The structure and properties of gluten: an elastic protein from wheat grain
TLDR
The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough.Abstract:
The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain. These form a continuous proteinaceous matrix in the cells of the mature dry grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough. These viscoelastic properties underpin the utilization of wheat to give bread and other processed foods. One group of gluten proteins, the HMM subunits of glutenin, is particularly important in conferring high levels of elasticity (i.e. dough strength). These proteins are present in HMM polymers that are stabilized by disulphide bonds and are considered to form the ‘elastic backbone’ of gluten. However, the glutamine–rich repetitive sequences that comprise the central parts of the HMM subunits also form extensive arrays of interchain hydrogen bonds that may contribute to the elastic properties via a ‘loop and train’ mechanism. Genetic engineering can be used to manipulate the amount and composition of the HMM subunits, leading to either increased dough strength or to more drastic changes in gluten structure and properties.read more
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EAACI Molecular Allergology User's Guide.
Paolo Maria Matricardi,Jörg Kleine-Tebbe,Hans Jürgen Hoffmann,Rudolf Valenta,Christiane Hilger,Stephanie Hofmaier,Rob C. Aalberse,Ioana Agache,Riccardo Asero,Barbara Ballmer-Weber,Domingo Barber,Kirsten Beyer,Tilo Biedermann,M. B. Bilò,Simon Blank,Barbara Bohle,Philipp P. Bosshard,Heimo Breiteneder,Helen A. Brough,Luis Caraballo,J-C Caubet,Reto Crameri,Janet M. Davies,Nikolaos Douladiris,M. Ebisawa,Philippe Eigenmann,Montserrat Fernandez-Rivas,Fatima Ferreira,Gabriele Gadermaier,Martin Glatz,Robert G. Hamilton,Thomas Hawranek,P W Hellings,Karin Hoffmann-Sommergruber,Thilo Jakob,Uta Jappe,Marek Jutel,Sandip D. Kamath,Edward F. Knol,Peter Korošec,Annette Kuehn,Gideon Lack,Gideon Lack,Andreas L. Lopata,Mika J. Mäkelä,Martine Morisset,Verena Niederberger,Anna Nowak-Wegrzyn,Nikolaos G. Papadopoulos,Elide A. Pastorello,Gabrielle Pauli,Thomas A.E. Platts-Mills,Daniela Posa,Lars K. Poulsen,Monika Raulf,Joaquín Sastre,Enrico Scala,Johannes Schmid,Peter Schmid-Grendelmeier,M. van Hage,R. van Ree,Stefan Vieths,Richard W. Weber,Magnus Wickman,Antonella Muraro,Markus Ollert +65 more
TL;DR: The European Academy of Allergy and Clinical Immunology (EAACI) Molecular Allergology User's Guide (MAUG) as mentioned in this paper provides comprehensive information on important allergens and describes the diagnostic options using component-resolved diagnosis (CRD).
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References
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Journal ArticleDOI
The relationship between HMW glutenin subunit composition and the bread‐making quality of British‐grown wheat varieties
TL;DR: In this paper, the grain proteins of 84 home-grown wheat varieties were fractionated by SDS-PAGE to determine their HMW glutenin subunit composition, and quality scores of each of the subunits were summed to create a Glu-1 quality score for each variety.
Journal ArticleDOI
High molecular weight subunits of wheat glutenin
TL;DR: The high molecular weight subunits of wheat glutenin are of considerable interest because of their relationship to breadmaking quality and how they may be assembled to form disulphide-bonded polymers that confer elasticity on wheat dough.
Journal ArticleDOI
Mini Review: On the Elasticity of Wheat Gluten
TL;DR: The role of high molecular weight subunits in protein-protein interactions in wheat gluten is discussed in this paper, with particular reference to the role of the high molecular-weight subunits.
Journal ArticleDOI
The classification and nomenclature of wheat gluten proteins: A reassessment
TL;DR: It is concluded that the classical division into gliadins and glutenins is based on a secondary characteristic, the formation of interor intra- molecular disulphide bonds, rather than on homology of the primary amino acid sequences.