Physicochemical studies of caroubin: A gluten-like protein

Yulan Wang, Peter S. Belton*, Helene Bridon, Elisabeth Garanger, Nikolaus Wellner, Mary L. Parker, Alex Grant, Pierre Feillet, Tim R. Noel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)

Abstract

It has been reported that caroubin, a protein mixture obtained from carob seeds, has rheological properties similar to those of gluten. Comparative studies of the effects of hydration and temperature on caroubin and gluten were carried out with the aid of NMR, FTIR, scanning electron microscopy, and differential scanning calorimetry techniques. The results show that caroubin has a more ordered structure than gluten and that hydration has little effect on its secondary structure when compared to gluten. Caroubin is more easily accessible to water than gluten, suggesting that caroubin is more hydrophilic in nature. On hydration, caroubin, like gluten, forms fibrillar structures and sheets.

Original languageEnglish
Pages (from-to)3414-3419
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume49
Issue number7
DOIs
Publication statusPublished - 2001
Externally publishedYes

ASJC Scopus Subject Areas

  • General Chemistry
  • General Agricultural and Biological Sciences

Keywords

  • Caroubin
  • DSC
  • Electron microscopy
  • FTIR
  • Gluten
  • NMR

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