Formation and stability of fibers obtained by cold gelation of pea protein isolate aggregates in a hydrodynamic spinning process - Archive ouverte HAL
Article Dans Une Revue Food Hydrocolloids Année : 2023

Formation and stability of fibers obtained by cold gelation of pea protein isolate aggregates in a hydrodynamic spinning process

Résumé

Using plant protein sources in the formulation of food products is an important option to reduce the overall carbon footprint of the human diet. However, the ability to convert plant proteins into functional ingredients can hamper their use by the food industry. Our objective was to assemble pea protein isolate (PPI) aggregates into edible fibers. They were obtained by co-injection of a suspension of PPI aggregates with a solution of calcium chloride by means of physico-chemical bonds, i.e. in the absence of thermal treatment or chemical reaction. As soon as specific hydrodynamic conditions were met, homogeneous fibers of few hundreds µm diameter and few cm length were obtained. Small angle X-ray scattering showed that the building blocks of these fibers were dense aggregates of 400 nm radius. Calcium and PPI concentrations required for the processing of fibers were roughly given by the sol-gel state diagram of PPI aggregates. Compared to their dairy protein based equivalent, PPI fibers were obtained with a low mass fraction of protein (3% w/w) and were stable regardless of the concentration of calcium chloride used. We concluded that the robustness of the hydrodynamic spinning process was attributed to the strong reactivity of PPI aggregates with calcium ions and the low tendency of PPI gels to syneresis.
Fichier principal
Vignette du fichier
main.pdf (897.3 Ko) Télécharger le fichier
Origine Fichiers produits par l'(les) auteur(s)
Licence

Dates et versions

hal-04144969 , version 1 (28-06-2023)

Licence

Identifiants

Citer

Alice Vilotte, Hugues Bodiguel, Deniz Gunes, Christophe Schmitt, Denis Roux, et al.. Formation and stability of fibers obtained by cold gelation of pea protein isolate aggregates in a hydrodynamic spinning process. Food Hydrocolloids, 2023, 145, pp.108999. ⟨10.1016/j.foodhyd.2023.108999⟩. ⟨hal-04144969⟩

Collections

UGA CNRS LRP ANR
59 Consultations
124 Téléchargements

Altmetric

Partager

More