A cysteine in the repetitive domain of a high-molecular-weight glutenin subunit interferes with the mixing properties of wheat dough

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dc.contributor.authorGao, X.
dc.contributor.authorZhang, Q.
dc.contributor.authorNewberry, M.
dc.contributor.authorChalmers, K.
dc.contributor.authorMather, D.
dc.date.issued2013
dc.description.abstractThe quality of wheat (Triticum aestivum L.) for making bread is largely due to the strength and extensibility of wheat dough, which in turn is due to the properties of polymeric glutenin. Polymeric glutenin consists of high- and low-molecular-weight glutenin protein subunits linked by disulphide bonds between cysteine residues. Glutenin subunits differ in their effects on dough mixing properties. The research presented here investigated the effect of a specific, recently discovered, glutenin subunit on dough mixing properties. This subunit, Bx7.1, is unusual in that it has a cysteine in its repetitive domain. With site-directed mutagenesis of the gene encoding Bx7.1, a guanine in the repetitive domain was replaced by an adenine, to provide a mutant gene encoding a subunit (MutBx7.1) in which the repetitive-domain cysteine was replaced by a tyrosine residue. Bx7.1, MutBx7.1 and other Bx-type glutenin subunits were heterologously expressed in Escherichia coli and purified. This made it possible to incorporate each individual subunit into wheat flour and evaluate the effect of the cysteine residue on dough properties. The Bx7.1 subunit affected dough mixing properties differently from the other subunits. These differences are due to the extra cysteine residue, which may interfere with glutenin polymerisation through cross-linkage within the Bx7.1 subunit, causing this subunit to act as a chain terminator.
dc.description.statementofresponsibilityXin Gao, Qisen Zhang, Marcus P. Newberry, Ken J. Chalmers, Diane E. Mather
dc.identifier.citationAmino Acids, 2013; 44(3):1061-1071
dc.identifier.doi10.1007/s00726-012-1441-5
dc.identifier.issn0939-4451
dc.identifier.issn1438-2199
dc.identifier.orcidChalmers, K. [0000-0002-9687-8680]
dc.identifier.orcidMather, D. [0000-0001-7506-2589]
dc.identifier.urihttp://hdl.handle.net/2440/78310
dc.language.isoen
dc.publisherSpringer-Verlag
dc.rights© Springer-Verlag Wien 2012
dc.source.urihttps://doi.org/10.1007/s00726-012-1441-5
dc.subjectTriticum
dc.subjectCysteine
dc.subjectProtein Subunits
dc.subjectSequence Alignment
dc.subjectAmino Acid Sequence
dc.subjectAmino Acid Motifs
dc.subjectMolecular Weight
dc.subjectBread
dc.subjectFlour
dc.subjectMolecular Sequence Data
dc.subjectGlutens
dc.titleA cysteine in the repetitive domain of a high-molecular-weight glutenin subunit interferes with the mixing properties of wheat dough
dc.typeJournal article
pubs.publication-statusPublished

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