Skip to main content
SLU publication database (SLUpub)

Research article2013Peer reviewedOpen access

Crosslinks in wheat gluten films with hexagonal close-packed protein structures

Rombouts, Ine; Lagrain, Bert; Delcour, Jan A.; Türe, Hasan; Hedenqvist, Mikael S.; Johansson, Eva; Kuktaite, Ramune


Wheat gluten/glycerol (WGG) films were extruded with aqueous ammonia/salicylic acid or urea to investigate the reactions contributing to their hexagonal close-packed protein structures and material properties. The addition of aqueous ammonia and salicylic acid increased the pH, which, in turn, increased the level of intermolecular disulfide and lanthionine cross-links in the WGG films. Increased protein cross-linking reactions resulted in higher material strength and tensile modulus. These cross-linking reactions and the resulting material properties were similar for WGG films with 7.5% and 10% aqueous ammonia. Added urea into WGG film partially degraded into cyanate and ammonium. Cyanate subsequently reacted with lysine and cysteine to epsilon-carbamyllysine and S-carbamylcysteine, respectively. Even though these reactions resulted in a more alkaline reaction environment, hereby favoring disulfide bond formation and decreasing protein extractability, they also prevented the involvement of cysteine and lysine in protein cross-linking. The alkylation of these reactive amino acids, together with the plasticizing effect of urea, led to lower material strength and elastic modulus with increasing levels of urea. (C) 2013 Published by Elsevier B.V.


Wheat gluten; Hexagonal close-packed structure; Biofilms; Urea; Homocitrulline; S-carbamylcysteine

Published in

Industrial Crops and Products
2013, Volume: 51, pages: 229-235