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Research article2015Peer reviewed

Macromolecular changes and nano-structural arrangements in gliadin and glutenin films upon chemical modification Relation to functionality

Rasheed, Faiza; Newson, William Roy; Plivelic, Tomas S.; Kuktaite, Ramune; Hedenqvist, Mikael S.; Gällstedt, Mikael; Johansson, Eva


Protein macromolecules adopted for biological and bio-based material functions are known to develop a structured protein network upon chemical modification. In this study, we aimed to evaluate the impact of chemical additives such as, NaOH, NH4OH and salicylic acid (SA), on the secondary and nano-structural transitions of wheat proteins. Further, the effect of chemically induced modifications in protein macromolecular structure was anticipated in relation to functional properties. The gliadin-NH4OH-SA film showed a supramolecular protein organization into hexagonal structures with 65 angstrom lattice parameter, and other not previously observed structural entities having a characteristic distance of 50 angstrom. Proteins in gliadin-NH4OH-SA films were highly polymerized, with increased amount of disulfide crosslinks and beta-sheets, causing improved strength and stiffness. Glutenin and WG proteins with NH4OH-SA showed extensive aggregation and an increase in beta-sheet content together with irreversible crosslinks. Irreversible crosslinks hindered a high order structure formation in glutenins, and this resulted in films with only moderately improved stiffness. Thus, formation of nano-hierarchical structures based on beta-sheets and disulfide crosslinks are the major reasons of high strength and stiffness in wheat protein based films. (C) 2015 Elsevier B.V. All rights reserved.


Gliadin; Glutenin; Molecular crosslinking; Hexagonal morphology

Published in

International Journal of Biological Macromolecules
2015, Volume: 79, pages: 151-159