Skip to Main content Skip to Navigation
Journal articles

Combined effects of ionic strength and enzymatic pre-treatment in thermal gelation of peanut proteins extracts

Abstract : Peanut proteins are mostly composed of arachins and conarachins, globular proteins that can form gels under thermal denaturation or enzymatic treatment. We explore here how ionic strength (0.5 M or 0.8 M) and gelation process (a thermal treatment preceded or not by an enzymatic pre-treatment) affect peanut protein gel properties. Gel formation and final properties are characterized by rheology, and gel structure by confocal microscopy. We show that the ionic strength imposed during protein extraction determines the arachins/conarachins ratio, and that conarachins-rich samples give stronger gels, which is attributed to their higher content in free thiol groups and lysine residues. The gel storage modulus exhibited a power-law dependence with the protein concentration, which exponent depends on the gelation process. Rheological results, together with confocal microscopy imaging, showed that an enzymatic pre-treatment results in denser structures.
Document type :
Journal articles
Complete list of metadatas

Cited literature [38 references]  Display  Hide  Download

https://hal-agroparistech.archives-ouvertes.fr/hal-02952722
Contributor : Benoît Basse <>
Submitted on : Tuesday, September 29, 2020 - 3:21:38 PM
Last modification on : Wednesday, October 14, 2020 - 4:21:42 AM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : 2020-12-09

Please log in to resquest access to the document

Licence


Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives 4.0 International License

Identifiers

Citation

Benoît Basse, Véronique Bosc, Jean-Marc Saiter, Monique Chan-Huot, Jean-Pierre Dupas, et al.. Combined effects of ionic strength and enzymatic pre-treatment in thermal gelation of peanut proteins extracts. Food Research International, Elsevier, 2020, 137, pp.109362. ⟨10.1016/j.foodres.2020.109362⟩. ⟨hal-02952722⟩

Share

Metrics

Record views

30