|BEKES, FERENC - Fbfd Pty Ltd
|D'OVIDIO, RENATO - University Of Tuscia
Submitted to: Journal of Cereal Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/30/2011
Publication Date: 11/1/2011
Citation: Anderson, O.D., Bekes, F., D'Ovidio, R. 2011. Effects of specific domains of high-molecular-weight glutenin subunits’ on dough properties by an in vitro assay. Journal of Cereal Science. 54:280-287.
Interpretive Summary: The wheat high-molecular-weight glutenin subunits (HMW-GS) are proteins essential for the formation of doughs from wheat flour/water mixtures. The HMW-GS form long polymers that confer the visco-elastic nature to wheat doughs, and are thus important both for wheat utilization and the US farm sector. This report used native and modified HMW-GS to supplement dough micro-mixing and extension experiments to study the effects of specific portions of the HMW-GS on dough properties. Results indicate a synergistic effects between HMW-GS is localized to a specific portion of the subunit. Other experiments show that the size of the HMW-GS has an effect on dough properties.
Technical Abstract: An in vitro system for incorporating bacterially produced high-molecular-weight glutenin subunits (HMW-GS) into doughs was used to study the effects of specific domains of the HMW-GS. Synergistic effects of incorporating into doughs both the Dx5 and Dy10 subunits are localized to the N-terminal domains. All single and pair wise combinations of original subunits and hybrid subunits with their N-terminal domains exchanged between Dx5 and Dy10 finds three classes of respondents: the greatest response is when the N-termini of both Dx5 and Dy10 are present, followed by presence of the Dx5 N-terminus alone, and the least response by the presence of the Dy10 N-terminus alone. In addition, studies of Dx5 variants possessing repetitive domains of different length and composition finds evidence that the length of the HMW-GS repetitive domain is important for dough properties and that the exact composition of the repeat domain has a detectible, though lesser contribution. Finally, in this experimental system, the Glu-D1 x- and y-subunits function in the mixing experiments as if they were a fused dimer, although the exact molecular basis of the effect is not known.