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Flour Quality and Related Molecular Characterization of High Molecular Weight Glutenin Subunit Genes from Wild Emmer Wheat Accession TD-256

Zhang, Da-Le, He, Ting-Ting, Liang, Hui-Hui, Huang, Lu-Yu, Su, Ya-Zhong, Li, Yu-Ge, Li, Suo-Ping
Journal of agricultural and food chemistry 2016 v.64 no.24 pp. 5128-5136
Triticum turgidum subsp. dicoccoides, cysteine, dough, genes, gliadin, glutenins, molecular weight, protein structure, rheological properties, wheat, wheat flour
To clarify the effect of high molecular weight glutenin subunit (HMW-GS) from wild emmer wheat on flour quality, which has the same mobility as that from common wheat, the composition and molecular characterization of HMW-GS from wild emmer wheat accession TD-256, as well as its flour quality, were intensively analyzed. It is found that the mobilities of Glu-A1 and Glu-B1 subunits from TD-256 are consistent with those of bread wheat cv. ‘XiaoYan 6’. Nevertheless, dough rheological properties of TD-256 reveal its poor flour quality. In the aspect of molecular structure from HMW-GS, only two conserved cysteine residues can be observed in the deduced protein sequence of 1Bx14* from TD-256, while most Glu-1Bx contain four conserved cysteine residues. In addition, as can be predicted from secondary structure, the quantity both of α-helixes and their amino acid residues of the subunits from TD-256 is fewer than those of common wheat. Though low molecular weight glutenin subunit (LMW-GS) and gliadin can also greatly influence flour quality, the protein structure of the HMW-GS revealed in this work can partly explain the poor flour quality of wild emmer accession TD-256.