The Gluten Complex Studied by Urea Denaturation and Red-ox Titration

  • N. Guerrieri
  • V. Lavelli
  • P. Cerletti
Conference paper

Summary

Gluten surface sites with low affinity for ANS, La low hydrophobicity, were more labile to urea than those with high hydrophobicity and disappeared nearly completely when urea was above 6 M. The surface of the gluten complex was only moderately affected by complete reduction, in which case less hydrophobic regions were more labile.

Keywords

Urea Titration Disulfide Tryptophan Macromolecule 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • N. Guerrieri
    • 1
  • V. Lavelli
    • 1
  • P. Cerletti
    • 1
  1. 1.DISMA, Dipartimento di Scienze Molecolari AgroalimentariUniversità degli Studi di MilanoMilanItaly

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