Dispersibility of wheat proteins in aqueous urea solutions--a new parameter to evaluate breadmaking potentialities of wheat flours.
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In this work is presented the first attempt to develop a fluorescence assay for detection of traces of gluten in food by utilizing the recombinant glutamine-binding protein (GlnBP) from E. coli. We found that GlnBP specifically binds the sequence of amino acids present both in gliadin and other prolamines classified as toxic for celiac patients. Affinity chromatography experiments together with mass spectrometry experiments demonstrated that GlnBP can bind the following amino acid sequence XXQPQPQQQQQQQQQQQQL. Sequence alignment experiments pointed out that this sequence is exclusively representative of the gliadin and the other prolamines considered toxic for celiac patients. These findings suggest the development of a competitive resonance energy transfer (RET) assay for an easy and rapid detection of this sequence in raw and cooked food.
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With the exception of the phloem and the crown of the parenchyma, which borders the medullary lacuna, the walls of the tissues of both treated and untreated straw were lignified. The walls of the treated straw were not fluorescent in the ultraviolet probably because the treatment had modified the phenolic acids. They also had a stronger reaction to Schiff reagent particularly in the sclerenchyma indicating that their polysaccharides were more accessible. The tissues of the treated straw degraded faster in the rumen. The walls of the sclerenchyma of the treated straw were attacked by micro-organisms. Both treated and normal straw were abundantly colonized by rumen fungi, especially in the sclerenchyma. The increase in the digestibility of the treated straw was due to the greater access the micro-organisms had to the polysaccharides of the lignified walls.
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