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Communication Dans Un Congrès Année : 2015

Rheological properties of milk derived peptides in high-protein matrices

Résumé

Proteins are one intrinsic part of many food products. They can be hydrolyzed into peptides during food processes or storage. Protein hydrolysis can enhance the functional properties of the food products depending on the type of peptides produced. Most of information on peptide functional properties currently comes from dilute solutions, in which both the composition and the protein concentration are far away from food products. However, additional information is required to understand the self-assembly of proteins and peptides in complex matrices. Pools of peptides are usually not characterized and a fortiori it is difficult to determine how, and to which extent, the protein functional properties are modified due to protein hydrolysis. To answer these questions, we produced pools of peptides with defined physicochemical characteristics (size, charges and hydrophobicity) through the action of two enzymes. Sodium caseinate was hydrolysed by trypsin and Glu-C, giving three pools per enzyme, which contain peptides quantitatively and qualitatively different. Peptides were identified by high resolution tandem mass-spectrometry and their structure was determined by Fourier transform infrared spectroscopy. Controlled amount of these peptides were incorporated into high-protein matrices made of casein micelles. Some of these matrices are liquids whereas the others are gels. Then, rheological properties of matrices were studied by flow and small amplitude oscillatory measurements Advances in sequence identification and structural determination have made possible to characterize the peptides present in the hydrolysates and those that interact with casein micelles. Under our conditions, peptides with specific physicochemical and structural characteristics modified the rheological properties of matrices. This innovative approach gives new ways to establish a relationship between physicochemical, structural characteristics of peptides and their functional properties in complex matrices. This method could be enlarged to various food matrices.
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Dates et versions

hal-02743117 , version 1 (03-06-2020)

Identifiants

  • HAL Id : hal-02743117 , version 1
  • PRODINRA : 307405

Citer

Lélia Lacou, Marie-Hélène Famelart, Chantal Cauty, Irina Kolotuev, Julien Jardin, et al.. Rheological properties of milk derived peptides in high-protein matrices. The 7. International Symposium on Food Rheology and Structure - ISFRS 2015, Jun 2015, Zurich, Switzerland. ⟨hal-02743117⟩
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