1979
DOI: 10.1002/jsfa.2740300507
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Glutenin structure

Abstract: The fall in viscosity of dispersions of gluten when treated with excess of mercaptoethanol does not exhibit an initial induction period. This finding appears to rule out the idea that glutenin is highly crosslinked in a branching mode. It is compatible with a linear model in which one SS bond, not two, joins adjacent chains, or a model with low levels of branching. However, it is unnecessary to postulate branching crosslinks to explain glutenin properties in the present state of knowledge. The insoluble residu… Show more

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Cited by 63 publications
(25 citation statements)
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“…The hydrated glutenin with a molecular weight above a certain value in wheat flour dough appears to determine its extensional properties (Singh and MacRitchie 2001). Ewart (1968Ewart ( , 1972Ewart ( , 1979 has proposed the structure of the glutenin in dough for dough development as linear (unbranched) glutenin molecules built up from subunits joined by disulfide linkage and continuity of the glutenin network depends on the secondary force (noncovalent cross-links). Ewart (1990) also pointed out that when the extensional stress is applied to the dough, the viscosity of the sheeted dough depends largely on cooperating intermolecular associations between protein molecules.…”
Section: Resultsmentioning
confidence: 99%
“…The hydrated glutenin with a molecular weight above a certain value in wheat flour dough appears to determine its extensional properties (Singh and MacRitchie 2001). Ewart (1968Ewart ( , 1972Ewart ( , 1979 has proposed the structure of the glutenin in dough for dough development as linear (unbranched) glutenin molecules built up from subunits joined by disulfide linkage and continuity of the glutenin network depends on the secondary force (noncovalent cross-links). Ewart (1990) also pointed out that when the extensional stress is applied to the dough, the viscosity of the sheeted dough depends largely on cooperating intermolecular associations between protein molecules.…”
Section: Resultsmentioning
confidence: 99%
“…Also a decrease in the size of gluten aggregates, due to the reduction of disulphide bridges, could result in increased viscosity (11). Ewart (12) has reported a decrease in Time H…”
Section: Reduction With 2-mercaptoethanolmentioning
confidence: 96%
“…HMW-prolamins contain Cys located also in nonrepeated sequences and those domains present the globular a-helical secondary structures. These Cys residues participate in the formation of intermolecular -S-S-bonds, which stabilise the elastic network of protein complexes (Ewart 1979).…”
Section: Highmoiecular Weight (Hmw) Prolaminsmentioning
confidence: 99%