Disulphide bond formation in food protein aggregation and gelation

R.W. Visschers, H.H.J. de Jongh

Research output: Contribution to journalArticleAcademicpeer-review

149 Citations (Scopus)


In this short review we discuss the role of cysteine residues and cystine bridges for the functional aggregation of food proteins. We evaluate how formation and cleavage of disulphide bonds proceeds at a molecular level, and how inter- and intramolecular disulfide bonds can be detected and modified. The differences between heat-, high-pressure-, and denaturant-induced unfolding and aggregation are discussed. The effect of disulphide bonding between aggregates of proteins and protein mixtures on the functional macroscopic properties of space filling networks in protein gels is briefly presented
Original languageEnglish
Pages (from-to)75-80
JournalBiotechnology Advances
Issue number1
Publication statusPublished - 2005


  • beta-lactoglobulin
  • egg-white
  • denaturation
  • ovalbumin
  • heat
  • gels


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