Abstract
The online version contains supplementary material available at 10.1007/s11032-021-01238-9.
Highlights
Common wheat (Triticum aestivum L.; AABBDD; 2n = 6x = 42) is an unusual food crop suitable for the production of various foods because of its unique processing quality, which is related to the continuous protein network in its grains (Shewry and Halford 2002)
A mutant with six High molecular weight glutenin subunits (HMW-GSs), which were detected as distinct bands on an SDS-PAGE gel, was isolated after treating ‘Shumai 482’ seeds with 0.8% ethyl methanesulfonate (EMS)
The basic molecular unit of glutenin polymers might consist of two y-type HMW-GSs, four x-type HMW-GSs, and many LMW-GSs covalently linked by interchain disulfide bonds (Wieser 2007)
Summary
Common wheat (Triticum aestivum L.; AABBDD; 2n = 6x = 42) is an unusual food crop suitable for the production of various foods because of its unique processing quality, which is related to the continuous protein network in its grains (Shewry and Halford 2002). As a ‘backbone’ for interactions with other glutenin subunits and gliadins, HMW-GSs are among the most important determinants of end-use quality, with key effects on dough strength and elasticity (Shewry et al 2003a; Wieser 2007). The number and distribution of Cys residues are important features of HMW-GSs because disulfide bonds between these residues determine the polymeric structure and conformation of proteins, which affect the dough strength (Shewry et al 1992, 2003a)
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