Gluten surface sites with low affinity for ANS, i.e. low hydrophobicity, were more labile to urea than those with high hygroscopicity 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.
The gluten complex studied by urea denaturation and red-ox titration / N. Guerrieri, V. Lavelli, P. Cerletti - In: Plant proteins from european crops; food and non food applications / [a cura di] Gueguen J. e Popineau Y.. - [s.l] : Springer-Verlag, Berlin-Heidelberg (D), 1998. - ISBN 3-540-63291-3. - pp. 243-247
The gluten complex studied by urea denaturation and red-ox titration
N. GuerrieriPrimo
;V. LavelliSecondo
;P. CerlettiUltimo
1998
Abstract
Gluten surface sites with low affinity for ANS, i.e. low hydrophobicity, were more labile to urea than those with high hygroscopicity 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.
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