Structure and rheological properties of acid-induced egg white protein gels

M. Weijers, F. van de Velde, A. Stijnman, A. van de Pijpekamp, R.W. Visschers

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71 Citations (Scopus)

Abstract

This study compares the rheological properties of acid-induced gels prepared of industrial spray-dried egg white proteins (EWP) with the acid-induced gels prepared of ovalbumin (OA) and whey protein isolate (WPI). Also we aimed to form transparent gels of EWP by means of the cold-gelation process. We showed that it was not possible to prepare cold-set gels because ovotransferrin (OT), present in EWP, was found to interfere with fibril formation. Therefore, we developed a new purification method in which first Or was selectively denatured by a heating step, subsequently precipitated by acidification and removed by centrifugation. Finally, the supernatant was desalted by ultra filtration. This resulted in a preheated EWP preparation, which mainly contains OA (> 80%). By removing OT using this new preheat procedure transparent gels were obtained after acid-induced gelation. Fracture properties of various EWP preparations were determined and compared with those of acid-induced gels of OA and WPI. Gels formed from different EWP preparations were weak (fracture stress 1-15 kPa, fracture strain 0.3-0.7), and the networks consisted of thin strands with hardly any additional disulphide bonds formed during the gelation step. In conclusion, the microstructure of the aggregates formed in the first step of the cold-gelation process and the amount of additional disulphide bonds formed during the second step appeared to be the determining factors contributing to the hardness and deformability of acid-induced gels of egg white proteins.
Original languageEnglish
Pages (from-to)146-159
JournalFood Hydrocolloids
Volume20
Issue number2-3
DOIs
Publication statusPublished - 2006

Keywords

  • heat-induced aggregation
  • induced gelation
  • beta-lactoglobulin
  • functional-properties
  • light-scattering
  • denatured whey
  • disulfide bond
  • ionic-strength
  • ovalbumin
  • lysozyme

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