C.W. Wrigley, Food Science Australia and Wheat CRC, North Ryde (Sydney), NSW 1670, Australia; F. Békés and Colin R. Cavanagh, CSIRO Plant Industry, Canberra, ACT 2600, Australia; W. Bushuk, Food Science, University of Manitoba, Winnipeg, MB R3T 2N2, Canada
Gliadin and Glutenin: The Unique Balance of Wheat Quality
Pages 447-451
DOI: https://doi.org/10.1094/9781891127519.020
ISBN: 978-1-891127-51-9
Abstract
Looking back a century or so to the late nineteenth century, we see a great contrast in knowledge about gluten composition and function as it was then, compared to our present position in the first decade of the twenty-first century. The naïve concept of two simple homogeneous proteins in balance—gliadin and glutenin—has been replaced by a view of their great complexity and heterogeneity. Nevertheless, the concept of their balance remains, with an awareness that gluten's unique rheological properties depend on the interaction of smaller monomeric gliadin proteins “lubricating” the elasticity of large glutenin polymers, ranging in size up to tens of millions in molecular weight.
The research assault on gliadin has made progress especially since the 1960s with the development of novel methods of protein fractionation with progressively greater resolving powers (Chapters 2–4). A decade or so later, the “black box” of glutenin was opened up to reveal the range of polypeptides that crosslink to make up its enormous polymers (Chapters 5–7). More recently, gene technologies have combined with recent methods of protein chemistry to provide specific details of composition, plus sequence information for both nucleotides and amino acids at the gene and polypeptide levels, respectively. Technologies of genetic manipulation now permit the tailoring of “designer” genes and proteins, providing variants of native gluten polypeptides, thereby to elucidate the significance of structural features (Chapter 12).
