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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Rasheed, Faiza Newson, William R. Plivelic, Tomás S. Kuktaite, Ramune Hedenqvist, Mikael S. Gällstedt, Mikael Johansson, Eva |
| Description | Author Affiliation: Rasheed F ( Department of Plant Breeding, The Swedish University of Agricultural Sciences, SE-230 53, Box 101, Alnarp, Sweden. Electronic address: Faiza.Rasheed@slu.se.); Newson WR ( Department of Plant Breeding, The Swedish University of Agricultural Sciences, SE-230 53, Box 101, Alnarp, Sweden.); Plivelic TS ( MAX IV Laboratory, Lund University, Box 118, SE-221 00 Lund, Sweden.); Kuktaite R ( Department of Plant Breeding, The Swedish University of Agricultural Sciences, SE-230 53, Box 101, Alnarp, Sweden.); Hedenqvist MS ( KTH Royal Institute of Technology, School of Chemical Science and Engineering, Fibre and Polymer Technology, SE-10044 Stockholm, Sweden.); Gällstedt M ( Innventia, Box 5604, SE-11486 Stockholm, Sweden.); Johansson E ( Department of Plant Breeding, The Swedish University of Agricultural Sciences, SE-230 53, Box 101, Alnarp, Sweden.) |
| Abstract | 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 Å lattice parameter, and other not previously observed structural entities having a characteristic distance of 50 Å. Proteins in gliadin-NH4OH-SA films were highly polymerized, with increased amount of disulfide crosslinks and ß-sheets, causing improved strength and stiffness. Glutenin and WG proteins with NH4OH-SA showed extensive aggregation and an increase in ß-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 ß-sheets and disulfide crosslinks are the major reasons of high strength and stiffness in wheat protein based films. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 79 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Gliadin Chemistry Glutens Membranes, Artificial Nanostructures Triticum Ammonium Hydroxide Disulfides Isolation & Purification Polymerization Protein Aggregates Protein Structure, Secondary Salicylic Acid Sodium Hydroxide Tensile Strength Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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