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GrainGenes Reference Report: CCM-77-193

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Reference
CCM-77-193
Title
Temperature-induced changes in the dynamic rheological behavior and size distribution of polymeric proteins for glutens from wheat near-isogenic lines differing in HMW glutenin subunit composition
Journal
Cereal Chemistry
Year
2000
Volume
77
Pages
193-201
Author
Lefebvre J
Popineau Y
Deshayes G
LAvenant L
Abstract
Summary: Viscoelasticity of hydrated gluten depends on composition of HMW gluten subunits (GS), size distribution of glutenin polymers, and protein-protein interactions. Glutens extracted from four near-isogenic lines with differing HMW-GS were analyzed. Rheological properties were studied by dynamic assay in shear. Size distribution of prolamins was determined by sequential extraction and size-exclusion HPLC. Assays performed at 20 degrees C confirmed that viscoelasticity was determined by large glutenin polymers. The abundance of large glutenin polymers depended on the HMW-GS composition of the lines. Difference of functionality linked to subunit structure was highlighted by comparing the behaviors of the 1A/1B null and 1A/1D null lines. Glutens were submitted to heating and cooling cycles, with or without an SH-blocking agent (N-ethylmaleimide [NEMI]). At 20-40 degrees C, no irreversible changes of the mechanical properties occurred. Thermal treatment affected chain mobility, and possibly H bonds, but not the chemical structure of the network. At >40 degrees C, irreversible rheological changes were observed without NEMI. Irreversibility was mainly due to chemical modifications affecting the polymer size distribution through SH-SS exchange reactions. The sensitivity of gluten to temperature depended on subunit composition
Keyword
allelic variation
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