Identification of Microphases in Mixed α- and ω-Gliadin Protein Films Investigated by Atomic Force Microscopy

• Published in: Journal of agricultural and food chemistry 1999-12, Vol.47 (12), p.5093-5099
• Main Authors: McMaster, Terence J, Miles, Mervyn J, Wannerberger, Lars, Eliasson, Ann-Charlotte, Shewry, Peter R, Tatham, Arthur S
• Format: Article
• Language: English
• Subjects: Applied sciences; Biological and medical sciences; Cereal and baking product industries; Exact sciences and technology; Food industries; Fundamental and applied biological sciences. Psychology; Gliadin - chemistry; Microscopy, Atomic Force; Natural polymers; Physicochemistry of polymers; Proteins
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf9904057

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. Keywords: Gliadin; atomic force microscopy; AFM; phase angle; protein film