The aim of this study was to identify and quantify disulfide bonds in wheat gluten. After enzymatic digestion of wheat flour 14 cystine-containing peptides were identified by means of liquid chromatography - mass spectrometry with alternating electron transfer and collision induced dissociation. One of the peptides represented a “head-to-tail” cross-link between HMW subunits of glutenin, which is an integral part of many gluten models. Finally, four cystine peptides were quantified by stable isotope dilution assays at different stages of breadmaking showing that disulfide bonds of wheat gluten change during mixing and baking.
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The aim of this study was to identify and quantify disulfide bonds in wheat gluten. After enzymatic digestion of wheat flour 14 cystine-containing peptides were identified by means of liquid chromatography - mass spectrometry with alternating electron transfer and collision induced dissociation. One of the peptides represented a “head-to-tail” cross-link between HMW subunits of glutenin, which is an integral part of many gluten models. Finally, four cystine peptides were quantified by stable iso...
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