Abstract
Pure and mixed films of α- and ω-gliadins were studied by tapping mode atomic force microscopy (AFM). The technique was sensitive to the chemistry of the surface properties of the films, allowing imaging of the mixed gliadin phases at different ratios. In addition to the study of the phases at the micrometer level, higher resolution images allowed visualization of the protein films at the molecular level. These studies may have relevance to the formation of phases in developing protein bodies in grain, where gliadins and glutenins are deposited together. It has been assumed that the protein bodies consist of a random network of proteins; these studies indicate that microphases could be present in protein bodies. The technique provides novel methods for studying mixed biopolymer systems.
Original language | English |
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Pages (from-to) | 5093-5099 |
Number of pages | 7 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 47 |
Issue number | 12 |
DOIs | |
Publication status | Published - Dec 1999 |
Externally published | Yes |
Keywords
- AFM
- Atomic force microscopy
- Gliadin
- Phase angle
- Protein film