Flours of four common wheat and one spelt genotypes were treated with thioredoxin-h (TR-h) in the presence of NADPH and NADP-thiore- doxin reductase to reduce intramolecular disulphide bonds in monomeric sulphur-rich prolamins. Effects on the breadmaking properties (determined by micro-baking) and gliadin's immunoreactivity (measured by Sandwich ELISA) were observed. Loaf volumes and estimated crumb of bread from TR-h-modified flours did not differ significantly from values for non-modified flours. TR-h modification significantly decreased gliadin immunoreactivity in common wheat genotypes, but only slightly decreased the reaction for spelt. These results suggest that TR-h modification may partially mitigate wheat gliadin's allergenic properties through reduction of intramolecular disulfide bonds.
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