The ability to store energy in pea protein gels is set by network dimensions smaller than 50nm

Claire Darizu Munialo, Erik van der Linden, Harmen H.J. de Jongh

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)


The objective of this study was to identify which length scales set the ability to elastically store energy in pea protein network structures. Various network structures were obtained from pea proteins by varying the pH and salt conditions during gel formation. The coarseness of the network structure was visualized by the use of confocal laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) and ranked from least coarse to most coarse networks. Least coarse networks were formed at a pH away from the isoelectric point (IEP) of pea proteins, and at a low ionic strength, whereas more coarse networks were formed at pH values close to the IEP and at a high ionic strength during gel formation. Mechanical deformation properties of the gels such as elastically stored (recoverable) energy, Young's moduli (stiffness of gels), fracture stress (gel strength), and fracture strain (brittleness of the gels) were measured by the use of a texture analyzer and correlated to the coarseness of the networks structure. The influence of coarseness on the ability of the networks to elastically store energy was observed for length scales below 50. nm. The findings show that elastically stored energy of pea protein gels can be modulated via the creation of different network structures below 50. nm length scales. The results from this study contribute to a better understanding of the dimensions that set the ability to elastically storage in pea protein gels. If the ability of pea proteins to store energy can be understood, products can be better tailored for consumers. © 2014 Elsevier Ltd.
Original languageEnglish
Pages (from-to)482-491
Number of pages10
JournalFood Research International
Early online date2 Aug 2014
Publication statusPublished - Oct 2014


  • Coarseness
  • Gel formation
  • Network structure
  • Pea proteins
  • Recoverable energy


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