Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-a-lactalbumin

Research output: Contribution to journalArticleAcademicpeer-review

15 Citations (Scopus)

Abstract

In this study, we explore the effect of peroxidase-catalyzed cross-linking on the molecular conformation of apo-a-lactalbumin (apo-a-LA) and the resulting changes in protein surface hydrophobicity. In studying conformational changes, we distinguish between early stages of the reaction (“partial cross-linking”), in which only protein oligomers (106 Da > Mw = 104 Da) are formed, and a later stage (“full cross-linking”), in which larger protein particles (Mw = 106 Da) are formed. Partial cross-linking induces a moderate loss of a-helical content. Surprisingly, further cross-linking leads to a partial return of a-helices that are lost upon early cross-linking. At the same time, for partially and fully cross-linked apo-a-LA, almost all tertiary structure is lost. The protein surface hydrophobicity first increases for partial cross-linking, but then decreases again at full cross-linking. Our results highlight the subtle changes in protein conformation and surface hydrophobicity of apo-a-LA upon peroxidase-catalyzed cross-linking.
Original languageEnglish
Pages (from-to)9345-9352
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number38
DOIs
Publication statusPublished - 2014

Keywords

  • secondary structure analyses
  • high hydrostatic-pressure
  • microbial transglutaminase
  • horseradish-peroxidase
  • circular-dichroism
  • whey proteins
  • beta-lactoglobulin
  • maillard reaction
  • oxygen radicals
  • dairy-products

Fingerprint Dive into the research topics of 'Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-a-lactalbumin'. Together they form a unique fingerprint.

  • Cite this