Wheat gluten structure

The ability of a degradable plastic to decay depends on the structure of its polymer chain. Biodegradable plastics are often manufactured from natural polymers, such as cornstarch and wheat gluten. Micro-organisms in the soil can break down these natural polymers. Ideally, a biodegradable plastic would break down completely into carbon dioxide, water, and biomass within six months, just like a natural material. 

Blanch, E.W., Kasarda, D.D., Hecht, L., Nielsen, K., Barron, L.D. 2003. New insight into the solution structures of wheat gluten proteins from Raman optical activity. Biochemistry 42 5665-5673. 

Structure of Wheat Gluten in Relation to Functionality in Breadmaking... 

Lysinoalanine formation in casein, lactalbumin, and wheat gluten was measured at 65°C at various pH s for 3 hours. Factors that control the extent of formation of the unnatural amino acid lysinoalanine during food processing and thus the degree of crosslinking in structurally different proteins are discussed. 

It is also important to remember that wheat gluten and dough are complex materials, consisting not only of protein and water, but also starch-, lipid-, water- and salt-soluble proteins and smaller carbohydrates, and so on. The properties of these materials and their interactions with the gluten proteins are poorly understood but can be expected to also influence the viscoelastic properties. The challenge therefore is to understand gluten structure at the molecular level and how this structure interacts... 

VPGVP, which tends to form a type II P turn with proline in position 2 (Fig. 2-24) is present in long tandem repeats e.g., (VPGVG). These extensible regions alternate with short a helices which are crosslinked to other chains. Similar structures are present in silks (Box 2-B) and in proteins of wheat gluten. ... 

The German chemist Karl Heinrich Ritthausen (1826-1912) first identified glutamic acid in wheat gluten in 1866, and its chemical structure was first identified in 1890 by the German chemist Wolff. Then in 1908, the Japanese chemist Kikunae Ikeda (1864-1936) discovered the flavor-enhancing properties of glutamic acid. He found in seaweed broth a... 

Cereals are an important protein source and are processed into bread, pasta and noodles, breakfast cereals, and fermented drink. For all these applications the quality is determined, to a greater or lesser extent, by the gluten proteins which account for about half of the total grain nitrogen. There are also opportunities to develop novel uses for cereal proteins in both the food and nonfood indns-tries. It is important to study the wheat gluten proteins, particularly the deamidated SWP (soluble wheat protein) in relation to their structure and function. 

Shewry, PR., Halford, N.G., Field, J.M., and Tatham, A.S. The structure and functionality of wheat gluten proteins. Proceedings of the 38th Australian Cereal Chemistry Conference, Sydney, NSW, Murray, L. ed.. Royal Australian Chemical Institute, Melbourne, VIC, Australia, 1989. 

Tatham, A.S., Shewry, PR., and Belton, PS. Structural studies of cereal prolamines, including wheat gluten. In Pomeranz, Y. (Ed.), Advances in Cereal Science and Technology, American Association of Cereal Chemists, St Paul, MN, 1990. 

By varying reaction condititnis, the optimum extent of esterification was obtained for each kind of proteins. Table 1 shows the highest esterification values obtained from an experimental design. Sunflower proteins underwent esterification in a larger extent than wheat gluten proteins. Only 25 % of the carboxyl groups of wheat gluten could be esterified with this experimental procedure. The different structure of proteins may account for this difference. 

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