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Protein insolubilization and thiol oxidation in sulfite-treated wheat gluten films during aging at various
M H Morel1, J Bonicel, V Micard
1Unité de Technologie des Céréales et des Agropolymères, ENSA.M - INRA, 2 place Viala, 34060 Montpellier Cedex 01, France. morel@ensam.inra.fr
Abstract:
Gluten films were prepared by casting an acidic and ethanolic solution of gluten previously treated with sodium sulfite. The effects of sulfitolysis on proteins were investigated by SE-HPLC and thiol/disulfide content measurements. During sulfitolysis, insoluble glutenin macropolymer was converted into its constitutive subunits. About 10% of gluten disulfide bonds were cleaved, of which three-fourths originated from interchain disulfide bonds. Oxidation of thiol groups released during sulfitolysis was followed for various temperatures (T) and relative humidities. Oxidation was shown to be a second-order rate process occurring below the glass transition temperature (T(g)) and related to T - T(g). Thiol oxidation ensured the formation of interchain bonds between specific classes of gluten proteins according to an ordered process. Intrachain bonds were also formed and through thiol/disulfide-exchange reactions were finally converted to interchain bonds. Thus, fully oxidized gluten films had more insoluble glutenin macropolymers than native gluten.
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