Author
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Bietz, Jerold |
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Lookhart, George |
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Submitted to: Cereal Foods World
Publication Type: Review Article Publication Acceptance Date: 4/16/1996 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Gluten, the storage protein of wheat endosperm, has long been recognized as having unique and valuable properties. Many studies have shown that gluten consists mainly of two protein subclasses, gliadin and glutenin. Each of these is a complex mixture of several protein types with unusual structures. These proteins interact, in the kernel and upon subsequent processing, through disulfide and noncovalent bonds to form complex gluten polymers. Upon rehydration and mixing, gluten orients and further associates into a unique viscoelastic network. These properties explain gluten's critical importance in breadmaking: the protein network expands to retain gas generated during fermentation and stabilizes upon heating into a light, porous structure. A major industry exists to isolate functional gluten. "Vital" gluten is used primarily in foods, but has many other possible industrial uses because of its elastic, viscous, adhesive, film-forming, and thermosetting properties. Native or modified gluten can be used in films, plastics, adhesives, graft polymers, and many other products. Most nonfood applications seem little used, however, mostly because of competition from petrochemical-based alternatives. Today, interest in such new uses is again growing, for many reasons. Gluten is abundant, renewable, domestically available, easily isolated, low in cost, "natural", and biodegradable. Further research on gluten's applications, and more fundamental information about its properties, are necessary to enhance gluten's industrial utilization, benefitting everyone from producer to consumer. |
