Effects of High and Low Molecular Weight Glutenin Subunits on Rheological Dough Properties and Breadmaking Quality of Wheat

Abstract

High molecular weight (HMW) or low molecular weight (LMW) subunits of different chemical state (reduced, reoxidized with KBrO3, or KIO3) or gliadins were added in 1% amounts to a base flour of the wheat cultivar Rektor and mixed with water. The corresponding doughs were then characterized by microscale extension tests and by microbaking tests and were compared to doughs from the base flour without additives. The maximum resistance of dough was strongly increased by HMW subunits in a reduced state and by HMW subunits reoxidized with KBrO3. A moderate increase of resistance was caused by HMW subunits reoxidized with KIO3 and by LMW subunits reoxidized with KBrO3 or KIO3. This resistance was strongly lowered by LMW subunits in a reduced state and by gliadins. The extensibility of dough was significantly increased only by gliadins and reduced HMW subunits; HMW subunits reoxidized with KBrO3 had no effect, and all other fractions had a decreasing effect. In particular, glutenin subunits reoxidized with KIO3 induced marked decrease of extensibility, resulting in bell‐shaped curve extensigrams, which are typical for plastic properties. The effect of reoxidized mixtures (2:1) of HMW and LMW subunits on maximum resistance depended on the oxidizing agent and on the conditions (reoxidation separated or together); extensibility was generally decreased. Bread volume was increased by addition of HMW subunits (reduced or reoxidized with KBrO3) and decreased by LMW subunits (reoxidized with KBrO3 or KIO3) and by a HMW‐LMW subunit mixture (reoxidized with KBrO3). The volume was strongly decreased by addition of reduced LMW subunits. A high bread volume was related to higher values for both resistance and extensibility.

Role of gluten and its components in influencing durum wheat dough properties and spaghetti cooking quality

“…According to Bekes et al 21 because glutenin subunits are part of the glutenin network, ‘addition’ of monomeric glutenin subunits to a flour provides a less realistic indication of their functional role than chemical ‘incorporation’ into the glutenin network. They developed ‘incorporation’ protocols to study these subunits in doughs and this approach has been adopted by others 15, 17, 18, 35, 40. However, others have found that there is a similarity between the effects of ‘addition’ and ‘incorporation’ of glutenin subunits on dough properties 14, 41.…”

Wet-milling properties of waxy wheat flours by two laboratory methods

“…The reasons for the reduced rate and strength of gluten agglomeration in flour-water doughs and slurries have not been fully understood. High molecular weight glutenins and glutenin macropolymer formed by the glutenin particles have been shown in the last 10 years to add strength (elasticity) to a wheat flour dough (Antes & Wieser, 2001;Bekkers, Lichtendonk, Graveland, & Plijter, 2000;Don, Lichtendonk, Plijter, & Hamer, 2003aSchropp & Weiser, 1996;Singh & MacRitchie, 2001;Southan & MacRitchie, 1999;Uthayakumaran, Stoddard, Gras, & Bekes, 2000;Veraverbeke, Verbruggen, & Delcour, 1998;Wooding, Kavale, MacRitchie, & Stoddard, 1999). However, the wet-processing quality of a wheat flour and its relationship to flour protein quality remain mostly unknown.…”

Wet-milling of wheat flour: industrial processes and small-scale test methods

“…The reasons for the various rates of the gluten aggregation in flour-water doughs and slurries are not fully understood. High-molecular weight gluten subunits (HMW-GS) and glutenin macropolymer (GMP) gel formed by the glutenin particles have been shown in the last 10 years to add strength (elasticity) to a wheat flour dough (Schropp & Wieser, 1996;Veraverbeke, Verbruggen, & Delcour, 1998;Southan & MacRitchie, 1999;Wooding, Kavale, MacRitchie, & Stoddard, 1999;Bekkers, Lichtendonk, Graveland, & Plijter, 2000;Uthayakumaran, Stoddard, Gras, & Bekes, 2000;Antes & Wieser, 2001;Singh & MacRitchie, 2001;Don, Lichtendonk, Plijter, & Hamer, 2003a, b). The aggregation rate of gluten proteins in a Batter process appears to be accelerated by the increasing level of glutenin proteins (Roels et al, 1998a, b).…”