Title: Impact of redox agents on the extractability of gluten proteins during bread making
Authors: Lagrain, Bert ×
Thewissen, Bert
Brijs, Kristof
Delcour, Jan #
Issue Date: Jun-2007
Publisher: American Chemical Society, Books and Journals Division
Series Title: Journal of Agricultural and Food Chemistry vol:55 issue:13 pages:5320-5325
Abstract: The gluten proteins gliadin and glutenin are important for dough and bread characteristics. In the present work, redox agents were used to impact gluten properties and to study gliadin-glutenin interactions in bread making. In control bread making, mixing increased the extractability of glutenin. The level of SDS-extractable glutenin decreased during fermentation and then further in the oven. The levels of extractable alpha- and gamma-gliadin also decreased during bread baking due to gliadin-glutenin polymerization. Neither oxidizing nor reducing agents had an impact on glutenin extractabilities after mixing. The redox additives did not affect omega-gliadin extractabilities during bread making due to their lack of cysteine residues. Potassium iodate (0.82-2.47 mumol/g of protein) and potassium bromate (1.07-3.17 mumol/g of protein) increased both alpha- and gamma-gliadin extractabilities during baking. Increasing concentrations of glutathione (1.15-3.45 mumol/g of protein) decreased levels of extractable alpha- and gamma-gliadins during baking. The work not only demonstrated that, during baking, glutenin and gliadin polymerize through heat-induced sulfhydryl-disulfide exchange reactions, but also demonstrated for the first time that oxidizing agents, besides their effect on dough rheology and hence bread volume, hinder gliadin-glutenin linking during baking, while glutathione increases the degree of covalent gliadin to glutenin linking. Keywords: Bread making; wheat gluten; gliadin-glutenin interaction; protein extractability.
ISSN: 0021-8561
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

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