Causeur D, Guérin-Dubiard C, Dupont D, Rutherfurd SM, Nau F (2014) Investigating the impact of ovalbumin aggregate morphology on in vitro ovalbumin digestion using label-free quantitative peptidomics and multivariate data analysis. Food Research International 63:192–202. http://dx.doi.org/10.1016/j.foodres.2014.03.041

Nyemb K, Guérin-Dubiard C, Pézennec S, Jardin J, Briard-Bion V, Cauty C, Rutherfurd SM, Dupont D, Nau F (2016) The structural properties of egg white gels impact the extent of in vitro protein digestion and the nature of peptides generated. Food Hydrocolloids 54:315-327. http://dx.doi.org/10.1016/j.foodhyd.2015.10.011

Nyemb-Diop K, Causeur D, Jardin J, Briard-Bion V, Guérin-Dubiard C, Rutherfurd SM, Dupont D, Nau F (2016) Investigating the impact of egg white gel structure on peptide kinetics profile during in vitro digestion. Food Research International 88:302–309. http://dx.doi.org/10.1016/j.foodres.2016.01.004

Contacts

Françoise NAU, francoise.nau@agrocampus-ouest.fr, Professor

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